NCBI Conserved Domain Search

Conserved domains on [gi|411147369|ref|NP_001258628|]

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iron-sulfur clusters transporter ABCB7, mitochondrial isoform 5 [Homo sapiens]

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 ...

116-672

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: 869.91 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 116 IVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLH 195
Cdd:COG5265   43 LLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLLLAYGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLH 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 196 NLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTVAVTRW 275
Cdd:COG5265  123 ALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEW 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 276 RTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMV 355
Cdd:COG5265  203 RTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMML 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 356 LASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLQITPqtATVAF 435
Cdd:COG5265  283 MAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGG--GEVRF 360

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQD 515
Cdd:COG5265  361 ENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 AVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDE 595
Cdd:COG5265  441 TVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 596 ATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQSSR 672
Cdd:COG5265  521 ATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQMWARQQEE 596

Name

Accession

Description

Interval

E-value

ATM1

COG5265

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...

116-672

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: 869.91 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 116 IVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLH 195
Cdd:COG5265   43 LLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLLLAYGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLH 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 196 NLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTVAVTRW 275
Cdd:COG5265  123 ALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEW 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 276 RTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMV 355
Cdd:COG5265  203 RTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMML 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 356 LASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLQITPqtATVAF 435
Cdd:COG5265  283 MAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGG--GEVRF 360

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQD 515
Cdd:COG5265  361 ENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 AVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDE 595
Cdd:COG5265  441 TVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 596 ATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQSSR 672
Cdd:COG5265  521 ATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQMWARQQEE 596

ABC_6TM_ATM1_ABCB7

cd18582

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

113-405

2.79e-163

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: 471.60 E-value: 2.79e-163

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLnqmsgnmlnlSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFL 192
Cdd:cd18582   10 LLNVAVPFLLKYAVDAL----------SAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRVFR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 193 HLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTVAV 272
Cdd:cd18582   80 HLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVALYVAFTIKV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 273 TRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTA 352
Cdd:cd18582  160 TEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGLTA 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 411147369 353 IMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 405
Cdd:cd18582  240 IMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292

MsbA_lipidA

TIGR02203

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...

152-656

2.15e-101

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: 322.44 E-value: 2.15e-101

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  152 AVLIGYGVSRAGAAFFNevrNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFN 231
Cdd:TIGR02203  58 LVVIGLAVLRGICSFVS---TYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTL---LSRITFDSEQVASAATDA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  232 LLPIMFEVMLVSGVLYYKCGAQFALvTLGTLGTYTAFTVAVTRWRTRFR---IEMNKADNDAGNAAIDSLLNYETVKYFN 308
Cdd:TIGR02203 132 FIVLVRETLTVIGLFIVLLYYSWQL-TLIVVVMLPVLSILMRRVSKRLRrisKEIQNSMGQVTTVAEETLQGYRVVKLFG 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  309 NERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFL 388
Cdd:TIGR02203 211 GQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSL 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  389 GTVYRETRQALIDMNTLFTLLkvDTQikDKVMASPLQITPQTATVAFDNVHFEYI-EGQKVLSGISFEVPAGKKVAIVGG 467
Cdd:TIGR02203 291 TNVNAPMQRGLAAAESLFTLL--DSP--PEKDTGTRAIERARGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGR 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  468 SGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNIS-ASPEEVYAVAKLA 546
Cdd:TIGR02203 367 SGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAA 446

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  547 GLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAH 626
Cdd:TIGR02203 447 YAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAH 526

                         490       500       510
                  ....*....|....*....|....*....|
gi 411147369  627 RLSTVVDADEIIVLDQGKVAERGTHHGLLA 656
Cdd:TIGR02203 527 RLSTIEKADRIVVMDDGRIVERGTHNELLA 556

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

184-656

1.94e-95

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 307.27 E-value: 1.94e-95

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 184 RRIA--KNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFV--------LSALV--FNLLPIMFEVmlvsgvlyykcG 251
Cdd:PRK13657  87 RRLAvlTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLwlefmrehLATLValVVLLPLALFM-----------N 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 252 AQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKS 331
Cdd:PRK13657 156 WRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPV 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 332 TSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNG---LLFQ-LSLPLNFLGTVYRETRQalidMNTLFT 407
Cdd:PRK13657 236 LSWWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGfatLLIGrLDQVVAFINQVFMAAPK----LEEFFE 311

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 408 LLKVDTQIKDKVMASPLQITpqTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQK 487
Cdd:PRK13657 312 VEDAVPDVRDPPGAIDLGRV--KGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQS 389

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 488 GSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERG 567
Cdd:PRK13657 390 GRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERG 469

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 568 LKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAE 647
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549


                 ....*....
gi 411147369 648 RGTHHGLLA 656
Cdd:PRK13657 550 SGSFDELVA 558

ABC_tran

pfam00005

ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...

449-598

2.53e-42

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

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 150.49 E-value: 2.53e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  449 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLF-HNTIYYNL 527
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369  528 LYGnisASPEEVYAVAKLAGLHDAI--LRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATS 598
Cdd:pfam00005  81 RLG---LLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

444-640

4.26e-14

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.11 E-value: 4.26e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 444 EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvsleslRRAVGVVPQdavlfhnti 523
Cdd:NF040873   3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQ--------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 524 yynllygnISASPEEVYA-VAKLAGL----HDAILRMPHGYDTQVGERGLK--------------LSGGEKQRVAIARAI 584
Cdd:NF040873  63 --------RSEVPDSLPLtVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALErvgladlagrqlgeLSGGQRQRALLAQGL 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 585 LKDPPVILYDEATSSLDSITEETILGAMKDVV-KHRTSIFIAHRLSTVVDADEIIVL 640
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

459-641

5.62e-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: 61.24 E-value: 5.62e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   459 GKKVAIVGGSGSGKSTIVRLLFRFYEPQKGS-IYLAGQNIQDVSLESLRravgvvpqdavlfhntiyynllygnisaspe 537
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------- 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   538 evyavaklaglhdailrmphgyDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK 617
Cdd:smart00382  51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108

                          170       180       190
                   ....*....|....*....|....*....|.
gi 411147369   618 HRTS-------IFIAHRLSTVVDADEIIVLD 641
Cdd:smart00382 109 LLLKseknltvILTTNDEKDLGPALLRRRFD 139

GguA

NF040905

sugar ABC transporter ATP-binding protein;

445-647

3.99e-09

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 3.99e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL-----FRFYEpqkGSIYLAGQ-----NIQDvsleSLRRAVGVVPQ 514
Cdd:NF040905  13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvypHGSYE---GEILFDGEvcrfkDIRD----SEALGIVIIHQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 D-AVLFHNTIYYNLLYGNISASP-----EEVYAVAK--LA--GLHDAilrmPhgyDTQVGERGLklsgGEKQRVAIARAI 584
Cdd:NF040905  86 ElALIPYLSIAENIFLGNERAKRgvidwNETNRRARelLAkvGLDES----P---DTLVTDIGV----GKQQLVEIAKAL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 585 LKDPPVILYDEATSSL---DSiteETILGAMKDVVKHR-TSIFIAHRLSTVVD-ADEIIVLDQGKVAE 647
Cdd:NF040905 155 SKDVKLLILDEPTAALneeDS---AALLDLLLELKAQGiTSIIISHKLNEIRRvADSITVLRDGRTIE 219

40850658_otr

NF000106

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

564-649

4.01e-04

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 4.01e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 564 GERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD--ADEIIVLD 641
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqlAHELTVID 218


                 ....*...
gi 411147369 642 QGKVAERG 649
Cdd:NF000106 219 RGRVIADG 226

Name

Accession

Description

Interval

E-value

ATM1

COG5265

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...

116-672

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: 869.91 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 116 IVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLH 195
Cdd:COG5265   43 LLLLLAAALALVVPPLLKDAIDALLSGAAALLVVPVGLLLAYGLLRLLSVLFGELRDALFARVTQRAVRRLALEVFRHLH 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 196 NLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTVAVTRW 275
Cdd:COG5265  123 ALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGILLVKYDWWFALITLVTVVLYIAFTVVVTEW 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 276 RTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMV 355
Cdd:COG5265  203 RTKFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMML 282

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 356 LASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLQITPqtATVAF 435
Cdd:COG5265  283 MAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMFDLLDQPPEVADAPDAPPLVVGG--GEVRF 360

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQD 515
Cdd:COG5265  361 ENVSFGYDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQD 440

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 AVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDE 595
Cdd:COG5265  441 TVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDE 520

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 596 ATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQSSR 672
Cdd:COG5265  521 ATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQMWARQQEE 596

MdlB

COG1132

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

111-671

2.35e-176

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 515.87 E-value: 2.35e-176

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 111 EGAMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIGYGVSRAGAAFFnevRNAVFGKVAQNSIRRIAKNV 190
Cdd:COG1132   33 SALLELLLPLLLGRIIDAL---------LAGGDLSALLLLLLLLLGLALLRALLSYL---QRYLLARLAQRVVADLRRDL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 191 FLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKcGAQFALVTLGTLGTYTAFTV 270
Cdd:COG1132  101 FEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVI-DWRLALIVLLVLPLLLLVLR 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 271 AVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGL 350
Cdd:COG1132  180 LFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGL 259

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 351 TAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKvmASPLQITPQT 430
Cdd:COG1132  260 ALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDP--PGAVPLPPVR 337

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 431 ATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVG 510
Cdd:COG1132  338 GEIEFENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIG 417

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 511 VVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPV 590
Cdd:COG1132  418 VVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPI 497

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 591 ILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQS 670
Cdd:COG1132  498 LILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRLQF 576


                 .
gi 411147369 671 S 671
Cdd:COG1132  577 G 577

ABC_6TM_ATM1_ABCB7

cd18582

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

113-405

2.79e-163

Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 471.60 E-value: 2.79e-163

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLnqmsgnmlnlSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFL 192
Cdd:cd18582   10 LLNVAVPFLLKYAVDAL----------SAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRVFR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 193 HLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTVAV 272
Cdd:cd18582   80 HLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVALYVAFTIKV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 273 TRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTA 352
Cdd:cd18582  160 TEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALIISLGLTA 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 411147369 353 IMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 405
Cdd:cd18582  240 IMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSLIDMEKL 292

ABCC_ATM1_transporter

cd03253

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...

433-669

2.56e-144

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 420.87 E-value: 2.56e-144

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 512
Cdd:cd03253    1 IEFENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 513 PQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVIL 592
Cdd:cd03253   81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 593 YDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLAnPHSIYSEMWHTQ 669
Cdd:cd03253  161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAEMWKAQ 236

SunT

COG2274

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...

112-669

1.94e-137

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: 420.39 E-value: 1.94e-137

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 112 GAMNIVVPFMFKYAVDSLnqMSGNMLNlsdapnTVATMATAVLIGYGVSragaAFFNEVRNAVFGKVAQNSIRRIAKNVF 191
Cdd:COG2274  169 NLLALATPLFTQVVIDRV--LPNQDLS------TLWVLAIGLLLALLFE----GLLRLLRSYLLLRLGQRIDLRLSSRFF 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 192 LHLHNLDLGFHLSRQTGALSKAIdRGTRGI-SFVLSALVFNLLPIMFevMLVSGVL--YYkcGAQFALVTLGTLGTYTAF 268
Cdd:COG2274  237 RHLLRLPLSFFESRSVGDLASRF-RDVESIrEFLTGSLLTALLDLLF--VLIFLIVlfFY--SPPLALVVLLLIPLYVLL 311

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 269 TVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSV 348
Cdd:COG2274  312 GLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQL 391

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 349 GLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLkvDTQIKDKVMASPLQITP 428
Cdd:COG2274  392 ATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDIL--DLPPEREEGRSKLSLPR 469

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 429 QTATVAFDNVHFEYIE-GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRR 507
Cdd:COG2274  470 LKGDIELENVSFRYPGdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR 549

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 508 AVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKD 587
Cdd:COG2274  550 QIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRN 629

                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 588 PPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWH 667
Cdd:COG2274  630 PRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELVQ 708


                 ..
gi 411147369 668 TQ 669
Cdd:COG2274  709 QQ 710

ABCC_MsbA

cd03251

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...

433-666

2.53e-102

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

Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 313.01 E-value: 2.53e-102

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYI-EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 511
Cdd:cd03251    1 VEFKNVTFRYPgDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVI 591
Cdd:cd03251   81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 592 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMW 666
Cdd:cd03251  161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKLH 234

MsbA_lipidA

TIGR02203

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...

152-656

2.15e-101

Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 322.44 E-value: 2.15e-101

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  152 AVLIGYGVSRAGAAFFNevrNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFN 231
Cdd:TIGR02203  58 LVVIGLAVLRGICSFVS---TYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTL---LSRITFDSEQVASAATDA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  232 LLPIMFEVMLVSGVLYYKCGAQFALvTLGTLGTYTAFTVAVTRWRTRFR---IEMNKADNDAGNAAIDSLLNYETVKYFN 308
Cdd:TIGR02203 132 FIVLVRETLTVIGLFIVLLYYSWQL-TLIVVVMLPVLSILMRRVSKRLRrisKEIQNSMGQVTTVAEETLQGYRVVKLFG 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  309 NERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFL 388
Cdd:TIGR02203 211 GQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSL 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  389 GTVYRETRQALIDMNTLFTLLkvDTQikDKVMASPLQITPQTATVAFDNVHFEYI-EGQKVLSGISFEVPAGKKVAIVGG 467
Cdd:TIGR02203 291 TNVNAPMQRGLAAAESLFTLL--DSP--PEKDTGTRAIERARGDVEFRNVTFRYPgRDRPALDSISLVIEPGETVALVGR 366

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  468 SGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNIS-ASPEEVYAVAKLA 546
Cdd:TIGR02203 367 SGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAA 446

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  547 GLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAH 626
Cdd:TIGR02203 447 YAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAH 526

                         490       500       510
                  ....*....|....*....|....*....|
gi 411147369  627 RLSTVVDADEIIVLDQGKVAERGTHHGLLA 656
Cdd:TIGR02203 527 RLSTIEKADRIVVMDDGRIVERGTHNELLA 556

CydD

COG4988

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...

295-657

5.04e-101

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: 5.04e-101

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 295 IDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKstsTLAMlNFGQSA----IFSVGLTAIMVLASQGIVAGTLTVGD 370
Cdd:COG4988  201 LDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMK---VLRV-AFLSSAvlefFASLSIALVAVYIGFRLLGGSLTLFA 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 371 LVMVngLLfqLS----LPLNFLGTVYRETRQALIDMNTLFTLLkvDTQIKDKVMASPLQITPQTATVAFDNVHFEYIEGQ 446
Cdd:COG4988  277 ALFV--LL--LApeffLPLRDLGSFYHARANGIAAAEKIFALL--DAPEPAAPAGTAPLPAAGPPSIELEDVSFSYPGGR 350

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYN 526
Cdd:COG4988  351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIREN 430

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 527 LLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEE 606
Cdd:COG4988  431 LRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEA 510

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 411147369 607 TILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLAN 657
Cdd:COG4988  511 EILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561

ABCC_Glucan_exporter_like

cd03254

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...

431-656

3.84e-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: 306.84 E-value: 3.84e-100

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 431 ATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVG 510
Cdd:cd03254    1 GEIEFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 511 VVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPV 590
Cdd:cd03254   81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 591 ILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLA 656
Cdd:cd03254  161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226

ABC_MTABC3_MDL1_MDL2

cd03249

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...

433-669

6.56e-99

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.

Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 304.08 E-value: 6.56e-99

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIE--GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVG 510
Cdd:cd03249    1 IEFKNVSFRYPSrpDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 511 VVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPV 590
Cdd:cd03249   81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147369 591 ILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQ 669
Cdd:cd03249  161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKLVKAQ 238

MsbA_rel

TIGR02204

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...

113-656

1.36e-98

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: 315.10 E-value: 1.36e-98

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  113 AMNIVVPFMFKYAVD-SLNQMSGNMLNLSDAPNTVATMATAVLIG---YGVSRAGAAFFNEVRNAVFGkvaqnsirriak 188
Cdd:TIGR02204  32 AATLSLPYAVRLMIDhGFSKDSSGLLNRYFAFLLVVALVLALGTAarfYLVTWLGERVVADIRRAVFA------------ 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  189 nvflHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNL-LPIMFEVMLVSGV-LYYKCGAQFALVTLGTLGTYT 266
Cdd:TIGR02204 100 ----HLISLSPSFFDKNRSGEV---VSRLTTDTTLLQSVIGSSLsMALRNALMCIGGLiMMFITSPKLTSLVLLAVPLVL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  267 AFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNfgQSAIF 346
Cdd:TIGR02204 173 LPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRALLT--AIVIV 250

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  347 SV--GLTAIMVLASQGIVAGTLTVGDL-------VMVNGLLFQLSlplnflgTVYRETRQALIDMNTLFTLLKVDTQIKd 417
Cdd:TIGR02204 251 LVfgAIVGVLWVGAHDVIAGKMSAGTLgqfvfyaVMVAGSIGTLS-------EVWGELQRAAGAAERLIELLQAEPDIK- 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  418 kVMASPLQI-TPQTATVAFDNVHFEYIE--GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAG 494
Cdd:TIGR02204 323 -APAHPKTLpVPLRGEIEFEQVNFAYPArpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDG 401

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  495 QNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGE 574
Cdd:TIGR02204 402 VDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQ 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  575 KQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGL 654
Cdd:TIGR02204 482 RQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAEL 561


                  ..
gi 411147369  655 LA 656
Cdd:TIGR02204 562 IA 563

ABC_6TM_ATM1_ABCB7_HMT1_ABCB6

cd18560

Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ...

113-405

1.38e-95

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: 297.60 E-value: 1.38e-95

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLnqmsgnmlnlSDAPNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFL 192
Cdd:cd18560   10 ACNVLAPLFLGRAVNAL----------TLAKVKDLESAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 193 HLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTVAV 272
Cdd:cd18560   80 HLHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVVSVVFAFHFGAWLALIVFLSVLLYGVFTIKV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 273 TRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTA 352
Cdd:cd18560  160 TEWRTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTL 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 411147369 353 IMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 405
Cdd:cd18560  240 GLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSLTDMENL 292

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

184-656

1.94e-95

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 307.27 E-value: 1.94e-95

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 184 RRIA--KNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFV--------LSALV--FNLLPIMFEVmlvsgvlyykcG 251
Cdd:PRK13657  87 RRLAvlTEYFERIIQLPLAWHSQRGSGRALHTLLRGTDALFGLwlefmrehLATLValVVLLPLALFM-----------N 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 252 AQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKS 331
Cdd:PRK13657 156 WRLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMPV 235

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 332 TSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNG---LLFQ-LSLPLNFLGTVYRETRQalidMNTLFT 407
Cdd:PRK13657 236 LSWWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVGfatLLIGrLDQVVAFINQVFMAAPK----LEEFFE 311

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 408 LLKVDTQIKDKVMASPLQITpqTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQK 487
Cdd:PRK13657 312 VEDAVPDVRDPPGAIDLGRV--KGAVEFDDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQS 389

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 488 GSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERG 567
Cdd:PRK13657 390 GRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERG 469

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 568 LKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAE 647
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549


                 ....*....
gi 411147369 648 RGTHHGLLA 656
Cdd:PRK13657 550 SGSFDELVA 558

CydC

COG4987

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...

220-667

2.40e-92

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: 298.60 E-value: 2.40e-92

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 220 GISFVLSALVFNLLPIMFEVMLVSGVLyykcgaqfalVTLGTLGTYTAFTVAVTRWRTRFRIemnkadndagnAAIDSLL 299
Cdd:COG4987  145 AAVAFLAFFSPALALVLALGLLLAGLL----------LPLLAARLGRRAGRRLAAARAALRA-----------RLTDLLQ 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 300 NYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVngLLF 379
Cdd:COG4987  204 GAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALL--VLA 281

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 380 QLSL--PLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLqitPQTATVAFDNVHFEY-IEGQKVLSGISFEV 456
Cdd:COG4987  282 ALALfeALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPA---PGGPSLELEDVSFRYpGAGRPVLDGLSLTL 358

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 457 PAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASP 536
Cdd:COG4987  359 PPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATD 438

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 537 EEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVV 616
Cdd:COG4987  439 EELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL 518

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|.
gi 411147369 617 KHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWH 667
Cdd:COG4987  519 AGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQ-NGRYRQLYQ 568

PRK11176

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

174-669

3.61e-87

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

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 285.37 E-value: 3.61e-87

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 174 VFGKVAQNsIRRiakNVFLHLHNLDLGFHLSRQTGAL-------SKAIDRGTRG--ISFVL-SALVFNLLPIMFevmlvs 243
Cdd:PRK11176  92 VSGKVVMT-MRR---RLFGHMMGMPVSFFDKQSTGTLlsritydSEQVASSSSGalITVVReGASIIGLFIMMF------ 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 244 gvlYYKCgaQFALVtLGTLGTYTAFTVAVTRwrTRFRIEMNKADNDAG---NAAIDSLLNYETVKYFNNERYEAQRYDGF 320
Cdd:PRK11176 162 ---YYSW--QLSLI-LIVIAPIVSIAIRVVS--KRFRNISKNMQNTMGqvtTSAEQMLKGHKEVLIFGGQEVETKRFDKV 233

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 321 LKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALI 400
Cdd:PRK11176 234 SNRMRQQGMKMVSASSISDPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMA 313

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 401 DMNTLFTLLKVDTQiKDKvmaSPLQITPQTATVAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL 479
Cdd:PRK11176 314 ACQTLFAILDLEQE-KDE---GKRVIERAKGDIEFRNVTFTYPGKEVpALRNINFKIPAGKTVALVGRSGSGKSTIANLL 389

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 480 FRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYG-NISASPEEVYAVAKLAGLHDAILRMPHG 558
Cdd:PRK11176 390 TRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAARMAYAMDFINKMDNG 469

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 559 YDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEII 638
Cdd:PRK11176 470 LDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEIL 549

                        490       500       510
                 ....*....|....*....|....*....|.
gi 411147369 639 VLDQGKVAERGTHHGLLANpHSIYSEMWHTQ 669
Cdd:PRK11176 550 VVEDGEIVERGTHAELLAQ-NGVYAQLHKMQ 579

ABC_6TM_ABCB6

cd18581

Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ...

113-402

9.81e-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: 261.80 E-value: 9.81e-82

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIGY-------GVSRAGAAFFNEVRNAVFGKVAQNSIRR 185
Cdd:cd18581   10 VVNVLVPILYKKIVDSL---------TPDSADSPLAFPWALILLYvflkflqGGGSGSVGLLSNLRSFLWIPVQQFTTRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 186 IAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTY 265
Cdd:cd18581   81 ISVKLFAHLHSLSLRWHLSRKTGEVLRVMDRGTSSINSLLSYVLFNIGPTIADIIIAIIYFAIAFNPWFGLIVFVTMALY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 266 TAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAI 345
Cdd:cd18581  161 LILTIIITEWRTKFRREMNKLDNEKRAKAVDSLLNFETVKYYNAERFEVERYRRAIDDYQVAEWKSNASLNLLNTAQNLI 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 346 FSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDM 402
Cdd:cd18581  241 ITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSFIDM 297

3a01208

TIGR00958

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

184-665

2.29e-79

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

Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 267.74 E-value: 2.29e-79

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  184 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGT----RGISFVLSALVFNLlpimfeVMLVsGVLYYKC--GAQFALV 257
Cdd:TIGR00958 234 LRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTqtmsRSLSLNVNVLLRNL------VMLL-GLLGFMLwlSPRLTMV 306

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  258 TLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKtyETASLKSTSTLA- 336
Cdd:TIGR00958 307 TLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALE--ETLQLNKRKALAy 384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  337 MLNFGQSAIFSVGL-TAIMVLASQGIVAGTLTVGDLVMVngLLFQLSL--PLNFLGTVYRETRQALIDMNTLFTLLKVDT 413
Cdd:TIGR00958 385 AGYLWTTSVLGMLIqVLVLYYGGQLVLTGKVSSGNLVSF--LLYQEQLgeAVRVLSYVYSGMMQAVGASEKVFEYLDRKP 462

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  414 QIKDKVMASPLqitPQTATVAFDNVHFEYIE--GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIY 491
Cdd:TIGR00958 463 NIPLTGTLAPL---NLEGLIEFQDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL 539

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  492 LAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLS 571
Cdd:TIGR00958 540 LDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLS 619

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  572 GGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKdvVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTH 651
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTH 697

                         490
                  ....*....|....
gi 411147369  652 HGLLANPhSIYSEM 665
Cdd:TIGR00958 698 KQLMEDQ-GCYKHL 710

ABCC_MRP_Like

cd03228

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...

433-644

1.34e-78

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

Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 248.45 E-value: 1.34e-78

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEG-QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 511
Cdd:cd03228    1 IEFKNVSFSYPGRpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VPQDAVLFHNTIYYNLlygnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVI 591
Cdd:cd03228   81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 411147369 592 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGK 644
Cdd:cd03228  119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171

ABCC_Hemolysin

cd03252

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...

433-669

9.49e-78

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.

Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 248.94 E-value: 9.49e-78

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEY-IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 511
Cdd:cd03252    1 ITFEHVRFRYkPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVI 591
Cdd:cd03252   81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 592 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQ 669
Cdd:cd03252  161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQLQ 237

ABCC_MRP_domain2

cd03244

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...

433-650

4.71e-72

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: 233.15 E-value: 4.71e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 511
Cdd:cd03244    3 IEFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VPQDAVLFHNTIYYNL-LYGniSASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPV 590
Cdd:cd03244   83 IPQDPVLFSGTIRSNLdPFG--EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 591 ILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGT 650
Cdd:cd03244  161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220

NHLM_micro_ABC1

TIGR03796

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...

184-656

5.53e-71

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

Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 245.24 E-value: 5.53e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  184 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAI---DRGTRGISFVLSALVFNLLPIMFEVMLVsgVLYykcGAQFALVTLG 260
Cdd:TIGR03796 227 VGMSARFLWHILRLPVRFFAQRHAGDIASRVqlnDQVAEFLSGQLATTALDAVMLVFYALLM--LLY---DPVLTLIGIA 301

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  261 TlgtyTAFTVAVTRWRTRFRIEMN-KADNDAG---NAAIDSLLNYETVKYFNNERYEAQRYDGflktYETASLKSTSTLA 336
Cdd:TIGR03796 302 F----AAINVLALQLVSRRRVDANrRLQQDAGkltGVAISGLQSIETLKASGLESDFFSRWAG----YQAKLLNAQQELG 373

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  337 MLNfgqsAIFSV------GLTAIMVLASQG--IVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTL 408
Cdd:TIGR03796 374 VLT----QILGVlptlltSLNSALILVVGGlrVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDV 449

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  409 LK--VDTQIKDKVMASPLQITPQ--TATVAFDNVHFEY-IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFY 483
Cdd:TIGR03796 450 LRnpVDPLLEEPEGSAATSEPPRrlSGYVELRNITFGYsPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLY 529

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  484 EPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQV 563
Cdd:TIGR03796 530 QPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAEL 609

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  564 GERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILgamkDVVKHR--TSIFIAHRLSTVVDADEIIVLD 641
Cdd:TIGR03796 610 AEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIID----DNLRRRgcTCIIVAHRLSTIRDCDEIIVLE 685

                         490
                  ....*....|....*
gi 411147369  642 QGKVAERGTHHGLLA 656
Cdd:TIGR03796 686 RGKVVQRGTHEELWA 700

bacteriocin_ABC

TIGR01193

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...

143-667

1.08e-70

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

Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 244.26 E-value: 1.08e-70

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  143 PNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGIS 222
Cdd:TIGR01193 188 PHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEI---VSRFTDASS 264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  223 FV--LSALVFNLLPIMFEVMLVSGVLYYKcGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLN 300
Cdd:TIGR01193 265 IIdaLASTILSLFLDMWILVIVGLFLVRQ-NMLLFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNG 343

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  301 YETVKYFNNERYEAQRYDGFLKTYetasLKSTSTLAMLNFGQSAIFSV-GLTAIMVL---ASQGIVAGTLTVGDLVMVNG 376
Cdd:TIGR01193 344 IETIKSLTSEAERYSKIDSEFGDY----LNKSFKYQKADQGQQAIKAVtKLILNVVIlwtGAYLVMRGKLTLGQLITFNA 419

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  377 LLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLqiTPQTATVAFDNVHFEYIEGQKVLSGISFEV 456
Cdd:TIGR01193 420 LLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFINKKKRTEL--NNLNGDIVINDVSYSYGYGSNILSDISLTI 497

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  457 PAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNI-SAS 535
Cdd:TIGR01193 498 KMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKeNVS 577

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  536 PEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDv 615
Cdd:TIGR01193 578 QDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN- 656

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|..
gi 411147369  616 VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLaNPHSIYSEMWH 667
Cdd:TIGR01193 657 LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL-DRNGFYASLIH 707

ABCC_bacteriocin_exporters

cd03245

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...

433-645

8.66e-70

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: 227.09 E-value: 8.66e-70

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQ-KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 511
Cdd:cd03245    3 IEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVI 591
Cdd:cd03245   83 VPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPIL 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 411147369 592 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKV 645
Cdd:cd03245  163 LLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216

chvA

TIGR01192

glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...

347-654

1.66e-66

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

Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 230.16 E-value: 1.66e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  347 SVGLTAIMVLASQGIVAGTLTVGDLVMVNG----LLFQLSLPLNFLGTVYrETRQALIDmntlFTLLKVDTQIKDKVMAS 422
Cdd:TIGR01192 251 TISMMCILVIGTVLVIKGELSVGEVIAFIGfanlLIGRLDQMSGFITQIF-EARAKLED----FFDLEDSVFQREEPADA 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  423 PlQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL 502
Cdd:TIGR01192 326 P-ELPNVKGAVEFRHITFEFANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTR 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  503 ESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIAR 582
Cdd:TIGR01192 405 ESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIAR 484

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147369  583 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGL 654
Cdd:TIGR01192 485 AILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQEL 556

ABC_6TM_HMT1

cd18583

Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...

113-405

1.76e-66

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: 220.86 E-value: 1.76e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLNQMSGNMlnlsdapntvatMATAVLIgYGVSR--AGAAFFNEVRNAVFGKVAQNSIRRIAKNV 190
Cdd:cd18583   10 VLNVLVPRQLGIIVDSLSGGSGKS------------PWKEIGL-YVLLRflQSGGGLGLLRSWLWIPVEQYSYRALSTAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 191 FLHLHNLDLGFHLSRQTGALSKAIDRGTrGISFVLSALVFNLLPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFTV 270
Cdd:cd18583   77 FNHVMNLSMDFHDSKKSGEVLKAIEQGS-SINDLLEQILFQIVPMIIDLVIAIVYLYYLFDPYMGLIVAVVMVLYVWSTI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 271 AVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGL 350
Cdd:cd18583  156 KLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKNYQKAERKYLFSLNLLNAVQSLILTLGL 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 351 TAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 405
Cdd:cd18583  236 LAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDAERL 290

ABCC_TAP

cd03248

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...

426-645

3.04e-65

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.

Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 215.41 E-value: 3.04e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 426 ITPQT--ATVAFDNVHFEYIE--GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS 501
Cdd:cd03248    3 LAPDHlkGIVKFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 502 LESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIA 581
Cdd:cd03248   83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147369 582 RAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKV 645
Cdd:cd03248  163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226

PRK10789

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

361-669

1.68e-61

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

Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 216.12 E-value: 1.68e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 361 IVAGTLTVGDL---VMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVdtqIKDKVMASPlqitPQTATVAFDN 437
Cdd:PRK10789 246 VVNGSLTLGQLtsfVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPV---VKDGSEPVP----EGRGELDVNI 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 438 VHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDA 516
Cdd:PRK10789 319 RQFTYPQTDHpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTP 398

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 517 VLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 596
Cdd:PRK10789 399 FLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDA 478

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369 597 TSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPhSIYSEMWHTQ 669
Cdd:PRK10789 479 LSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS-GWYRDMYRYQ 550

CydD

TIGR02857

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...

161-640

1.36e-60

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD

Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 212.53 E-value: 1.36e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  161 RAGAAFFNEVRNAVFGKVAQNSIRRIAKnvflhlhnldlgfhlsRQTGALSKAIDRGTRGisfvLSALVFNLLPIMFEVM 240
Cdd:TIGR02857  70 RAAAAVKSQLRERLLEAVAALGPRWLQG----------------RPSGELATLALEGVEA----LDGYFARYLPQLVLAV 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  241 LVSGVLYYKCGAQ---FALVTLGTLGTYTAFtVAVTRWRTRFRIEMN-KADNDAGNAAIDSLLNYETVKYFNNERYEAQR 316
Cdd:TIGR02857 130 IVPLAILAAVFPQdwiSGLILLLTAPLIPIF-MILIGWAAQAAARKQwAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAA 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  317 ydgfLKTYETASLKST-STLAMlNFGQSAIF------SVGLTAIMVlasqGIvagTLTVGDLVMVNGLLFQL-----SLP 384
Cdd:TIGR02857 209 ----IRRSSEEYRERTmRVLRI-AFLSSAVLelfatlSVALVAVYI----GF---RLLAGDLDLATGLFVLLlapefYLP 276

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  385 LNFLGTVYRETRQALIDMNTLFTLLKVDTQI----KDKVMASPLQITpqtatvaFDNVHFEYIEGQKVLSGISFEVPAGK 460
Cdd:TIGR02857 277 LRQLGAQYHARADGVAAAEALFAVLDAAPRPlagkAPVTAAPASSLE-------FSGVSVAYPGRRPALRPVSFTVPPGE 349

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  461 KVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVY 540
Cdd:TIGR02857 350 RVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIR 429

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  541 AVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRT 620
Cdd:TIGR02857 430 EALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRT 509

                         490       500
                  ....*....|....*....|
gi 411147369  621 SIFIAHRLSTVVDADEIIVL 640
Cdd:TIGR02857 510 VLLVTHRLALAALADRIVVL 529

PRK11160

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

425-657

4.28e-60

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

Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 212.38 E-value: 4.28e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 425 QITPQTATVAFDNVHFEYIEG-QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE 503
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYPDQpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEA 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 504 SLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLhDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARA 583
Cdd:PRK11160 411 ALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAWLGEGGRQLSGGEQRRLGIARA 489

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147369 584 ILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLAN 657
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ 563

PRK10790

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

311-669

2.79e-59

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

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 210.34 E-value: 2.79e-59

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 311 RYEAQRYDGFLkTYETASLKSTSTLA--MLNFGQSAifsvgltaimvlasqgivAGTLTVGDLVMVNGLLFQLSLPLNFL 388
Cdd:PRK10790 241 RMQTLRLDGFL-LRPLLSLFSALILCglLMLFGFSA------------------SGTIEVGVLYAFISYLGRLNEPLIEL 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 389 GTVYRETRQALIDMNTLFTLlkvdtqikdkvMASPLQ------ITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKV 462
Cdd:PRK10790 302 TTQQSMLQQAVVAGERVFEL-----------MDGPRQqygnddRPLQSGRIDIDNVSFAYRDDNLVLQNINLSVPSRGFV 370

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 463 AIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYG-NISAspEEVYA 541
Cdd:PRK10790 371 ALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGrDISE--EQVWQ 448

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 542 VAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTS 621
Cdd:PRK10790 449 ALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTL 528

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 411147369 622 IFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANpHSIYSEMWHTQ 669
Cdd:PRK10790 529 VVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA-QGRYWQMYQLQ 575

CydC

TIGR02868

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...

