NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1277238834|gb|PIS31804|]
View 

ABC transporter ATP-binding protein [Candidatus Saganbacteria bacterium CG08_land_8_20_14_0_20_45_16]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11438555)

ABC transporter ATP-binding protein ABC transporter ATP-binding protein containing both ATPase and permease components of an ABC-type transport system

CATH:  3.40.50.300
EC:  7.-.-.-
Gene Ontology:  GO:0055052|GO:0140359|GO:0042626|GO:0005524|GO:0016887
PubMed:  19234479|26517916|10529352|24638992|25750732
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-571 0e+00

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


:

Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 707.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   1 MKLYARLLKFIKPYYSQIIGGTICTALVTSTTLLIAPLVGYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLS 79
Cdd:COG1132     6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  80 YFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSL 159
Cdd:COG1132    86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 160 LTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILA 239
Cdd:COG1132   166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 240 TQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLDVKPSIA 319
Cdd:COG1132   246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 320 DLPGAKKLPRINGEINFENISFAYENEE-VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIK 398
Cdd:COG1132   326 DPPGAVPLPPVRGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 399 TAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRV 478
Cdd:COG1132   406 DLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRI 485

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 479 AIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKD 558
Cdd:COG1132   486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARG 565

                         570
                  ....*....|...
gi 1277238834 559 GLYKYLYAIQFNN 571
Cdd:COG1132   566 GLYARLYRLQFGE 578
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-571 0e+00

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 707.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   1 MKLYARLLKFIKPYYSQIIGGTICTALVTSTTLLIAPLVGYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLS 79
Cdd:COG1132     6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  80 YFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSL 159
Cdd:COG1132    86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 160 LTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILA 239
Cdd:COG1132   166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 240 TQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLDVKPSIA 319
Cdd:COG1132   246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 320 DLPGAKKLPRINGEINFENISFAYENEE-VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIK 398
Cdd:COG1132   326 DPPGAVPLPPVRGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 399 TAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRV 478
Cdd:COG1132   406 DLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRI 485

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 479 AIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKD 558
Cdd:COG1132   486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARG 565

                         570
                  ....*....|...
gi 1277238834 559 GLYKYLYAIQFNN 571
Cdd:COG1132   566 GLYARLYRLQFGE 578
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 3-569 1.92e-167

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: 487.69  E-value: 1.92e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   3 LYARLLKFIKPYYSQIIGGTICTALVTSTTLLIAPLVGYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYF 81
Cdd:TIGR02203   1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  82 VAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLT 161
Cdd:TIGR02203  81 VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 162 LVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQ 241
Cdd:TIGR02203 161 VVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSIS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 242 NPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLDVKPSIADl 321
Cdd:TIGR02203 241 SPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDT- 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 322 pGAKKLPRINGEINFENISFAY--ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKT 399
Cdd:TIGR02203 320 -GTRAIERARGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 400 AKLESLRKQIAVVPQEIALFSGTIKDNIAYGRP-NASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRV 478
Cdd:TIGR02203 399 YTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRL 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 479 AIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKD 558
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARN 558

                         570
                  ....*....|.
gi 1277238834 559 GLYKYLYAIQF 569
Cdd:TIGR02203 559 GLYAQLHNMQF 569
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
1-571 1.01e-133

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 401.70  E-value: 1.01e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   1 MKLYARLLKFIKPYYSQIIGGTIctALV---TSTTLLIA---PLVGYIFQLIEdkNMFLLNLsALGMIGLFVLKGLFQYG 74
Cdd:PRK11176   10 WQTFRRLWPTIAPFKAGLIVAGV--ALIlnaASDTFMLSllkPLLDDGFGKAD--RSVLKWM-PLVVIGLMILRGITSFI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  75 QEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLN 154
Cdd:PRK11176   85 SSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYS 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 155 WQLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRA 234
Cdd:PRK11176  165 WQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKM 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 235 VQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSlPQLIS--FATALGIMTdPGNTLSKAYSIIQQGMASTKRIFEVL 312
Cdd:PRK11176  245 VSASSISDPIIQLIASLALAFVLYAASFPSVMDTLT-AGTITvvFSSMIALMR-PLKSLTNVNAQFQRGMAACQTLFAIL 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 313 DVKPSIADlpGAKKLPRINGEINFENISFAYENEEV--LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRI 390
Cdd:PRK11176  323 DLEQEKDE--GKRVIERAKGDIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 391 LVDGQDIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNA-SEAEIIEAAKFANIHDFINSLPKKYETQVAERGSR 469
Cdd:PRK11176  401 LLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVL 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 470 LSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIG 549
Cdd:PRK11176  481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERG 560