316-628

2.92e-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: 197.97 E-value: 2.92e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  316 RYDGFLKTYETASLKST----STLAMLNFGQSA-IFSVGLTAIMVL--ASQGIVAGTLTVGDLVMVngLLFQLSL--PLN 386
Cdd:TIGR02868 211 ALPAALAQVEEADRELTraerRAAAATALGAALtLLAAGLAVLGALwaGGPAVADGRLAPVTLAVL--VLLPLAAfeAFA 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  387 FLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVG 466
Cdd:TIGR02868 289 ALPAAAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAPPVLDGVSLDLPPGERVAILG 368

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  467 GSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLA 546
Cdd:TIGR02868 369 PSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERV 448

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  547 GLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAH 626
Cdd:TIGR02868 449 GLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528


                  ..
gi 411147369  627 RL 628
Cdd:TIGR02868 529 HL 530

ArpD

COG4618

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...

254-646

4.66e-55

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: 198.05 E-value: 4.66e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 254 FALVTLGTLGTYTAFTVAvTRWRTRFRI-EMNKADNDAGNAAIDSLLNYETVkyfnneryEA------------QRYDGF 320
Cdd:COG4618  157 LGLLALVGALVLVALALL-NERLTRKPLkEANEAAIRANAFAEAALRNAEVI--------EAmgmlpalrrrwqRANARA 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 321 LKTYETASLKSTSTLAML----NFGQSAIFSVGltAIMVLASQ----GIVAGTLTVG------DLVMVNGLLFQlslpln 386
Cdd:COG4618  228 LALQARASDRAGGFSALSkflrLLLQSAVLGLG--AYLVIQGEitpgAMIAASILMGralapiEQAIGGWKQFV------ 299

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 387 flgtvyrETRQALIDMNTLFTLLKVDtqikDKVMASPlqiTPQtATVAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIV 465
Cdd:COG4618  300 -------SARQAYRRLNELLAAVPAE----PERMPLP---RPK-GRLSVENLTVVPPGSKRpILRGVSFSLEPGEVLGVI 364

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 466 GGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYynllyGNIS----ASPEEVYA 541
Cdd:COG4618  365 GPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIA-----ENIArfgdADPEKVVA 439

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 542 VAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTS 621
Cdd:COG4618  440 AAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGAT 519

                        410       420
                 ....*....|....*....|....*.
gi 411147369 622 IF-IAHRLSTVVDADEIIVLDQGKVA 646
Cdd:COG4618  520 VVvITHRPSLLAAVDKLLVLRDGRVQ 545

ABCC_NFT1

cd03369

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...

428-650

9.97e-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: 183.77 E-value: 9.97e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 428 PQTATVAFDNVHFEYI-EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLR 506
Cdd:cd03369    2 PEHGEIEVENLSVRYApDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 507 RAVGVVPQDAVLFHNTIYYNL-LYGNIsaSPEEVYAVAKlaglhdailrmphgydtqVGERGLKLSGGEKQRVAIARAIL 585
Cdd:cd03369   82 SSLTIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 586 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGT 650
Cdd:cd03369  142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206

PRK11174

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

384-658

2.69e-52

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

Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 190.83 E-value: 2.69e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 384 PLNFLGTVYRETRQALIDMNTLFTLLKVDTQikdkvmasplqiTPQTATVAFDNVHFEYIEGQ---------KVLSG-IS 453
Cdd:PRK11174 303 PLRDLGTFYHAKAQAVGAAESLVTFLETPLA------------HPQQGEKELASNDPVTIEAEdleilspdgKTLAGpLN 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 454 FEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNIS 533
Cdd:PRK11174 371 FTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPD 449

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 534 ASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMK 613
Cdd:PRK11174 450 ASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALN 529

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 411147369 614 DVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:PRK11174 530 AASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574

EcfA2

COG1122

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...

433-658

1.37e-51

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

Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 178.68 E-value: 1.37e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 512
Cdd:COG1122    1 IELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 513 PQDAV--LFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAI 584
Cdd:COG1122   81 FQNPDdqLFAPTVEEDVAFGpeNLGLPREEirerVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGVL 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 585 LKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:COG1122  150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225

ABCC_cytochrome_bd

cd03247

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...

433-649

2.55e-49

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.

Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 170.57 E-value: 2.55e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIE-GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSlESLRRAVGV 511
Cdd:cd03247    1 LSINNVSFSYPEqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VPQDAVLFHNTIYYNLlygnisaspeevyavaklaglhdailrmphgydtqvgerGLKLSGGEKQRVAIARAILKDPPVI 591
Cdd:cd03247   80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 592 LYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERG 649
Cdd:cd03247  121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178

ABC_Org_Solvent_Resistant

cd03261

ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...

435-659

4.23e-48

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

Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 169.60 E-value: 4.23e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 435 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGV 511
Cdd:cd03261    3 LRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VPQDAVLF-HNTIYYNL---LYGNISASPEEVYAVA--KLA--GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARA 583
Cdd:cd03261   82 LFQSGALFdSLTVFENVafpLREHTRLSEEEIREIVleKLEavGLRGAEDLYPA-----------ELSGGMKKRVALARA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 584 ILKDPPVILYDEATSSLDSIT----EETILgAMKDVVKHrTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:cd03261  151 LALDPELLLYDEPTAGLDPIAsgviDDLIR-SLKKELGL-TSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRASD 228


                 .
gi 411147369 659 H 659
Cdd:cd03261  229 D 229

GsiA

COG1123

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...

433-662

5.22e-48

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

Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 177.40 E-value: 5.22e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEY----IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESL 505
Cdd:COG1123  261 LEVRNLSKRYpvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 506 RRAVGVVPQD--AVLF-HNTIYYNL-----LYGNISAS--PEEVYAVAKLAGLHDAIL-RMPHGydtqvgerglkLSGGE 574
Cdd:COG1123  341 RRRVQMVFQDpySSLNpRMTVGDIIaeplrLHGLLSRAerRERVAELLERVGLPPDLAdRYPHE-----------LSGGQ 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 575 KQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTH 651
Cdd:COG1123  410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELglTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489

                        250
                 ....*....|.
gi 411147369 652 HGLLANPHSIY 662
Cdd:COG1123  490 EEVFANPQHPY 500

FetA

COG4619

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

435-645

1.43e-47

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

Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 166.92 E-value: 1.43e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 435 FDNVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 514
Cdd:COG4619    3 LEGLSFR-VGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 DAVLFHNTIYYNLL----YGNISASPEEVYAVAKLAGLHDAILrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPV 590
Cdd:COG4619   82 EPALWGGTVRDNLPfpfqLRERKFDRERALELLERLGLPPDIL------DKPVER----LSGGERQRLALIRALLLQPDV 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369 591 ILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAH------RLstvvdADEIIVLDQGKV 645
Cdd:COG4619  152 LLLDEPTSALDPENTRRVEELLREYLAEegRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209

MlaF

COG1127

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...

433-659

2.53e-47

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

Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 167.46 E-value: 2.53e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAV 509
Cdd:COG1127    6 IEVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 510 GVVPQDAVLFHN-TIYYNLLYG---NISASPEEVYAVA--KLA--GLHDAILRMPhgydtqvGErglkLSGGEKQRVAIA 581
Cdd:COG1127   85 GMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVleKLElvGLPGAADKMP-------SE----LSGGMRKRVALA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 582 RAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:COG1127  154 RALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLASD 233


                 .
gi 411147369 659 H 659
Cdd:COG1127  234 D 234

FtsE

COG2884

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

433-647

1.80e-45

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

Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 161.76 E-value: 1.80e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAV 509
Cdd:COG2884    2 IRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRRRI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 510 GVVPQDA-VLFHNTIYYNLLY-----GnisASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVA 579
Cdd:COG2884   82 GVVFQDFrLLPDRTVYENVALplrvtG---KSRKEirrrVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVA 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369 580 IARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVvdaDE----IIVLDQGKVAE 647
Cdd:COG2884  148 IARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELV---DRmpkrVLELEDGRLVR 217

DppF

COG1124

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...

436-663

3.52e-45

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

Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 161.89 E-value: 3.52e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEY---IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 512
Cdd:COG1124    5 RNLSVSYgqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 513 PQDAVL-FH--NTIYYNL-----LYGnISASPEEVYAVAKLAGLHDAIL-RMPHgydtqvgerglKLSGGEKQRVAIARA 583
Cdd:COG1124   85 FQDPYAsLHprHTVDRILaeplrIHG-LPDREERIAELLEQVGLPPSFLdRYPH-----------QLSGGQRQRVAIARA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 584 ILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLStVVD--ADEIIVLDQGKVAERGTHHGLLANPH 659
Cdd:COG1124  153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLA-VVAhlCDRVAVMQNGRIVEELTVADLLAGPK 231


                 ....
gi 411147369 660 SIYS 663
Cdd:COG1124  232 HPYT 235

PLN03130

ABC transporter C family member; Provisional

376-700

6.69e-45

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 174.16 E-value: 6.69e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  376 GLLfqLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIkDKVMASPLQIT--------PQTATVAFDNVHFEY-IEGQ 446
Cdd:PLN03130 1176 GLL--LSYALNITSLLTAVLRLASLAENSLNAVERVGTYI-DLPSEAPLVIEnnrpppgwPSSGSIKFEDVVLRYrPELP 1252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYN 526
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFN 1332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  527 LLYGNiSASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEE 606
Cdd:PLN03130 1333 LDPFN-EHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDA 1411

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  607 TILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMwhTQSSRVQNHDNPKWEA--K 684
Cdd:PLN03130 1412 LIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM--VQSTGAANAQYLRSLVfgG 1489

                         330
                  ....*....|....*.
gi 411147369  685 KENISKEEERKKLQEE 700
Cdd:PLN03130 1490 DEDRLAREESKALDGQ 1505

ABC_cobalt_CbiO_domain1

cd03225

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...

435-644

2.00e-44

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

Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 158.40 E-value: 2.00e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 435 FDNVHFEYIEG-QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVP 513
Cdd:cd03225    2 LKNLSFSYPDGaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 514 QDA--VLFHNTIYYNLLYG--NISASPEEVYAVAKLA----GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAIL 585
Cdd:cd03225   82 QNPddQFFGPTVEEEVAFGleNLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVLA 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147369 586 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGK 644
Cdd:cd03225  151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211

PLN03232

ABC transporter C family member; Provisional

332-689

2.65e-44

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 172.08 E-value: 2.65e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  332 TSTLAMLNFGQSAiFSVGLTAIMVLasqgIVAGTLTVGDLVmvNGLLFQLSLPLNFLGTVYRETRqaLIDMNTLFTLLKV 411
Cdd:PLN03232 1151 TATFAVLRNGNAE-NQAGFASTMGL----LLSYTLNITTLL--SGVLRQASKAENSLNSVERVGN--YIDLPSEATAIIE 1221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  412 DTQikdkvmasPLQITPQTATVAFDNVHFEYIEG-QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI 490
Cdd:PLN03232 1222 NNR--------PVSGWPSRGSIKFEDVHLRYRPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRI 1293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  491 YLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLlygnisaSPEEVYAVAKL------AGLHDAILRMPHGYDTQVG 564
Cdd:PLN03232 1294 MIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI-------DPFSEHNDADLwealerAHIKDVIDRNPFGLDAEVS 1366

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  565 ERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGK 644
Cdd:PLN03232 1367 EGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQ 1446

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 411147369  645 VAERGTHHGLLANPHSIYSEMWH-TQSSRVQNHDNPKWEAKKENIS 689
Cdd:PLN03232 1447 VLEYDSPQELLSRDTSAFFRMVHsTGPANAQYLSNLVFERRENGMS 1492

ABC_NikE_OppD_transporters

cd03257

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...

437-649

1.21e-43

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

Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 156.90 E-value: 1.21e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 437 NVHF-EYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVV 512
Cdd:cd03257    8 SVSFpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 513 PQDAVLFHN---TIYYNL---LYGNISASPEEVYAVAKLA-----GLHDAILRM-PHgydtqvgerglKLSGGEKQRVAI 580
Cdd:cd03257   88 FQDPMSSLNprmTIGEQIaepLRIHGKLSKKEARKEAVLLllvgvGLPEEVLNRyPH-----------ELSGGQRQRVAI 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147369 581 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 649
Cdd:cd03257  157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELglTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228

ABCC_Protease_Secretion

cd03246

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...

436-645

5.02e-43

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.

Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 153.14 E-value: 5.02e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 514
Cdd:cd03246    4 ENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 DAVLFHNTIyynllYGNIsaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYD 594
Cdd:cd03246   84 DDELFSGSI-----AENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 411147369 595 EATSSLDSITEETILGAMKDV-VKHRTSIFIAHRLSTVVDADEIIVLDQGKV 645
Cdd:cd03246  122 EPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173

ABC_Carb_Solutes_like

cd03259

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...

445-649

6.06e-43

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: 154.21 E-value: 6.06e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTI 523
Cdd:cd03259   12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFpHLTV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 524 YYNLLYG-NISASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEAT 597
Cdd:cd03259   90 AENIAFGlKLRGVPKAeirarVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAREPSLLLLDEPL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 598 SSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 649
Cdd:cd03259  159 SALDAKLREELREELKELQRelGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213

ABC_OpuCA_Osmoprotection

cd03295

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...

433-660

9.78e-43

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

Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 154.77 E-value: 9.78e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVV 512
Cdd:cd03295    1 IEFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 513 PQDAVLF-HNTIYYNL-LYGNISASPEE-----VYAVAKLAGLHDAIL--RMPHgydtqvgerglKLSGGEKQRVAIARA 583
Cdd:cd03295   81 IQQIGLFpHMTVEENIaLVPKLLKWPKEkirerADELLALVGLDPAEFadRYPH-----------ELSGGQQQRVGVARA 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 584 ILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRL-STVVDADEIIVLDQGKVAERGTHHGLLANPHS 660
Cdd:cd03295  150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN 229

PTZ00243

ABC transporter; Provisional

421-665

1.02e-42

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 167.26 E-value: 1.02e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  421 ASPLQITP---QTATVAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQN 496
Cdd:PTZ00243 1294 ASPTSAAPhpvQAGSLVFEGVQMRYREGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGRE 1373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  497 IQDVSLESLRRAVGVVPQDAVLFHNTIYYNlLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQ 576
Cdd:PTZ00243 1374 IGAYGLRELRRQFSMIPQDPVLFDGTVRQN-VDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQ 1452

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  577 RVAIARAILK-DPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLL 655
Cdd:PTZ00243 1453 LMCMARALLKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELV 1532

                         250
                  ....*....|
gi 411147369  656 ANPHSIYSEM 665
Cdd:PTZ00243 1533 MNRQSIFHSM 1542

ABC_PstB_phosphate_transporter

cd03260

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...

433-649

2.18e-42

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).

Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 153.49 E-value: 2.18e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE-----PQKGSIYLAGQNI--QDVSLESL 505
Cdd:cd03260    1 IELRDLNVYYGDKH-ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 506 RRAVGVVPQDAVLFHNTIYYNLLYG-------NISASPEEVYAVAKLAGLHDAILRMPHGydtqvgergLKLSGGEKQRV 578
Cdd:cd03260   80 RRRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKDRLHA---------LGLSGGQQQRL 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 579 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAH------RLstvvdADEIIVLDQGKVAERG 649
Cdd:cd03260  151 CLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHnmqqaaRV-----ADRTAFLLNGRLVEFG 222

ABC_tran

pfam00005

ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...

449-598

2.53e-42

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 150.49 E-value: 2.53e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  449 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLF-HNTIYYNL 527
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369  528 LYGnisASPEEVYAVAKLAGLHDAI--LRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATS 598
Cdd:pfam00005  81 RLG---LLLKGLSKREKDARAEEALekLGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

CcmA

COG1131

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

433-656

1.20e-41

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

Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 151.75 E-value: 1.20e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEsLRRAVGVV 512
Cdd:COG1131    1 IEVRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 513 PQDAVLFHN-TIYYNL-----LYG-NISASPEEVYAVAKLAGLHDAIlrmphgyDTQVGerglKLSGGEKQRVAIARAIL 585
Cdd:COG1131   79 PQEPALYPDlTVRENLrffarLYGlPRKEARERIDELLELFGLTDAA-------DRKVG----TLSGGMKQRLGLALALL 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369 586 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHGLLA 656
Cdd:COG1131  148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKA 220

ECF_ATPase_1

TIGR04520

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...

433-650

1.96e-41

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]

Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 152.20 E-value: 1.96e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  433 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVG 510
Cdd:TIGR04520   1 IEVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  511 VVPQ--DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 582
Cdd:TIGR04520  81 MVFQnpDNQFVGATVEDDVAFGleNLGVPREEmrkrVDEALKLVGMEDFRDREPH-----------LLSGGQKQRVAIAG 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  583 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGT 650
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEgiTVISITHDMEEAVLADRVIVMNKGKIVAEGT 219

ABC_MetN_methionine_transporter

cd03258

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...

433-658

2.49e-41

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 150.42 E-value: 2.49e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 506
Cdd:cd03258    2 IELKNVSKVFGDTGGkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 507 RAVGVVPQdavlfhntiYYNLL-----YGNI-----------SASPEEVYAVAKLAGLHDAIlrmpHGYDTQvgerglkL 570
Cdd:cd03258   82 RRIGMIFQ---------HFNLLssrtvFENValpleiagvpkAEIEERVLELLELVGLEDKA----DAYPAQ-------L 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 571 SGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAE 647
Cdd:cd03258  142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRiCDRVAVMEKGEVVE 221

                        250
                 ....*....|.
gi 411147369 648 RGTHHGLLANP 658
Cdd:cd03258  222 EGTVEEVFANP 232

GsiA

COG1123

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...

433-658

2.88e-41

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

Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 158.14 E-value: 2.88e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLRRA 508
Cdd:COG1123    5 LEVRDLSVRYPGGDVpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 509 VGVVPQD--AVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 580
Cdd:COG1123   85 IGMVFQDpmTQLNPVTVGDQIAEAleNLGLSRAEararVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVAI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 581 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLAN 657
Cdd:COG1123  154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233


                 .
gi 411147369 658 P 658
Cdd:COG1123  234 P 234

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

379-663

6.08e-41

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

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 161.65 E-value: 6.08e-41

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   379 FQLSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMAS-PLQITPQTATVAFDNVHFEYIEGQK-VLSGISFEV 456
Cdd:TIGR00957 1230 LQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWQIQETaPPSGWPPRGRVEFRNYCLRYREDLDlVLRHINVTI 1309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   457 PAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNL-LYGniSAS 535
Cdd:TIGR00957 1310 HGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS--QYS 1387

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   536 PEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDV 615
Cdd:TIGR00957 1388 DEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQ 1467

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 411147369   616 VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYS 663
Cdd:TIGR00957 1468 FEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515

GlnQ

COG1126

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...

433-660

7.59e-41

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

Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 149.37 E-value: 7.59e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD--VSLESLRRAVG 510
Cdd:COG1126    2 IEIENLHKSF-GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskKDINKLRRKVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 511 VVPQDAVLF-HNTIYYNLLYGNISA---SPEEVYAVAK--LA--GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 582
Cdd:COG1126   81 MVFQQFNLFpHLTVLENVTLAPIKVkkmSKAEAEERAMelLErvGLADKADAYPA-----------QLSGGQQQRVAIAR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 583 AILKDPPVILYDEATSSLD--SITEetILGAMKDVVK-HRTSIFIAHRLS---TVvdADEIIVLDQGKVAERGTHHGLLA 656
Cdd:COG1126  150 ALAMEPKVMLFDEPTSALDpeLVGE--VLDVMRDLAKeGMTMVVVTHEMGfarEV--ADRVVFMDGGRIVEEGPPEEFFE 225


                 ....
gi 411147369 657 NPHS 660
Cdd:COG1126  226 NPQH 229

ABC_Class3

cd03229

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...

435-644

9.49e-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: 146.95 E-value: 9.49e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 435 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES--LRRAVGVV 512
Cdd:cd03229    3 LKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGMV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 513 PQDAVLF-HNTIYYNLLYGnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVI 591
Cdd:cd03229   82 FQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDVL 122

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 592 LYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVD-ADEIIVLDQGK 644
Cdd:cd03229  123 LLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARlADRVVVLRDGK 178

LolD

COG1136

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

433-647

4.36e-40

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

Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 146.73 E-value: 4.36e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 506
Cdd:COG1136    5 LELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSereLARLR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 507 R-AVGVVPQdavlFHN-----TIYYN----LLYGNISAS--PEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGE 574
Cdd:COG1136   85 RrHIGFVFQ----FFNllpelTALENvalpLLLAGVSRKerRERARELLERVGLGDRLDHRPS-----------QLSGGQ 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 575 KQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVVDADEIIVLDQGKVAE 647
Cdd:COG1136  150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224

PTZ00265

multidrug resistance protein (mdr1); Provisional

138-664

5.08e-40

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 159.04 E-value: 5.08e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  138 NLSDAPNTVATMATAVLIGYGVSRAGAAFFNevrNAVFGKVAQNSIRRIAKNVFLHlhnlDLGF--HLSRQTGALSKAID 215
Cdd:PTZ00265  860 NLEANSNKYSLYILVIAIAMFISETLKNYYN---NVIGEKVEKTMKRRLFENILYQ----EISFfdQDKHAPGLLSAHIN 932

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  216 RGtrgISFVLSALVFNLLPIMFEVML--VSGVL-YYKCGAQFALVTlgtlGTYTAFT-VAVTRWRTRFRIEMNKAD-NDA 290
Cdd:PTZ00265  933 RD---VHLLKTGLVNNIVIFTHFIVLflVSMVMsFYFCPIVAAVLT----GTYFIFMrVFAIRARLTANKDVEKKEiNQP 1005

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  291 GNAAI----------------DSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAML-NFGQSAIFSVGLTAI 353
Cdd:PTZ00265 1006 GTVFAynsddeifkdpsfliqEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLwGFSQSAQLFINSFAY 1085

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  354 MvLASQGIVAGTLTVGDLVMVnglLFQLSLPLNFLGTVYR---ETRQALIDMNTLFTLL--KVDTQIKDKVMASPLQITP 428
Cdd:PTZ00265 1086 W-FGSFLIRRGTILVDDFMKS---LFTFLFTGSYAGKLMSlkgDSENAKLSFEKYYPLIirKSNIDVRDNGGIRIKNKND 1161

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  429 QTATVAFDNVHFEYIEGQKV--LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE---------------------- 484
Cdd:PTZ00265 1162 IKGKIEIMDVNFRYISRPNVpiYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqd 1241

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  485 --------------------------------PQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGNI 532
Cdd:PTZ00265 1242 yqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKE 1321

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  533 SASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAM 612
Cdd:PTZ00265 1322 DATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTI 1401

                         570       580       590       600       610
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 411147369  613 KDVVKH--RTSIFIAHRLSTVVDADEIIVLDQGK-----VAERGTHHGLLANPHSIYSE 664
Cdd:PTZ00265 1402 VDIKDKadKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVYKK 1460

cbiO

PRK13632

cobalt transporter ATP-binding subunit; Provisional

430-650

9.41e-40

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 147.44 E-value: 9.41e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 430 TATVAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA 508
Cdd:PRK13632   5 SVMIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 509 VGVVPQ--DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 580
Cdd:PRK13632  85 IGIIFQnpDNQFIGATVEDDIAFGleNKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAI 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147369 581 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGT 650
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGK 225

PTZ00265

multidrug resistance protein (mdr1); Provisional

428-694

1.08e-39

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 157.88 E-value: 1.08e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  428 PQTATVAFDNVHFEYIEGQKV--LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLA-GQNIQDVSLES 504
Cdd:PTZ00265  378 KDIKKIQFKNVRFHYDTRKDVeiYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKW 457

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  505 LRRAVGVVPQDAVLFHNTIYYNLLYG----------------NISASPE------------------------------- 537
Cdd:PTZ00265  458 WRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyyneDGNDSQEnknkrnscrakcagdlndmsnttdsneliem 537

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  538 ----------EVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEET 607
Cdd:PTZ00265  538 rknyqtikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYL 617

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  608 ILGAMKDVV--KHRTSIFIAHRLSTVVDADEIIVL------------------------------DQGK----------- 644
Cdd:PTZ00265  618 VQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnKDDNnnnnnnnnnki 697

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 411147369  645 ------VAERGTHHGLLANPHSIYSEMWHTQ---SSRVQNHDNPKWEAKKENISKEEER 694
Cdd:PTZ00265  698 nnagsyIIEQGTHDALMKNKNGIYYTMINNQkvsSKKSSNNDNDKDSDMKSSAYKDSER 756

ABC_ATPase

cd00267

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...

435-644

3.79e-39

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

Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 141.61 E-value: 3.79e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 435 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 514
Cdd:cd00267    2 IENLSFRY-GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 davlfhntiyynllygnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYD 594
Cdd:cd00267   81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 411147369 595 EATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVDA-DEIIVLDQGK 644
Cdd:cd00267  106 EPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAaDRVIVLKDGK 157

ABC_MJ0796_LolCDE_FtsE

cd03255

ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...

433-645

1.28e-38

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

Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 142.63 E-value: 1.28e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEG---QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 506
Cdd:cd03255    1 IELKNLSKTYGGGgekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekeLAAFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 507 RA-VGVVPQdavlFHN-----TIYYN-----LLYGNISASPEE-VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGE 574
Cdd:cd03255   81 RRhIGFVFQ----SFNllpdlTALENvelplLLAGVPKKERRErAEELLERVGLGDRLNHYPS-----------ELSGGQ 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369 575 KQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKV 645
Cdd:cd03255  146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAEYADRIIELRDGKI 218

ABCC_MRP_domain1

cd03250

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...

433-644

2.41e-38

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

Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 141.07 E-value: 2.41e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQ----KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvsleslrra 508
Cdd:cd03250    1 ISVEDASFTWDSGEqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 509 VGVVPQDAVLFHNTIYYNLLYGnisaSP--EEVY-AVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAIL 585
Cdd:cd03250   68 IAYVSQEPWIQNGTIRENILFG----KPfdEERYeKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147369 586 KDPPVILYDEATSSLDS-----ITEETILGAMKDvvkHRTSIFIAHRLSTVVDADEIIVLDQGK 644
Cdd:cd03250  144 SDADIYLLDDPLSAVDAhvgrhIFENCILGLLLN---NKTRILVTHQLQLLPHADQIVVLDNGR 204

ABC_ModC_like

cd03299

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...

448-660

5.35e-37

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

Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 138.62 E-value: 5.35e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 448 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYN 526
Cdd:cd03299   14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 527 LLYG------NISASPEEVYAVAKLAGLHDAILRMPhgydtqvgergLKLSGGEKQRVAIARAILKDPPVILYDEATSSL 600
Cdd:cd03299   92 IAYGlkkrkvDKKEIERKVLEIAEMLGIDHLLNRKP-----------ETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369 601 DSITEETILGAMKDVVKHR--TSIFIAHRLSTV-VDADEIIVLDQGKVAERGTHHGLLANPHS 660
Cdd:cd03299  161 DVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKKPKN 223

PotA

COG3842

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...

429-664

1.33e-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: 141.00 E-value: 1.33e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 429 QTATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRA 508
Cdd:COG3842    2 AMPALELENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 509 VGVVPQDAVLF-HNTIYYNLLYG---------NISASPEEVYAVAKLAGLHDailRMPHgydtqvgerglKLSGGEKQRV 578
Cdd:COG3842   79 VGMVFQDYALFpHLTVAENVAFGlrmrgvpkaEIRARVAELLELVGLEGLAD---RYPH-----------QLSGGQQQRV 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 579 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHrlstvvD-------ADEIIVLDQGKVAERG 649
Cdd:COG3842  145 ALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELgiTFIYVTH------DqeealalADRIAVMNDGRIEQVG 218

                        250
                 ....*....|....*
gi 411147369 650 ThhgllanPHSIYSE 664
Cdd:COG3842  219 T-------PEEIYER 226

ABC_Iron-Siderophores_B12_Hemin

cd03214

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...

436-649

1.38e-36

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.

Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 135.26 E-value: 1.38e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQd 515
Cdd:cd03214    3 ENLSVGY-GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 avlfhntiyynllygnisaspeevyaVAKLAGLHDAILRmphGYDTqvgerglkLSGGEKQRVAIARAILKDPPVILYDE 595
Cdd:cd03214   81 --------------------------ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPILLLDE 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 596 ATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 649
Cdd:cd03214  124 PTSHLDIAHQIELLELLRRLARERgkTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180

ABC_NrtD_SsuB_transporters

cd03293

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...

433-648

1.48e-36

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

Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 136.83 E-value: 1.48e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrRAV 509
Cdd:cd03293    1 LEVRNVSKTYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 510 GVVPQDAVLF-HNTIYYNLLYG----NISASP--EEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 582
Cdd:cd03293   76 GYVFQQDALLpWLTVLDNVALGlelqGVPKAEarERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147369 583 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQ--GKVAER 648
Cdd:cd03293  145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETgkTVLLVTHDIDEAVFlADRVVVLSArpGRIVAE 215

ABC_HisP_GlnQ

cd03262

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...

433-645

1.96e-36

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.

Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 136.12 E-value: 1.96e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI--QDVSLESLRRAVG 510
Cdd:cd03262    1 IEIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 511 VVPQDAVLF-HNTIYYNLLYGNISA---SPEEVYAVA----KLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIAR 582
Cdd:cd03262   80 MVFQQFNLFpHLTVLENITLAPIKVkgmSKAEAEERAlellEKVGLADKADAYPA-----------QLSGGQQQRVAIAR 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 583 AILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTSIFIAHRLSTVVD-ADEIIVLDQGKV 645
Cdd:cd03262  149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREvADRVIFMDDGRI 213

DppD

COG0444

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...

437-658

2.05e-36

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

Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 139.42 E-value: 2.05e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 437 NVHFEYIEGQ-KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLR----RA 508
Cdd:COG0444    8 KVYFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRkirgRE 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 509 VGVVPQD-----------------AVLFHNtiyynllygniSASPEEVYAVA----KLAGLHDAILRM---PHgydtQvg 564
Cdd:COG0444   88 IQMIFQDpmtslnpvmtvgdqiaePLRIHG-----------GLSKAEARERAiellERVGLPDPERRLdryPH----E-- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 565 erglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTS-IFIAHRLSTVVD-ADEIIVLD 641
Cdd:COG0444  151 -----LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAiLFITHDLGVVAEiADRVAVMY 225

                        250
                 ....*....|....*..
gi 411147369 642 QGKVAERGTHHGLLANP 658
Cdd:COG0444  226 AGRIVEEGPVEELFENP 242

FepC

COG1120

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...

436-650

3.33e-36

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

Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 136.71 E-value: 3.33e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ- 514
Cdd:COG1120    5 ENLSVGY-GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQe 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 ----------DAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDaiLRmphgyDTQVGErglkLSGGEKQRVAIARAI 584
Cdd:COG1120   84 ppapfgltvrELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEH--LA-----DRPVDE----LSGGERQRVLIARAL 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147369 585 LKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 650
Cdd:COG1120  153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGP 221

ABC_FtsE

cd03292

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...

433-645

1.29e-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: 134.07 E-value: 1.29e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDV---SLESLRRAV 509
Cdd:cd03292    1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLrgrAIPYLRRKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 510 GVVPQDA-VLFHNTIYYNLLYGN--ISASPEE----VYAVAKLAGLHDAILRMPHGydtqvgerglkLSGGEKQRVAIAR 582
Cdd:cd03292   81 GVVFQDFrLLPDRNVYENVAFALevTGVPPREirkrVPAALELVGLSHKHRALPAE-----------LSGGEQQRVAIAR 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 583 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDA--DEIIVLDQGKV 645
Cdd:cd03292  150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTtrHRVIALERGKL 214

ZnuC

COG1121

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

428-647

1.46e-35

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

Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 134.83 E-value: 1.46e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 428 PQTATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVsleslRR 507
Cdd:COG1121    2 MMMPAIELENLTVSY-GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 508 AVGVVPQdavlfHNTIYYNL-----------LYGNISASP-------EEVYAVAKLAGLHDaiLRmphgyDTQVGErglk 569
Cdd:COG1121   76 RIGYVPQ-----RAEVDWDFpitvrdvvlmgRYGRRGLFRrpsradrEAVDEALERVGLED--LA-----DRPIGE---- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 570 LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAE 647
Cdd:COG1121  140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREyFDRVLLLNRGLVAH 219

ABC_DR_subfamily_A

cd03230

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...

445-645

1.84e-35

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

Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 132.14 E-value: 1.84e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvSLESLRRAVGVVPQDAVLfhntiY 524
Cdd:cd03230   12 KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPEEPSL-----Y 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 525 YNLlygnisaSPEEVyavaklaglhdailrmphgydtqvgergLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 604
Cdd:cd03230   86 ENL-------TVREN----------------------------LKLSGGMKQRLALAQALLHDPELLILDEPTSGLDPES 130

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 411147369 605 EETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKV 645
Cdd:cd03230  131 RREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173

PhnC

COG3638

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...

433-645

1.87e-35

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

Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 134.41 E-value: 1.87e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAV 509
Cdd:COG3638    3 LELRNLSKRYPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRRRI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 510 GVVPQDavlfHN-----TIYYNLLYGNISA-----------SPEEV-YAVAKLA--GLHDAILRmphgydtqvgeRGLKL 570
Cdd:COG3638   83 GMIFQQ----FNlvprlSVLTNVLAGRLGRtstwrsllglfPPEDReRALEALErvGLADKAYQ-----------RADQL 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 571 SGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKV 645
Cdd:COG3638  148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDgiTVVVNLHQVDLARRyADRIIGLRDGRV 225

ABC_membrane

pfam00664

ABC transporter transmembrane region; This family represents a unit of six transmembrane ...

112-385

2.99e-35

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

Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 134.69 E-value: 2.99e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  112 GAMNIVVPFMFKYAVDSLNQmsgnmlNLSDAPNTVATMATAVLIGYgvsrAGAAFFNEVRNAVFGKVAQNSIRRIAKNVF 191
Cdd:pfam00664  12 GAISPAFPLVLGRILDVLLP------DGDPETQALNVYSLALLLLG----LAQFILSFLQSYLLNHTGERLSRRLRRKLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  192 LHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKcGAQFALVTLGTLGTYTAFTVA 271
Cdd:pfam00664  82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYY-GWKLTLVLLAVLPLYILVSAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  272 VTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLT 351
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 411147369  352 AIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPL 385
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274

AbcC

COG1135

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

433-660

8.53e-35

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

Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 135.21 E-value: 8.53e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLR 506
Cdd:COG1135    2 IELENLSKTFPTKGGpvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSereLRAAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 507 RAVGVVPQdavlfHntiyYNLL-----YGNIsASPEEVYAVAK---------------LAGLHDAilrmphgYDTQvger 566
Cdd:COG1135   82 RKIGMIFQ-----H----FNLLssrtvAENV-ALPLEIAGVPKaeirkrvaellelvgLSDKADA-------YPSQ---- 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 567 glkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQG 643
Cdd:COG1135  141 ---LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELglTIVLITHEMDVVRRiCDRVAVLENG 217

                        250
                 ....*....|....*..
gi 411147369 644 KVAERGTHHGLLANPHS 660
Cdd:COG1135  218 RIVEQGPVLDVFANPQS 234

modC_ABC

TIGR02142

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...

452-658

2.79e-34

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

Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 134.47 E-value: 2.79e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  452 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD----VSLESLRRAVGVVPQDAVLF-HNTIYYN 526
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFpHLSVRGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  527 LLYGNISASPEEVYAVaklaglHDAILRMpHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEE 606
Cdd:TIGR02142  96 LRYGMKRARPSERRIS------FERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 411147369  607 TILGAMKDVVKHRT--SIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:TIGR02142 169 EILPYLERLHAEFGipILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223

cbiO

PRK13648

cobalt transporter ATP-binding subunit; Provisional

433-663

5.61e-34

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 131.03 E-value: 5.61e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 511
Cdd:PRK13648   8 IVFKNVSFQYQSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAKLAgLHDAILRMPHGYDTQvgerglKLSGGEKQRVAIARAILKD 587
Cdd:PRK13648  88 VFQnpDNQFVGSIVKYDVAFGleNHAVPYDEMHRRVSEA-LKQVDMLERADYEPN------ALSGGQKQRVAIAGVLALN 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 588 PPVILYDEATSSLDSITEETILGAMKDV--VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGThhgllanPHSIYS 663
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVksEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGT-------PTEIFD 231

TauB

COG1116

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...

427-647

2.49e-33

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

Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 128.67 E-value: 2.49e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 427 TPQTATVAFDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdvslE 503
Cdd:COG1116    2 SAAAPALELRGVSKRFPTGGGgvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----T 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 504 SLRRAVGVVPQDAVLF-HNTIYYNLLYG--NISASPEEVYAVA----KLAGLHDAILRMPHgydtQvgerglkLSGGEKQ 576
Cdd:COG1116   77 GPGPDRGVVFQEPALLpWLTVLDNVALGleLRGVPKAERRERArellELVGLAGFEDAYPH----Q-------LSGGMRQ 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 577 RVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAH------RLstvvdADEIIVLDQ--GKVA 646
Cdd:COG1116  146 RVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIV 220


                 .
gi 411147369 647 E 647
Cdd:COG1116  221 E 221

ABC_PhnC_transporter

cd03256

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...

435-650

2.75e-33

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

Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 128.07 E-value: 2.75e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 435 FDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI---QDVSLESLRRAVGV 511
Cdd:cd03256    3 VENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQIGM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VPQDavlfHN-----TIYYNLLYGNISASPeevyavaklagLHDAILRMPHGYDTQ--------VG------ERGLKLSG 572
Cdd:cd03256   83 IFQQ----FNlierlSVLENVLSGRLGRRS-----------TWRSLFGLFPKEEKQralaalerVGlldkayQRADQLSG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 573 GEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 649
Cdd:cd03256  148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREyADRIVGLKDGRIVFDG 227


                 .
gi 411147369 650 T 650
Cdd:cd03256  228 P 228

ABC_cobalt_CbiO_domain2

cd03226

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...

436-645

3.27e-33

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

Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 126.60 E-value: 3.27e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdvSLESLRRAVGVVPQD 515
Cdd:cd03226    3 ENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 A--VLFHNTIYYNLLYGN--ISASPEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVI 591
Cdd:cd03226   80 VdyQLFTDSVREELLLGLkeLDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLL 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 592 LYDEATSSLDSITEETILGAMKDVVKHRTSIF-IAHR---LSTVvdADEIIVLDQGKV 645
Cdd:cd03226  149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIvITHDyefLAKV--CDRVLLLANGAI 204

cbiO

PRK13635

energy-coupling factor ABC transporter ATP-binding protein;

436-650

4.56e-33

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 128.59 E-value: 4.56e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 514
Cdd:PRK13635   9 EHISFRYPDAATyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMVFQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 --DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 586
Cdd:PRK13635  89 npDNQFVGATVQDDVAFGleNIGVPREEmverVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAGVLAL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 587 DPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGT 650
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGT 223

ABC_6TM_exporters

cd07346

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...

113-402

5.74e-33

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: 128.82 E-value: 5.74e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIGYGVSRAGAAFFnevRNAVFGKVAQNSIRRIAKNVFL 192
Cdd:cd07346   13 ALGLALPLLTKLLIDDV---------IPAGDLSLLLWIALLLLLLALLRALLSYL---RRYLAARLGQRVVFDLRRDLFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 193 HLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKcGAQFALVTLGTLgtytAFTVAV 272
Cdd:cd07346   81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYL-NWKLTLVALLLL----PLYVLI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 273 TRW-----RTRFRIEMNKADNDAGNAAiDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFS 347
Cdd:cd07346  156 LRYfrrriRKASREVRESLAELSAFLQ-ESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTA 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 348 VGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDM 402
Cdd:cd07346  235 LGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289

PRK11264

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

445-658

6.71e-33

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

Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 127.17 E-value: 6.71e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI--------QDVSLESLRRAVGVVPQDA 516
Cdd:PRK11264  15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqQKGLIRQLRQHVGFVFQNF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 517 VLF-HNTIYYNLLYGNISASPE----------EVYAVAKLAGLHDAILRmphgydtqvgerglKLSGGEKQRVAIARAIL 585
Cdd:PRK11264  95 NLFpHRTVLENIIEGPVIVKGEpkeeatararELLAKVGLAGKETSYPR--------------RLSGGQQQRVAIARALA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 586 KDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235

ABC_Metallic_Cations

cd03235

ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...

435-646

1.10e-32

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.

Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 125.34 E-value: 1.10e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 435 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVsleslRRAVGVVPQ 514
Cdd:cd03235    2 VEDLTVSY-GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 -------------DAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRmphgydtQVGErglkLSGGEKQRVAIA 581
Cdd:cd03235   76 rrsidrdfpisvrDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADR-------QIGE----LSGGQQQRVLLA 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 582 RAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVA 646
Cdd:cd03235  145 RALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211

ABC_PotA_N

cd03300

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...

433-664

1.47e-32

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

Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 125.81 E-value: 1.47e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsLESLRRAVGVV 512
Cdd:cd03300    1 IELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN--LPPHKRPVNTV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 513 PQDAVLF-HNTIYYNLLYG------NISASPEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAIL 585
Cdd:cd03300   78 FQNYALFpHLTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARALV 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 586 KDPPVILYDEATSSLDSITEETILGAMKDVvkHR----TSIFIAHRLS-TVVDADEIIVLDQGKVAERGThhgllanPHS 660
Cdd:cd03300  147 NEPKVLLLDEPLGALDLKLRKDMQLELKRL--QKelgiTFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT-------PEE 217


                 ....
gi 411147369 661 IYSE 664
Cdd:cd03300  218 IYEE 221

ABC_Pro_Gly_Betaine

cd03294

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...

452-662

1.57e-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: 126.99 E-value: 1.57e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 452 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL----RRAVGVVPQDAVLF-HNTIYYN 526
Cdd:cd03294   43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLEN 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 527 LLYG-NISASPEEV-YAVA----KLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSL 600
Cdd:cd03294  123 VAFGlEVQGVPRAErEERAaealELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147369 601 DSiteeTILGAMKDVV------KHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIY 662
Cdd:cd03294  192 DP----LIRREMQDELlrlqaeLQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEILTNPANDY 256

cbiO

PRK13637

energy-coupling factor transporter ATPase;

436-650

5.59e-32

energy-coupling factor transporter ATPase;

Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.93 E-value: 5.59e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYIEG----QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD--VSLESLRRAV 509
Cdd:PRK13637   6 ENLTHIYMEGtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 510 GVVPQ--DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHdailrmphgYDTQVGERGLKLSGGEKQRVAIA 581
Cdd:PRK13637  86 GLVFQypEYQLFEETIEKDIAFGpiNLGLSEEEienrVKRAMNIVGLD---------YEDYKDKSPFELSGGQKRRVAIA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147369 582 RAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 650
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYnmTIILVSHSMEDVAKlADRIIVMNKGKCELQGT 228

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

447-662

1.09e-31

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

Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 130.19 E-value: 1.09e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 447 KVLSGISFEVPAGKKVAIVGGSGSGKST----IVRLLfrfyePQKGSIYLAGQNIQDVS---LESLRRAVGVVPQD---- 515
Cdd:COG4172  300 KAVDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDpfgs 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 ---------------AVLFhntiyynllygnISASPEEVYA-VAKL---AGLH-DAILRMPHgydtqvgerglKLSGGEK 575
Cdd:COG4172  375 lsprmtvgqiiaeglRVHG------------PGLSAAERRArVAEAleeVGLDpAARHRYPH-----------EFSGGQR 431

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 576 QRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLStVVDA--DEIIVLDQGKVAERGTH 651
Cdd:COG4172  432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHglAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGPT 510

                        250
                 ....*....|.
gi 411147369 652 HGLLANPHSIY 662
Cdd:COG4172  511 EQVFDAPQHPY 521

ABC_ModC_molybdenum_transporter

cd03297

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...

452-649

1.61e-31

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

Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 122.40 E-value: 1.61e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 452 ISFEVPAGKkVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD----VSLESLRRAVGVVPQDAVLF-HNTIYYN 526
Cdd:cd03297   17 IDFDLNEEV-TGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFpHLNVREN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 527 LLYGNISASPEE----VYAVAKLAGLhdailrmphgydTQVGERG-LKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 601
Cdd:cd03297   96 LAFGLKRKRNREdrisVDELLDLLGL------------DHLLNRYpAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 411147369 602 SITEETILGAMKDVVK--HRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 649
Cdd:cd03297  164 RALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214

AppF

COG4608

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

447-664

1.97e-31

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

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 125.23 E-value: 1.97e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVVPQD--AVLfhN 521
Cdd:COG4608   32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDpyASL--N 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 522 ---TIyynllyGNISASPEEVYAVAKLAGLHDAILRM--------------PHgydtqvgerglKLSGGEKQRVAIARAI 584
Cdd:COG4608  110 prmTV------GDIIAEPLRIHGLASKAERRERVAELlelvglrpehadryPH-----------EFSGGQRQRIGIARAL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 585 LKDPPVILYDEATSSLD-SItEETILGAMKDVVKHR--TSIFIAHRLStVVD--ADEIIVLDQGKVAERGTHHGLLANPH 659
Cdd:COG4608  173 ALNPKLIVCDEPVSALDvSI-QAQVLNLLEDLQDELglTYLFISHDLS-VVRhiSDRVAVMYLGKIVEIAPRDELYARPL 250


                 ....*
gi 411147369 660 SIYSE 664
Cdd:COG4608  251 HPYTQ 255

CysA

COG1118

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...

447-662

2.13e-31

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

Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 125.64 E-value: 2.13e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqDVSLESLRRAVGVVPQDAVLF-HNTIYY 525
Cdd:COG1118   16 TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVGFVFQHYALFpHMTVAE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 526 NLLYG--NISASPEEVYAVA-------KLAGLHDailRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEA 596
Cdd:COG1118   95 NIAFGlrVRPPSKAEIRARVeellelvQLEGLAD---RYPS-----------QLSGGQRQRVALARALAVEPEVLLLDEP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147369 597 TSSLDSITEETILGAMKDVVK--HRTSIFIAH------RLstvvdADEIIVLDQGKVAERGTHHGLLANPHSIY 662
Cdd:COG1118  161 FGALDAKVRKELRRWLRRLHDelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDRPATPF 229

PstB

COG1117

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

420-609

3.85e-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: 3.85e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 420 MASPLQITPQTATVafDNVHFEYieGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQ---KGSIYLA 493
Cdd:COG1117    1 MTAPASTLEPKIEV--RNLNVYY--GDKqALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 494 GQNI--QDVSLESLRRAVGVVPQDAVLFHNTIYYNLLYGnisaspeevyavAKLAGLH-----DAI----LRmphgydtQ 562
Cdd:COG1117   77 GEDIydPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYG------------LRLHGIKskselDEIveesLR-------K 137

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147369 563 VG----------ERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT----EETIL 609
Cdd:COG1117  138 AAlwdevkdrlkKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPIStakiEELIL 198

metN

PRK11153

DL-methionine transporter ATP-binding subunit; Provisional

435-660

6.37e-31

DL-methionine transporter ATP-binding subunit; Provisional

Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 124.14 E-value: 6.37e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 435 FDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRA 508
Cdd:PRK11153   4 LKNISKVFPQGGRtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKARRQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 509 VGVVPQdavlfHntiyYNLL-----YGNIsASPEEVYAVAK------------LAGL---HDAilrmphgYDTQvgergl 568
Cdd:PRK11153  84 IGMIFQ-----H----FNLLssrtvFDNV-ALPLELAGTPKaeikarvtelleLVGLsdkADR-------YPAQ------ 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 569 kLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLStVVD--ADEIIVLDQGK 644
Cdd:PRK11153 141 -LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMD-VVKriCDRVAVIDAGR 218

                        250
                 ....*....|....*.
gi 411147369 645 VAERGTHHGLLANPHS 660
Cdd:PRK11153 219 LVEQGTVSEVFSHPKH 234

ABCC_SUR2

cd03288

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...

448-663

1.31e-30

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

Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 121.17 E-value: 1.31e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 448 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNL 527
Cdd:cd03288   36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 528 lYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEET 607
Cdd:cd03288  116 -DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 608 ILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYS 663
Cdd:cd03288  195 LQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFA 250

ABCG_EPDR

cd03213

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...

431-649

1.69e-30

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.

Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 118.81 E-value: 1.69e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 431 ATVAFDNV-----HFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL--FRFYEPQKGSIYLAGQNIqdvSLE 503
Cdd:cd03213    2 VTLSFRNLtvtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 504 SLRRAVGVVPQDAVLF-HNTIYYNLLYgnisaspeevyaVAKLAGLhdailrmphgydtqvgerglklSGGEKQRVAIAR 582
Cdd:cd03213   79 SFRKIIGYVPQDDILHpTLTVRETLMF------------AAKLRGL----------------------SGGERKRVSIAL 124

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 583 AILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTSIFIAHRLSTVV--DADEIIVLDQGKVAERG 649
Cdd:cd03213  125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194

ABC_TM1139_LivF_branched

cd03224

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...

436-657

3.90e-30

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

Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 118.31 E-value: 3.90e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYIEGQkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES-LRRAVGVVPQ 514
Cdd:cd03224    4 ENLNAGYGKSQ-ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 DAVLFHN-TIYYNLLYG-------NISASPEEVYAV--------AKLAGLhdailrmphgydtqvgerglkLSGGEKQRV 578
Cdd:cd03224   83 GRRIFPElTVEENLLLGayarrraKRKARLERVYELfprlkerrKQLAGT---------------------LSGGEQQML 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 579 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFI----AHRLSTVvdADEIIVLDQGKVAERGTHHGL 654
Cdd:cd03224  142 AIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARFALEI--ADRAYVLERGRVVLEGTAAEL 219


                 ...
gi 411147369 655 LAN 657
Cdd:cd03224  220 LAD 222

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

381-691

8.77e-30

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 126.98 E-value: 8.77e-30

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   381 LSLPLNFLGTVYRETRQALIDMNTLFTLLKVDTQIKDKVMASPLQITPQTAtVAFDNVHFEYIEGQK-VLSGISFEVPAG 459
Cdd:TIGR00957  586 LRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKPGEGNS-ITVHNATFTWARDLPpTLNGITFSIPEG 664

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   460 KKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvsleslrrAVGVVPQDAVLFHNTIYYNLLYGNiSASPEEV 539
Cdd:TIGR00957  665 ALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGK-ALNEKYY 730

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   540 YAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITE----ETILGAMkDV 615
Cdd:TIGR00957  731 QQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGkhifEHVIGPE-GV 809

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369   616 VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMWHTQSSRVQNHDNPKWEAKKENISKE 691
Cdd:TIGR00957  810 LKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYAPDEQQGHLEDSWTALVSGEGKE 885

MalK

COG3839

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

431-650

1.16e-29

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

Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 120.56 E-value: 1.16e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 431 ATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVG 510
Cdd:COG3839    2 ASLELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 511 VVPQDAVLF-HNTIYYNLLYG--NISASPEE----VYAVAKLAGLhDAIL-RMPhgydtqvgergLKLSGGEKQRVAIAR 582
Cdd:COG3839   79 MVFQSYALYpHMTVYENIAFPlkLRKVPKAEidrrVREAAELLGL-EDLLdRKP-----------KQLSGGQRQRVALGR 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147369 583 AILKDPPVILYDEATSSLDSITEETILGAMKDVvkHR----TSIFIAHrlstvvD-------ADEIIVLDQGKVAERGT 650
Cdd:COG3839  147 ALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRL--HRrlgtTTIYVTH------DqveamtlADRIAVMNDGRIQQVGT 217

ABCC_CFTR2

cd03289

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...

437-699

1.36e-29

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

Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 118.42 E-value: 1.36e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 437 NVHFEYIE-GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQkGSIYLAGQNIQDVSLESLRRAVGVVPQD 515
Cdd:cd03289    7 DLTAKYTEgGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 AVLFHNTIYYNL-LYGniSASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYD 594
Cdd:cd03289   86 VFIFSGTFRKNLdPYG--KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 595 EATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANPHSIYSEMWHTQSSRV- 673
Cdd:cd03289  164 EPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPSDRLKLf 243

                        250       260
                 ....*....|....*....|....*....
gi 411147369 674 -QNHDNPKWEAKKENIS--KEEERKKLQE 699
Cdd:cd03289  244 pRRNSSKSKRKPRPQIQalQEETEEEVQD 272

ModC

COG4148

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...

452-658

2.29e-29

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

Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 120.21 E-value: 2.29e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 452 ISFEVPAGKKVAIVGGSGSGKSTIVRL---LFRfyePQKGSIYLAGQNIQD----VSLESLRRAVGVVPQDAVLF-HNTI 523
Cdd:COG4148   18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLQDsargIFLPPHRRRIGYVFQEARLFpHLSV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 524 YYNLLYG----NISASPEEVYAVAKLAGLhDAIL-RMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATS 598
Cdd:COG4148   95 RGNLLYGrkraPRAERRISFDEVVELLGI-GHLLdRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLA 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147369 599 SLDSITEETILGAMKDvVKHRTSI---FIAH------RLstvvdADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:COG4148  163 ALDLARKAEILPYLER-LRDELDIpilYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSRP 225

glnQ

PRK09493

glutamine ABC transporter ATP-binding protein GlnQ;

433-660

2.51e-29

glutamine ABC transporter ATP-binding protein GlnQ;

Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 116.73 E-value: 2.51e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNV--HFeyieGQ-KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD--VSLESLRR 507
Cdd:PRK09493   2 IEFKNVskHF----GPtQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 508 AVGVVPQDAVLF-HNTIYYNLLYGNI---SASPEEVYAVAK--LA--GLHDailRMPHgYDTQvgerglkLSGGEKQRVA 579
Cdd:PRK09493  78 EAGMVFQQFYLFpHLTALENVMFGPLrvrGASKEEAEKQARelLAkvGLAE---RAHH-YPSE-------LSGGQQQRVA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 580 IARAILKDPPVILYDEATSSLDSITEETILGAMKD---------VVKHRtsIFIAHRLSTvvdadEIIVLDQGKVAERGT 650
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDlaeegmtmvIVTHE--IGFAEKVAS-----RLIFIDKGRIAEDGD 219

                        250
                 ....*....|
gi 411147369 651 HHGLLANPHS 660
Cdd:PRK09493 220 PQVLIKNPPS 229

cbiO

PRK13647

cobalt transporter ATP-binding subunit; Provisional

436-658

5.53e-29

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 116.76 E-value: 5.53e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQD 515
Cdd:PRK13647   8 EDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 A--VLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKD 587
Cdd:PRK13647  88 PddQVFSSTVWDDVAFGpvNMGLDKDEverrVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGVLAMD 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369 588 PPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHgLLANP 658
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLAEGDKS-LLTDE 228

ABC_CysA_sulfate_importer

cd03296

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...

449-660

6.68e-29

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

Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 115.51 E-value: 6.68e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 449 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYNL 527
Cdd:cd03296   18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVFQHYALFrHMTVFDNV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 528 LYG-------------NISASPEEVYAVAKLAGLHDailRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYD 594
Cdd:cd03296   96 AFGlrvkprserppeaEIRAKVHELLKLVQLDWLAD---RYPA-----------QLSGGQRQRVALARALAVEPKVLLLD 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 595 EATSSLDS-ITEE--TILGAMKDVVkHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHS 660
Cdd:cd03296  162 EPFGALDAkVRKElrRWLRRLHDEL-HVTTVFVTHDQEEALEvADRVVVMNKGRIEQVGTPDEVYDHPAS 230

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

447-658

7.66e-29

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 117.76 E-value: 7.66e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE---SLRRAVGVVpqdavlFHNTi 523
Cdd:PRK11308  29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEaqkLLRQKIQIV------FQNP- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 524 yYNLL-----YGNISASP-------------EEVYAVAKLAGL---HDAilRMPHGYdtqvgerglklSGGEKQRVAIAR 582
Cdd:PRK11308 102 -YGSLnprkkVGQILEEPllintslsaaerrEKALAMMAKVGLrpeHYD--RYPHMF-----------SGGQRQRIAIAR 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 583 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTS-IFIAHRLStVVD--ADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSyVFISHDLS-VVEhiADEVMVMYLGRCVEKGTKEQIFNNP 246

ABC_Carb_Monos_I

cd03216

First domain of the ATP-binding cassette component of monosaccharide transport system; This ...

445-646

7.92e-29

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

Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 112.91 E-value: 7.92e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQdavlfhnti 523
Cdd:cd03216   12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ--------- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 524 yynllygnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSI 603
Cdd:cd03216   83 ----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPA 116

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 411147369 604 TEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVA 646
Cdd:cd03216  117 EVERLFKVIRRLRAQgVAVIFISHRLDEVFEiADRVTVLRDGRVV 161

ABC_ThiQ_thiamine_transporter

cd03298

ATP-binding cassette domain of the thiamine transport system; Part of the ...

456-649

9.59e-29

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

Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 114.13 E-value: 9.59e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 456 VPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdVSLESLRRAVGVVPQDAVLF-HNTIYYNLLYG---N 531
Cdd:cd03298   21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV--TAAPPADRPVSMLFQENNLFaHLTVEQNVGLGlspG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 532 ISASPEEVYAVAKLA---GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETI 608
Cdd:cd03298   99 LKLTAEDRQAIEVALarvGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 411147369 609 LGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 649
Cdd:cd03298  168 LDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211

ThiQ

COG3840

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

435-658

2.16e-28

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

Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 113.70 E-value: 2.16e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 435 FDNVHFEYieGQKVLSgISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqdVSLESLRRAVGVVPQ 514
Cdd:COG3840    4 LDDLTYRY--GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL--TALPPAERPVSMLFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 DAVLF-HNTIYYNLLYG---NISASPEEVYAVAKLA---GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKD 587
Cdd:COG3840   79 ENNLFpHLTVAQNIGLGlrpGLKLTAEQRAQVEQALervGLAGLLDRLPG-----------QLSGGQRQRVALARCLVRK 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147369 588 PPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:COG3840  148 RPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221

ABC_MalK_N

cd03301

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...

433-649

2.34e-28

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

Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 113.12 E-value: 2.34e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVslESLRRAVGVV 512
Cdd:cd03301    1 VELENVTKRF-GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL--PPKDRDIAMV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 513 PQDAVLF-HNTIYYNLLYG-NISASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAIL 585
Cdd:cd03301   78 FQNYALYpHMTVYDNIAFGlKLRKVPKDeiderVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIV 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 586 KDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAH-RLSTVVDADEIIVLDQGKVAERG 649
Cdd:cd03301  147 REPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213

PLN03130

ABC transporter C family member; Provisional

343-657

4.80e-28

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 121.38 E-value: 4.80e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  343 SAIFSVGLTAIMVLA---SQGIVagTLTVGDLVMVNGL----LFQ-LSLPLNFLGTVYRETRQALIDMNTLFTLLKVDtq 414
Cdd:PLN03130  523 SAFNSFILNSIPVLVtvvSFGVF--TLLGGDLTPARAFtslsLFAvLRFPLFMLPNLITQAVNANVSLKRLEELLLAE-- 598

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  415 ikDKVMASPLQITPQTATVAFDNVHFEY-IEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYL 492
Cdd:PLN03130  599 --ERVLLPNPPLEPGLPAISIKNGYFSWdSKAERpTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV 676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  493 agqniqdvslesLRRAVGVVPQDAVLFHNTIYYNLLYGNiSASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSG 572
Cdd:PLN03130  677 ------------IRGTVAYVPQVSWIFNATVRDNILFGS-PFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISG 743

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  573 GEKQRVAIARAILKDPPVILYDEATSSLDS-ITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTH 651
Cdd:PLN03130  744 GQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTY 823


                  ....*.
gi 411147369  652 HGLLAN 657
Cdd:PLN03130  824 EELSNN 829

PLN03232

ABC transporter C family member; Provisional

293-657

4.92e-28

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 121.24 E-value: 4.92e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  293 AAIDSLLNYETVKYFNNeRYEAQRYDGfLKTYETASLKSTSTLAMLNfgqsaifsvGLTAIMVLASQGIVagTLTVGDLV 372
Cdd:PLN03232  487 ASMDTVKCYAWEKSFES-RIQGIRNEE-LSWFRKAQLLSAFNSFILN---------SIPVVVTLVSFGVF--VLLGGDLT 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  373 MVNGL----LFQ-LSLPLNFLGTVYRETRQALIDMNTLFTLLKVDtqikDKVMASPLQITPQTATVAFDNVHFEYIE--G 445
Cdd:PLN03232  554 PARAFtslsLFAvLRSPLNMLPNLLSQVVNANVSLQRIEELLLSE----ERILAQNPPLQPGAPAISIKNGYFSWDSktS 629

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  446 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPqkgsiylagqnIQDVSLEsLRRAVGVVPQDAVLFHNTIYY 525
Cdd:PLN03232  630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-----------AETSSVV-IRGSVAYVPQVSWIFNATVRE 697

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  526 NLLYGNISASPEEVYAVAKLAGLHDaiLRMPHGYD-TQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDS-I 603
Cdd:PLN03232  698 NILFGSDFESERYWRAIDVTALQHD--LDLLPGRDlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhV 775

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 411147369  604 TEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLAN 657
Cdd:PLN03232  776 AHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

295-699

5.97e-27

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 117.70 E-value: 5.97e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   295 IDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLA------SQGIVAGTLTV 368
Cdd:TIGR01271 1068 ITSLKGLWTIRAFGRQSYFETLFHKALNLHTANWFLYLSTLRWFQMRIDIIFVFFFIAVTFIAigtnqdGEGEVGIILTL 1147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   369 GDLVM------------VNGLLFQLSLPLNFLGTVYRETR-QALIDMNTLFTLLKVDTQIKDKVMASPLQITPQTATVAF 435
Cdd:TIGR01271 1148 AMNILstlqwavnssidVDGLMRSVSRVFKFIDLPQEEPRpSGGGGKYQLSTVLVIENPHAQKCWPSGGQMDVQGLTAKY 1227

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   436 DNvhfeyiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQkGSIYLAGQNIQDVSLESLRRAVGVVPQD 515
Cdd:TIGR01271 1228 TE------AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQK 1300

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   516 AVLFHNTIYYNLlYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDE 595
Cdd:TIGR01271 1301 VFIFSGTFRKNL-DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDE 1379

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   596 ATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLaNPHSIYSEMWhTQSSRVQ- 674
Cdd:TIGR01271 1380 PSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLL-NETSLFKQAM-SAADRLKl 1457

                          410       420       430
                   ....*....|....*....|....*....|
gi 411147369   675 ---NHDNPKWEAKKENIS--KEEERKKLQE 699
Cdd:TIGR01271 1458 fplHRRNSSKRKPQPKITalREEAEEEVQN 1487

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

416-664

9.22e-27

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 112.73 E-value: 9.22e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 416 KDKVMASPLQITPqtaTVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQ 495
Cdd:PRK09452   1 SKKLNKQPSSLSP---LVELRGISKSF-DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 496 NIQDVSLEslRRAVGVVPQDAVLF-HNTIYYNLLYG---------NISASPEEVYAVAKLAGLHDailRMPHgydtqvge 565
Cdd:PRK09452  77 DITHVPAE--NRHVNTVFQSYALFpHMTVFENVAFGlrmqktpaaEITPRVMEALRMVQLEEFAQ---RKPH-------- 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 566 rglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSiteeTILGAMKDVVKH--R----TSIFIAH----RLSTvvdAD 635
Cdd:PRK09452 144 ---QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDY----KLRKQMQNELKAlqRklgiTFVFVTHdqeeALTM---SD 213

                        250       260
                 ....*....|....*....|....*....
gi 411147369 636 EIIVLDQGKVAERGThhgllanPHSIYSE 664
Cdd:PRK09452 214 RIVVMRDGRIEQDGT-------PREIYEE 235

cbiO

PRK13644

energy-coupling factor transporter ATPase;

433-658

1.21e-26

energy-coupling factor transporter ATPase;

Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.08 E-value: 1.21e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGV 511
Cdd:PRK13644   2 IRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAKLA----GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARA 583
Cdd:PRK13644  82 VFQnpETQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRAlaeiGLEKYRHRSPK-----------TLSGGQGQCVALAGI 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 584 ILKDPPVILYDEATSSLDSITEETILGAMKDV-VKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDV 226

LivF

COG0410

ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...

448-659

1.43e-26

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

Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 108.53 E-value: 1.43e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 448 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL-RRAVGVVPQDAVLFHN-TIYY 525
Cdd:COG0410   18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlTVEE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 526 NLLYG--------NISASPEEVYAV--------AKLAGLhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPP 589
Cdd:COG0410   98 NLLLGayarrdraEVRADLERVYELfprlkerrRQRAGT---------------------LSGGEQQMLAIGRALMSRPK 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 590 VILYDEATSSLD-SITEEtILGAMKDVVKHRTSIFI----AHRLSTVvdADEIIVLDQGKVAERGTHHGLLANPH 659
Cdd:COG0410  157 LLLLDEPSLGLApLIVEE-IFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELLADPE 228

PRK13633

energy-coupling factor transporter ATPase;

436-664

2.20e-26

energy-coupling factor transporter ATPase;

Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 109.41 E-value: 2.20e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYIEGQK-----VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAV 509
Cdd:PRK13633   8 KNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDIRNKA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 510 GVVPQ--DAVLFHNTIYYNLLYG--NISASPEEV-----YAVAKLaGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 580
Cdd:PRK13633  88 GMVFQnpDNQIVATIVEEDVAFGpeNLGIPPEEIrervdESLKKV-GMYEYRRHAPH-----------LLSGGQKQRVAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 581 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVVDADEIIVLDQGKVAERGThhgllanP 658
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGT-------P 228


                 ....*.
gi 411147369 659 HSIYSE 664
Cdd:PRK13633 229 KEIFKE 234

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

432-665

2.92e-26

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

Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 113.63 E-value: 2.92e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 432 TVAFDNVHFEyiegQKVLSGISFEVPAGKKVAIVGGSGSGKS----TIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRR 507
Cdd:COG4172   13 SVAFGQGGGT----VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 508 ----AVGVVPQDA----------------VLfhntiyynLLYGNISASPEEVYAVAKLA--GLHDAILRM---PHgydtq 562
Cdd:COG4172   89 irgnRIAMIFQEPmtslnplhtigkqiaeVL--------RLHRGLSGAAARARALELLErvGIPDPERRLdayPH----- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 563 vgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTSI-FIAHRLSTVVD-ADEIIV 639
Cdd:COG4172  156 ------QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQReLGMALlLITHDLGVVRRfADRVAV 229

                        250       260
                 ....*....|....*....|....*.
gi 411147369 640 LDQGKVAERGTHHGLLANPHSIYSEM 665
Cdd:COG4172  230 MRQGEIVEQGPTAELFAAPQHPYTRK 255

PRK10619

histidine ABC transporter ATP-binding protein HisP;

437-660

3.29e-26

histidine ABC transporter ATP-binding protein HisP;

Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 108.13 E-value: 3.29e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 437 NVHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDV-------------SLE 503
Cdd:PRK10619  10 DLHKRYGE-HEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 504 SLRRAVGVVPQDAVLF-HNTIYYNLLygnisASPEEVYAVAKLAGLHDAILRMPH-GYDTQV-GERGLKLSGGEKQRVAI 580
Cdd:PRK10619  89 LLRTRLTMVFQHFNLWsHMTVLENVM-----EAPIQVLGLSKQEARERAVKYLAKvGIDERAqGKYPVHLSGGQQQRVSI 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 581 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNP 243


                 ..
gi 411147369 659 HS 660
Cdd:PRK10619 244 QS 245

YbbA

COG4181

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...

428-612

3.30e-26

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

Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 107.52 E-value: 3.30e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 428 PQTATVAFDNVHFEYIEGQK---VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES 504
Cdd:COG4181    4 SSAPIIELRGLTKTVGTGAGeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 505 L----RRAVGVVPQDavlFHntiyynlLYGNISASpEEVYAVAKLAGLHDA------IL-------RMPHgYDTQvgerg 567
Cdd:COG4181   84 RarlrARHVGFVFQS---FQ-------LLPTLTAL-ENVMLPLELAGRRDArararaLLervglghRLDH-YPAQ----- 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 411147369 568 lkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAM 612
Cdd:COG4181  147 --LSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLL 189

ABC_drug_resistance_like

cd03264

ABC-type multidrug transport system, ATPase component; The biological function of this family ...

436-649

3.31e-26

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

Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 106.89 E-value: 3.31e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYiEGQKVLSGISFEVPAGKkVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvSLESLRRAVGVVPQD 515
Cdd:cd03264    4 ENLTKRY-GKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 AVLFHN-TIYYNLLY----GNISAS--PEEVYAVAKLAGLHDAilrmphgYDTQVGerglKLSGGEKQRVAIARAILKDP 588
Cdd:cd03264   81 FGVYPNfTVREFLDYiawlKGIPSKevKARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVGDP 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147369 589 PVILYDEATSSLDSitEETI--LGAMKDVVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 649
Cdd:cd03264  150 SILIVDEPTAGLDP--EERIrfRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211

CcmA

COG4133

ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...