                         570       580
                  ....*....|....*....|..
gi 1277238834 550 SHQELLQKDGLYKYLYAIQFNN 571
Cdd:PRK11176  561 THAELLAQNGVYAQLHKMQFGQ 582
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 334-565 8.17e-127

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: 371.18  E-value: 8.17e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAV 411
Cdd:cd03251     1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRIL 491
Cdd:cd03251    81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 492 ILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDGLYKYLY 565
Cdd:cd03251   161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 349-498 1.69e-47

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: 162.82  E-value: 1.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEIALFSG-TIKDNI 427
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 428 AYGRP------NASEAEIIEAAKFANIHDFINSLpkkyetqVAERGSRLSGGERQRVAIARAILRDPRILILDEATS 498
Cdd:pfam00005  81 RLGLLlkglskREKDARAEEALEKLGLGDLADRP-------VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
342-540 2.10e-26

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 106.16  E-value: 2.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 342 AYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGqdiktakleslRKQIAVVPQEIAL--- 418
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpds 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 419 FSGTIKDNIAYG---------RPNASEAEIIEAAKFA-NIHDFINSlpkkyetQVAErgsrLSGGERQRVAIARAILRDP 488
Cdd:NF040873   70 LPLTVRDLVAMGrwarrglwrRLTRDDRAAVDDALERvGLADLAGR-------QLGE----LSGGQRQRALLAQGLAQEA 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 489 RILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLYAVEHANRIVVI 540
Cdd:NF040873  139 DLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
GguA NF040905
sugar ABC transporter ATP-binding protein;
349-540 1.72e-18

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 88.69  E-value: 1.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYdPT---SGRILVDGQ-----DIKtaklESLRKQIAVVPQEIALFS 420
Cdd:NF040905   17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcrfkDIR----DSEALGIVIIHQELALIP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 421 G-TIKDNIAYGRPNAS------EAEIIEAAKfanihdfinsLPKKY------ETQVAERGSrlsgGERQRVAIARAILRD 487
Cdd:NF040905   92 YlSIAENIFLGNERAKrgvidwNETNRRARE----------LLAKVgldespDTLVTDIGV----GKQQLVEIAKALSKD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 488 PRILILDEATSSL-DAETESLIRDALERLMKGRTTFIIAHRLYAVEH-ANRIVVI 540
Cdd:NF040905  158 VKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVL 212
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
351-526 3.28e-10

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 63.22  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 351 NINLKVKPGEIIALVGRTGAGKST----LTSLLlrfyDPTSGRIL-----VDGQDIKTakleslRKQIAVVPQEIALFSG 421
Cdd:NF033858  284 HVSFRIRRGEIFGFLGSNGCGKSTtmkmLTGLL----PASEGEAWlfgqpVDAGDIAT------RRRVGYMSQAFSLYGE 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 422 -TIKDNIA-----YGRPNASEAEIIE--AAKFaNIHDFINSLPkkyetqvaergSRLSGGERQRVAIARAILRDPRILIL 493
Cdd:NF033858  354 lTVRQNLElharlFHLPAAEIAARVAemLERF-DLADVADALP-----------DSLPLGIRQRLSLAVAVIHKPELLIL 421

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1277238834 494 DEATSSLD--AetesliRDALERLM------KGRTTFIIAH 526
Cdd:NF033858  422 DEPTSGVDpvA------RDMFWRLLielsreDGVTIFISTH 456
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 358-519 6.60e-10