445-644

4.09e-26

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

Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 106.41 E-value: 4.09e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIY 524
Cdd:COG4133   14 ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGHADGLKPELTVR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 525 YNL-----LYGnISASPEEVYAVAKLAGLHDAIlrmphgyDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEATSS 599
Cdd:COG4133   94 ENLrfwaaLYG-LRADREAIDEALEAVGLAGLA-------DLPVR----QLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 411147369 600 LDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGK 644
Cdd:COG4133  162 LDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGDFK 206

ABC_Mj1267_LivG_branched

cd03219

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...

445-659

7.12e-26

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).

Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 106.75 E-value: 7.12e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFHN-T 522
Cdd:cd03219   12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPhEIARLGIGRTFQIPRLFPElT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 523 IYYNLLYGNISASPEEVYAVAKLAGLHDA---------ILRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILY 593
Cdd:cd03219   92 VLENVMVAAQARTGSGLLLARARREEREAreraeelleRVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLL 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147369 594 DEATSSLdSITE-ETILGAMKDVVKHRTSI-FIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPH 659
Cdd:cd03219  168 DEPAAGL-NPEEtEELAELIRELRERGITVlLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235

ABC_subfamily_A

cd03263

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...

446-645

8.71e-26

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: 106.05 E-value: 8.71e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 446 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvSLESLRRAVGVVPQDAVLFHN-TI- 523
Cdd:cd03263   15 KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDElTVr 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 524 ----YYNLLYG-NISASPEEVYAVAKLAGLHDAIlrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATS 598
Cdd:cd03263   94 ehlrFYARLKGlPKSEIKEEVELLLRVLGLTDKA-------NKRART----LSGGMKRKLSLAIALIGGPSVLLLDEPTS 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 411147369 599 SLDSITEETILGAMKDVVKHRTSIFIAHRLSTV-VDADEIIVLDQGKV 645
Cdd:cd03263  163 GLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKL 210

ABC_NatA_sodium_exporter

cd03266

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...

426-649

8.96e-26

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

Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 105.91 E-value: 8.96e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 426 ITPQTATVAFDNVHFEYiegqKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL 505
Cdd:cd03266    2 ITADALTKRFRDVKKTV----QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 506 RRaVGVVPQDAVLF------HNTIYYNLLYGnisASPEEVYA-VAKLAGLhdaiLRMPHGYDTQVGErglkLSGGEKQRV 578
Cdd:cd03266   78 RR-LGFVSDSTGLYdrltarENLEYFAGLYG---LKGDELTArLEELADR----LGMEELLDRRVGG----FSTGMRQKV 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 579 AIARAILKDPPVILYDEATSSLDSITEETILgamkDVVKH-----RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 649
Cdd:cd03266  146 AIARALVHDPPVLLLDEPTTGLDVMATRALR----EFIRQlralgKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218

cbiO

PRK13641

energy-coupling factor transporter ATPase;

432-658

1.71e-25

energy-coupling factor transporter ATPase;

Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.84 E-value: 1.71e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 432 TVAFDNVHFEYIEG----QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ----DVSLE 503
Cdd:PRK13641   2 SIKFENVDYIYSPGtpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 504 SLRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEvyavAKLAGLhDAILRMphGYDTQVGERG-LKLSGGEKQRV 578
Cdd:PRK13641  82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDE----AKEKAL-KWLKKV--GLSEDLISKSpFELSGGQMRRV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 579 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLA 656
Cdd:PRK13641 155 AIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAgHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFS 234


                 ..
gi 411147369 657 NP 658
Cdd:PRK13641 235 DK 236

cbiO

PRK13652

cobalt transporter ATP-binding subunit; Provisional

437-650

2.02e-25

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.43 E-value: 2.02e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 437 NVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ-- 514
Cdd:PRK13652   8 DLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnp 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 DAVLFHNTIYYNLLYGNISASPEE------VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDP 588
Cdd:PRK13652  88 DDQIFSPTVEQDIAFGPINLGLDEetvahrVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEP 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 589 PVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 650
Cdd:PRK13652 157 QVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGT 221

artP

PRK11124

arginine transporter ATP-binding subunit; Provisional

432-660

2.57e-25

arginine transporter ATP-binding subunit; Provisional

Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 105.10 E-value: 2.57e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 432 TVAFDNVHFEYIEGQkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAG------QNIQDVSLESL 505
Cdd:PRK11124   2 SIQLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 506 RRAVGVVPQDAVLF-HNTIYYNLlygnISAsPEEVYAVAKLAGLHDAI-----LRMphgydTQVGER-GLKLSGGEKQRV 578
Cdd:PRK11124  81 RRNVGMVFQQYNLWpHLTVQQNL----IEA-PCRVLGLSKDQALARAEkllerLRL-----KPYADRfPLHLSGGQQQRV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 579 AIARAILKDPPVILYDEATSSLD--------SITEE-TILGAMKDVVKHRTSifIAHRLSTVVdadeiIVLDQGKVAERG 649
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDpeitaqivSIIRElAETGITQVIVTHEVE--VARKTASRV-----VYMENGHIVEQG 223

                        250
                 ....*....|.
gi 411147369 650 THHGlLANPHS 660
Cdd:PRK11124 224 DASC-FTQPQT 233

YddA

COG4178

ABC-type uncharacterized transport system, permease and ATPase components [General function ...

338-648

4.42e-25

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

Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 110.28 E-value: 4.42e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 338 LNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRE--TRQALIDmnTLFTLLKVDTQI 415
Cdd:COG4178  268 LTFFTTGYGQLAVIFPILVAAPRYFAGEITLGGLMQAASAFGQVQGALSWFVDNYQSlaEWRATVD--RLAGFEEALEAA 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 416 KDKVMASPLQITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVR------------------ 477
Cdd:COG4178  346 DALPEAASRIETSEDGALALEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRaiaglwpygsgriarpag 425

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 478 --LLFRfyePQKgsIYLAgqniqdvsLESLRRAvgvvpqdavlfhntiyynLLYGNI--SASPEEVYAVAKLAGLHDAIL 553
Cdd:COG4178  426 arVLFL---PQR--PYLP--------LGTLREA------------------LLYPATaeAFSDAELREALEAVGLGHLAE 474

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 554 RMphgydTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD 633
Cdd:COG4178  475 RL-----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAF 549

                        330
                 ....*....|....*
gi 411147369 634 ADEIIVLDQGKVAER 648
Cdd:COG4178  550 HDRVLELTGDGSWQL 564

PRK10247

putative ABC transporter ATP-binding protein YbbL; Provisional

429-640

6.78e-25

putative ABC transporter ATP-binding protein YbbL; Provisional

Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 103.64 E-value: 6.78e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 429 QTATVAFDNVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA 508
Cdd:PRK10247   4 NSPLLQLQNVGYL-AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 509 VGVVPQDAVLFHNTIYYNLL--YGNISASPEEVYAVAKLA--GLHDAILRMPhgydtqVGErglkLSGGEKQRVAIARAI 584
Cdd:PRK10247  83 VSYCAQTPTLFGDTVYDNLIfpWQIRNQQPDPAIFLDDLErfALPDTILTKN------IAE----LSGGEKQRISLIRNL 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 585 LKDPPVILYDEATSSLDS----ITEETILGAMKDvvKHRTSIFIAHRLSTVVDADEIIVL 640
Cdd:PRK10247 153 QFMPKVLLLDEITSALDEsnkhNVNEIIHRYVRE--QNIAVLWVTHDKDEINHADKVITL 210

cbiO

PRK13634

cobalt transporter ATP-binding subunit; Provisional

435-658

7.01e-25

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 105.10 E-value: 7.01e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 435 FDNVHFEYIEG----QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ----DVSLESLR 506
Cdd:PRK13634   5 FQKVEHRYQYKtpfeRRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKPLR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 507 RAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAK----LAGLHDAIL-RMPhgydtqvgergLKLSGGEKQR 577
Cdd:PRK13634  85 KKVGIVFQfpEHQLFEETVEKDICFGpmNFGVSEEDAKQKARemieLVGLPEELLaRSP-----------FELSGGQMRR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 578 VAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGL 654
Cdd:PRK13634 154 VAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREI 233


                 ....
gi 411147369 655 LANP 658
Cdd:PRK13634 234 FADP 237

cbiO

PRK13650

energy-coupling factor transporter ATPase;

437-656

7.68e-25

energy-coupling factor transporter ATPase;

Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.81 E-value: 7.68e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 437 NVHFEYIEGQK--VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ 514
Cdd:PRK13650   9 NLTFKYKEDQEkyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 --DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 586
Cdd:PRK13650  89 npDNQFVGATVEDDVAFGleNKGIPHEEmkerVNEALELVGMQDFKEREPA-----------RLSGGQKQRVAIAGAVAM 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147369 587 DPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLA 656
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGIRDDYqmTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229

cbiO

PRK13639

cobalt transporter ATP-binding subunit; Provisional

437-661

8.30e-25

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.77 E-value: 8.30e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 437 NVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ--DVSLESLRRAVGVVPQ 514
Cdd:PRK13639   6 DLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRKTVGIVFQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 --DAVLFHNTIYYNLLYG--NISASPEEVYAVAKLA----GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 586
Cdd:PRK13639  86 npDDQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEAlkavGMEGFENKPPH-----------HLSGGQKKRVAIAGILAM 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 587 DPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTV-VDADEIIVLDQGKVAERGTHHGLLANPHSI 661
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231

ModF

COG1119

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...

433-649

8.97e-25

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: 104.01 E-value: 8.97e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKG-SIYLAGQNIQDVSLESLRRAVGV 511
Cdd:COG1119    4 LELRNVTVRR-GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VPQDavlFHNTIYYNL---------LYGNI----SASPEEVYAVAKLAglhdAILRMPHGYDTQVGErglkLSGGEKQRV 578
Cdd:COG1119   83 VSPA---LQLRFPRDEtvldvvlsgFFDSIglyrEPTDEQRERARELL----ELLGLAHLADRPFGT----LSQGEQRRV 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147369 579 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVDA-DEIIVLDQGKVAERG 649
Cdd:COG1119  152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAG 225

ABCC_SUR1_N

cd03290

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...

433-643

9.50e-25

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

Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 102.79 E-value: 9.50e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL----RRA 508
Cdd:cd03290    1 VQVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 509 VGVVPQDAVLFHNTIYYNLLYGnisaSP---EEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAIL 585
Cdd:cd03290   81 VAYAAQKPWLLNATVEENITFG----SPfnkQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALY 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369 586 KDPPVILYDEATSSL-----DSITEETILGAMKDvvKHRTSIFIAHRLSTVVDADEIIVLDQG 643
Cdd:cd03290  157 QNTNIVFLDDPFSALdihlsDHLMQEGILKFLQD--DKRTLVLVTHKLQYLPHADWIIAMKDG 217

COG4559

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

436-650

1.82e-24

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

Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 103.27 E-value: 1.82e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYieGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL--RRAVgvV 512
Cdd:COG4559    5 ENLSVRL--GGRtLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELarRRAV--L 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 513 PQDAVLfhntiyynllygnisASPEEVYAVAKLAglhdailRMPHGYDT------------QVGERGLK------LSGGE 574
Cdd:COG4559   81 PQHSSL---------------AFPFTVEEVVALG-------RAPHGSSAaqdrqivrealaLVGLAHLAgrsyqtLSGGE 138

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 575 KQRVAIARAIL-------KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIF-IAHRLS-TVVDADEIIVLDQGKV 645
Cdd:COG4559  139 QQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVaVLHDLNlAAQYADRILLLHQGRL 218


                 ....*
gi 411147369 646 AERGT 650
Cdd:COG4559  219 VAQGT 223

PTZ00243

ABC transporter; Provisional

427-702

2.34e-24

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 109.48 E-value: 2.34e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  427 TPQTATVAFdnvhFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAgqniqdvsleslr 506
Cdd:PTZ00243  659 TPKMKTDDF----FE-LEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------- 720

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  507 RAVGVVPQDAVLFHNTIYYNLLYGNisaspEEvyavaKLAGLHDAI---------LRMPHGYDTQVGERGLKLSGGEKQR 577
Cdd:PTZ00243  721 RSIAYVPQQAWIMNATVRGNILFFD-----EE-----DAARLADAVrvsqleadlAQLGGGLETEIGEKGVNLSGGQKAR 790

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  578 VAIARAILKDPPVILYDEATSSLDS-----ITEETILGAMKDvvkhRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHH 652
Cdd:PTZ00243  791 VSLARAVYANRDVYLLDDPLSALDAhvgerVVEECFLGALAG----KTRVLATHQVHVVPRADYVVALGDGRVEFSGSSA 866

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 411147369  653 GLLANPhsIYSEMwhtqssRVQNHDNPkwEAKKENISKEEERKKLQEEIV 702
Cdd:PTZ00243  867 DFMRTS--LYATL------AAELKENK--DSKEGDADAEVAEVDAAPGGA 906

hmuV

PRK13548

hemin importer ATP-binding subunit; Provisional

443-650

2.47e-24

hemin importer ATP-binding subunit; Provisional

Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.93 E-value: 2.47e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 443 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLfhnt 522
Cdd:PRK13548  12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSL---- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 523 iyynllygNISASPEEVYAVAklaglhdailRMPHGYD------------TQVGERGLK------LSGGEKQRVAIARAI 584
Cdd:PRK13548  88 --------SFPFTVEEVVAMG----------RAPHGLSraeddalvaaalAQVDLAHLAgrdypqLSGGEQQRVQLARVL 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 585 L------KDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLS-TVVDADEIIVLDQGKVAERGT 650
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERglAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224

thiQ

PRK10771

thiamine ABC transporter ATP-binding protein ThiQ;

453-656

2.54e-24

thiamine ABC transporter ATP-binding protein ThiQ;

Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 101.97 E-value: 2.54e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 453 SFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYNLLYG- 530
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFsHLTVAQNIGLGl 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 531 ------NiSASPEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 604
Cdd:PRK10771  97 npglklN-AAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 605 EETILGAMKDVVKHR--TSIFIAHRLStvvDADEI----IVLDQGKVAERGTHHGLLA 656
Cdd:PRK10771 165 RQEMLTLVSQVCQERqlTLLMVSHSLE---DAARIaprsLVVADGRIAWDGPTDELLS 219

cbiO

PRK13640

energy-coupling factor transporter ATPase;

433-650

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 411147369 433 VAFDNVHFEYIEGQK-VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLRRA 508
Cdd:PRK13640   6 VEFKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDIREK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 509 VGVVPQ--DAVLFHNTIYYNLLYG--NISASPEE----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAI 580
Cdd:PRK13640  86 VGIVFQnpDNQFVGATVGDDVAFGleNRAVPRPEmikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVAI 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147369 581 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVDADEIIVLDQGKVAERGT 650
Cdd:PRK13640 155 AGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGS 226

ArtP

COG4161

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

432-660

3.06e-24

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

Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.01 E-value: 3.06e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 432 TVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAG------QNIQDVSLESL 505
Cdd:COG4161    2 SIQLKNINCFY-GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 506 RRAVGVVPQDAVLF-HNTIYYNLLygnisASPEEVYAVAKLAGLHDAI-----LRMphgydTQVGER-GLKLSGGEKQRV 578
Cdd:COG4161   81 RQKVGMVFQQYNLWpHLTVMENLI-----EAPCKVLGLSKEQAREKAMkllarLRL-----TDKADRfPLHLSGGQQQRV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 579 AIARAILKDPPVILYDEATSSLDS---------ITEETILGAMKDVVKHRTSifIAHRLSTVVdadeiIVLDQGKVAERG 649
Cdd:COG4161  151 AIARALMMEPQVLLFDEPTAALDPeitaqvveiIRELSQTGITQVIVTHEVE--FARKVASQV-----VYMEKGRIIEQG 223

                        250
                 ....*....|.
gi 411147369 650 THHgLLANPHS 660
Cdd:COG4161  224 DAS-HFTQPQT 233

MglA

COG1129

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

445-645

3.87e-24

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.64 E-value: 3.87e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQDAVLFHN-T 522
Cdd:COG1129   16 GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVPNlS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 523 IYYNLLYGNISASP-----EEVYAVAK--LAGLH---DAilrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPVIL 592
Cdd:COG1129   96 VAENIFLGREPRRGglidwRAMRRRARelLARLGldiDP--------DTPVGD----LSVAQQQLVEIARALSRDARVLI 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 593 YDEATSSLDSiTE-ETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKV 645
Cdd:COG1129  164 LDEPTASLTE-REvERLFRIIRRLKAQgVAIIYISHRLDEVFEiADRVTVLRDGRL 218

modC

PRK11144

molybdenum ABC transporter ATP-binding protein ModC;

455-645

1.04e-23

molybdenum ABC transporter ATP-binding protein ModC;

Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 103.03 E-value: 1.04e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 455 EVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI----QDVSLESLRRAVGVVPQDAVLF-HNTIYYNLLY 529
Cdd:PRK11144  20 TLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFpHYKVRGNLRY 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 530 GNISASPEEVYAVAKLAGLHDAILRMPHGydtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETIL 609
Cdd:PRK11144 100 GMAKSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 411147369 610 GAMKDVVKH-RTSI-FIAHRLSTVVD-ADEIIVLDQGKV 645
Cdd:PRK11144 169 PYLERLAREiNIPIlYVSHSLDEILRlADRVVVLEQGKV 207

cbiO

PRK13631

cobalt transporter ATP-binding subunit; Provisional

447-659

1.33e-23

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 102.24 E-value: 1.33e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYL----AGQNIQDVS------------LESLRRAVG 510
Cdd:PRK13631  40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHElitnpyskkiknFKELRRRVS 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 511 VVPQ--DAVLFHNTIYYNLLYGNISASPEEVYAvAKLAGLHdaILRMphGYDTQVGERG-LKLSGGEKQRVAIARAILKD 587
Cdd:PRK13631 120 MVFQfpEYQLFKDTIEKDIMFGPVALGVKKSEA-KKLAKFY--LNKM--GLDDSYLERSpFGLSGGQKRRVAIAGILAIQ 194

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147369 588 PPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPH 659
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEIFTDQH 268

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

448-663

1.39e-23

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 105.17 E-value: 1.39e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 448 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQkGSIYLAGQNIQDVS---LESLRRAVGVVPQDAVLFHN--- 521
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNrrqLLPVRHRIQVVFQDPNSSLNprl 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 522 ----------TIYYNLLygNISASPEEVYAVAKLAGLhDAILRmpHGYDTQvgerglkLSGGEKQRVAIARAILKDPPVI 591
Cdd:PRK15134 380 nvlqiieeglRVHQPTL--SAAQREQQVIAVMEEVGL-DPETR--HRYPAE-------FSGGQRQRIAIARALILKPSLI 447

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 592 LYDEATSSLDSITEETILGAMKDV-VKHRTS-IFIAHRLStVVDA--DEIIVLDQGKVAERGTHHGLLANPHSIYS 663
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLqQKHQLAyLFISHDLH-VVRAlcHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522

SapF

COG4167

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

452-658

1.72e-23

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

Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 100.68 E-value: 1.72e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 452 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAG------------QNI----QDVSlESL--RRAVGvvp 513
Cdd:COG4167   32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGhkleygdykyrcKHIrmifQDPN-TSLnpRLNIG--- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 514 Q--DAVLFHNTiyyNLlygNISASPEEVYAVAKLAGLH-DAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPV 590
Cdd:COG4167  108 QilEEPLRLNT---DL---TAEEREERIFATLRLVGLLpEHANFYPH-----------MLSSGQKQRVALARALILQPKI 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147369 591 ILYDEATSSLDSITEETILGAMKDV-VKHRTS-IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:COG4167  171 IIADEALAALDMSVRSQIINLMLELqEKLGISyIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFANP 241

nikE

PRK10419

nickel ABC transporter ATP-binding protein NikE;

446-647

2.99e-23

nickel ABC transporter ATP-binding protein NikE;

Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 100.15 E-value: 2.99e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 446 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE---SLRRAVGVVPQD---AVLF 519
Cdd:PRK10419  25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDsisAVNP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 520 HNTIyynllyGNISASP-------------EEVYAVAKLAGLHDAIL-RMPHgydtqvgerglKLSGGEKQRVAIARAIL 585
Cdd:PRK10419 105 RKTV------REIIREPlrhllsldkaerlARASEMLRAVDLDDSVLdKRPP-----------QLSGGQLQRVCLARALA 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 586 KDPPVILYDEATSSLDSITEETILGAMKDvVKHRTSI---FIAHRLSTVVD-ADEIIVLDQGKVAE 647
Cdd:PRK10419 168 VEPKLLILDEAVSNLDLVLQAGVIRLLKK-LQQQFGTaclFITHDLRLVERfCQRVMVMDNGQIVE 232

PRK10908

cell division ATP-binding protein FtsE;

433-653

4.02e-23

cell division ATP-binding protein FtsE;

Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 98.41 E-value: 4.02e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI---QDVSLESLRRAV 509
Cdd:PRK10908   2 IRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 510 GVVPQDA-VLFHNTIYYNLLYGNI--SASPEE----VYAVAKLAGLHDAILRMPhgydtqvgergLKLSGGEKQRVAIAR 582
Cdd:PRK10908  82 GMIFQDHhLLMDRTVYDNVAIPLIiaGASGDDirrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVGIAR 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369 583 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVDAD-EIIVLDQGKVAerGTHHG 653
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMAtHDIGLISRRSyRMLTLSDGHLH--GGVGG 221

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

448-662

7.14e-23

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.56 E-value: 7.14e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 448 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF-HNTIYYN 526
Cdd:PRK11432  21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 527 LLYG---------NISASPEEVYAVAKLAGLHDAilrmphgYDTQVgerglklSGGEKQRVAIARAILKDPPVILYDEAT 597
Cdd:PRK11432  99 VGYGlkmlgvpkeERKQRVKEALELVDLAGFEDR-------YVDQI-------SGGQQQRVALARALILKPKVLLFDEPL 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147369 598 SSLDSiteeTILGAMKDVVKHR------TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIY 662
Cdd:PRK11432 165 SNLDA----NLRRSMREKIRELqqqfniTSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQPASRF 232

PRK14243

phosphate transporter ATP-binding protein; Provisional

449-655

9.12e-23

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 98.32 E-value: 9.12e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 449 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE-----PQKGSIYLAGQNI--QDVSLESLRRAVGVVPQDAVLFHN 521
Cdd:PRK14243  26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 522 TIYYNLLYG-NISASP----EEVYAVAKLAGLHDAIlrmphgyDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 596
Cdd:PRK14243 106 SIYDNIAYGaRINGYKgdmdELVERSLRQAALWDEV-------KDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 411147369 597 TSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLL 655
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYL 237

PRK14258

phosphate ABC transporter ATP-binding protein; Provisional

433-659

1.38e-22

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 97.80 E-value: 1.38e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-----KGSIYLAGQNIQD--VSLESL 505
Cdd:PRK14258   8 IKVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYErrVNLNRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 506 RRAVGVVPQDAVLFHNTIYYNLLYGN--ISASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgERGLKLSGGEKQRV 578
Cdd:PRK14258  87 RRQVSMVHPKPNLFPMSVYDNVAYGVkiVGWRPKLeiddiVESALKDADLWDEIKHKIH-------KSALDLSGGQQQRL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 579 AIARAILKDPPVILYDEATSSLDSITEETILGAMKDVV--KHRTSIFIAHRLSTVVDADEIIVLDQG------KVAERGT 650
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSRLSDFTAFFKGnenrigQLVEFGL 239


                 ....*....
gi 411147369 651 HHGLLANPH 659
Cdd:PRK14258 240 TKKIFNSPH 248

PRK10851

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

447-672

1.50e-22

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.77 E-value: 1.50e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqDVSLESLR-RAVGVVPQDAVLF-HNTIY 524
Cdd:PRK10851  16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSRLHARdRKVGFVFQHYALFrHMTVF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 525 YNLLYGnISASPE----EVYAV-AKLAGLHDaILRMPH---GYDTQvgerglkLSGGEKQRVAIARAILKDPPVILYDEA 596
Cdd:PRK10851  93 DNIAFG-LTVLPRrerpNAAAIkAKVTQLLE-MVQLAHladRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 597 TSSLDSITEETI---LGAMKDVVKHrTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGThhgllanPhsiySEMWHTQSSR 672
Cdd:PRK10851 164 FGALDAQVRKELrrwLRQLHEELKF-TSVFVTHDQEEAMEvADRVVVMSQGNIEQAGT-------P----DQVWREPATR 231

YnjD

COG4136

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...

443-601

3.61e-22

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

Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 95.24 E-value: 3.61e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 443 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLEslRRAVGVVPQDAVLF 519
Cdd:COG4136   11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQDDLLF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 520 -HNTIYYNLLYG-----NISASPEEVYAVAKLAGLHDAILRMPhgyDTqvgerglkLSGGEKQRVAIARAILKDPPVILY 593
Cdd:COG4136   89 pHLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDP---AT--------LSGGQRARVALLRALLAEPRALLL 157


                 ....*...
gi 411147369 594 DEATSSLD 601
Cdd:COG4136  158 DEPFSKLD 165

cbiO

PRK13646

energy-coupling factor transporter ATPase;

432-667

3.72e-22

energy-coupling factor transporter ATPase;

Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 97.16 E-value: 3.72e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 432 TVAFDNVHFEYIEG----QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNI----QDVSLE 503
Cdd:PRK13646   2 TIRFDNVSYTYQKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 504 SLRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAklaglHDaiLRMPHGYDTQVGERG-LKLSGGEKQRV 578
Cdd:PRK13646  82 PVRKRIGMVFQfpESQLFEDTVEREIIFGpkNFKMNLDEVKNYA-----HR--LLMDLGFSRDVMSQSpFQMSGGQMRKI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 579 AIARAILKDPPVILYDEATSSLDSITEETILGAMKD--VVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLL 655
Cdd:PRK13646 155 AIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKELF 234

                        250
                 ....*....|..
gi 411147369 656 ANPHsiYSEMWH 667
Cdd:PRK13646 235 KDKK--KLADWH 244

PhnL

COG4778

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...

448-601

4.16e-22

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

Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 95.58 E-value: 4.16e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 448 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYL--AGQNIqDVS-------LESLRRAVGVVPQdavl 518
Cdd:COG4778   26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWV-DLAqaspreiLALRRRTIGYVSQ---- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 519 FHNTIyynllyGNISAspEEVyaVAklaglhDAILRMphGYDTQVG-ERGLKL------------------SGGEKQRVA 579
Cdd:COG4778  101 FLRVI------PRVSA--LDV--VA------EPLLER--GVDREEArARARELlarlnlperlwdlppatfSGGEQQRVN 162

                        170       180
                 ....*....|....*....|..
gi 411147369 580 IARAILKDPPVILYDEATSSLD 601
Cdd:COG4778  163 IARGFIADPPLLLLDEPTASLD 184

PRK14247

phosphate ABC transporter ATP-binding protein; Provisional

425-668

4.91e-22

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 96.14 E-value: 4.91e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 425 QITPQTATVAFDNVhfeyiegqKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQ---KGSIYLAGQNIQD 499
Cdd:PRK14247   3 KIEIRDLKVSFGQV--------EVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 500 VSLESLRRAVGVVPQDAVLFHN-TIYYNLLYG----NISASPEEVYAVAKLAgLHDAIL--RMPHGYDTQVGerglKLSG 572
Cdd:PRK14247  75 MDVIELRRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWA-LEKAQLwdEVKDRLDAPAG----KLSG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 573 GEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAH------RLStvvdaDEIIVLDQGKVA 646
Cdd:PRK14247 150 GQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIV 224

                        250       260
                 ....*....|....*....|..
gi 411147369 647 ERGTHHGLLANPHSIYSEMWHT 668
Cdd:PRK14247 225 EWGPTREVFTNPRHELTEKYVT 246

ABC_BcrA_bacitracin_resist

cd03268

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...

445-649

5.77e-22

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

Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 94.59 E-value: 5.77e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsLESLRRAVGVVpqdavlfhntIY 524
Cdd:cd03268   12 KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK--NIEALRRIGAL----------IE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 525 YNLLYGNISASpEEVYAVAKLAGL----HDAILRMPhGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSL 600
Cdd:cd03268   80 APGFYPNLTAR-ENLRLLARLLGIrkkrIDEVLDVV-GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 601 D--SITE--ETILgamkDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERG 649
Cdd:cd03268  158 DpdGIKElrELIL----SLRDQGITVLISsHLLSEIQKvADRIGIINKGKLIEEG 208

PRK10070

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

453-662

9.44e-22

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

Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 98.18 E-value: 9.44e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 453 SFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESL----RRAVGVVPQD-AVLFHNTIYYNL 527
Cdd:PRK10070  48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTVLDNT 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 528 LYG-NISASPEEVYAVAKLAGLHDAILR-MPHGYDTQvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITE 605
Cdd:PRK10070 128 AFGmELAGINAEERREKALDALRQVGLEnYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 606 ETILGAM-KDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIY 662
Cdd:PRK10070 201 TEMQDELvKLQAKHqRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDY 260

cbiO

PRK13645

energy-coupling factor transporter ATPase;

430-657

1.61e-21

energy-coupling factor transporter ATPase;

Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 95.46 E-value: 1.61e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 430 TATVAFDNVHFEYIEGQ----KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI----YLAGQNIQDV- 500
Cdd:PRK13645   4 SKDIILDNVSYTYAKKTpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIk 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 501 SLESLRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAvaKLAGLHDaILRMPHGYdtqVGERGLKLSGGEKQ 576
Cdd:PRK13645  84 EVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGpvNLGENKQEAYK--KVPELLK-LVQLPEDY---VKRSPFELSGGQKR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 577 RVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHG 653
Cdd:PRK13645 158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGSPFE 237


                 ....
gi 411147369 654 LLAN 657
Cdd:PRK13645 238 IFSN 241

PRK13537

nodulation factor ABC transporter ATP-binding protein NodI;

430-656

2.35e-21

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 95.26 E-value: 2.35e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 430 TATVAFDNVHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESlRRAV 509
Cdd:PRK13537   5 VAPIDFRNVEKRYGD-KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 510 GVVPQdavlFHN-----TIYYNLL----YGNISASPeevyAVAKLAGLHDaILRMPHGYDTQVGErglkLSGGEKQRVAI 580
Cdd:PRK13537  83 GVVPQ----FDNldpdfTVRENLLvfgrYFGLSAAA----ARALVPPLLE-FAKLENKADAKVGE----LSGGMKRRLTL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 581 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFI-------AHRLstvvdADEIIVLDQG-KVAErGTHH 652
Cdd:PRK13537 150 ARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGrKIAE-GAPH 223


                 ....
gi 411147369 653 GLLA 656
Cdd:PRK13537 224 ALIE 227

PRK10535

macrolide ABC transporter ATP-binding protein/permease MacB;

430-645

2.71e-21

macrolide ABC transporter ATP-binding protein/permease MacB;

Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 98.64 E-value: 2.71e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 430 TATVAFDNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDV---SLE 503
Cdd:PRK10535   2 TALLELKDIRRSYPSGEeqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 504 SLRRA-VGVVPQDavlfhntiyYNLLYGNISASPEEVYAV-------AKLAGLHDAILRMphGYDTQVGERGLKLSGGEK 575
Cdd:PRK10535  82 QLRREhFGFIFQR---------YHLLSHLTAAQNVEVPAVyaglerkQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQ 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369 576 QRVAIARAILKDPPVILYDEATSSLDSITEE---TILGAMKDvvKHRTSIFIAHRLSTVVDADEIIVLDQGKV 645
Cdd:PRK10535 151 QRVSIARALMNGGQVILADEPTGALDSHSGEevmAILHQLRD--RGHTVIIVTHDPQVAAQAERVIEIRDGEI 221

ABCG_White

cd03234

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...

447-604

2.84e-21

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.

Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 93.10 E-value: 2.84e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQK---GSIYLAGQniqDVSLESLRRAVGVVPQ-DAVLFHNT 522
Cdd:cd03234   21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQ---PRKPDQFQKCVAYVRQdDILLPGLT 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 523 IYYNLLYGNISASPEEVYAVAKLAglHDAILRMPHGYDTQVGERGLK-LSGGEKQRVAIARAILKDPPVILYDEATSSLD 601
Cdd:cd03234   98 VRETLTYTAILRLPRKSSDAIRKK--RVEDVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175


                 ...
gi 411147369 602 SIT 604
Cdd:cd03234  176 SFT 178

cbiO

PRK13642

energy-coupling factor transporter ATPase;

436-656

4.86e-21

energy-coupling factor transporter ATPase;

Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 93.62 E-value: 4.86e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYIEGQKV--LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVP 513
Cdd:PRK13642   8 ENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 514 Q--DAVLFHNTIYYNLLYG--NISASPEEVyavakLAGLHDAILRMpHGYDTQVGERGlKLSGGEKQRVAIARAILKDPP 589
Cdd:PRK13642  88 QnpDNQFVGATVEDDVAFGmeNQGIPREEM-----IKRVDEALLAV-NMLDFKTREPA-RLSGGQKQRVAVAGIIALRPE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147369 590 VILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVVDADEIIVLDQGKVAERGTHHGLLA 656
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229

cbiO

PRK13636

cobalt transporter ATP-binding subunit; Provisional

437-650

5.33e-21

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.76 E-value: 5.33e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 437 NVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqDVS---LESLRRAVGVVP 513
Cdd:PRK13636  10 ELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSrkgLMKLRESVGMVF 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 514 Q--DAVLFHNTIYYNLLYG--NISASPEEVYAVAKLAGLHDAILRMPHgydtqvgERGLKLSGGEKQRVAIARAILKDPP 589
Cdd:PRK13636  89 QdpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLVMEPK 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147369 590 VILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTV-VDADEIIVLDQGKVAERGT 650
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVpLYCDNVFVMKEGRVILQGN 225

ABCC_CFTR1

cd03291

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...

445-650

5.88e-21

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

Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 93.77 E-value: 5.88e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvsleslrraVGVVPQDAVLFHNTIY 524
Cdd:cd03291   49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIK 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 525 YNLLYGnISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 604
Cdd:cd03291  116 ENIIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 411147369 605 EETIL-GAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQGKVAERGT 650
Cdd:cd03291  195 EKEIFeSCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGT 241

ugpC

PRK11650

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

431-650

1.72e-20

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

Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 93.75 E-value: 1.72e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 431 ATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsLESLRRAVG 510
Cdd:PRK11650   2 AGLKLQAVRKSYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE--LEPADRDIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 511 VVPQDAVLF-HNTIYYNLLYG-NISASPEE-----VYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARA 583
Cdd:PRK11650  80 MVFQNYALYpHMSVRENMAYGlKIRGMPKAeieerVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAMGRA 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147369 584 ILKDPPVILYDEATSSLDSiteeTILGAMKDVVK--HR----TSIFIAH-RLSTVVDADEIIVLDQGKVAERGT 650
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDA----KLRVQMRLEIQrlHRrlktTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGT 218

lolD

PRK11629

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

436-629

1.75e-20

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.03 E-value: 1.75e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES---LR-RA 508
Cdd:PRK11629   9 DNLCKRYQEGSvqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 509 VGVVPQdavlFHN---------TIYYNLLYGNISASPEEVYAVAKLAGLhdailrmphGYDTQVGERGLKLSGGEKQRVA 579
Cdd:PRK11629  89 LGFIYQ----FHHllpdftaleNVAMPLLIGKKKPAEINSRALEMLAAV---------GLEHRANHRPSELSGGERQRVA 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 580 IARAILKDPPVILYDEATSSLDSITEETI---LGAMKD-------VVKHrtSIFIAHRLS 629
Cdd:PRK11629 156 IARALVNNPRLVLADEPTGNLDARNADSIfqlLGELNRlqgtaflVVTH--DLQLAKRMS 213

cbiO

PRK13649

energy-coupling factor transporter ATPase;

433-650

2.21e-20

energy-coupling factor transporter ATPase;

Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.73 E-value: 2.21e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQ----KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS----LES 504
Cdd:PRK13649   3 INLQNVSYTYQAGTpfegRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknkdIKQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 505 LRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVA--KLAGLhdailrmphGYDTQVGERG-LKLSGGEKQR 577
Cdd:PRK13649  83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAreKLALV---------GISESLFEKNpFELSGGQMRR 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 578 VAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVvkHR---TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 650
Cdd:PRK13649 154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKL--HQsgmTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228

potG

PRK11607

putrescine ABC transporter ATP-binding subunit PotG;

414-663

2.46e-20

putrescine ABC transporter ATP-binding subunit PotG;

Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.75 E-value: 2.46e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 414 QIKDKVMASPLqITPQTATVAFDnvhfeyieGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLA 493
Cdd:PRK11607   9 QAKTRKALTPL-LEIRNLTKSFD--------GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 494 GQNIQDVSleSLRRAVGVVPQDAVLF-HNTIYYNLLYG---------NISASPEEVYAvakLAGLHDAILRMPHgydtqv 563
Cdd:PRK11607  80 GVDLSHVP--PYQRPINMMFQSYALFpHMTVEQNIAFGlkqdklpkaEIASRVNEMLG---LVHMQEFAKRKPH------ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 564 gerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAH-RLSTVVDADEIIVL 640
Cdd:PRK11607 149 -----QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERvgVTCVMVTHdQEEAMTMAGRIAIM 223

                        250       260
                 ....*....|....*....|...
gi 411147369 641 DQGKVAERGTHHGLLANPHSIYS 663
Cdd:PRK11607 224 NRGKFVQIGEPEEIYEHPTTRYS 246

PRK15079

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

394-663

3.16e-20

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.46 E-value: 3.16e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 394 ETRQALIDMNTLftllKVDTQIKDKvMASPLQiTPQTAtvafdnvhfeyiegqKVLSGISFEVPAGKKVAIVGGSGSGKS 473
Cdd:PRK15079   3 EGKKVLLEVADL----KVHFDIKDG-KQWFWQ-PPKTL---------------KAVDGVTLRLYEGETLGVVGESGCGKS 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 474 TIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA---VGVVPQDAVLFHN---TIyynllyGNISASPEEVY------- 540
Cdd:PRK15079  62 TFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLASLNprmTI------GEIIAEPLRTYhpklsrq 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 541 --------AVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAM 612
Cdd:PRK15079 136 evkdrvkaMMLKVGLLPNLINRYPH-----------EFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLL 204

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 411147369 613 KDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYS 663
Cdd:PRK15079 205 QQLQREMglSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPLHPYT 258

PRK14246

phosphate ABC transporter ATP-binding protein; Provisional

442-666

3.91e-20

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.49 E-value: 3.91e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 442 YIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE------PQKGSIYLAGQNIQDVSLESLRRAVGVVPQD 515
Cdd:PRK14246  19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQ 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 AVLF-HNTIYYNLLYGNISASPEEVYAVAKLagLHDAILRMphGYDTQVGER----GLKLSGGEKQRVAIARAILKDPPV 590
Cdd:PRK14246  99 PNPFpHLSIYDNIAYPLKSHGIKEKREIKKI--VEECLRKV--GLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKV 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 591 ILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYSEMW 666
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTSPKNELTEKY 251

fecE

PRK11231

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

446-652

5.27e-20

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

Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 90.07 E-value: 5.27e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 446 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQ-----DAVLFH 520
Cdd:PRK11231  15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQhhltpEGITVR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 521 NTIYY-----NLLYGNISASPEEVYAVAklaglhdailrMPHGYDTQVGERGL-KLSGGEKQRVAIARAILKDPPVILYD 594
Cdd:PRK11231  95 ELVAYgrspwLSLWGRLSAEDNARVNQA-----------MEQTRINHLADRRLtDLSGGQRQRAFLAMVLAQDTPVVLLD 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 595 EATSSLDSITEETILGAMKDV-VKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHH 652
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQGTPE 223

TauB

COG4525

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

436-648

5.39e-20

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

Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 90.31 E-value: 5.39e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEY---IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslrRAVgVV 512
Cdd:COG4525    7 RHVSVRYpggGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD---RGV-VF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 513 PQDAVLFHNTIYYNLLYG----NISASPEEVYAVAKLA--GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILK 586
Cdd:COG4525   83 QKDALLPWLNVLDNVAFGlrlrGVPKAERRARAEELLAlvGLADFARRRIW-----------QLSGGMRQRVGIARALAA 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 587 DPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRL-STVVDADEIIVLD--QGKVAER 648
Cdd:COG4525  152 DPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITHSVeEALFLATRLVVMSpgPGRIVER 218

ssuB

PRK11247

aliphatic sulfonates transport ATP-binding subunit; Provisional

420-645

8.26e-20

aliphatic sulfonates transport ATP-binding subunit; Provisional

Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 89.74 E-value: 8.26e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 420 MASPLQITPQTAtVAFDNVHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIyLAGQniqd 499
Cdd:PRK11247   1 MMNTARLNQGTP-LLLNAVSKRYGE-RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT---- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 500 VSLESLRRAVGVVPQDAVLFH-NTIYYNL---LYGNISASPEEVYAVAKLAglhdailrmphgydTQVGERGLKLSGGEK 575
Cdd:PRK11247  74 APLAEAREDTRLMFQDARLLPwKKVIDNVglgLKGQWRDAALQALAAVGLA--------------DRANEWPAALSGGQK 139

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 576 QRVAIARAILKDPPVILYDEATSSLDSITE-EtilgaMKDVVK------HRTSIFIAHRLSTVVD-ADEIIVLDQGKV 645
Cdd:PRK11247 140 QRVALARALIHRPGLLLLDEPLGALDALTRiE-----MQDLIEslwqqhGFTVLLVTHDVSEAVAmADRVLLIEEGKI 212

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

435-645

9.02e-20

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.21 E-value: 9.02e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 435 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvslesLRraVGVVPQ 514
Cdd:COG0488    1 LENLSKSF-GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---------LR--IGYLPQ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 DAVLF-HNTIYYNLLYGN------------ISASPEEVYAV-AKLAGLHDAILRMpHGY--DTQVGE--RGLK------- 569
Cdd:COG0488   69 EPPLDdDLTVLDTVLDGDaelraleaeleeLEAKLAEPDEDlERLAELQEEFEAL-GGWeaEARAEEilSGLGfpeedld 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 570 -----LSGGEKQRVAIARAILKDPPVILYDEATSSLD--SIT--EETIL---GAMkdvvkhrtsIFIAH-R--LSTVVda 634
Cdd:COG0488  148 rpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDleSIEwlEEFLKnypGTV---------LVVSHdRyfLDRVA-- 216

                        250
                 ....*....|.
gi 411147369 635 DEIIVLDQGKV 645
Cdd:COG0488  217 TRILELDRGKL 227

PRK13651

cobalt transporter ATP-binding subunit; Provisional

447-657

1.19e-19

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.15 E-value: 1.19e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI------------------YLAGQNIQDV------SL 502
Cdd:PRK13651  21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekekVLEKLVIQKTrfkkikKI 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 503 ESLRRAVGVVPQDA--VLFHNTIYYNLLYGNIS--ASPEEVYAVAK----LAGLHDAIL-RMPHGydtqvgerglkLSGG 573
Cdd:PRK13651 101 KEIRRRVGVVFQFAeyQLFEQTIEKDIIFGPVSmgVSKEEAKKRAAkyieLVGLDESYLqRSPFE-----------LSGG 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 574 EKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTH 651
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVLEwTKRTIFFKDGKIIKDGDT 249


                 ....*.
gi 411147369 652 HGLLAN 657
Cdd:PRK13651 250 YDILSD 255

PRK10261

glutathione transporter ATP-binding protein; Provisional

452-663

1.23e-19

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.38 E-value: 1.23e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 452 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVVPQD--AVLF-HNTIYY 525
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDpyASLDpRQTVGD 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 526 ---------NLLYGNisASPEEVYAVAKLAGLH-DAILRMPHGYdtqvgerglklSGGEKQRVAIARAILKDPPVILYDE 595
Cdd:PRK10261 423 simeplrvhGLLPGK--AAAARVAWLLERVGLLpEHAWRYPHEF-----------SGGQRQRICIARALALNPKVIIADE 489

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147369 596 ATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYS 663
Cdd:PRK10261 490 AVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560

PvdE

COG4615

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...

146-657

1.45e-19

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

Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 92.94 E-value: 1.45e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 146 VATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKnvflhlhnldLGFHlsRQTGALSKAIDrgtrgisfVL 225
Cdd:COG4615   59 VLLLLSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLER----------IGAA--RLLAALTEDVR--------TI 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 226 SALVFNLLPIMFEVMLVSGVLYYKC--GAQFALVTLGTLGtytaFTVAVTRWRT-RFRIEMNKA--DNDAGNAAIDSL-- 298
Cdd:COG4615  119 SQAFVRLPELLQSVALVLGCLAYLAwlSPPLFLLTLVLLG----LGVAGYRLLVrRARRHLRRAreAEDRLFKHFRALle 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 299 ------LNYETVKYFNNERYEAQrydgfLKTYETASLKSTSTLAML-NFGQSAIFsvGLTAIMVLASQGIVAGTL-TVGD 370
Cdd:COG4615  195 gfkelkLNRRRRRAFFDEDLQPT-----AERYRDLRIRADTIFALAnNWGNLLFF--ALIGLILFLLPALGWADPaVLSG 267

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 371 LVMVngLLFqLSLPL-NFLGTV--YRETRQALIDMNTLFtlLKVDTQIKDKVMASPLQITPQTATVAFDNVHFEYIEGQK 447
Cdd:COG4615  268 FVLV--LLF-LRGPLsQLVGALptLSRANVALRKIEELE--LALAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDG 342

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 448 ----VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNti 523
Cdd:COG4615  343 degfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR-- 420

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 524 yynlLYG-NISASPEEVYAVAKLaglhdaiLRMphgyDTQVGERG-----LKLSGGEKQRVAIARAILKDPPVILYDEAT 597
Cdd:COG4615  421 ----LLGlDGEADPARARELLER-------LEL----DHKVSVEDgrfstTDLSQGQRKRLALLVALLEDRPILVFDEWA 485

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 598 SSLD----SITEETILGAMKDvvKHRTSIFIAHrlstvvD------ADEIIVLDQGKVAERGTHHGLLAN 657
Cdd:COG4615  486 ADQDpefrRVFYTELLPELKA--RGKTVIAISH------DdryfdlADRVLKMDYGKLVELTGPAALAAS 547

PRK11000

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

431-649

1.86e-19

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.86 E-value: 1.86e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 431 ATVAFDNVHFEYieGQKVLS-GISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVslESLRRAV 509
Cdd:PRK11000   2 ASVTLRNVTKAY--GDVVISkDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV--PPAERGV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 510 GVVPQDAVLF-HNTIYYNLLYGnisaspeevyavAKLAGLHDA-----------ILRMPHGYDTQVGErglkLSGGEKQR 577
Cdd:PRK11000  78 GMVFQSYALYpHLSVAENMSFG------------LKLAGAKKEeinqrvnqvaeVLQLAHLLDRKPKA----LSGGQRQR 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 578 VAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAH-RLSTVVDADEIIVLDQGKVAERG 649
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRlgRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216

PRK14239

phosphate transporter ATP-binding protein; Provisional

442-629

1.95e-19

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 88.29 E-value: 1.95e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 442 YIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYE--PQ---KGSIYLAGQNIQDVSLES--LRRAVGVVPQ 514
Cdd:PRK14239  14 YYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDTvdLRKEIGMVFQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 DAVLFHNTIYYNLLYGnisaspeevyavAKLAGLHD-AILrmphgyDTQVgERGLK------------------LSGGEK 575
Cdd:PRK14239  94 QPNPFPMSIYENVVYG------------LRLKGIKDkQVL------DEAV-EKSLKgasiwdevkdrlhdsalgLSGGQQ 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147369 576 QRVAIARAILKDPPVILYDEATSSLDSIT----EETILGAMKD----VVKHrtSIFIAHRLS 629
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISagkiEETLLGLKDDytmlLVTR--SMQQASRIS 214

btuD

PRK09536

corrinoid ABC transporter ATPase; Reviewed

445-649

2.43e-19

corrinoid ABC transporter ATPase; Reviewed

Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 91.06 E-value: 2.43e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAvlfhnTIY 524
Cdd:PRK09536  15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT-----SLS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 525 YNLlygnisaspeEVYAVAKLAglhdailRMPH--------GYDTQVGERGLK--------------LSGGEKQRVAIAR 582
Cdd:PRK09536  90 FEF----------DVRQVVEMG-------RTPHrsrfdtwtETDRAAVERAMErtgvaqfadrpvtsLSGGERQRVLLAR 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147369 583 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 649
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

420-664

2.58e-19

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.08 E-value: 2.58e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 420 MASPLqITPQTATVAFDNVHfeyiEGQKVLSGISFEVPAGKKVAIVGGSGSGKS----TIVRLLFR---FYePQkGSIYL 492
Cdd:PRK15134   1 MTQPL-LAIENLSVAFRQQQ----TVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppvVY-PS-GDIRF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 493 AGQNIQDVSLESLRRAVGvvPQDAVLFHNTI-----YYNL---LYGNIS--------ASPEEVYAVAKLAGLHDAILRM- 555
Cdd:PRK15134  74 HGESLLHASEQTLRGVRG--NKIAMIFQEPMvslnpLHTLekqLYEVLSlhrgmrreAARGEILNCLDRVGIRQAAKRLt 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 556 --PHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTV 631
Cdd:PRK15134 152 dyPH-----------QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIV 220

                        250       260       270
                 ....*....|....*....|....*....|....
gi 411147369 632 VD-ADEIIVLDQGKVAERGTHHGLLANPHSIYSE 664
Cdd:PRK15134 221 RKlADRVAVMQNGRCVEQNRAATLFSAPTHPYTQ 254

ntrCD

TIGR01184

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...

449-649

3.27e-19

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]

Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 87.14 E-value: 3.27e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  449 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrravgvvPQDAVLFHNtiyYNLL 528
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-----------PDRMVVFQN---YSLL 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  529 -----YGNISASPEEVYAVA------KLAGLHDAILRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEAT 597
Cdd:TIGR01184  67 pwltvRENIALAVDRVLPDLskserrAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPF 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 411147369  598 SSLDSITEETILGAMKDVVK--HRTSIFIAHRL-STVVDADEIIVLDQGKVAERG 649
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNGPAANIG 197

ABC_DrrA

cd03265

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...

451-650

3.63e-19

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 86.65 E-value: 3.63e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 451 GISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniQDVSLES--LRRAVGVVPQDAVL------FHNT 522
Cdd:cd03265   18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG---HDVVREPreVRRRIGIVFQDLSVddeltgWENL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 523 IYYNLLYGNISAS-PEEVYAVAKLAGLHDAilrmphgYDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 601
Cdd:cd03265   95 YIHARLYGVPGAErRERIDELLDFVGLLEA-------ADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 602 SITEETILGAMKDVVK-HRTSIFI-------AHRLstvvdADEIIVLDQGKVAERGT 650
Cdd:cd03265  164 PQTRAHVWEYIEKLKEeFGMTILLtthymeeAEQL-----CDRVAIIDHGRIIAEGT 215

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

449-645

5.97e-19

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.47 E-value: 5.97e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 449 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniQDVSLESLRRA----VGVVPQDAVLFHN-TI 523
Cdd:COG3845   21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIRSPRDAialgIGMVHQHFMLVPNlTV 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 524 YYNLLYG---------NISASPEEVYAVAKLAGLH---DAIlrmphgydtqVGErglkLSGGEKQRVAIARAILKDPPVI 591
Cdd:COG3845   98 AENIVLGleptkggrlDRKAARARIRELSERYGLDvdpDAK----------VED----LSVGEQQRVEILKALYRGARIL 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147369 592 LYDEATSSLdsiT-EET-----ILGAMKDvvKHRTSIFIAHRLSTVVD-ADEIIVLDQGKV 645
Cdd:COG3845  164 ILDEPTAVL---TpQEAdelfeILRRLAA--EGKSIIFITHKLREVMAiADRVTVLRRGKV 219

PRK13536

nodulation factor ABC transporter ATP-binding protein NodI;

414-651

1.08e-18

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 87.96 E-value: 1.08e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 414 QIKDKVMASPLQITPQTAtVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLA 493
Cdd:PRK13536  24 QGISEAKASIPGSMSTVA-IDLAGVSKSY-GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 494 GQNIQDVSlESLRRAVGVVPQ-DAVLFHNTIYYNLL-YGN-ISASPEEVYAVakLAGLHDaILRMPHGYDTQVGErglkL 570
Cdd:PRK13536 102 GVPVPARA-RLARARIGVVPQfDNLDLEFTVRENLLvFGRyFGMSTREIEAV--IPSLLE-FARLESKADARVSD----L 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 571 SGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFI-------AHRLstvvdADEIIVLDQG 643
Cdd:PRK13536 174 SGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVLEAG 248


                 ....*....
gi 411147369 644 -KVAERGTH 651
Cdd:PRK13536 249 rKIAEGRPH 257

ABC_putative_ATPase

cd03269

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...

447-645

1.08e-18

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

Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 85.02 E-value: 1.08e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsleSLRRAVGVVPQDAVLFHN-TIYY 525
Cdd:cd03269   14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI----AARNRIGYLPEERGLYPKmKVID 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 526 NLLYgnisaspeevyaVAKLAGL-HDAILRMPHGYDTQVGERGLK------LSGGEKQRVAIARAILKDPPVILYDEATS 598
Cdd:cd03269   90 QLVY------------LAQLKGLkKEEARRRIDEWLERLELSEYAnkrveeLSKGNQQKVQFIAAVIHDPELLILDEPFS 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 411147369 599 SLDSITEETILGAMKDVV-KHRTSIFIAHRLSTVVD-ADEIIVLDQGKV 645
Cdd:cd03269  158 GLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRA 206

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

445-643

1.23e-18

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 91.13 E-value: 1.23e-18

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvsleslrraVGVVPQDAVLFHNTIY 524
Cdd:TIGR01271  438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIK 504

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   525 YNLLYGnISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSIT 604
Cdd:TIGR01271  505 DNIIFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 411147369   605 EETIL-GAMKDVVKHRTSIFIAHRLSTVVDADEIIVLDQG 643
Cdd:TIGR01271  584 EKEIFeSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623

3a01204

TIGR00955

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

449-650

1.27e-18

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

Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.11 E-value: 1.27e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  449 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLfRFYEPQ----KGSIYLAGQNIQdvsLESLRRAVGVVPQDAVLF-HNTI 523
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKgvkgSGSVLLNGMPID---AKEMRAISAYVQQDDLFIpTLTV 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  524 YYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHG--YDTQVGERGLK--LSGGEKQRVAIARAILKDPPVILYDEATSS 599
Cdd:TIGR00955 117 REHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRkcANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 411147369  600 LDSITEETILGAMKDVV-KHRTSIFIAHRLSTVVDA--DEIIVLDQGKVAERGT 650
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAqKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGS 250

TagH

COG1134

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...

448-650

1.37e-18

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

Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.90 E-value: 1.37e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 448 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdVS--LEslrraVGVVpqdavlFH----- 520
Cdd:COG1134   41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR----VSalLE-----LGAG------FHpeltg 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 521 --NtIYYN-LLYGNISASPEEVYA-VAKLAGLHDAIlrmphgyDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEA 596
Cdd:COG1134  106 reN-IYLNgRLLGLSRKEIDEKFDeIVEFAELGDFI-------DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEV 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 597 TSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 650
Cdd:COG1134  174 LAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229

tauB

PRK11248

taurine ABC transporter ATP-binding subunit;

436-648

2.05e-18

taurine ABC transporter ATP-binding subunit;

Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.52 E-value: 2.05e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLEslrRAVgVVPQD 515
Cdd:PRK11248   5 SHLYADY-GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE---RGV-VFQNE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 AVLFHNTIYYNLLYG----NISASPEEVYAVAKLA--GLHDAILRMPhgydtqvgergLKLSGGEKQRVAIARAILKDPP 589
Cdd:PRK11248  80 GLLPWRNVQDNVAFGlqlaGVEKMQRLEIAHQMLKkvGLEGAEKRYI-----------WQLSGGQRQRVGIARALAANPQ 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 590 VILYDEATSSLDSITEETilgaMKDV---VKHRTS---IFIAHRL-STVVDADEIIVL--DQGKVAER 648
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQ----MQTLllkLWQETGkqvLLITHDIeEAVFMATELVLLspGPGRVVER 212

PRK11831

phospholipid ABC transporter ATP-binding protein MlaF;

446-658

2.25e-18

phospholipid ABC transporter ATP-binding protein MlaF;

Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 85.59 E-value: 2.25e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 446 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS---LESLRRAVGVVPQDAVLFHN- 521
Cdd:PRK11831  20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRMSMLFQSGALFTDm 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 522 TIYYNLLYG--NISASPEEVY---AVAKL--AGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYD 594
Cdd:PRK11831 100 NVFDNVAYPlrEHTQLPAPLLhstVMMKLeaVGLRGAAKLMPS-----------ELSGGMARRAALARAIALEPDLIMFD 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 411147369 595 EATSSLDSITeETILGAMKDVVKHR---TSIFIAHRLSTVVD-AD-EIIVLDQGKVAErGTHHGLLANP 658
Cdd:PRK11831 169 EPFVGQDPIT-MGVLVKLISELNSAlgvTCVVVSHDVPEVLSiADhAYIVADKKIVAH-GSAQALQANP 235

PRK14267

phosphate ABC transporter ATP-binding protein; Provisional

442-668

3.64e-18

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 84.89 E-value: 3.64e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 442 YIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-----KGSIYLAGQNI--QDVSLESLRRAVGVVPQ 514
Cdd:PRK14267  13 YYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQ 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 DAVLF-HNTIYYNLLYG----NISAS----PEEVYAVAKLAGLHDAILRMPHGYDTQvgerglkLSGGEKQRVAIARAIL 585
Cdd:PRK14267  93 YPNPFpHLTIYDNVAIGvklnGLVKSkkelDERVEWALKKAALWDEVKDRLNDYPSN-------LSGGQRQRLVIARALA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 586 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYSE 664
Cdd:PRK14267 166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVGPTRKVFENPEHELTE 245


                 ....
gi 411147369 665 MWHT 668
Cdd:PRK14267 246 KYVT 249

ABC_6TM_exporter_like

cd18564

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

111-397

4.06e-18

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: 85.64 E-value: 4.06e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 111 EGAMNIVVPFMFKYAVDS------LNQMSGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFFNEVrnaVFGKVAQNSIR 184
Cdd:cd18564   11 ETALRLLEPWPLKVVIDDvlgdkpLPGLLGLAPLLGPDPLALLLLAAAALVGIALLRGLASYAGTY---LTALVGQRVVL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 185 RIAKNVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLLPI---------MFEVMLVsgvlyykCGAQFA 255
Cdd:cd18564   88 DLRRDLFAHLQRLSLSFHDRRRTGDL---LSRLTGDVGAIQDLLVSGVLPLltnlltlvgMLGVMFW-------LDWQLA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 256 LVTLGTLgtyTAFTVAVTRWRTRFRIEMNKADNDAGN-AAI--DSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKST 332
Cdd:cd18564  158 LIALAVA---PLLLLAARRFSRRIKEASREQRRREGAlASVaqESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAA 234

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 333 STLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLvmvngLLFqlslpLNFLGTVYRETRQ 397
Cdd:cd18564  235 RLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDL-----LVF-----LAYLKNLYKPVRD 289

PRK13539

cytochrome c biogenesis protein CcmA; Provisional

448-612

5.74e-18

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 83.00 E-value: 5.74e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 448 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGvvPQDAVLFHNTIYYNL 527
Cdd:PRK13539  17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVAENL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 528 -----LYGNisaSPEEVYAVAKLAGLHDaILRMPHGYdtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDS 602
Cdd:PRK13539  95 efwaaFLGG---EELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160

                        170
                 ....*....|
gi 411147369 603 ITEETILGAM 612
Cdd:PRK13539 161 AAVALFAELI 170

cbiO

PRK13643

energy-coupling factor transporter ATPase;

433-665

9.25e-18

energy-coupling factor transporter ATPase;

Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.40 E-value: 9.25e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIE----GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS----LES 504
Cdd:PRK13643   2 IKFEKVNYTYQPnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkqkeIKP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 505 LRRAVGVVPQ--DAVLFHNTIYYNLLYG--NISASPEEVYAVAKlaglhdAILRMPhGYDTQVGERG-LKLSGGEKQRVA 579
Cdd:PRK13643  82 VRKKVGVVFQfpESQLFEETVLKDVAFGpqNFGIPKEKAEKIAA------EKLEMV-GLADEFWEKSpFELSGGQMRRVA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 580 IARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGThhgllan 657
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT------- 227


                 ....*...
gi 411147369 658 PHSIYSEM 665
Cdd:PRK13643 228 PSDVFQEV 235

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

426-650

1.90e-17

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

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 86.01 E-value: 1.90e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  426 ITPQTATVAFDnvhfeyieGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL--FRFYEPQKGSI-----------YL 492
Cdd:TIGR03269   1 IEVKNLTKKFD--------GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgYV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  493 -----AGQNI---------QDVSL----ESLRRAVgvVPQDAVLFHNTIyynLLYGN-------ISASPEEVYAVAKLAG 547
Cdd:TIGR03269  73 erpskVGEPCpvcggtlepEEVDFwnlsDKLRRRI--RKRIAIMLQRTF---ALYGDdtvldnvLEALEEIGYEGKEAVG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  548 LHDAILRMphgydTQVGER----GLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TS 621
Cdd:TIGR03269 148 RAVDLIEM-----VQLSHRithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSM 222

                         250       260       270
                  ....*....|....*....|....*....|
gi 411147369  622 IFIAHRLSTVVD-ADEIIVLDQGKVAERGT 650
Cdd:TIGR03269 223 VLTSHWPEVIEDlSDKAIWLENGEIKEEGT 252

ABC_FeS_Assembly

cd03217

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...

437-649

1.91e-17

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.

Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 81.03 E-value: 1.91e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 437 NVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRF--YEPQKGSIYLAGQNIQDVSL-ESLRRAVGVVP 513
Cdd:cd03217    5 DLHVS-VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeERARLGIFLAF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 514 QdavlfhntiyynllygnisaSPEEVYAVaKLAGLhdaiLRmphgydtQVGErglKLSGGEKQRVAIARAILKDPPVILY 593
Cdd:cd03217   84 Q--------------------YPPEIPGV-KNADF----LR-------YVNE---GFSGGEKKRNEILQLLLLEPDLAIL 128

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147369 594 DEATSSLD----SITEETIlGAMKDvvKHRTSIFIAH--RLSTVVDADEIIVLDQGKVAERG 649
Cdd:cd03217  129 DEPDSGLDidalRLVAEVI-NKLRE--EGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187

ABC_KpsT_Wzt

cd03220

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...

448-649

2.06e-17

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

Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 81.81 E-value: 2.06e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 448 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniQDVSLesLRRAVGVVPqDAVLFHNTIYYNL 527
Cdd:cd03220   37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG---RVSSL--LGLGGGFNP-ELTGRENIYLNGR 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 528 LYGnisASPEEVYA----VAKLAGLHDAIlrmphgyDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSI 603
Cdd:cd03220  111 LLG---LSRKEIDEkideIIEFSELGDFI-------DLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 411147369 604 TEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 649
Cdd:cd03220  177 FQEKCQRRLRELLKQgKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224

PRK10895

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

431-659

2.36e-17

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 2.36e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 431 ATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRRAV 509
Cdd:PRK10895   2 ATLTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 510 GVVPQDAVLFHN-TIYYNLL-----YGNISASPEEVYAVAKLAGLHDAILRmphgydtqvGERGLKLSGGEKQRVAIARA 583
Cdd:PRK10895  81 GYLPQEASIFRRlSVYDNLMavlqiRDDLSAEQREDRANELMEEFHIEHLR---------DSMGQSLSGGERRRVEIARA 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 584 ILKDPPVILYDEATSSLDSITEETIlgamKDVVKH-RTS----IFIAHRLSTVVDADE-IIVLDQGKVAERGTHHGLLAN 657
Cdd:PRK10895 152 LAANPKFILLDEPFAGVDPISVIDI----KRIIEHlRDSglgvLITDHNVRETLAVCErAYIVSQGHLIAHGTPTEILQD 227


                 ..
gi 411147369 658 PH 659
Cdd:PRK10895 228 EH 229

PRK15056

manganese/iron ABC transporter ATP-binding protein;

429-649

3.85e-17

manganese/iron ABC transporter ATP-binding protein;

Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.24 E-value: 3.85e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 429 QTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLrra 508
Cdd:PRK15056   3 QQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL--- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 509 VGVVPQD-------AVLFHNTIYYNlLYGnisaspeevyavaklaglHDAILRMPHGYDTQVGERGL------------- 568
Cdd:PRK15056  80 VAYVPQSeevdwsfPVLVEDVVMMG-RYG------------------HMGWLRRAKKRDRQIVTAALarvdmvefrhrqi 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 569 -KLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVDADEIIVLDQGKVA 646
Cdd:PRK15056 141 gELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220


                 ...
gi 411147369 647 ERG 649
Cdd:PRK15056 221 ASG 223

ABC_YhbG

cd03218

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...

447-658

4.01e-17

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.

Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 81.05 E-value: 4.01e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFHN-TIY 524
Cdd:cd03218   14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFRKlTVE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 525 YNLLygnisaspeevyAVAKLAGLHDAILRmpHGYDTQVGE---------RGLKLSGGEKQRVAIARAILKDPPVILYDE 595
Cdd:cd03218   94 ENIL------------AVLEIRGLSKKERE--EKLEELLEEfhithlrksKASSLSGGERRRVEIARALATNPKFLLLDE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 596 ATSSLDSITEETILGAMKDVVKHRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:cd03218  160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSiTDRAYIIYEGKVLAEGTPEEIAANE 224

ABCF_EF-3

cd03221

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...

435-644

4.23e-17

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

Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 78.64 E-value: 4.23e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 435 FDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIyLAGQNIQdvsleslrraVGVVPQ 514
Cdd:cd03221    3 LENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-TWGSTVK----------IGYFEQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 davlfhntiyynllygnisaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYD 594
Cdd:cd03221   71 -------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLD 95

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 411147369 595 EATSSLDSITEETILGAMKDvvKHRTSIFIAH-R--LSTVvdADEIIVLDQGK 644
Cdd:cd03221   96 EPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

433-647

5.24e-17

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.73 E-value: 5.24e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLaGQNIQdvsleslrraVGVV 512
Cdd:COG0488  316 LELEGLSKSY-GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYF 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 513 PQDAVLFH--NTIYYNLLYGNISASPEEVYAVakLAGL----HDAilrmphgyDTQVGerglKLSGGEKQRVAIARAILK 586
Cdd:COG0488  384 DQHQEELDpdKTVLDELRDGAPGGTEQEVRGY--LGRFlfsgDDA--------FKPVG----VLSGGEKARLALAKLLLS 449

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147369 587 DPPVILYDEATSSLD--SIT--EETIL---GAMkdvvkhrtsIFIAH-R--LSTVvdADEIIVLDQGKVAE 647
Cdd:COG0488  450 PPNVLLLDEPTNHLDieTLEalEEALDdfpGTV---------LLVSHdRyfLDRV--ATRILEFEDGGVRE 509

PRK15112

peptide ABC transporter ATP-binding protein SapF;

452-658

5.50e-17

peptide ABC transporter ATP-binding protein SapF;

Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 81.76 E-value: 5.50e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 452 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ--DVSLESLRraVGVVPQDAVLFHN------TI 523
Cdd:PRK15112  32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQR--IRMIFQDPSTSLNprqrisQI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 524 YYNLLYGNISASPEE----VYAVAKLAGL-HDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVILYDEATS 598
Cdd:PRK15112 110 LDFPLRLNTDLEPEQrekqIIETLRQVGLlPDHASYYPH-----------MLAPGQKQRLGLARALILRPKVIIADEALA 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369 599 SLDSITEETILGAMKDVV-KHRTS-IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:PRK15112 179 SLDMSMRSQLINLMLELQeKQGISyIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241

ABC_Carb_Monos_II

cd03215

Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...