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: 57.77  E-value: 6.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  358 PGEIIALVGRTGAGKSTLTSLLLRFYDPTSGR-ILVDGQDIKTAKLESLRKQIavvpqeialfsgtikdniaygrpnase 436
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLII--------------------------- 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  437 aeiieaakfanihdfinslpkkyetqVAERGSRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLM 516
Cdd:smart00382  54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107


                   ...
gi 1277238834  517 KGR 519
Cdd:smart00382 108 LLL 110
GguA NF040905
sugar ABC transporter ATP-binding protein;
348-501 1.97e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 53.64  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLT-SLLLRFYDP-TSGRILVDGQDIKTAKL-ESLRKQIAVVPQ---EIAL-FS 420
Cdd:NF040905  275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKEVDVSTVsDAIDAGLAYVTEdrkGYGLnLI 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 421 GTIKDNI-AYGRPNASEAEII---EAAKFANihDFINSLPKKYETqVAERGSRLSGGERQRVAIARAILRDPRILILDEA 496
Cdd:NF040905  355 DDIKRNItLANLGKVSRRGVIdenEEIKVAE--EYRKKMNIKTPS-VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEP 431


                  ....*
gi 1277238834 497 TSSLD 501
Cdd:NF040905  432 TRGID 436
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
461-559 3.40e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 49.35  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 461 TQVAERGS-RLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK-GRTTFIIAHRLYAVEH-ANRI 537
Cdd:NF000106  135 TEAAGRAAaKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQlAHEL 214

                          90       100
                  ....*....|....*....|..
gi 1277238834 538 VVIDNKQILEIGSHQELLQKDG 559
Cdd:NF000106  215 TVIDRGRVIADGKVDELKTKVG 236
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
337-559 3.98e-06

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 49.74  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLL-----LRfydptSGRILVDGQDIKTAK-LESLRKQIA 410
Cdd:NF033858    5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIagarkIQ-----QGRVEVLGGDMADARhRRAVCPRIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 411 VVPQeialfsG---------TIKDNIAY-GR---PNASE--AEIIEAAKFANIHDFinslpkkyetqvAER-GSRLSGGE 474
Cdd:NF033858   80 YMPQ------GlgknlyptlSVFENLDFfGRlfgQDAAErrRRIDELLRATGLAPF------------ADRpAGKLSGGM 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 475 RQRVAIARAILRDPRILILDEATSSLDaeteSLIR----DALERLMKGRT--TFIIAhRLYaVEHANR---IVVIDNKQI 545
Cdd:NF033858  142 KQKLGLCCALIHDPDLLILDEPTTGVD----PLSRrqfwELIDRIRAERPgmSVLVA-TAY-MEEAERfdwLVAMDAGRV 215

                         250
                  ....*....|....
gi 1277238834 546 LEIGSHQELLQKDG 559
Cdd:NF033858  216 LATGTPAELLARTG 229
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-571 0e+00

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 707.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   1 MKLYARLLKFIKPYYSQIIGGTICTALVTSTTLLIAPLVGYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLS 79
Cdd:COG1132     6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIdALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  80 YFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSL 159
Cdd:COG1132    86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 160 LTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILA 239
Cdd:COG1132   166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 240 TQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLDVKPSIA 319
Cdd:COG1132   246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 320 DLPGAKKLPRINGEINFENISFAYENEE-VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIK 398
Cdd:COG1132   326 DPPGAVPLPPVRGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIR 405

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 399 TAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRV 478
Cdd:COG1132   406 DLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRI 485

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 479 AIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKD 558
Cdd:COG1132   486 AIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARG 565

                         570
                  ....*....|...
gi 1277238834 559 GLYKYLYAIQFNN 571
Cdd:COG1132   566 GLYARLYRLQFGE 578
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 6-568 0e+00