443-645

5.88e-17

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

Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 79.40 E-value: 5.88e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 443 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQD---AVL 518
Cdd:cd03215   10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDrkrEGL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 519 FHN-TIYYNLLYGNIsaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEAT 597
Cdd:cd03215   90 VLDlSVAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPT 132

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 411147369 598 SSLDSITEETILGAMKDVVKHRTSIFIahrLSTVVD-----ADEIIVLDQGKV 645
Cdd:cd03215  133 RGVDVGAKAEIYRLIRELADAGKAVLL---ISSELDellglCDRILVMYEGRI 182

PRK14271

phosphate ABC transporter ATP-binding protein; Provisional

445-658

9.12e-17

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 81.30 E-value: 9.12e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP-----QKGSIYLAGQNI---QDVsLEsLRRAVGVVPQDA 516
Cdd:PRK14271  33 GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIfnyRDV-LE-FRRRVGMLFQRP 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 517 VLFHNTIYYNLLYGNISAS--PEEVY---AVAKLA--GLHDAIlrmphgyDTQVGERGLKLSGGEKQRVAIARAILKDPP 589
Cdd:PRK14271 111 NPFPMSIMDNVLAGVRAHKlvPRKEFrgvAQARLTevGLWDAV-------KDRLSDSPFRLSGGQQQLLCLARTLAVNPE 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 590 VILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFSSP 253

YhaQ

COG4152

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

445-650

1.00e-16

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

Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 81.31 E-value: 1.00e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDvsleSLRRAVGvvpqdavlfhntiY 524
Cdd:COG4152   13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP----EDRRRIG-------------Y 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 525 ynL-----LYGNISASpEEVYAVAKLAGL--HDAILRMPHGYDT-QVGERGLK----LSGGEKQRVAIARAILKDPPVIL 592
Cdd:COG4152   76 --LpeergLYPKMKVG-EQLVYLARLKGLskAEAKRRADEWLERlGLGDRANKkveeLSKGNQQKVQLIAALLHDPELLI 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147369 593 YDEATSSLDSITEETilgaMKDVVKH-----RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGT 650
Cdd:COG4152  153 LDEPFSGLDPVNVEL----LKDVIRElaakgTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

429-665

1.06e-16

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.42 E-value: 1.06e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 429 QTATVAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL-ESLRR 507
Cdd:PRK11288   1 SSPYLSFDGIGKTF-PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 508 AVGVVPQDAVLFHN-TIYYNLLYGNISASPEEV-------YAVAKLAGLHDAIlrMPhgyDTQVGErglkLSGGEKQRVA 579
Cdd:PRK11288  80 GVAIIYQELHLVPEmTVAENLYLGQLPHKGGIVnrrllnyEAREQLEHLGVDI--DP---DTPLKY----LSIGQRQMVE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 580 IARAILKDPPVILYDEATSSLdSITEETIL----GAMKDvvKHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAErgTHHGL 654
Cdd:PRK11288 151 IAKALARNARVIAFDEPTSSL-SAREIEQLfrviRELRA--EGRVILYVSHRMEEIFAlCDAITVFKDGRYVA--TFDDM 225

                        250
                 ....*....|..
gi 411147369 655 LANPH-SIYSEM 665
Cdd:PRK11288 226 AQVDRdQLVQAM 237

BtuD

COG4138

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

449-650

1.81e-16

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

Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 79.50 E-value: 1.81e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 449 LSGISFEVPAGKKVAIVGGSGSGKSTivrLLFRF--YEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVL------FH 520
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPpfampvFQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 521 ntiyYNLLYGNISASPEEV-YAVAKLA---GLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVI----- 591
Cdd:COG4138   89 ----YLALHQPAGASSEAVeQLLAQLAealGLEDKLSRPLT-----------QLSGGEWQRVRLAAVLLQVWPTInpegq 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 592 --LYDEATSSLDsITEETilgAMKDVVKH-----RTSIFIAHRLS-TVVDADEIIVLDQGKVAERGT 650
Cdd:COG4138  154 llLLDEPMNSLD-VAQQA---ALDRLLRElcqqgITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216

ABC_6TM_YknU_like

cd18542

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...

113-389

4.72e-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: 79.40 E-value: 4.72e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLnQMSGNMLNLsdapntvaTMATAVLIGYGVSRAGAAFfneVRNAVFGKVAQNSIRRIAKNVFL 192
Cdd:cd18542   13 ALNLLIPLLIRRIIDSV-IGGGLRELL--------WLLALLILGVALLRGVFRY---LQGYLAEKASQKVAYDLRNDLYD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 193 HLHNLDLGFHLSRQTGALskaIDRGT-------RGISFVLSALVFNLLpiMFevmLVSGVLYYKCGAQFALVTLGTlgty 265
Cdd:cd18542   81 HLQRLSFSFHDKARTGDL---MSRCTsdvdtirRFLAFGLVELVRAVL--LF---IGALIIMFSINWKLTLISLAI---- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 266 TAFTVAVTRW-----RTRFRI------EMNKA--DNDAGNaaidsllnyETVKYFNNERYEAQRYDGFLKTYETASLKST 332
Cdd:cd18542  149 IPFIALFSYVffkkvRPAFEEireqegELNTVlqENLTGV---------RVVKAFAREDYEIEKFDKENEEYRDLNIKLA 219

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147369 333 STLA----MLNFgqsaIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLG 389
Cdd:cd18542  220 KLLAkywpLMDF----LSGLQIVLVLWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLG 276

PRK10575

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

425-650

6.06e-16

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

Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 6.06e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 425 QITPQTATVAFDNVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLES 504
Cdd:PRK10575   4 YTNHSDTTFALRNVSFR-VPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 505 LRRAVGVVPQDavlfhntiyynlLYGNISASPEEVYAVAKLAgLHDAILRMPHGYDTQVGER----GLK---------LS 571
Cdd:PRK10575  83 FARKVAYLPQQ------------LPAAEGMTVRELVAIGRYP-WHGALGRFGAADREKVEEAislvGLKplahrlvdsLS 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 572 GGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAER 648
Cdd:PRK10575 150 GGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARyCDYLVALRGGEMIAQ 229


                 ..
gi 411147369 649 GT 650
Cdd:PRK10575 230 GT 231

ABC_6TM_exporter_like

cd18563

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

113-399

6.49e-16

Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 79.09 E-value: 6.49e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMAtavligygVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFL 192
Cdd:cd18563   13 ALGLVPPYLTKILIDDVLIQLGPGGNTSLLLLLVLGLA--------GAYVLSALLGILRGRLLARLGERITADLRRDLYE 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 193 HLHNLDLGFHLSRQTGALskaIDRGTRG-------ISFVLSALVFNLLPIMFevmlVSGVLYYkCGAQFALVTLGTLgty 265
Cdd:cd18563   85 HLQRLSLSFFDKRQTGSL---MSRVTSDtdrlqdfLSDGLPDFLTNILMIIG----IGVVLFS-LNWKLALLVLIPV--- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 266 tAFTVAVTRW---RTRFRIEMNKADNDAGNAAI-DSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFG 341
Cdd:cd18563  154 -PLVVWGSYFfwkKIRRLFHRQWRRWSRLNSVLnDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPL 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 342 QSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 399
Cdd:cd18563  233 LTFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRAL 290

ABC_NatA_like

cd03267

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...

448-645

7.38e-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: 77.37 E-value: 7.38e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 448 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRaVGVV------------PQD 515
Cdd:cd03267   36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVfgqktqlwwdlpVID 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 AVLFHNTIYynllygNIsaspEEVYAVAKLAGLHDaILRMPHGYDTQVgeRglKLSGGEKQRVAIARAILKDPPVILYDE 595
Cdd:cd03267  115 SFYLLAAIY------DL----PPARFKKRLDELSE-LLDLEELLDTPV--R--QLSLGQRMRAEIAAALLHEPEILFLDE 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 411147369 596 ATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKV 645
Cdd:cd03267  180 PTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232

nikD

PRK10418

nickel transporter ATP-binding protein NikD; Provisional

443-660

7.75e-16

nickel transporter ATP-binding protein NikD; Provisional

Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.82 E-value: 7.75e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 443 IEGQKVL-SGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPqkGSIYLAGQNIQD---VSLESLR-RAVGVV---PQ 514
Cdd:PRK10418  12 LQAAQPLvHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDgkpVAPCALRgRKIATImqnPR 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 DAvlfhntiyYNLLYGNISASPEEVYAVAKLAglHDAilRMPHGYDtQVG----ERGLKL-----SGGEKQRVAIARAIL 585
Cdd:PRK10418  90 SA--------FNPLHTMHTHARETCLALGKPA--DDA--TLTAALE-AVGlenaARVLKLypfemSGGMLQRMMIALALL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 586 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTS--IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHS 660
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALgmLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFNAPKH 234

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

447-665

1.06e-15

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 80.62 E-value: 1.06e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIY-LAGQNIQDVS----LESLR--RAVGVVPQDAVLF 519
Cdd:TIGR03269 298 KAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWVDMTkpgpDGRGRakRYIGILHQEYDLY 377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  520 -HNTIYYNLLYGNISASPEE------VYaVAKLAGLHD----AIL-RMPHgydtqvgerglKLSGGEKQRVAIARAILKD 587
Cdd:TIGR03269 378 pHRTVLDNLTEAIGLELPDElarmkaVI-TLKMVGFDEekaeEILdKYPD-----------ELSEGERHRVALAQVLIKE 445

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  588 PPVILYDEATSSLDSITE----ETILGAMKDVvkHRTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGthhgllaNPHSIY 662
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKvdvtHSILKAREEM--EQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIG-------DPEEIV 516


                  ...
gi 411147369  663 SEM 665
Cdd:TIGR03269 517 EEL 519

PRK10522

multidrug transporter membrane component/ATP-binding component; Provisional

432-647

2.24e-15

multidrug transporter membrane component/ATP-binding component; Provisional

Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 79.63 E-value: 2.24e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 432 TVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGV 511
Cdd:PRK10522 322 TLELRNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VPQDAVLFHNTIyynllygnisaSPEEVYAVAKLAGLHDAILRMPHGYDTQVGE-RGLKLSGGEKQRVAIARAILKDPPV 590
Cdd:PRK10522 402 VFTDFHLFDQLL-----------GPEGKPANPALVEKWLERLKMAHKLELEDGRiSNLKLSKGQKKRLALLLALAEERDI 470

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147369 591 ILYDEATSSLD----SITEETILGAMKDVVKhrTSIFIAHRLSTVVDADEIIVLDQGKVAE 647
Cdd:PRK10522 471 LLLDEWAADQDphfrREFYQVLLPLLQEMGK--TIFAISHDDHYFIHADRLLEMRNGQLSE 529

ABC_6TM_bac_exporter_ABCB8_10_like

cd18576

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...

111-399

2.56e-15

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: 77.14 E-value: 2.56e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 111 EGAMNIVVPFMFKYAVDSLNQmSGNMLNLsdapNTVATMATAVLigygVSRAGAAFFnevRNAVFGKVAQNSIRRIAKNV 190
Cdd:cd18576    8 SSAIGLVFPLLAGQLIDAALG-GGDTASL----NQIALLLLGLF----LLQAVFSFF---RIYLFARVGERVVADLRKDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 191 FLHLHNLDLGFHLSRQTGALSKaidRGTRGISFVLSALVFNLLPIMFEVMLVSG--VLYYKCGAQFALVTLGTLGTYTAF 268
Cdd:cd18576   76 YRHLQRLPLSFFHERRVGELTS---RLSNDVTQIQDTLTTTLAEFLRQILTLIGgvVLLFFISWKLTLLMLATVPVVVLV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 269 TVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSV 348
Cdd:cd18576  153 AVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFG 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 411147369 349 GLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 399
Cdd:cd18576  233 AIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKAL 283

livF

PRK11614

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

429-657

3.73e-15

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

Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 75.69 E-value: 3.73e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 429 QTATVAFDNVHFEYIEGQkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD-VSLESLRR 507
Cdd:PRK11614   2 EKVMLSFDKVSAHYGKIQ-ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 508 AVGVVPQDAVLFHN-TIYYNLLYGNISASPEEVYA-VAKLAGLhdailrMPHGYDTQVgERGLKLSGGEKQRVAIARAIL 585
Cdd:PRK11614  81 AVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQErIKWVYEL------FPRLHERRI-QRAGTMSGGEQQMLAIGRALM 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147369 586 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLS--TVVDADEIIVLDQGKVAERGTHHGLLAN 657
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLAN 227

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

463-650

3.82e-15

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 80.06 E-value: 3.82e-15

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   463 AIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQdVSLESLRRAVGVVPQDAVLFHNTIY--YNLLYGNISASPEEVY 540
Cdd:TIGR01257  960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGMCPQHNILFHHLTVaeHILFYAQLKGRSWEEA 1038

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   541 AVAKLAGLHDAilrmphGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRT 620
Cdd:TIGR01257 1039 QLEMEAMLEDT------GLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRT 1112

                          170       180       190
                   ....*....|....*....|....*....|.
gi 411147369   621 SIFIAHRLSTV-VDADEIIVLDQGKVAERGT 650
Cdd:TIGR01257 1113 IIMSTHHMDEAdLLGDRIAIISQGRLYCSGT 1143

ABCD_peroxisomal_ALDP

cd03223

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...

433-627

9.64e-15

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).

Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 72.57 E-value: 9.64e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvsleslRRAVGVV 512
Cdd:cd03223    1 IELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDLLFL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 513 PQDAvlfhntiYYNLlyGNisaspeevyavaklagLHDAILRmPHGydtqvgergLKLSGGEKQRVAIARAILKDPPVIL 592
Cdd:cd03223   70 PQRP-------YLPL--GT----------------LREQLIY-PWD---------DVLSGGEQQRLAFARLLLHKPKFVF 114

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 411147369 593 YDEATSSLDSITEETILGAMKDvvKHRTSIFIAHR 627
Cdd:cd03223  115 LDEATSALDEESEDRLYQLLKE--LGITVISVGHR 147

MK0520

COG2401

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...

403-647

1.36e-14

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

Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 73.45 E-value: 1.36e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 403 NTLFTLLKVDtqikdKVMASPLQITPQTATV--AFdNVHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF 480
Cdd:COG2401    5 NPFFVLMRVT-----KVYSSVLDLSERVAIVleAF-GVELRVVE-RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 481 RFYE--PQKGSIYLAGQNI-QDVSLeslrravgvvpQDAVLfhntiyynllygnISASPEEVYAVAKLAGLHDAILrmph 557
Cdd:COG2401   78 GALKgtPVAGCVDVPDNQFgREASL-----------IDAIG-------------RKGDFKDAVELLNAVGLSDAVL---- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 558 gYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRlSTVVDA- 634
Cdd:COG2401  130 -WLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAgiTLVVATHH-YDVIDDl 203

                        250
                 ....*....|....*
gi 411147369 635 --DEIIVLDQGKVAE 647
Cdd:COG2401  204 qpDLLIFVGYGGVPE 218

PRK10584

putative ABC transporter ATP-binding protein YbbA; Provisional

448-608

2.85e-14

putative ABC transporter ATP-binding protein YbbA; Provisional

Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.89 E-value: 2.85e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 448 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLE---SLR-RAVGVVPQDAVL----- 518
Cdd:PRK10584  25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLiptln 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 519 -FHNTIYYNLLYG-NISASPEEVYAVAKLAGLHDAILRMPhgydtqvgergLKLSGGEKQRVAIARAILKDPPVILYDEA 596
Cdd:PRK10584 105 aLENVELPALLRGeSSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173

                        170
                 ....*....|..
gi 411147369 597 TSSLDSITEETI 608
Cdd:PRK10584 174 TGNLDRQTGDKI 185

ABC_6TM_MsbA_like

cd18552

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...

112-399

3.50e-14

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: 73.61 E-value: 3.50e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 112 GAMNIVVPFMFKYAVDSLNQmsgnmlnlSDAPNTVATMATAVLIGYGVsRAGAAFFNEVrnaVFGKVAQNSIRRIAKNVF 191
Cdd:cd18552   12 AATTAALAWLLKPLLDDIFV--------EKDLEALLLVPLAIIGLFLL-RGLASYLQTY---LMAYVGQRVVRDLRNDLF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 192 LHLHNLDLGFHLSRQTGAL-SKA---IDRGTRGISFVLSALVFNLLPIMFevmLVSGVLYYkcGAQFALVTLGTLGtytA 267
Cdd:cd18552   80 DKLLRLPLSFFDRNSSGDLiSRItndVNQVQNALTSALTVLVRDPLTVIG---LLGVLFYL--DWKLTLIALVVLP---L 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 268 FTVAVTRWRTRFRIEMNKADNDAGN---AAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSA 344
Cdd:cd18552  152 AALPIRRIGKRLRKISRRSQESMGDltsVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMEL 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 345 IFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 399
Cdd:cd18552  232 LGAIAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGL 286

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

444-640

4.26e-14

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 71.11 E-value: 4.26e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 444 EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvsleslRRAVGVVPQdavlfhnti 523
Cdd:NF040873   3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQ--------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 524 yynllygnISASPEEVYA-VAKLAGL----HDAILRMPHGYDTQVGERGLK--------------LSGGEKQRVAIARAI 584
Cdd:NF040873  63 --------RSEVPDSLPLtVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALErvgladlagrqlgeLSGGQRQRALLAQGL 134

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 585 LKDPPVILYDEATSSLDSITEETILGAMKDVV-KHRTSIFIAHRLSTVVDADEIIVL 640
Cdd:NF040873 135 AQEADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

445-644

5.12e-14

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

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.25 E-value: 5.12e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQ---KGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFH 520
Cdd:TIGR02633  13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIrDTERAGIVIIHQELTLVP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  521 N-TIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSS 599
Cdd:TIGR02633  92 ElSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 411147369  600 LDSITEETILGAMKDVVKHRTS-IFIAHRLSTV-VDADEIIVLDQGK 644
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAHGVAcVYISHKLNEVkAVCDTICVIRDGQ 218

PRK10253

iron-enterobactin ABC transporter ATP-binding protein;

448-649

5.33e-14

iron-enterobactin ABC transporter ATP-binding protein;

Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.71 E-value: 5.33e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 448 VLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIYYNL 527
Cdd:PRK10253  22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQEL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 528 L-YGNISASP-------EEVYAVAK---LAGLHDAILRmphGYDTqvgerglkLSGGEKQRVAIARAILKDPPVILYDEA 596
Cdd:PRK10253 102 VaRGRYPHQPlftrwrkEDEEAVTKamqATGITHLADQ---SVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEP 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 597 TSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERG 649
Cdd:PRK10253 171 TTWLDISHQIDLLELLSELNREKgyTLAAVLHDLNQACRyASHLIALREGKIVAQG 226

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

445-646

6.05e-14

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.09 E-value: 6.05e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSlESLRRAVGV--VPQDAVLFHN- 521
Cdd:PRK15439  23 GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT-PAKAHQLGIylVPQEPLLFPNl 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 522 TIYYNLLYGnisaSPEEVYAVAKLAGLHdAILRMPHGYDTQVGerglKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 601
Cdd:PRK15439 102 SVKENILFG----LPKRQASMQKMKQLL-AALGCQLDLDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTASLT 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 411147369 602 SITEETILGAMKDVVKHRTSI-FIAHRLSTVVD-ADEIIVLDQGKVA 646
Cdd:PRK15439 173 PAETERLFSRIRELLAQGVGIvFISHKLPEIRQlADRISVMRDGTIA 219

ABC_CcmA_heme_exporter

cd03231

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...

445-612

6.09e-14

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

Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 70.98 E-value: 6.09e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVGVVPQDAVLFHNTIY 524
Cdd:cd03231   12 GRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 525 YNLLY---GNISASPEEVYAVAKLAGLHDAilrmPHGYdtqvgerglkLSGGEKQRVAIARAILKDPPVILYDEATSSLD 601
Cdd:cd03231   92 ENLRFwhaDHSDEQVEEALARVGLNGFEDR----PVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157

                        170
                 ....*....|.
gi 411147369 602 SITEETILGAM 612
Cdd:cd03231  158 KAGVARFAEAM 168

PRK13549

xylose transporter ATP-binding subunit; Provisional

445-644

6.56e-14

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.97 E-value: 6.56e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYePQ---KGSIYLAGQNIQDVSL-ESLRRAVGVVPQDAVLFH 520
Cdd:PRK13549  17 GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIrDTERAGIAIIHQELALVK 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 521 N-TIYYNLLYGN-ISASP----EEVYAVAK--LAGLHDAIlrmphGYDTQVGErglkLSGGEKQRVAIARAILKDPPVIL 592
Cdd:PRK13549  96 ElSVLENIFLGNeITPGGimdyDAMYLRAQklLAQLKLDI-----NPATPVGN----LGLGQQQLVEIAKALNKQARLLI 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 411147369 593 YDEATSSLDSITEETILGAMKDVVKHR-TSIFIAHRLSTVVD-ADEIIVLDQGK 644
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAHGiACIYISHKLNEVKAiSDTICVIRDGR 220

PRK10261

glutathione transporter ATP-binding protein; Provisional

437-664

6.92e-14

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 75.28 E-value: 6.92e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 437 NVHFEYiEGQKV--LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEP-----QKGSIYLAGQNIQDVSLESLRRA- 508
Cdd:PRK10261  19 NIAFMQ-EQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQagglvQCDKMLLRRRSRQVIELSEQSAAq 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 509 --------VGVVPQDAVLFHNTIY---------YNLLYGnisASPEEVYAVAK-------LAGLHDAILRMPHgydtqvg 564
Cdd:PRK10261  98 mrhvrgadMAMIFQEPMTSLNPVFtvgeqiaesIRLHQG---ASREEAMVEAKrmldqvrIPEAQTILSRYPH------- 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 565 erglKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKdVVKHRTS---IFIAHRLSTVVD-ADEIIVL 640
Cdd:PRK10261 168 ----QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIK-VLQKEMSmgvIFITHDMGVVAEiADRVLVM 242

                        250       260
                 ....*....|....*....|....
gi 411147369 641 DQGKVAERGTHHGLLANPHSIYSE 664
Cdd:PRK10261 243 YQGEAVETGSVEQIFHAPQHPYTR 266

ABC_6TM_TAP_ABCB8_10_like

cd18557

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...

113-399

1.06e-13

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: 72.21 E-value: 1.06e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLNQMSGnmlnlSDAPNTVATMATAVLIGYGVsragaafFNEVRNAVFGKVAQNSIRRIAKNVFL 192
Cdd:cd18557   10 AAQLLLPYLIGRLIDTIIKGGD-----LDVLNELALILLAIYLLQSV-------FTFVRYYLFNIAGERIVARLRRDLFS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 193 HLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLY--YKCGAQFALVTLGTLGTYTAFTV 270
Cdd:cd18557   78 SLLRQEIAFFDKHKTGEL---TSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIilFILSWKLTLVLLLVIPLLLIASK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 271 AVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGL 350
Cdd:cd18557  155 IYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSL 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 411147369 351 TAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 399
Cdd:cd18557  235 LLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKAL 283

PRK10762

D-ribose transporter ATP binding protein; Provisional

445-648

1.08e-13

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 74.27 E-value: 1.08e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ-DVSLESLRRAVGVVPQDAVLFHN-T 522
Cdd:PRK10762  16 GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQlT 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 523 IYYNLLYGNISASP------EEVYAVAklaglhDAILR---MPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILY 593
Cdd:PRK10762  96 IAENIFLGREFVNRfgridwKKMYAEA------DKLLArlnLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIM 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 594 DEATSSL-DSITEE--TILGAMKDvvKHRTSIFIAHRLSTVVD-ADEIIVLDQGK-VAER 648
Cdd:PRK10762 166 DEPTDALtDTETESlfRVIRELKS--QGRGIVYISHRLKEIFEiCDDVTVFRDGQfIAER 223

PRK03695

vitamin B12-transporter ATPase; Provisional

449-681

1.15e-13

vitamin B12-transporter ATPase; Provisional

Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.50 E-value: 1.15e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 449 LSGISFEVPAGKKVAIVGGSGSGKSTivrLLFRF--YEPQKGSIYLAGQNIQDVSLESL--RRAVgVVPQDAVLFHNTIY 524
Cdd:PRK03695  12 LGPLSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELarHRAY-LSQQQTPPFAMPVF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 525 YNL-LYG----NISASPEEVYAVAKLAGLHDAILRMPHgydtqvgerglKLSGGEKQRVAIARAILKDPPVI-------L 592
Cdd:PRK03695  88 QYLtLHQpdktRTEAVASALNEVAEALGLDDKLGRSVN-----------QLSGGEWQRVRLAAVVLQVWPDInpagqllL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 593 YDEATSSLDsITEEtilGAMKDVVKH-----RTSIFIAHRLS-TVVDADEIIVLDQGKVAERGTHHGLLANPhsIYSEMW 666
Cdd:PRK03695 157 LDEPMNSLD-VAQQ---AALDRLLSElcqqgIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPE--NLAQVF 230

                        250
                 ....*....|....*
gi 411147369 667 HTQSSRVQNHDNPKW 681
Cdd:PRK03695 231 GVNFRRLDVEGHPML 245

cbiO

PRK13638

energy-coupling factor ABC transporter ATP-binding protein;

433-649

1.31e-13

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 1.31e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQ--NIQDVSLESLRRAVG 510
Cdd:PRK13638   2 LATSDLWFRY-QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 511 VVPQDAvlfHNTIYYNLLYGNISaspeevYAVAKLAGLHDAILRMPHGYDTQVGERGLK------LSGGEKQRVAIARAI 584
Cdd:PRK13638  81 TVFQDP---EQQIFYTDIDSDIA------FSLRNLGVPEAEITRRVDEALTLVDAQHFRhqpiqcLSHGQKKRVAIAGAL 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 585 LKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFI-AHRLSTVVD-ADEIIVLDQGKVAERG 649
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIYEiSDAVYVLRQGQILTHG 218

PRK09984

phosphonate ABC transporter ATP-binding protein;

447-652

1.43e-13

phosphonate ABC transporter ATP-binding protein;

Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.58 E-value: 1.43e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGS---IYLAGQNIQDV-----SLESLRRAVGVVPQDAVL 518
Cdd:PRK09984  18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGRTVQREgrlarDIRKSRANTGYIFQQFNL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 519 FHN-TIYYNLLYGNISASP---------------EEVYAVAKLAGLHDAILRMPhgydtqvgerglKLSGGEKQRVAIAR 582
Cdd:PRK09984  98 VNRlSVLENVLIGALGSTPfwrtcfswftreqkqRALQALTRVGMVHFAHQRVS------------TLSGGQQQRVAIAR 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369 583 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHH 652
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRyCERIVALRQGHVFYDGSSQ 238

LptB

COG1137

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...

445-658

2.21e-13

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

Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.44 E-value: 2.21e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIvrllfrFY------EPQKGSIYLAGQNIQDVSLEslRRA---VGVVPQD 515
Cdd:COG1137   15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPMH--KRArlgIGYLPQE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 AVLFHN-TIYYNLLygnisaspeevyAVAKLAGLH--------DAIL---RMPHGYDTqvgeRGLKLSGGEKQRVAIARA 583
Cdd:COG1137   87 ASIFRKlTVEDNIL------------AVLELRKLSkkereerlEELLeefGITHLRKS----KAYSLSGGERRRVEIARA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 584 ILKDPPVILYDEATSSLDSITEETIlgamKDVVKHRTS----IFIA-HR----LSTVvdaDEIIVLDQGKVAERGTHHGL 654
Cdd:COG1137  151 LATNPKFILLDEPFAGVDPIAVADI----QKIIRHLKErgigVLITdHNvretLGIC---DRAYIISEGKVLAEGTPEEI 223


                 ....
gi 411147369 655 LANP 658
Cdd:COG1137  224 LNNP 227

COG4586

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

438-657

3.77e-13

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

Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.89 E-value: 3.77e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 438 VHFEYIEgQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRaVGVV----- 512
Cdd:COG4586   28 FRREYRE-VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARR-IGVVfgqrs 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 513 -------PQDAVLFHNTIYynllygNIsasPEEVYA--VAKLAGLhdaiLRMPHGYDTQVgeRglKLSGGEKQRVAIARA 583
Cdd:COG4586  106 qlwwdlpAIDSFRLLKAIY------RI---PDAEYKkrLDELVEL----LDLGELLDTPV--R--QLSLGQRMRCELAAA 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 584 ILKDPPVILYDEATSSLDSITEETILGAMKDVVK-HRTSIFIA-HRLSTVVD-ADEIIVLDQGKVAERGTHHGLLAN 657
Cdd:COG4586  169 LLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNReRGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245

dppD

PRK11022

dipeptide transporter ATP-binding subunit; Provisional

452-664

4.73e-13

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 70.93 E-value: 4.73e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 452 ISFEVPAGKKVAIVGGSGSGKS----TIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRAVG----VVPQDAVLFHN-- 521
Cdd:PRK11022  26 ISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGaevaMIFQDPMTSLNpc 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 522 -TIYYNLLY-------GNISASPEEVYAVAKLAGLHDAILRM---PHgydtqvgerglKLSGGEKQRVAIARAILKDPPV 590
Cdd:PRK11022 106 yTVGFQIMEaikvhqgGNKKTRRQRAIDLLNQVGIPDPASRLdvyPH-----------QLSGGMSQRVMIAMAIACRPKL 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 591 ILYDEATSSLDSITEETILGAMKDVVKHRTS--IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIYSE 664
Cdd:PRK11022 175 LIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQ 251

PRK13540

cytochrome c biogenesis protein CcmA; Provisional

437-619

5.18e-13

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.44 E-value: 5.18e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 437 NVHFEYiEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIqDVSLESLRRAV------- 509
Cdd:PRK13540   6 ELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI-KKDLCTYQKQLcfvghrs 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 510 GVVPQdaVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDailrMPHGYdtqvgerglkLSGGEKQRVAIARAILKDPP 589
Cdd:PRK13540  84 GINPY--LTLRENCLYDIHFSPGAVGITELCRLFSLEHLID----YPCGL----------LSSGQKRQVALLRLWMSKAK 147

                        170       180       190
                 ....*....|....*....|....*....|
gi 411147369 590 VILYDEATSSLDSITEETIlgaMKDVVKHR 619
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTI---ITKIQEHR 174

ABC_6TM_PCAT1_LagD_like

cd18570

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...

112-436

1.98e-12

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

Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 68.63 E-value: 1.98e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 112 GAMNIVVPFMFKYAVDS-LNQMSGNMLNLsdapntvatMATAVLIGYGVSragaAFFNEVRNAVFGKVAQNSIRRIAKNV 190
Cdd:cd18570   15 TLLGIAGSFFFQILIDDiIPSGDINLLNI---------ISIGLILLYLFQ----SLLSYIRSYLLLKLSQKLDIRLILGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 191 FLHLHNLDLGFHLSRQTGA-LSKAIDrgTRGISFVLSALVFNLlPIMFEVMLVSGVLYYKCGAQFALVTLGTLGTYTAFT 269
Cdd:cd18570   82 FKHLLKLPLSFFETRKTGEiISRFND--ANKIREAISSTTISL-FLDLLMVIISGIILFFYNWKLFLITLLIIPLYILII 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 270 VA-VTRWRTRFRIEMNK-ADNDAgnAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYetasLKSTSTLAMLNFGQSAIF- 346
Cdd:cd18570  159 LLfNKPFKKKNREVMESnAELNS--YLIESLKGIETIKSLNAEEQFLKKIEKKFSKL----LKKSFKLGKLSNLQSSIKg 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 347 ---SVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLfqlslpLNFLGTVyretrQALIDmntlftllkvdtqikdkvmasp 423
Cdd:cd18570  233 lisLIGSLLILWIGSYLVIKGQLSLGQLIAFNALL------GYFLGPI-----ENLIN---------------------- 279

                        330
                 ....*....|...
gi 411147369 424 LQITPQTATVAFD 436
Cdd:cd18570  280 LQPKIQEAKVAAD 292

3a01203

TIGR00954

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...

350-635

2.38e-12

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

Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 70.16 E-value: 2.38e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  350 LTAIMVLASQGIVAGTLTVGDLV---MVNG-LLFQLSLPLNFLGTVYRETRQALIDMNTLFTLLKV-------------- 411
Cdd:TIGR00954 344 AVSIPIFDKTHPAFLEMSEEELMqefYNNGrLLLKAADALGRLMLAGRDMTRLAGFTARVDTLLQVlddvksgnfkrprv 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  412 --DTQIKDKVMASPL-----QITPQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF---- 480
Cdd:TIGR00954 424 eeIESGREGGRNSNLvpgrgIVEYQDNGIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwp 503

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  481 ----RFYEPQKGSIYLAGQNIQdVSLESLRravgvvpqDAVLFHNTIYYNLLYGNISASPEEVYAVAKLaglhDAILRMP 556
Cdd:TIGR00954 504 vyggRLTKPAKGKLFYVPQRPY-MTLGTLR--------DQIIYPDSSEDMKRRGLSDKDLEQILDNVQL----THILERE 570

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  557 HGYDTqVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDV------VKHRTSIFIAHRLST 630
Cdd:TIGR00954 571 GGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREFgitlfsVSHRKSLWKYHEYLL 649


                  ....*
gi 411147369  631 VVDAD 635
Cdd:TIGR00954 650 YMDGR 654

ABC_6TM_Pgp_ABCB1_D1_like

cd18577

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...

112-374

2.65e-12

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.

Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 68.27 E-value: 2.65e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 112 GAMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVATMATA-VLIGygvsrAGAAFFNEVRNAVFGKVAQNSIRRIAKNV 190
Cdd:cd18577   12 GAALPLMTIVFGDLFDAFTDFGSGESSPDEFLDDVNKYALYfVYLG-----IGSFVLSYIQTACWTITGERQARRIRKRY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 191 FLHLHNLDLGFHLSRQTGALSKAIDRGTR----GISFVLSALVFNLlpimfeVMLVSGV---LYYkcGAQFALVTLGTLG 263
Cdd:cd18577   87 LKALLRQDIAWFDKNGAGELTSRLTSDTNliqdGIGEKLGLLIQSL------STFIAGFiiaFIY--SWKLTLVLLATLP 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 264 TYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMlnfgQS 343
Cdd:cd18577  159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGL----GL 234

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 411147369 344 AIFSVGLTAIMVLA----SQGIVAGTLTVGDLVMV 374
Cdd:cd18577  235 GLLFFIIFAMYALAfwygSRLVRDGEISPGDVLTV 269

ABC_6TM_Rv0194_D1_like

cd18543

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...