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: 537.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   6 RLLKFIKPY---YSQIIGGTICTALVTsttlLIAPLvgyIFQLIEDK-----NMFLLNLSALGMIGLFVLKGLFQYGQEY 77
Cdd:COG2274   146 WFLRLLRRYrrlLLQVLLASLLINLLA----LATPL---FTQVVIDRvlpnqDLSTLWVLAIGLLLALLFEGLLRLLRSY 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  78 LSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVmNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQL 157
Cdd:COG2274   219 LLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPL 297

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 158 SLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQI 237
Cdd:COG2274   298 ALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRL 377

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 238 LATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLDVKPS 317
Cdd:COG2274   378 SNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPE 457

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 318 IADLPGAKKLPRINGEINFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQ 395
Cdd:COG2274   458 REEGRSKLSLPRLKGDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI 537

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 396 DIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGER 475
Cdd:COG2274   538 DLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQR 617

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 476 QRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELL 555
Cdd:COG2274   618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL 697

                         570
                  ....*....|...
gi 1277238834 556 QKDGLYKYLYAIQ 568
Cdd:COG2274   698 ARKGLYAELVQQQ 710
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 3-569 1.92e-167

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: 487.69  E-value: 1.92e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   3 LYARLLKFIKPYYSQIIGGTICTALVTSTTLLIAPLVGYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYF 81
Cdd:TIGR02203   1 TFRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLdDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  82 VAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLT 161
Cdd:TIGR02203  81 VSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 162 LVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQ 241
Cdd:TIGR02203 161 VVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSIS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 242 NPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLDVKPSIADl 321
Cdd:TIGR02203 241 SPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDT- 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 322 pGAKKLPRINGEINFENISFAY--ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKT 399
Cdd:TIGR02203 320 -GTRAIERARGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 400 AKLESLRKQIAVVPQEIALFSGTIKDNIAYGRP-NASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRV 478
Cdd:TIGR02203 399 YTLASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRL 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 479 AIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKD 558
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARN 558

                         570
                  ....*....|.
gi 1277238834 559 GLYKYLYAIQF 569
Cdd:TIGR02203 559 GLYAQLHNMQF 569
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
 5-569 1.57e-163

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: 478.04  E-value: 1.57e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   5 ARLLKFIKPYYSQIIGGTICTALVTSTTLLiaplVGYIFQLIEDK-----NMFLLNLSALGMIGLFVLKGLFQYGQEYLS 79
Cdd:TIGR02204   7 AALWPFVRPYRGRVLAALVALLITAAATLS----LPYAVRLMIDHgfskdSSGLLNRYFAFLLVVALVLALGTAARFYLV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  80 YFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSL 159
Cdd:TIGR02204  83 TWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 160 LTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILA 239
Cdd:TIGR02204 163 LVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRA 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 240 TQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLDVKPSIA 319
Cdd:TIGR02204 243 LLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIK 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 320 DLPGAKKLP-RINGEINFENISFAYE---NEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQ 395
Cdd:TIGR02204 323 APAHPKTLPvPLRGEIEFEQVNFAYParpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGV 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 396 DIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGER 475
Cdd:TIGR02204 403 DLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQR 482

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 476 QRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELL 555
Cdd:TIGR02204 483 QRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELI 562

                         570
                  ....*....|....
gi 1277238834 556 QKDGLYKYLYAIQF 569
Cdd:TIGR02204 563 AKGGLYARLARLQF 576
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 3-568 1.28e-152

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: 451.20  E-value: 1.28e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   3 LYARLLKFIKPYYSQIIGGTICTALVTSTTLLIAPLVGYIFQLIEDKN--MFLLNLSALGMI----GLFVLKGLFQYGQE 76
Cdd:COG5265    20 LRLLLLLLLPPYLRRRRRALAALLLLLLAAALALVVPPLLKDAIDALLsgAAALLVVPVGLLlaygLLRLLSVLFGELRD 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  77 YLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELvSRVM----NDIQTL-QATLFTGFVTLIPhslllLGLMGYIF 151
Cdd:COG5265   100 ALFARVTQRAVRRLALEVFRHLHALSLRFHLERQTGGL-SRDIergtKGIEFLlRFLLFNILPTLLE-----IALVAGIL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 152 WLN--WQLSLLTLVALPL------IVQVIRI-FAKEIREISEGVQQKAADitSHLQ-ETisqvktVKSFAMEKEELAKFK 221
Cdd:COG5265   174 LVKydWWFALITLVTVVLyiaftvVVTEWRTkFRREMNEADSEANTRAVD--SLLNyET------VKYFGNEAREARRYD 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 222 GKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLIsFATALGI-MTDPGNTLSKAYSIIQQ 300
Cdd:COG5265   246 EALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFV-LVNAYLIqLYIPLNFLGFVYREIRQ 324