113-398

3.82e-12

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: 67.51 E-value: 3.82e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLnqmsgnmlnLSDAPNTVATMATAVLIGYGVSRAGAAFfneVRNAVFGKVA---QNSIRRiakN 189
Cdd:cd18543   13 LAGLAIPLLTRRAIDGP---------IAHGDRSALWPLVLLLLALGVAEAVLSF---LRRYLAGRLSlgvEHDLRT---D 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 190 VFLHLHNLDLGFHLSRQTGAL-SKAI-DRGT--RGISFVLSALVFNL-LPIMFEVMLVSGVLyykcgaqFALVTLGTLGt 264
Cdd:cd18543   78 LFAHLQRLDGAFHDRWQSGQLlSRATsDLSLvqRFLAFGPFLLGNLLtLVVGLVVMLVLSPP-------LALVALASLP- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 265 ytAFTVAVTRWRTRFRIEMNKADNDAGNAA--ID-SLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFG 341
Cdd:cd18543  150 --PLVLVARRFRRRYFPASRRAQDQAGDLAtvVEeSVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPL 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 342 QSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQA 398
Cdd:cd18543  228 LEALPELGLAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRA 284

ABC_RNaseL_inhibitor_domain2

cd03237

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

442-665

4.12e-12

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

Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 66.66 E-value: 4.12e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 442 YIEGQKVLSGISFEVPAG-----KKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIylagqniqdvslESLRRAVGVVPQDA 516
Cdd:cd03237    3 YPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI------------EIELDTVSYKPQYI 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 517 VLFHNTIYYNLLYGNISASPEEVYAVAKLAGlhdaILRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEA 596
Cdd:cd03237   71 KADYEGTVRDLLSSITKDFYTHPYFKTEIAK----PLQIEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEP 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 597 TSSLDSitEETILGAmkDVVKHrtsiFIAHRLST--VVD---------ADEIIVLDqGKVAERGTHHGllanPHSIYSEM 665
Cdd:cd03237  143 SAYLDV--EQRLMAS--KVIRR----FAENNEKTafVVEhdiimidylADRLIVFE-GEPSVNGVANP----PQSLRSGM 209

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

445-601

4.14e-12

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 68.90 E-value: 4.14e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRA-VGVVPQD-----AVL 518
Cdd:COG3845  270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDrlgrgLVP 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 519 fHNTIYYNLLYGNISASP---------EEVYAVAKlaglhDAILRM---PHGYDTQVGerglKLSGGEKQRVAIARAILK 586
Cdd:COG3845  350 -DMSVAENLILGRYRRPPfsrggfldrKAIRAFAE-----ELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARELSR 419

                        170
                 ....*....|....*
gi 411147369 587 DPPVILYDEATSSLD 601
Cdd:COG3845  420 DPKLLIAAQPTRGLD 434

ABC_6TM_exporter_like

cd18565

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

113-391

5.59e-12

Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 67.21 E-value: 5.59e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDS-LNQMSGNMLNLSDAPNTVATMATAVLIGY--GVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKN 189
Cdd:cd18565   13 LFDLAPPLLIGVAIDAvFNGEASFLPLVPASLGPADPRGQLWLLGGltVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTD 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 190 VFLHLHNLDLGFHLSRQTG----ALSKAIDRGTRgisfVLSALVFNLLPIMFEVMLVSGVLYYkCGAQFALVTLGTLgty 265
Cdd:cd18565   93 TYDHVQRLDMAFFEDRQTGdlmsVLNNDVNQLER----FLDDGANSIIRVVVTVLGIGAILFY-LNWQLALVALLPV--- 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 266 tAFTVAVTRWRTRfRIEMNKAD--NDAG--NAAI-DSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNF 340
Cdd:cd18565  165 -PLIIAGTYWFQR-RIEPRYRAvrEAVGdlNARLeNNLSGIAVIKAFTAEDFERERVADASEEYRDANWRAIRLRAAFFP 242

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 341 GQSAIFSVGLTAI------MVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTV 391
Cdd:cd18565  243 VIRLVAGAGFVATfvvggyWVLDGPPLFTGTLTVGTLVTFLFYTQRLLWPLTRLGDL 299

phnK

PRK11701

phosphonate C-P lyase system protein PhnK; Provisional

445-665

6.52e-12

phosphonate C-P lyase system protein PhnK; Provisional

Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.49 E-value: 6.52e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSL----ESLRRAV-----GVVPQD 515
Cdd:PRK11701  18 PRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalsEAERRRLlrtewGFVHQH 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 A-------VLFHNTIYYNLL------YGNISASpeevyAVAKLAGLHDAILRM---PHGYdtqvgerglklSGGEKQRVA 579
Cdd:PRK11701  98 PrdglrmqVSAGGNIGERLMavgarhYGDIRAT-----AGDWLERVEIDAARIddlPTTF-----------SGGMQQRLQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 580 IARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTV-VDADEIIVLDQGKVAERGTHHGLLA 656
Cdd:PRK11701 162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVArLLAHRLLVMKQGRVVESGLTDQVLD 241


                 ....*....
gi 411147369 657 NPHSIYSEM 665
Cdd:PRK11701 242 DPQHPYTQL 250

znuC

PRK09544

high-affinity zinc transporter ATPase; Reviewed

430-601

6.93e-12

high-affinity zinc transporter ATPase; Reviewed

Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 66.29 E-value: 6.93e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 430 TATVAFDNVHFEYieGQ-KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQniqdvslesLRra 508
Cdd:PRK09544   2 TSLVSLENVSVSF--GQrRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR-- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 509 VGVVPQ----DAVLFHNTIYYNLLYGNI-SASPEEVYAVAKLAGLHDAILRmphgydtqvgerglKLSGGEKQRVAIARA 583
Cdd:PRK09544  69 IGYVPQklylDTTLPLTVNRFLRLRPGTkKEDILPALKRVQAGHLIDAPMQ--------------KLSGGETQRVLLARA 134

                        170
                 ....*....|....*...
gi 411147369 584 ILKDPPVILYDEATSSLD 601
Cdd:PRK09544 135 LLNRPQLLVLDEPTQGVD 152

livG

PRK11300

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

451-661

7.21e-12

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

Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.17 E-value: 7.21e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 451 GISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESLRRaVGVVP--QDAVLFHN-TIYYNL 527
Cdd:PRK11300  23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIAR-MGVVRtfQHVRLFREmTVIENL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 528 LygnisaspeevyaVAK--------LAGL----------HDAILRMPHGYDtQVGERGL------KLSGGEKQRVAIARA 583
Cdd:PRK11300 102 L-------------VAQhqqlktglFSGLlktpafrraeSEALDRAATWLE-RVGLLEHanrqagNLAYGQQRRLEIARC 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 584 ILKDPPVILYDEATSSLDSitEETI-LGAMKDVVK--HRTSI-FIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANP 658
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNP--KETKeLDELIAELRneHNVTVlLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNP 245


                 ...
gi 411147369 659 HSI 661
Cdd:PRK11300 246 DVI 248

MglA

COG1129

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

445-597

2.74e-11

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.58 E-value: 2.74e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQ--NIQDVSlESLRRAVGVVPQD----AVL 518
Cdd:COG1129  264 VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPR-DAIRAGIAYVPEDrkgeGLV 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 519 FHNTIYYNLLYGNISA-------SPEEVYAVAKlaglhDAILRM---PHGYDTQVGErglkLSGGEKQRVAIARAILKDP 588
Cdd:COG1129  343 LDLSIRENITLASLDRlsrggllDRRRERALAE-----EYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDP 413


                 ....*....
gi 411147369 589 PVILYDEAT 597
Cdd:COG1129  414 KVLILDEPT 422

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

459-641

5.62e-11

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 61.24 E-value: 5.62e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   459 GKKVAIVGGSGSGKSTIVRLLFRFYEPQKGS-IYLAGQNIQDVSLESLRravgvvpqdavlfhntiyynllygnisaspe 537
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------- 50

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   538 evyavaklaglhdailrmphgyDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVK 617
Cdd:smart00382  51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108

                          170       180       190
                   ....*....|....*....|....*....|.
gi 411147369   618 HRTS-------IFIAHRLSTVVDADEIIVLD 641
Cdd:smart00382 109 LLLKseknltvILTTNDEKDLGPALLRRRFD 139

ABC_6TM_TAP

cd18572

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...

154-399

5.63e-11

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

Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 64.10 E-value: 5.63e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 154 LIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSaLVFNll 233
Cdd:cd18572   39 VLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDATKTGELTSRLTSDCQKVSDPLS-TNLN-- 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 234 pIMFE--VMLVSGVLY-YKCGAQFALVTLGTLGtytaFTVAVTRWRTRFRIEMNKADND----AGNAAIDSLLNYETVKY 306
Cdd:cd18572  116 -VFLRnlVQLVGGLAFmFSLSWRLTLLAFITVP----VIALITKVYGRYYRKLSKEIQDalaeANQVAEEALSNIRTVRS 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 307 FNNERYEAQRYDGFLKTYETASLKStstlAMLNFGQSAIFSVGLTAIMVLA----SQGIVAGTLTVGDLVMVngLLFQLS 382
Cdd:cd18572  191 FATEEREARRYERALDKALKLSVRQ----ALAYAGYVAVNTLLQNGTQVLVlfygGHLVLSGRMSAGQLVTF--MLYQQQ 264

                        250
                 ....*....|....*....
gi 411147369 383 L--PLNFLGTVYRETRQAL 399
Cdd:cd18572  265 LgeAFQSLGDVFSSLMQAV 283

PLN03211

ABC transporter G-25; Provisional

441-644

1.22e-10

ABC transporter G-25; Provisional

Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.90 E-value: 1.22e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 441 EYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF-RFYEPQKGSIYLAgqNIQDVSLESLRRaVGVVPQDAVLF 519
Cdd:PLN03211  76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNFTGTILA--NNRKPTKQILKR-TGFVTQDDILY 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 520 -HNTIYYNLLYGNISASPEEVYAVAKLAGLHDAI--LRMPHGYDTQVGERGLK-LSGGEKQRVAIARAILKDPPVILYDE 595
Cdd:PLN03211 153 pHLTVRETLVFCSLLRLPKSLTKQEKILVAESVIseLGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDE 232

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 411147369 596 ATSSLDSITEETILGAMKDVV-KHRTSIFIAHRLSTVVDA--DEIIVLDQGK 644
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQPSSRVYQmfDSVLVLSEGR 284

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

420-643

1.90e-10

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 63.65 E-value: 1.90e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 420 MASPLqITPQTATVAFDNVHfeyiegqkVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQD 499
Cdd:PRK09700   1 MATPY-ISMAGIGKSFGPVH--------ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 500 VSLE-SLRRAVGVVPQD-AVLFHNTIYYNLLYGNISASP---------EEVYAVAKLAGLHDAILRMPhgyDTQVGErgl 568
Cdd:PRK09700  72 LDHKlAAQLGIGIIYQElSVIDELTVLENLYIGRHLTKKvcgvniidwREMRVRAAMMLLRVGLKVDL---DEKVAN--- 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 569 kLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSI-FIAHRLSTVVD-ADEIIVLDQG 643
Cdd:PRK09700 146 -LSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIvYISHKLAEIRRiCDRYTVMKDG 221

ABC_6TM_TmrA_like

cd18544

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...

113-373

6.07e-10

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: 60.86 E-value: 6.07e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDS-LNQMSGNMLNLsdapntvatmaTAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVF 191
Cdd:cd18544   13 ALELLGPLLIKRAIDDyIVPGQGDLQGL-----------LLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 192 LHLHNLDLGFHLSRQTGALSkaidrgTRGIS--------F--VLSALVFNLLPI--MFEVMLVSGVlyykcgaQFALVTL 259
Cdd:cd18544   82 SHIQRLPLSFFDRTPVGRLV------TRVTNdtealnelFtsGLVTLIGDLLLLigILIAMFLLNW-------RLALISL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 260 GTLgtytAFTVAVTRWrtrFRIEMNKADND--AGNAAIDSLLNyE------TVKYFNNERYEAQRYDGFLKTYETASLKS 331
Cdd:cd18544  149 LVL----PLLLLATYL---FRKKSRKAYREvrEKLSRLNAFLQ-EsisgmsVIQLFNREKREFEEFDEINQEYRKANLKS 220

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 411147369 332 TSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVM 373
Cdd:cd18544  221 IKLFALFRPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYA 262

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

445-601

7.37e-10

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

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 7.37e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLfrfyepqkgsiylAG--QNIQDVSLESLRRAVGVVPQDAVLFHN- 521
Cdd:TIGR03719  17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------------AGvdKDFNGEARPQPGIKVGYLPQEPQLDPTk 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  522 TIYYNLLYG-----NISASPEEVYA------------VAKLAGLHDAI------------------LRMPHGyDTQVGer 566
Cdd:TIGR03719  84 TVRENVEEGvaeikDALDRFNEISAkyaepdadfdklAAEQAELQEIIdaadawdldsqleiamdaLRCPPW-DADVT-- 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 411147369  567 glKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 601
Cdd:TIGR03719 161 --KLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193

ABC_UvrA

cd03238

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...

449-638

8.65e-10

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

Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 58.49 E-value: 8.65e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 449 LSGISFEVPAGKKVAIVGGSGSGKSTIVrllfrfyepqKGSIYLAGQNIQDVSLESlrravgvvpqdavlfhntiyynll 528
Cdd:cd03238   11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV----------NEGLYASGKARLISFLPK------------------------ 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 529 ygnisASPEEVYAVAKLAGLHDAILrmphGYDTqVGERGLKLSGGEKQRVAIARAILKDPPVILY--DEATSSLDSITEE 606
Cdd:cd03238   57 -----FSRNKLIFIDQLQFLIDVGL----GYLT-LGQKLSTLSGGELQRVKLASELFSEPPGTLFilDEPSTGLHQQDIN 126

                        170       180       190
                 ....*....|....*....|....*....|...
gi 411147369 607 TILGAMKDVV-KHRTSIFIAHRLSTVVDADEII 638
Cdd:cd03238  127 QLLEVIKGLIdLGNTVILIEHNLDVLSSADWII 159

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

440-653

1.27e-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: 1.27e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 440 FEYIEGQKVLSGISFEVPAGK-----KVAIVGGSGSGKSTIVRLLFRFYEPQKGSI-----------YLagQNIQDVSLE 503
Cdd:COG1245  342 VEYPDLTKSYGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkisykpqYI--SPDYDGTVE 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 504 S-LRRAVGVVpqdavlFHNTIYYNLlygnisaspeevyaVAKLAGLHdailRMphgYDTQVGErglkLSGGEKQRVAIAR 582
Cdd:COG1245  420 EfLRSANTDD------FGSSYYKTE--------------IIKPLGLE----KL---LDKNVKD----LSGGELQRVAIAA 468

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 583 AILKDPPVILYDEATSSLDSitEETILGA--MKDVV--KHRTSIFIAHRLsTVVD--ADEIIVLDqGKVAERGTHHG 653
Cdd:COG1245  469 CLSRDADLYLLDEPSAHLDV--EQRLAVAkaIRRFAenRGKTAMVVDHDI-YLIDyiSDRLMVFE-GEPGVHGHASG 541

ABC_6TM_HetC_like

cd18568

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...

191-405

3.18e-09

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

Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 58.73 E-value: 3.18e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 191 FLHLHNLDLGFHLSRQTGALskaIDR-----------GTRGISFVLSAL-VFNLLPIMFevmlvsgvlYYKcgAQFALVT 258
Cdd:cd18568   82 YKHLLSLPLSFFASRKVGDI---ITRfqenqkirrflTRSALTTILDLLmVFIYLGLMF---------YYN--LQLTLIV 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 259 LGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAML 338
Cdd:cd18568  148 LAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVL 227

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 339 NFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 405
Cdd:cd18568  228 QLISSLINHLGTIAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

441-653

3.43e-09

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.82 E-value: 3.43e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 441 EYIEGQKVLSGISFEVPAGKK-----VAIVGGSGSGKSTIVRLLFRFYEPQKGSI-----------YLAGQniQDVSLES 504
Cdd:PRK13409 342 EYPDLTKKLGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelkisykpqYIKPD--YDGTVED 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 505 LRRAVGVVpqdavlFHNTIYYNLLygnisASPeevyavaklaglhdaiLRMPHGYDTQVGErglkLSGGEKQRVAIARAI 584
Cdd:PRK13409 420 LLRSITDD------LGSSYYKSEI-----IKP----------------LQLERLLDKNVKD----LSGGELQRVAIAACL 468

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 585 LKDPPVILYDEATSSLDSitEETILGA--MKDVVKHR--TSIFIAHRLsTVVD--ADEIIVLDqGKVAERGTHHG 653
Cdd:PRK13409 469 SRDADLYLLDEPSAHLDV--EQRLAVAkaIRRIAEEReaTALVVDHDI-YMIDyiSDRLMVFE-GEPGKHGHASG 539

GguA

NF040905

sugar ABC transporter ATP-binding protein;

445-647

3.99e-09

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.42 E-value: 3.99e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL-----FRFYEpqkGSIYLAGQ-----NIQDvsleSLRRAVGVVPQ 514
Cdd:NF040905  13 GVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvypHGSYE---GEILFDGEvcrfkDIRD----SEALGIVIIHQ 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 D-AVLFHNTIYYNLLYGNISASP-----EEVYAVAK--LA--GLHDAilrmPhgyDTQVGERGLklsgGEKQRVAIARAI 584
Cdd:NF040905  86 ElALIPYLSIAENIFLGNERAKRgvidwNETNRRARelLAkvGLDES----P---DTLVTDIGV----GKQQLVEIAKAL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 585 LKDPPVILYDEATSSL---DSiteETILGAMKDVVKHR-TSIFIAHRLSTVVD-ADEIIVLDQGKVAE 647
Cdd:NF040905 155 SKDVKLLILDEPTAALneeDS---AALLDLLLELKAQGiTSIIISHKLNEIRRvADSITVLRDGRTIE 219

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

445-644

4.28e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.36 E-value: 4.28e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQ-DVSLESLRRAVGVVPQDAVLF-HNT 522
Cdd:PRK10982  10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVlQRS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 523 IYYNLLYGNisaspeevYAVAKLAGLHDAILRMPH------GYDTQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 596
Cdd:PRK10982  90 VMDNMWLGR--------YPTKGMFVDQDKMYRDTKaifdelDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 597 TSSLdsiTEE------TILGAMKDvvKHRTSIFIAHRLSTVVD-ADEIIVLDQGK 644
Cdd:PRK10982 162 TSSL---TEKevnhlfTIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQ 211

3a01205

TIGR00956

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

537-644

4.49e-09

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

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 4.49e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   537 EEVYAvAKLAGLHDAILRMPHGYDTQVGE---RGLklSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMK 613
Cdd:TIGR00956  177 REEYA-KHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALK 253

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 411147369   614 dvvkhrTSIFIAHRLSTVV------DA----DEIIVLDQGK 644
Cdd:TIGR00956  254 ------TSANILDTTPLVAiyqcsqDAyelfDKVIVLYEGY 288

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

449-646

4.63e-09

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 4.63e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 449 LSG-----ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSLESlRRAVGVV--PQD------ 515
Cdd:PRK15439 274 LTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ-RLARGLVylPEDrqssgl 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 ---AVLFHNTiyYNLLYGNISASPEEVYAVAKLAGLHDAI-LRMPHGyDTQVGerglKLSGGEKQRVAIARAILKDPPVI 591
Cdd:PRK15439 353 yldAPLAWNV--CALTHNRRGFWIKPARENAVLERYRRALnIKFNHA-EQAAR----TLSGGNQQKVLIAKCLEASPQLL 425

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 592 LYDEATSSLDSITEETILGAMKDVVKHRTSI-FIAHRLSTVVD-ADEIIVLDQGKVA 646
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIRSIAAQNVAVlFISSDLEEIEQmADRVLVMHQGEIS 482

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

459-641

8.43e-09

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

Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.64 E-value: 8.43e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 459 GKKVAIVGGSGSGKSTIVRLLfrfyepqkgsiylAGQ---NIQDVSLEslrravgvVPQDAVL--FHNTI---YYNLLY- 529
Cdd:COG1245   99 GKVTGILGPNGIGKSTALKIL-------------SGElkpNLGDYDEE--------PSWDEVLkrFRGTElqdYFKKLAn 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 530 GNISAS--PEEVYAVAKL--------------AGLHDAI---LRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPV 590
Cdd:COG1245  158 GEIKVAhkPQYVDLIPKVfkgtvrellekvdeRGKLDELaekLGLENILDRDISE----LSGGELQRVAIAAALLRDADF 233

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 411147369 591 ILYDEATSSLDsITEE-TILGAMKDVVKHRTSIFiahrlstVVDADeIIVLD 641
Cdd:COG1245  234 YFFDEPSSYLD-IYQRlNVARLIRELAEEGKYVL-------VVEHD-LAILD 276

ABCG_PDR_domain1

cd03233

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...

430-645

1.20e-08

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 55.73 E-value: 1.20e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 430 TATVAFDNVHFEYIEGQ---KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLL---FRFYEPQKGSIYLAGQNIQDVSlE 503
Cdd:cd03233    1 ASTLSWRNISFTTGKGRskiPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFA-E 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 504 SLRRAVGVVPQDAVLFHN-TIYynllygnisaspEEVYAVAKLAGlhDAILRmphgydtqvgerglKLSGGEKQRVAIAR 582
Cdd:cd03233   80 KYPGEIIYVSEEDVHFPTlTVR------------ETLDFALRCKG--NEFVR--------------GISGGERKRVSIAE 131

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 411147369 583 AILKDPPVILYDEATSSLDSITEETILGAMKDVVKhrtsifiAHRLSTVVDA-----------DEIIVLDQGKV 645
Cdd:cd03233  132 ALVSRASVLCWDNSTRGLDSSTALEILKCIRTMAD-------VLKTTTFVSLyqasdeiydlfDKVLVLYEGRQ 198

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

447-654

1.25e-08

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.91 E-value: 1.25e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ-KGSIYLAGQNIQDVS-LESLRRAVGVVPQDAVlfHNTIY 524
Cdd:TIGR02633 274 KRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRK--RHGIV 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  525 YNLLYG-NISASPEEVY-------AVAKLAGLHDAILRM---PHGYDTQVGerglKLSGGEKQRVAIARAILKDPPVILY 593
Cdd:TIGR02633 352 PILGVGkNITLSVLKSFcfkmridAAAELQIIGSAIQRLkvkTASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLIL 427

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369  594 DEATSSLDSITEETILGAMKDVVKHRTS-IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGL 654
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAiIVVSSELAEVLGlSDRVLVIGEGKLKGDFVNHAL 490

ABC_6TM_CyaB_HlyB_like

cd18588

Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...

190-405

1.52e-08

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

Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 56.74 E-value: 1.52e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 190 VFLHLHNLDLGFHLSRQTGALskaIDRgTRGIS----FVLSALVFNLLPIMFEVMLVSGVLYYKcgAQFALVTLGTLGTY 265
Cdd:cd18588   81 LFRHLLRLPLSYFESRQVGDT---VAR-VRELEsirqFLTGSALTLVLDLVFSVVFLAVMFYYS--PTLTLIVLASLPLY 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 266 TAFTVAVTRwRTRFRIEmNKADNDAGNAA--IDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKsTSTLAmlNFGQS 343
Cdd:cd18588  155 ALLSLLVTP-ILRRRLE-EKFQRGAENQSflVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFK-TANLS--NLASQ 229

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 344 AIFSVGLT---AIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMNTL 405
Cdd:cd18588  230 IVQLIQKLttlAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294

oppD

PRK09473

oligopeptide transporter ATP-binding component; Provisional

452-664

1.81e-08

oligopeptide transporter ATP-binding component; Provisional

Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 56.66 E-value: 1.81e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 452 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ---KGSIYLAGQNIQDVSLESLRR----AVGVVPQDAVLFHNTiy 524
Cdd:PRK09473  35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKELNKlraeQISMIFQDPMTSLNP-- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 525 ynllYGNISASPEEVYAVAKLAGLHDAI---LRM----------------PHgydtqvgerglKLSGGEKQRVAIARAIL 585
Cdd:PRK09473 113 ----YMRVGEQLMEVLMLHKGMSKAEAFeesVRMldavkmpearkrmkmyPH-----------EFSGGMRQRVMIAMALL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 586 KDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTS-IFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANPHSIY 662
Cdd:PRK09473 178 CRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAiIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARDVFYQPSHPY 257


                 ..
gi 411147369 663 SE 664
Cdd:PRK09473 258 SI 259

PRK13538

cytochrome c biogenesis heme-transporting ATPase CcmA;

443-601

1.98e-08

cytochrome c biogenesis heme-transporting ATPase CcmA;

Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 55.20 E-value: 1.98e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 443 IEGQKVL-SGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQdvsleSLRRAvgvvpqdavlFHn 521
Cdd:PRK13538  10 ERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR-----RQRDE----------YH- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 522 tiyYNLLY-GNISA-----SPEE-VYAVAKLAGLHD-----AILRmphgydtQVGERGLK------LSGGEKQRVAIARA 583
Cdd:PRK13538  74 ---QDLLYlGHQPGiktelTALEnLRFYQRLHGPGDdealwEALA-------QVGLAGFEdvpvrqLSAGQQRRVALARL 143

                        170
                 ....*....|....*...
gi 411147369 584 ILKDPPVILYDEATSSLD 601
Cdd:PRK13538 144 WLTRAPLWILDEPFTAID 161

ABC_6TM_YknV_like

cd18545

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...

113-392

2.34e-08

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: 55.94 E-value: 2.34e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSlNQMSGNMLNLsdapntvatmaTAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFL 192
Cdd:cd18545   14 AASLAGPYLIKIAIDE-YIPNGDLSGL-----------LIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 193 HLHNLDLGFHLSRQTGA-LSKAI-DRGTrgISFVLSALVFNLLPIMFEVMLVSGVLYYKcGAQFALVTLGTLgtyTAFTV 270
Cdd:cd18545   82 HLQKLSFSFFDSRPVGKiLSRVInDVNS--LSDLLSNGLINLIPDLLTLVGIVIIMFSL-NVRLALVTLAVL---PLLVL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 271 AVTRW----RTRFRIEMNKADNdaGNAAI-DSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAI 345
Cdd:cd18545  156 VVFLLrrraRKAWQRVRKKISN--LNAYLhESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELI 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 411147369 346 FSVGLTAIMVLASQGIVAGTLTVGDLV-MVN--GLLFQlslPLNFLGTVY 392
Cdd:cd18545  234 SALGTALVYWYGGKLVLGGAITVGVLVaFIGyvGRFWQ---PIRNLSNFY 280

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

443-663

2.92e-08

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.84 E-value: 2.92e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 443 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNiqdVSLESLRRAV--GVV--PQD--- 515
Cdd:PRK11288 263 LKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKP---IDIRSPRDAIraGIMlcPEDrka 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 -AVLFHNTIYYNLlygNISASPEEVYA--------VAKLAGLHDAILRM--PHGyDTQVGerglKLSGGEKQRVAIARAI 584
Cdd:PRK11288 340 eGIIPVHSVADNI---NISARRHHLRAgclinnrwEAENADRFIRSLNIktPSR-EQLIM----NLSGGNQQKAILGRWL 411

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 585 LKDPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGllANPHSIY 662
Cdd:PRK11288 412 SEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQgVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ--ATERQAL 489


                 .
gi 411147369 663 S 663
Cdd:PRK11288 490 S 490

ABC_6TM_Tm287_like

cd18548

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...

145-391

2.97e-08

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

Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 55.87 E-value: 2.97e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 145 TVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSirriaknvflhLHNLDlgfHLSrqTGALskaIDRGTRGISFV 224
Cdd:cd18548   49 ALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFS-----------FAEID---KFG--TSSL---ITRLTNDVTQV 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 225 LSAlVFNLL------PIMFevmLVSGVLYYKCGAQFALVTLGTLGTYTAFTVAVTRW-RTRFRIEMNKadNDAGNAAI-D 296
Cdd:cd18548  110 QNF-VMMLLrmlvraPIML---IGAIIMAFRINPKLALILLVAIPILALVVFLIMKKaIPLFKKVQKK--LDRLNRVVrE 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 297 SLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNG 376
Cdd:cd18548  184 NLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFIN 263

                        250
                 ....*....|....*
gi 411147369 377 LLFQLSLPLNFLGTV 391
Cdd:cd18548  264 YLMQILMSLMMLSMV 278

PLN03073

ABC transporter F family; Provisional

428-652

4.43e-08

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 56.41 E-value: 4.43e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 428 PQTATVAFDNVHFEYIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYlagqniqdvslESLRR 507
Cdd:PLN03073 504 PGPPIISFSDASFGYPGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKV 572

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 508 AVGVVPQdavlfHNTIYYNLlygniSASPEeVYAVAKLAGLHDAILRMPHGYDTQVGERGLK----LSGGEKQRVAIARA 583
Cdd:PLN03073 573 RMAVFSQ-----HHVDGLDL-----SSNPL-LYMMRCFPGVPEQKLRAHLGSFGVTGNLALQpmytLSGGQKSRVAFAKI 641

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147369 584 ILKDPPVILYDEATSSLDSITEETILGAMkdVVKHRTSIFIAHRLSTVVDA-DEIIVLDQGKVAE-RGTHH 652
Cdd:PLN03073 642 TFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHDEHLISGSvDELWVVSEGKVTPfHGTFH 710

ABC_6TM_exporter_like

cd18778

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

113-372

4.81e-08

Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 55.24 E-value: 4.81e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLnqmsgnmlnlsdapnTVATMATAVLIGYGVSRAGA----AFFNEVRNAVFGKVAQNSIRRIAK 188
Cdd:cd18778   13 LLGLVPPWLIRELVDLV---------------TIGSKSLGLLLGLALLLLGAyllrALLNFLRIYLNHVAEQKVVADLRS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 189 NVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKcGAQFALVTLGTLGTYTAF 268
Cdd:cd18778   78 DLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSI-NPKLALLTLIPIPFLALG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 269 TVAVTRW-RTRFRI------EMNKA--DNDAGNAAIdsllnyetvKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMln 339
Cdd:cd18778  157 AWLYSKKvRPRYRKvrealgELNALlqDNLSGIREI---------QAFGREEEEAKRFEALSRRYRKAQLRAMKLWAI-- 225

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 411147369 340 FGQSAIFSVGLTAIMVLASQG--IVAGTLTVGDLV 372
Cdd:cd18778  226 FHPLMEFLTSLGTVLVLGFGGrlVLAGELTIGDLV 260

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

459-640

5.85e-08

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 5.85e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 459 GKKVAIVGGSGSGKSTIVRLLfrfyepqkgsiylAGQ---NIQDVSLES-----LRRAVGVVPQDavlfhntiYYNLLY- 529
Cdd:PRK13409  99 GKVTGILGPNGIGKTTAVKIL-------------SGElipNLGDYEEEPswdevLKRFRGTELQN--------YFKKLYn 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 530 GNISAS--PEEVYAVAK-LAGLHDAILRmphgydtQVGERGL-------------------KLSGGEKQRVAIARAILKD 587
Cdd:PRK13409 158 GEIKVVhkPQYVDLIPKvFKGKVRELLK-------KVDERGKldevverlglenildrdisELSGGELQRVAIAAALLRD 230

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 588 PPVILYDEATSSLDsITEE-TILGAMKDVVKHRTSIFIAHRLsTVVD--ADEIIVL 640
Cdd:PRK13409 231 ADFYFFDEPTSYLD-IRQRlNVARLIRELAEGKYVLVVEHDL-AVLDylADNVHIA 284

ABCG_PDR_domain2

cd03232

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...

447-643

6.60e-08

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 53.40 E-value: 6.60e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 447 KVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQ--KGSIYLAGQNIQdvslESLRRAVGVVPQDAVLFHN-TI 523
Cdd:cd03232   21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLD----KNFQRSTGYVEQQDVHSPNlTV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 524 YYNLLYGnisaspeevyavAKLaglhdailrmphgydtqvgeRGLKLSggEKQRVAIARAILKDPPVILYDEATSSLDSI 603
Cdd:cd03232   97 REALRFS------------ALL--------------------RGLSVE--QRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 411147369 604 TEETILGAMKDVVKH-RTSIFIAHRLSTVVDA--DEIIVLDQG 643
Cdd:cd03232  143 AAYNIVRFLKKLADSgQAILCTIHQPSASIFEkfDRLLLLKRG 185

sufC

PRK09580

cysteine desulfurase ATPase component; Reviewed

443-651

7.98e-08

cysteine desulfurase ATPase component; Reviewed

Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.03 E-value: 7.98e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 443 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF--RFYEPQKGSIYLAGQNIQDVSLESlRRAVGV--------- 511
Cdd:PRK09580  11 VEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGIfmafqypve 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VPQDAVLFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPHGYDTQVGERGlkLSGGEKQRVAIARAILKDPPVI 591
Cdd:PRK09580  90 IPGVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELC 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 592 LYDEATSSLD----SITEETIlGAMKDvvKHRTSIFIAH--RLSTVVDADEIIVLDQGKVAERGTH 651
Cdd:PRK09580 168 ILDESDSGLDidalKIVADGV-NSLRD--GKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

445-609

8.78e-08

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 55.33 E-value: 8.78e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  445 GQKVL-SGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLaGQNIQdvsleslrraVGVVPQ--DAVLFHN 521
Cdd:TIGR03719 333 GDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LAYVDQsrDALDPNK 401

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  522 TIYynllygnisaspEEVyavaklAGLHDAIL----RMP----------HGYDTQ--VGErglkLSGGEKQRVAIARAIL 585
Cdd:TIGR03719 402 TVW------------EEI------SGGLDIIKlgkrEIPsrayvgrfnfKGSDQQkkVGQ----LSGGERNRVHLAKTLK 459

                         170       180
                  ....*....|....*....|....*...
gi 411147369  586 KDPPVILYDEATSSLDSIT----EETIL 609
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETlralEEALL 487

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

452-647

1.51e-07

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.41 E-value: 1.51e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 452 ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESLRRAVGVVPQ---DAVLFHN-TIYYN 526
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpLDAVKKGMAYITEsrrDNGFFPNfSIAQN 361

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 527 L-------------LYGNISASPEevyavAKLAGLHDAILRMP-HGYDTQVGErglkLSGGEKQRVAIARAILKDPPVIL 592
Cdd:PRK09700 362 MaisrslkdggykgAMGLFHEVDE-----QRTAENQRELLALKcHSVNQNITE----LSGGNQQKVLISKWLCCCPEVII 432

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 593 YDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVDA-DEIIVLDQGKVAE 647
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489

PRK15064

ABC transporter ATP-binding protein; Provisional

444-626

1.63e-07

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 1.63e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 444 EGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAgQNIQdvsleslrraVGVVPQD-AVLFHNT 522
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS-ENAN----------IGYYAQDhAYDFEND 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 523 IyyNLLygnisaspeEVYAVAKLAGlHD-----AIL-RMPHGYDtQVGERGLKLSGGEKQRVAIARAILKDPPVILYDEA 596
Cdd:PRK15064 399 L--TLF---------DWMSQWRQEG-DDeqavrGTLgRLLFSQD-DIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465

                        170       180       190
                 ....*....|....*....|....*....|..
gi 411147369 597 TSSLD--SIteETILGAMKDVvkHRTSIFIAH 626
Cdd:PRK15064 466 TNHMDmeSI--ESLNMALEKY--EGTLIFVSH 493

ABC_6TM_ABCB10_like

cd18573

Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...

113-382

2.12e-07

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: 53.29 E-value: 2.12e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLNQMSGNMLNLSDAPNTVAT-MATAVLIGygvsragaAFFNEVRNAVFGKVAQNSIRRIAKNVF 191
Cdd:cd18573   10 AVTMSVPFAIGKLIDVASKESGDIEIFGLSLKTFALaLLGVFVVG--------AAANFGRVYLLRIAGERIVARLRKRLF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 192 LHLHNLDLGFHLSRQTG---------------ALSKAIDRGTRGISFVLSALVfnllpIMFevmLVSgvlyykcgAQFAL 256
Cdd:cd18573   82 KSILRQDAAFFDKNKTGelvsrlssdtsvvgkSLTQNLSDGLRSLVSGVGGIG-----MML---YIS--------PKLTL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 257 VTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGflKTYETASLKSTSTLA 336
Cdd:cd18573  146 VMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAK--KVDEVFDLAKKEALA 223

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 337 MLNFGQSAIFSVGLTAIMVLASQG--IVAGTLTVGDL-------VMVNGLLFQLS 382
Cdd:cd18573  224 SGLFFGSTGFSGNLSLLSVLYYGGslVASGELTVGDLtsflmyaVYVGSSVSGLS 278

ABC_6TM_AtABCB27_like

cd18780

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...