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 301 GMASTKRIFEVLDVKPSIADLPGAKKLPRINGEINFENISFAYENE-EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLL 379
Cdd:COG5265   325 ALADMERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPErPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL 404

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 380 LRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKY 459
Cdd:COG5265   405 FRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGY 484

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 460 ETQVAERGSRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVV 539
Cdd:COG5265   485 DTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILV 564

                         570       580
                  ....*....|....*....|....*....
gi 1277238834 540 IDNKQILEIGSHQELLQKDGLYKYLYAIQ 568
Cdd:COG5265   565 LEAGRIVERGTHAELLAQGGLYAQMWARQ 593
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 6-559 4.48e-136

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: 407.22  E-value: 4.48e-136
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   6 RLLKFIKPYYSQIIGGTICTALVTSTTLLIAPLVGYIFQ--LIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVA 83
Cdd:COG4988     7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAglIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFRAA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  84 QRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQaTLFTGFVT------LIPhsLLLLGlmgYIFWLNWQL 157
Cdd:COG4988    87 ARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLTEGVEALD-GYFARYLPqlflaaLVP--LLILV---AVFPLDWLS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 158 SLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMR--AV 235
Cdd:COG4988   161 GLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRKRTMKvlRV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 236 QILATQnpVIALLQTIAVVGIVWFGGREIISGSLSLPQLIsfaTALGIMTD---PGNTLSKAYSIIQQGMASTKRIFEVL 312
Cdd:COG4988   241 AFLSSA--VLEFFASLSIALVAVYIGFRLLGGSLTLFAAL---FVLLLAPEfflPLRDLGSFYHARANGIAAAEKIFALL 315

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 313 DvKPSIADLPGAKKLPRING-EINFENISFAYENE-EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRI 390
Cdd:COG4988   316 D-APEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGrPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI 394

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 391 LVDGQDIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRL 470
Cdd:COG4988   395 LINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGL 474

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 471 SGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGS 550
Cdd:COG4988   475 SGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGT 554


                  ....*....
gi 1277238834 551 HQELLQKDG 559
Cdd:COG4988   555 HEELLAKNG 563
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
1-571 1.01e-133

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 401.70  E-value: 1.01e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   1 MKLYARLLKFIKPYYSQIIGGTIctALV---TSTTLLIA---PLVGYIFQLIEdkNMFLLNLsALGMIGLFVLKGLFQYG 74
Cdd:PRK11176   10 WQTFRRLWPTIAPFKAGLIVAGV--ALIlnaASDTFMLSllkPLLDDGFGKAD--RSVLKWM-PLVVIGLMILRGITSFI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  75 QEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLN 154
Cdd:PRK11176   85 SSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYS 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 155 WQLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRA 234
Cdd:PRK11176  165 WQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKM 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 235 VQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSlPQLIS--FATALGIMTdPGNTLSKAYSIIQQGMASTKRIFEVL 312
Cdd:PRK11176  245 VSASSISDPIIQLIASLALAFVLYAASFPSVMDTLT-AGTITvvFSSMIALMR-PLKSLTNVNAQFQRGMAACQTLFAIL 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 313 DVKPSIADlpGAKKLPRINGEINFENISFAYENEEV--LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRI 390
Cdd:PRK11176  323 DLEQEKDE--GKRVIERAKGDIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEI 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 391 LVDGQDIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNA-SEAEIIEAAKFANIHDFINSLPKKYETQVAERGSR 469
Cdd:PRK11176  401 LLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVL 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 470 LSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIG 549
Cdd:PRK11176  481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERG 560