115-399

2.51e-07

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

Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 53.02 E-value: 2.51e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 115 NIVVPFMFKYAVDSLNQMSGNmlNLSDAPNTVATMATAVLIGYGVSragaAFFNEVRNAVFGKVAQNSIRRIAKNVFLHL 194
Cdd:cd18780   12 NLALPYFFGQVIDAVTNHSGS--GGEEALRALNQAVLILLGVVLIG----SIATFLRSWLFTLAGERVVARLRKRLFSAI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 195 HNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKCgaqfALVTLGTLGTYTAFTVAvTR 274
Cdd:cd18780   86 IAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTS----WKLTLVMLSVVPPLSIG-AV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 275 WRTRFRIEMNKADND----AGNAAIDSLLNYETVKYFNNERYEAQRYDGflKTYETASL--KSTSTLAMLNFGQSAIFSV 348
Cdd:cd18780  161 IYGKYVRKLSKKFQDalaaASTVAEESISNIRTVRSFAKETKEVSRYSE--KINESYLLgkKLARASGGFNGFMGAAAQL 238

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 411147369 349 GLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 399
Cdd:cd18780  239 AIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAV 289

ABC_6TM_TAP1

cd18589

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...

184-399

2.59e-07

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

Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 52.86 E-value: 2.59e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 184 RRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSAlvfNLLPIMFEVMLVSGVLYY--KCGAQFALVTLGT 261
Cdd:cd18589   69 SRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSE---NLSLLMWYLARGLFLFIFmlWLSPKLALLTALG 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 262 LGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFL-KTYETASLKSTS-TLAMLN 339
Cdd:cd18589  146 LPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLqKTYRLNKKEAAAyAVSMWT 225

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369 340 FGQSAIF-SVGltaIMVLASQGIVAGTLTVGDLVMVngLLFQL--SLPLNFLGTVYRETRQAL 399
Cdd:cd18589  226 SSFSGLAlKVG---ILYYGGQLVTAGTVSSGDLVTF--VLYELqfTSAVEVLLSYYPSVMKAV 283

ABC_6TM_Pgp_ABCB1_D2_like

cd18578

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...

162-379

2.64e-07

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.

Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 53.22 E-value: 2.64e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 162 AGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFH--LSRQTGALSKAIDRGT---RGI-SFVLSALVFNLlpi 235
Cdd:cd18578   63 IVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFddPENSTGALTSRLSTDAsdvRGLvGDRLGLILQAI--- 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 236 mfeVMLVSGV---LYYkcGAQFALVTLGTLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERY 312
Cdd:cd18578  140 ---VTLVAGLiiaFVY--GWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDY 214

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 313 EAQRYDGFLKTYETASLKStSTLAMLNFG--QSAIFSVglTAI-----MVLasqgIVAGTLTVGDLVMV-NGLLF 379
Cdd:cd18578  215 FLEKYEEALEEPLKKGLRR-ALISGLGFGlsQSLTFFA--YALafwygGRL----VANGEYTFEQFFIVfMALIF 282

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

445-601

3.17e-07

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 3.17e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLA-GQNI------------QDVsLESLRRAVGV 511
Cdd:PRK11819  19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKVgylpqepqldpeKTV-RENVEEGVAE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VpQDAVLFHNTIYynLLYGNISASPEEVyaVAKLAGLHDAI------------------LRMPHGyDTQVGerglKLSGG 573
Cdd:PRK11819  98 V-KAALDRFNEIY--AAYAEPDADFDAL--AAEQGELQEIIdaadawdldsqleiamdaLRCPPW-DAKVT----KLSGG 167

                        170       180
                 ....*....|....*....|....*...
gi 411147369 574 EKQRVAIARAILKDPPVILYDEATSSLD 601
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLD 195

ycf16

CHL00131

sulfate ABC transporter protein; Validated

443-650

4.38e-07

sulfate ABC transporter protein; Validated

Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.95 E-value: 4.38e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 443 IEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRF--YEPQKGSIYLAGQNIQDvsLESLRRA------------ 508
Cdd:CHL00131  17 VNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILD--LEPEERAhlgiflafqypi 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 509 --VGVVPQDavlFHNTIYYNLL--YGNISASPEEVYAV----AKLAGLHdailrmPHGYDTQVGErglKLSGGEKQRVAI 580
Cdd:CHL00131  95 eiPGVSNAD---FLRLAYNSKRkfQGLPELDPLEFLEIinekLKLVGMD------PSFLSRNVNE---GFSGGEKKRNEI 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 411147369 581 ARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSI-FIAH--RLSTVVDADEIIVLDQGKVAERGT 650
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIiLITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235

ABC_6TM_LmrA_like

cd18551

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...

113-399

6.40e-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: 51.67 E-value: 6.40e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLNQMSGNMlnlsdapNTVATMATAVLIGygvsragaAFFNEVRNAVFGKVAQNSIRRIAKNVFL 192
Cdd:cd18551   13 AASLAQPLLVKNLIDALSAGGSSG-------GLLALLVALFLLQ--------AVLSALSSYLLGRTGERVVLDLRRRLWR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 193 HLHNLDLGFHLSRQTG-----------ALSKAIDRGTrgISFVLSALVFNL-LPIMFevmLVSGVLyykcgaqfALVTLG 260
Cdd:cd18551   78 RLLRLPVSFFDRRRSGdlvsrvtndttLLRELITSGL--PQLVTGVLTVVGaVVLMF---LLDWVL--------TLVTLA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 261 TLGTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNF 340
Cdd:cd18551  145 VVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGP 224

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147369 341 GQSAIFSVGLTAIMVLASQGIVAGTLTVGDLV---MvngLLFQLSLPLNFLGTVYRETRQAL 399
Cdd:cd18551  225 LMGLAVQLALLVVLGVGGARVASGALTVGTLVaflL---YLFQLITPLSQLSSFFTQLQKAL 283

ABC_6TM_Tm288_like

cd18547

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...

113-386

8.81e-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: 51.25 E-value: 8.81e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLNQMSGNMLNlsDAPNTVATMATAVLIGYGVSragaAFFNEVRNAVFGKVAQNSIRRIAKNVFL 192
Cdd:cd18547   13 LLSVLGPYLLGKAIDLIIEGLGGGGG--VDFSGLLRILLLLLGLYLLS----ALFSYLQNRLMARVSQRTVYDLRKDLFE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 193 HLHNLDLGFHLSRQTGA-LSKA---IDRGTRGISFVLSALVFNLLPI--MFEVMLV-SGVLyykcgaqfALVTLGTLGTY 265
Cdd:cd18547   87 KLQRLPLSYFDTHSHGDiMSRVtndVDNISQALSQSLTQLISSILTIvgTLIMMLYiSPLL--------TLIVLVTVPLS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 266 TAFTVAVTRW-RTRFRIEMNKadndAG--NAAID-SLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAML--- 338
Cdd:cd18547  159 LLVTKFIAKRsQKYFRKQQKA----LGelNGYIEeMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLmpi 234

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 411147369 339 -----NFGQSAIFSVGltAIMVLasqgivAGTLTVGDLV----MVNgllfQLSLPLN 386
Cdd:cd18547  235 mnfinNLGYVLVAVVG--GLLVI------NGALTVGVIQaflqYSR----QFSQPIN 279

ABC_6TM_exporter_like

cd18550

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

113-399

1.24e-06

Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 50.94 E-value: 1.24e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDS---------LNQMSGNMLNLsdapnTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGkvaqnsi 183
Cdd:cd18550   13 LLGLLPPLLLREIIDDalpqgdlglLVLLALGMVAV-----AVASALLGVVQTYLSARIGQGVMYDLRVQLYA------- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 184 rriaknvflHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYYKcGAQFALVTLGTLg 263
Cdd:cd18550   81 ---------HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLAL-DWRLALLSLVLL- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 264 tytAFTVAVTRW--RTRFRIEMNKADNdagNAAIDSLLNyET--------VKYFNNERYEAQRYDGflKTYETASLKSTS 333
Cdd:cd18550  150 ---PLFVLPTRRvgRRRRKLTREQQEK---LAELNSIMQ-ETlsvsgallVKLFGREDDEAARFAR--RSRELRDLGVRQ 220

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 334 TLAMLNFGQ--SAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 399
Cdd:cd18550  221 ALAGRWFFAalGLFTAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSL 288

tagH

PRK13545

teichoic acids export protein ATP-binding subunit; Provisional

449-703

1.24e-06

teichoic acids export protein ATP-binding subunit; Provisional

Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 51.81 E-value: 1.24e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 449 LSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGqniqdvSLESLRRAVGVVPQDAVLfHNTIYYNLL 528
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGLNGQLTGI-ENIELKGLM 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 529 YGNISASPEEVY-AVAKLAGLHDAILRMPHGYdtqvgerglklSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEET 607
Cdd:PRK13545 113 MGLTKEKIKEIIpEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 608 ILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVAERGTHHGLLANphsiYSEMwhtqssrvqnhdnpkweAKK 685
Cdd:PRK13545 182 CLDKMNEFKEQgKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDH----YDEF-----------------LKK 240

                        250
                 ....*....|....*...
gi 411147369 686 ENISKEEERKKLQEEIVN 703
Cdd:PRK13545 241 YNQMSVEERKDFREEQIS 258

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

446-646

1.27e-06

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 1.27e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 446 QKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVS-LESL----------RRAVGVVPQ 514
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAInhgfalvteeRRSTGIYAY 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 515 DAVLFhNTIYYNL--------LYGNISASPEEVYAVaklaglhDAILRMPHGYDTQVGErglkLSGGEKQRVAIARAILK 586
Cdd:PRK10982 341 LDIGF-NSLISNIrnyknkvgLLDNSRMKSDTQWVI-------DSMRVKTPGHRTQIGS----LSGGNQQKVIIGRWLLT 408

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147369 587 DPPVILYDEATSSLDSITEETILGAMKDVVKH-RTSIFIAHRLSTVVD-ADEIIVLDQGKVA 646
Cdd:PRK10982 409 QPEILMLDEPTRGIDVGAKFEIYQLIAELAKKdKGIIIISSEMPELLGiTDRILVMSNGLVA 470

hmuV

PRK13547

heme ABC transporter ATP-binding protein;

445-659

1.44e-06

heme ABC transporter ATP-binding protein;

Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.60 E-value: 1.44e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLF-RFYEPQ-------KGSIYLAGQNIQDVSLESLRRAVGVVPQDA 516
Cdd:PRK13547  13 HRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 517 V-LFHNTIYYNLLYGNISASPEEVYAVAKLAGLHDAILRMPhGYDTQVGERGLKLSGGEKQRVAIARAILK--------- 586
Cdd:PRK13547  93 QpAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALA-GATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 587 DPPVILYDEATSSLDSITEETILGAMKDVVK--HRTSIFIAHRLSTVV-DADEIIVLDQGKVAERGTHHGLLANPH 659
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAArHADRIAMLADGAIVAHGAPADVLTPAH 247

PRK11147

ABC transporter ATPase component; Reviewed

436-606

1.51e-06

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.49 E-value: 1.51e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 436 DNVHFEyIEGQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYlAGQNIQDVSLESLRRAVGvvPQd 515
Cdd:PRK11147 323 ENVNYQ-IDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH-CGTKLEVAYFDQHRAELD--PE- 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 516 avlfhNTIYYNLLYGN----ISASPEEVyavakLAGLHDaILRMPHGYDTQVGerglKLSGGEKQRVAIARAILKDPPVI 591
Cdd:PRK11147 398 -----KTVMDNLAEGKqevmVNGRPRHV-----LGYLQD-FLFHPKRAMTPVK----ALSGGERNRLLLARLFLKPSNLL 462

                        170
                 ....*....|....*
gi 411147369 592 LYDEATSSLDSITEE 606
Cdd:PRK11147 463 ILDEPTNDLDVETLE 477

ABC_6TM_Rv0194_D2_like

cd18546

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...

111-398

2.99e-06

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: 49.41 E-value: 2.99e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 111 EGAMNIVVPFMFKYAVDS-LNQMSGNMLNLsdapnTVATMATAVLIGYGVSRAgaaffnevRNAVFGKVAQNSIRRIAKN 189
Cdd:cd18546   11 DTAASLAGPLLVRYGIDSgVRAGDLGVLLL-----AAAAYLAVVLAGWVAQRA--------QTRLTGRTGERLLYDLRLR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 190 VFLHLHNLDLGFH--------LSRQTG---ALSKAIDRGtrgisfvLSALVFNLLPIMF-EVMLVsgVLyykcGAQFALV 257
Cdd:cd18546   78 VFAHLQRLSLDFHeretsgriMTRMTSdidALSELLQTG-------LVQLVVSLLTLVGiAVVLL--VL----DPRLALV 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 258 TLGTLgtytAFTVAVTRWrtrFRIEMNKADNDAGNAAIDSLLNY-ET------VKYFNNERYEAQRYDGFLKTYETASLK 330
Cdd:cd18546  145 ALAAL----PPLALATRW---FRRRSSRAYRRARERIAAVNADLqETlagirvVQAFRRERRNAERFAELSDDYRDARLR 217

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 411147369 331 STSTLAMLNFGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLV---MVNGLLFQlslPLNFLGTVYRETRQA 398
Cdd:cd18546  218 AQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVaflLYLRRFFA---PIQQLSQVFDSYQQA 285

PRK10762

D-ribose transporter ATP binding protein; Provisional

449-656

6.22e-06

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 49.23 E-value: 6.22e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 449 LSG-----ISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrravgvvPQDAVlfHNTI 523
Cdd:PRK10762 263 LSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRS-----------PQDGL--ANGI 329

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 524 YY--------NLLYG-----NISASP--------------EEVYAVAKLAGLHDaiLRMPhGYDTQVGerglKLSGGEKQ 576
Cdd:PRK10762 330 VYisedrkrdGLVLGmsvkeNMSLTAlryfsraggslkhaDEQQAVSDFIRLFN--IKTP-SMEQAIG----LLSGGNQQ 402

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 577 RVAIARAILKDPPVILYDEATSSLDsiteetiLGAMKDVVKhRTSIFIAHRLSTVV----------DADEIIVLDQGKV- 645
Cdd:PRK10762 403 KVAIARGLMTRPKVLILDEPTRGVD-------VGAKKEIYQ-LINQFKAEGLSIILvssempevlgMSDRILVMHEGRIs 474

                        250
                 ....*....|....*
gi 411147369 646 ----AERGTHHGLLA 656
Cdd:PRK10762 475 geftREQATQEKLMA 489

PRK15093

peptide ABC transporter ATP-binding protein SapD;

569-664

7.34e-06

peptide ABC transporter ATP-binding protein SapD;

Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 48.65 E-value: 7.34e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 569 KLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHR--TSIFIAHRLSTVVD-ADEIIVLDQGKV 645
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINVLYCGQT 237

                         90
                 ....*....|....*....
gi 411147369 646 AERGTHHGLLANPHSIYSE 664
Cdd:PRK15093 238 VETAPSKELVTTPHHPYTQ 256

ABC_6TM_PrtD_LapB_HlyB_like

cd18566

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...

143-386

7.39e-06

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

Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 48.35 E-value: 7.39e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 143 PNTVATMATAVLIGYGVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGIS 222
Cdd:cd18566   34 PNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLERLNSLEQIRE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 223 FVLSALVFNLLPIMFEVMLVSGVLYYkcGAQFALVTLGTLGTYTAFTVAV-TRWRTRFRiEMNKADNDAGNAAIDSLLNY 301
Cdd:cd18566  114 FLTGQALLALLDLPFVLIFLGLIWYL--GGKLVLVPLVLLGLFVLVAILLgPILRRALK-ERSRADERRQNFLIETLTGI 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 302 ETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNfGQSAIFSVgLTAIMVLA--SQGIVAGTLTVGDLVMVNGLLF 379
Cdd:cd18566  191 HTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQ-TLGQLFSQ-VSMVAVVAfgALLVINGDLTVGALIACTMLSG 268


                 ....*..
gi 411147369 380 QLSLPLN 386
Cdd:cd18566  269 RVLQPLQ 275

PRK13549

xylose transporter ATP-binding subunit; Provisional

445-645

7.43e-06

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 7.43e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 445 GQKVLSGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQK-GSIYLAGQniqDVSLESLRRAV-------------- 509
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGK---PVKIRNPQQAIaqgiamvpedrkrd 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 510 GVVPQDAVLfHNTIYYNL----LYGNISASPEEVYAVAKLAGLHdaiLRMPHGyDTQVGerglKLSGGEKQRVAIARAIL 585
Cdd:PRK13549 351 GIVPVMGVG-KNITLAALdrftGGSRIDDAAELKTILESIQRLK---VKTASP-ELAIA----RLSGGNQQKAVLAKCLL 421

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 411147369 586 KDPPVILYDEATSSLDSITEETILGAMKDVVKHRTS-IFIAHRLSTVVD-ADEIIVLDQGKV 645
Cdd:PRK13549 422 LNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAiIVISSELPEVLGlSDRVLVMHEGKL 483

ABC_6TM_McjD_like

cd18556

Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ...

181-399

7.59e-06

Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.

Pssm-ID: 350000 Cd Length: 298 Bit Score: 48.40 E-value: 7.59e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 181 NSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTRGISFVLSALVFNLLP----IMFEVMLVSGVLYYKCGAQFAL 256
Cdd:cd18556   74 ELIISISSSYFRYLYEQPKTFFVKENSGDITQRLNQASNDLYTLVRNLSTNILPpllqLIIAIVVILSSGDYFVAALFLL 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 257 VTLgtlgTYTAFTVAVTRWRTRFRIEMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETAS---LKSTS 333
Cdd:cd18556  154 YAV----LFVINNTIFTKKIVSLRNDLMDAGRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEATLTNDRNSQkryWKLTF 229

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 334 TLAMLNFGQSAIFsVGLTAIMVLAsqGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQAL 399
Cdd:cd18556  230 KMLILNSLLNVIL-FGLSFFYSLY--GVVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSV 292

PRK11147

ABC transporter ATPase component; Reviewed

570-645

8.72e-06

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 8.72e-06

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 570 LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDvvkHRTSI-FIAHRLSTVVD-ADEIIVLDQGKV 645
Cdd:PRK11147 157 LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT---FQGSIiFISHDRSFIRNmATRIVDLDRGKL 231

ABC_RNaseL_inhibitor_domain1

cd03236

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

456-601

9.98e-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: 47.75 E-value: 9.98e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 456 VPA-GKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSI-----------YLAGQNIQDVsLESLRRA---VGVVPQDAVLFH 520
Cdd:cd03236   22 VPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNY-FTKLLEGdvkVIVKPQYVDLIP 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 521 NTIYynllyGNISASPEEVYAVAKLAGLHDAiLRMPHGYDTQVGErglkLSGGEKQRVAIARAILKDPPVILYDEATSSL 600
Cdd:cd03236  101 KAVK-----GKVGELLKKKDERGKLDELVDQ-LELRHVLDRNIDQ----LSGGELQRVAIAAALARDADFYFFDEPSSYL 170


                 .
gi 411147369 601 D 601
Cdd:cd03236  171 D 171

ABC_6TM_Sav1866_like

cd18554

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...

116-403

1.04e-05

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

Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 47.80 E-value: 1.04e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 116 IVVPFMFKYAVDSLNQmsGNMLNLSDAPNTVATMATAVLIGYGVSRAGAAFfneVRNAVFGKVAQNSIRRIAKNVFLHLH 195
Cdd:cd18554   16 LLLPLILKYIVDDVIQ--GSSLTLDEKVYKLFTIIGIMFFIFLILRPPVEY---YRQYFAQWIANKILYDIRKDLFDHLQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 196 NLDLGFHLSRQTGAL-SKAIDRGTRGISFVLSALVfNLLPIMFEVMLVSGVLyYKCGAQFALVTLGTLGTYtafTVAVTR 274
Cdd:cd18554   91 KLSLRYYANNRSGEIiSRVINDVEQTKDFITTGLM-NIWLDMITIIIAICIM-LVLNPKLTFVSLVIFPFY---ILAVKY 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 275 WRTRFRI---EMNKADNDAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTS----TLAMLNfgqsAIFS 347
Cdd:cd18554  166 FFGRLRKltkERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRwnakTFSAVN----TITD 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 348 VGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRETRQALIDMN 403
Cdd:cd18554  242 LAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMD 297

ABC_6TM_TmrB_like

cd18541

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...

113-389

3.25e-05

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: 46.25 E-value: 3.25e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLNQMSGNMLNLsdapntvaTMATAVLIGYGVSRAGAAFFneVRNAVFGkvaqnSIRRIAK---- 188
Cdd:cd18541   13 LLQLLIPRIIGRAIDALTAGTLTASQL--------LRYALLILLLALLIGIFRFL--WRYLIFG-----ASRRIEYdlrn 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 189 NVFLHLHNLDLGFHLSRQTGALskaIDRGTRGISFVLSALVFNLLPIMFEVMLVSGVLYykcgAQFAL---VTLGTLGTY 265
Cdd:cd18541   78 DLFAHLLTLSPSFYQKNRTGDL---MARATNDLNAVRMALGPGILYLVDALFLGVLVLV----MMFTIspkLTLIALLPL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 266 TAFTVAVTRW----RTRFRI------EMNkadndagNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKststL 335
Cdd:cd18541  151 PLLALLVYRLgkkiHKRFRKvqeafsDLS-------DRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLR----L 219

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 336 AMLN--FGQSAIFSVGLTAIMVLA--SQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLG 389
Cdd:cd18541  220 ARVDalFFPLIGLLIGLSFLIVLWygGRLVIRGTITLGDLVAFNSYLGMLIWPMMALG 277

ABC_RNaseL_inhibitor

cd03222

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...

568-641

3.71e-05

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

Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.87 E-value: 3.71e-05

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 411147369 568 LKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKH--RTSIFIAHRLsTVVD--ADEIIVLD 641
Cdd:cd03222   70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDL-AVLDylSDRIHVFE 146

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

456-628

4.25e-05

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.32 E-value: 4.25e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   456 VPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQdVSLESLRRAVGVVPQ-DAVlfhntiyYNLLYGNisa 534
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIL-TNISDVHQNMGYCPQfDAI-------DDLLTGR--- 2030

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369   535 spEEVYAVAKLAGLHDAILRMPHGYDTQvgERGLKL---------SGGEKQRVAIARAILKDPPVILYDEATSSLDSITE 605
Cdd:TIGR01257 2031 --EHLYLYARLRGVPAEEIEKVANWSIQ--SLGLSLyadrlagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106

                          170       180
                   ....*....|....*....|....
gi 411147369   606 ETILGAMKDVVKH-RTSIFIAHRL 628
Cdd:TIGR01257 2107 RMLWNTIVSIIREgRAVVLTSHSM 2130

ABC_6TM_T1SS_like

cd18555

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...

113-394

7.43e-05

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

Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 45.19 E-value: 7.43e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 113 AMNIVVPFMFKYAVDSLNqMSGNMLNLsdapNTVATMATAVLIGYGVsragaafFNEVRNAVFGKVaQNSI-RRIAKNVF 191
Cdd:cd18555   16 LLTLLIPILTQYVIDNVI-VPGNLNLL----NVLGIGILILFLLYGL-------FSFLRGYIIIKL-QTKLdKSLMSDFF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 192 LHLHNLDLGFHLSRQTGAL-----SKAIDRG---TRGISFVLSALvfnLLPIMFEVMLVSGVLYykcgaqfALVTLgTLG 263
Cdd:cd18555   83 EHLLKLPYSFFENRSSGDLlfranSNVYIRQilsNQVISLIIDLL---LLVIYLIYMLYYSPLL-------TLIVL-LLG 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 264 TYTAFTVAVTRWRTRFRIEMNKADN-DAGNAAIDSLLNYETVKYFNNERyeaQRYDGFLKTYET---ASLKSTSTLAMLN 339
Cdd:cd18555  152 LLIVLLLLLTRKKIKKLNQEEIVAQtKVQSYLTETLYGIETIKSLGSEK---NIYKKWENLFKKqlkAFKKKERLSNILN 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 411147369 340 FGQSAIFSVGLTAIMVLASQGIVAGTLTVGDLVMVNGLLFQLSLPLNFLGTVYRE 394
Cdd:cd18555  229 SISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQ 283

ABC_6TM_bac_exporter_ABCB8_10_like

cd18575

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...

289-372

1.12e-04

Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 44.78 E-value: 1.12e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 289 DAGNAAIDSLLNYETVKYFNNERYEAQRYDGFLKTYETASLKSTSTLAMLNFgqSAIFSV--GLTAIMVLASQGIVAGTL 366
Cdd:cd18575  173 DLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTA--LVIFLVfgAIVFVLWLGAHDVLAGRM 250


                 ....*.
gi 411147369 367 TVGDLV 372
Cdd:cd18575  251 SAGELS 256

ABC_Class2

cd03227

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...

457-638

1.21e-04

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

Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 1.21e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 457 PAGKKVAIVGGSGSGKSTIVR-----LLFRFYEPQKGSIYLAGQNIQDVSLEslrrAVGVVPQdavlfhntiyynllygn 531
Cdd:cd03227   19 GEGSLTIITGPNGSGKSTILDaiglaLGGAQSATRRRSGVKAGCIVAAVSAE----LIFTRLQ----------------- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 532 isaspeevyavaklaglhdailrmphgydtqvgerglkLSGGEKQRVAIARAI----LKDPPVILYDEATSSLDSITEET 607
Cdd:cd03227   78 --------------------------------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQA 119

                        170       180       190
                 ....*....|....*....|....*....|..
gi 411147369 608 ILGAMKD-VVKHRTSIFIAHRLSTVVDADEII 638
Cdd:cd03227  120 LAEAILEhLVKGAQVIVITHLPELAELADKLI 151

ABC_6TM_ABCB9_like

cd18784

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...

220-392

1.25e-04

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

Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 44.61 E-value: 1.25e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 220 GISFVLSALVFNLLPIMFEVMLVSGVlYYKcgaqfalvtlgtlgtytaftvavtrwrtRFRIEMNKADNDAGNAAIDSLL 299
Cdd:cd18784  133 KLSWQLSLVTLIGLPLIAIVSKVYGD-YYK----------------------------KLSKAVQDSLAKANEVAEETIS 183

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 300 NYETVKYFNNERYEAQRYDGFLKtyETASLKSTSTLAMLNF-GQSAIFSVGLTAIMvLASQG--IVAGTLTVGDLVMVng 376
Cdd:cd18784  184 SIRTVRSFANEDGEANRYSEKLK--DTYKLKIKEALAYGGYvWSNELTELALTVST-LYYGGhlVITGQISGGNLISF-- 258

                        170
                 ....*....|....*...
gi 411147369 377 LLFQLSL--PLNFLGTVY 392
Cdd:cd18784  259 ILYQLELgsCLESVGSVY 276

ABC_6TM_TAP2

cd18590

Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...

155-392

1.29e-04

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

Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 44.64 E-value: 1.29e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 155 IGY-GVSRAGAAFFNEVRNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDRGTrgisfvlsALVFNLL 233
Cdd:cd18590   39 IGLmCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDT--------TLMSRSV 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 234 PIMFEVMLVS-----GVLYYKCGA--QFALVTL-GTLGTYTAFTVAVTRWRtRFRIEMNKADNDAGNAAIDSLLNYETVK 305
Cdd:cd18590  111 ALNANVLLRSlvktlGMLGFMLSLswQLTLLTLiEMPLTAIAQKVYNTYHQ-KLSQAVQDSIAKAGELAREAVSSIRTVR 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 306 YFNNERYEAQRYDGFLK-TYETASLKSTSTLAMLNFGQsaIFSVGLTAIMV-LASQGIVAGTLTVGDLVMVngLLFQLSL 383
Cdd:cd18590  190 SFKAEEEEACRYSEALErTYNLKDRRDTVRAVYLLVRR--VLQLGVQVLMLyCGRQLIQSGHLTTGSLVSF--ILYQKNL 265


                 ....*....
gi 411147369 384 PLNFLGTVY 392
Cdd:cd18590  266 GSYVRTLVY 274

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

433-614

1.37e-04

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 1.37e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 433 VAFDNVHFEYieGQKVL-SGISFEVPAGKKVAIVGGSGSGKSTIVRLLFRFYEPQKGSIYLaGQNIQdvsleslrraVGV 511
Cdd:PRK11819 325 IEAENLSKSF--GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVK----------LAY 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 512 VPQ--DAVLFHNTIYynllygnisaspEEVyavaklAGLHDAIL----RMP----------HGYDTQ--VGErglkLSGG 573
Cdd:PRK11819 392 VDQsrDALDPNKTVW------------EEI------SGGLDIIKvgnrEIPsrayvgrfnfKGGDQQkkVGV----LSGG 449

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 411147369 574 EKQRVAIARAILKDPPVILYDEATSSLDSiteETiLGAMKD 614
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDV---ET-LRALEE 486

PRK13541

cytochrome c biogenesis protein CcmA; Provisional

464-601

1.49e-04

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.32 E-value: 1.49e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 464 IVGGSGSGKSTIVRLLFRFYEPQKGSIYLAGQNIQDVSleslrravgvVPQDAVLFHN-------TIYYNL-LYGNISAS 535
Cdd:PRK13541  31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----------KPYCTYIGHNlglklemTVFENLkFWSEIYNS 100

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 411147369 536 PEEVYAVAKLAGLHDAIlrmphgydtqvGERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLD 601
Cdd:PRK13541 101 AETLYAAIHYFKLHDLL-----------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155

40850658_otr

NF000106

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

564-649

4.01e-04

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.19 E-value: 4.01e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 564 GERGLKLSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVD--ADEIIVLD 641
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqlAHELTVID 218


                 ....*...
gi 411147369 642 QGKVAERG 649
Cdd:NF000106 219 RGRVIADG 226

PLN03140

ABC transporter G family member; Provisional

463-679

9.62e-04

ABC transporter G family member; Provisional

Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 9.62e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  463 AIVGGSGSGKSTIVRLLfrfyEPQKGSIYLAGqniqDVSL-------ESLRRAVGVVPQDAVlfHN---TIYYNLLYGNI 532
Cdd:PLN03140  910 ALMGVSGAGKTTLMDVL----AGRKTGGYIEG----DIRIsgfpkkqETFARISGYCEQNDI--HSpqvTVRESLIYSAF 979

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  533 SASPEEVYAVAK------------LAGLHDAILRMPhgydtqvGERGlkLSGGEKQRVAIARAILKDPPVILYDEATSSL 600
Cdd:PLN03140  980 LRLPKEVSKEEKmmfvdevmelveLDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  601 DSITEETILGAMKDVVKH-RTSIFIAHRLST-VVDA-DEIIVLDQ-GKVAERGThhgLLANPHSI--YSEMWHtQSSRVQ 674
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVDTgRTVVCTIHQPSIdIFEAfDELLLMKRgGQVIYSGP---LGRNSHKIieYFEAIP-GVPKIK 1126


                  ....*
gi 411147369  675 NHDNP 679
Cdd:PLN03140 1127 EKYNP 1131

PLN03140

ABC transporter G family member; Provisional

560-656

1.04e-03

ABC transporter G family member; Provisional

Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 1.04e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369  560 DTQVGERGLK-LSGGEKQRVAIARAILKDPPVILYDEATSSLDSITEETILGAMKDVVKHRTSIFIAHRLSTVVDA---- 634
Cdd:PLN03140  326 DTIVGDEMIRgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETfdlf 405

                          90       100
                  ....*....|....*....|..
gi 411147369  635 DEIIVLDQGKVAERGTHHGLLA 656
Cdd:PLN03140  406 DDIILLSEGQIVYQGPRDHILE 427

ABC_6TM_YwjA_like

cd18549

Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...

112-372

1.49e-03

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

Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 41.28 E-value: 1.49e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 112 GAMNIVVPFMFKYAVDSLNQmSGNMlnlsdapNTVATMATAVLIGYGVsRAGAAFFNEVRNAVFGKVAQNSIRRiakNVF 191
Cdd:cd18549   15 AALDLVFPLIVRYIIDDLLP-SKNL-------RLILIIGAILLALYIL-RTLLNYFVTYWGHVMGARIETDMRR---DLF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 192 LHLHNLDLGFHLSRQTGALSkaidrgTRGIS--FVLSALVFNLLpimfEVMLVSGVLYykCGA---------QFALVTLG 260
Cdd:cd18549   83 EHLQKLSFSFFDNNKTGQLM------SRITNdlFDISELAHHGP----EDLFISIITI--IGSfiilltinvPLTLIVFA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 261 TLGTYTAFTVAVT-RWRTRFRieMNKADNDAGNAAI-DSLLNYETVKYFNNERYEAQRYDGFLKTYETAslKSTSTLAML 338
Cdd:cd18549  151 LLPLMIIFTIYFNkKMKKAFR--RVREKIGEINAQLeDSLSGIRVVKAFANEEYEIEKFDEGNDRFLES--KKKAYKAMA 226

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 411147369 339 NFGQSAIFSVGLTAIMVLASQG--IVAGTLTVGDLV 372
Cdd:cd18549  227 YFFSGMNFFTNLLNLVVLVAGGyfIIKGEITLGDLV 262

ABC_6TM_PrtD_LapB_HlyB_like

cd18782

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...

150-382

5.88e-03

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

Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 39.50 E-value: 5.88e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 150 ATAVLIGYGVSRAGAAFFNEV----RNAVFGKVAQNSIRRIAKNVFLHLHNLDLGFHLSRQTGALSKAIDR--------- 216
Cdd:cd18782   37 DLATLYVIGVVMLVAALLEAVltalRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFDKRPVGELSTRISEldtirgflt 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 217 GTRGISFVLSALVFNLLPIMFevmLVSGVLyykcgaqfALVTLGTLGTYTAFTVAVTRwRTRFRIEMNKADNDAGNAA-I 295
Cdd:cd18782  117 GTALTTLLDVLFSVIYIAVLF---SYSPLL--------TLVVLATVPLQLLLTFLFGP-ILRRQIRRRAEASAKTQSYlV 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 411147369 296 DSLLNYETVKYFNNE---RYEAQ-RYDGFL-KTYETASLKSTS--TLAMLNFGQSAIFsVGLTAIMVLAsqgivaGTLTV 368
Cdd:cd18782  185 ESLTGIQTVKAQNAElkaRWRWQnRYARSLgEGFKLTVLGTTSgsLSQFLNKLSSLLV-LWVGAYLVLR------GELTL 257

                        250       260
                 ....*....|....*....|.
gi 411147369 369 GDLV-------MVNGLLFQLS 382
Cdd:cd18782  258 GQLIafrilsgYVTGPILRLS 278

Blast search parameters

Data Source:	Precalculated data, version = cdd.v.3.21
Preset Options:	Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01