                         570       580
                  ....*....|....*....|..
gi 1277238834 550 SHQELLQKDGLYKYLYAIQFNN 571
Cdd:PRK11176  561 THAELLAQNGVYAQLHKMQFGQ 582
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 6-564 2.86e-130

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 397.17  E-value: 2.86e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   6 RLLKFIKPYYSQIIGGTICTALVTSTTLLIAPLVGYIFQ-LIEDK-------NMFLLN-LSALGMIGLFVLKGLFQYGQE 76
Cdd:TIGR00958 151 RLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDtLGGDKgppalasAIFFMClLSIASSVSAGLRGGSFNYTMA 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  77 ylsyfvaqRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQ 156
Cdd:TIGR00958 231 --------RINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPR 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 157 LSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQ 236
Cdd:TIGR00958 303 LTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKAL 382

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 237 ILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLDVKP 316
Cdd:TIGR00958 383 AYAGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKP 462

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 317 SIaDLPGAKKLPRINGEINFENISFAYENE---EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVD 393
Cdd:TIGR00958 463 NI-PLTGTLAPLNLEGLIEFQDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLD 541

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 394 GQDIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGG 473
Cdd:TIGR00958 542 GVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGG 621

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 474 ERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERlmKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQE 553
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQ 699

                         570
                  ....*....|.
gi 1277238834 554 LLQKDGLYKYL 564
Cdd:TIGR00958 700 LMEDQGCYKHL 710
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
1-569 1.43e-127

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 386.24  E-value: 1.43e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   1 MKLYARLLKFIKPYysQIIGGTICTALVTSTTLLIAP--LVGYIFQLIEDKNmfllnlSALGMIGLFVLKGLFQYGQEYL 78
Cdd:PRK13657    4 FRLYARVLQYLGAE--KRLGILLAVANVLLAAATFAEpiLFGRIIDAISGKG------DIFPLLAAWAGFGLFNIIAGVL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  79 SYFVAQRIIVDLRNQV----YEHLQDLSLDFYAKWNTGELVSRVMNDIQTLqATLFTGF-----VTLIphSLLLLGLMGy 149
Cdd:PRK13657   76 VARHADRLAHRRRLAVlteyFERIIQLPLAWHSQRGSGRALHTLLRGTDAL-FGLWLEFmrehlATLV--ALVVLLPLA- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 150 iFWLNWQLSLLtLVALPLIVQVIRIFAkeIREISEG---VQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEK 226
Cdd:PRK13657  152 -LFMNWRLSLV-LVVLGIVYTLITTLV--MRKTKDGqaaVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADN 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 227 sfdismravqILATQNPVI---ALLQ-------TIAVVGIVWFGGREIISGSLSLPQLI---SFATALGIMTDpgNTLSK 293
Cdd:PRK13657  228 ----------LLAAQMPVLswwALASvlnraasTITMLAILVLGAALVQKGQLRVGEVVafvGFATLLIGRLD--QVVAF 295

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 294 AYSIIQQGmASTKRIFEVLDVKPSIADLPGAKKLPRINGEINFENISFAYENE-EVLQNINLKVKPGEIIALVGRTGAGK 372
Cdd:PRK13657  296 INQVFMAA-PKLEEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGK 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 373 STLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFI 452
Cdd:PRK13657  375 STLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFI 454

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 453 NSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVE 532
Cdd:PRK13657  455 ERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVR 534

                         570       580       590
                  ....*....|....*....|....*....|....*..
gi 1277238834 533 HANRIVVIDNKQILEIGSHQELLQKDGLYKYLYAIQF 569
Cdd:PRK13657  535 NADRILVFDNGRVVESGSFDELVARGGRFAALLRAQG 571
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 5-567 3.13e-127

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: 384.50  E-value: 3.13e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   5 ARLLKFIKPYYSQIIGGTI--CTALVTSTTLL-----------IAPLVgyifqliedknmFLLNLSALGMIGLFVLKGLF 71
Cdd:COG4987     4 LRLLRLLRPHRGRLLLGVLlgLLTLLAGIGLLalsgwliaaaaLAPPI------------LNLFVPIVGVRAFAIGRTVF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  72 QYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIF 151
Cdd:COG4987    72 RYLERLVSHDATLRLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 152 WLNWQLSLLTLVALPLIVQVI-RIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDI 230
Cdd:COG4987   152 FFSPALALVLALGLLLAGLLLpLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 231 SMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFA-TALGiMTDPGNTLSKAYSIIQQGMASTKRIF 309
Cdd:COG4987   232 QRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVlAALA-LFEALAPLPAAAQHLGRVRAAARRLN 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 310 EVLDVKPSIADLPGAKKLPRiNGEINFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTS 387
Cdd:COG4987   311 ELLDAPPAVTEPAEPAPAPG-GPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQS 389

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 388 GRILVDGQDIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERG 467
Cdd:COG4987   390 GSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGG 469

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 468 SRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILE 547
Cdd:COG4987   470 RRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVE 549

                         570       580
                  ....*....|....*....|
gi 1277238834 548 IGSHQELLQKDGLYKYLYAI 567
Cdd:COG4987   550 QGTHEELLAQNGRYRQLYQR 569
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 334-565 8.17e-127

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: 371.18  E-value: 8.17e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAV 411
Cdd:cd03251     1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRIL 491
Cdd:cd03251    81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 492 ILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDGLYKYLY 565
Cdd:cd03251   161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 15-568 2.58e-126

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


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 386.41  E-value: 2.58e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  15 YSQIIGGTICTALVTSTTLLIAPLvgyIFQLIEDK-----NMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVD 89
Cdd:TIGR01846 137 YRKQFREVLLISLALQLFALVTPL---LFQVVIDKvlvhrGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVE 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  90 LRNQVYEHLQDLSLDFYAKWNTGELVSRVmNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIV 169
Cdd:TIGR01846 214 LGARLYRHLLGLPLGYFESRRVGDTVARV-RELEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYA 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 170 QVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQ 249
Cdd:TIGR01846 293 LLSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQ 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 250 TIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLDvKPSIADLPGAKKLPR 329
Cdd:TIGR01846 373 KLTFAILLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPRSAGLAALPE 451

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 330 INGEINFENISFAYENE--EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRK 407
Cdd:TIGR01846 452 LRGAITFENIRFRYAPDspEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRR 531

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 408 QIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRD 487
Cdd:TIGR01846 532 QMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGN 611

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 488 PRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDGLYKYLYAI 567
Cdd:TIGR01846 612 PRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQ 691


                  .
gi 1277238834 568 Q 568
Cdd:TIGR01846 692 Q 692
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 334-568 1.71e-121

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: 358.01  E-value: 1.71e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAY---ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIA 410
Cdd:cd03249     1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 411 VVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRI 490
Cdd:cd03249    81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 491 LILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDGLYKYLYAIQ 568
Cdd:cd03249   161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 334-568 4.67e-118

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: 349.22  E-value: 4.67e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENE-EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVV 412
Cdd:cd03253     1 IEFENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 PQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRILI 492
Cdd:cd03253    81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 493 LDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDGLYKYLYAIQ 568
Cdd:cd03253   161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 332-559 2.95e-112

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: 333.81  E-value: 2.95e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 332 GEINFENISFAYENEE-VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIA 410
Cdd:cd03254     1 GEIEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 411 VVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRI 490
Cdd:cd03254    81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 491 LILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDG 559
Cdd:cd03254   161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
27-568 1.46e-103

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 323.59  E-value: 1.46e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  27 LVTSTTLLIAP-LVGYIFQLIEDKNMFLLNLsaLGMIGLFVLKGLFQYGQEY----LSYFVAQRIIVDLRNQVYEHLQDL 101
Cdd:PRK10789    5 IIIAMLQLIPPkVVGIIVDGVTEQHMTTGQI--LMWIGTMVLIAVVVYLLRYvwrvLLFGASYQLAVELREDFYRQLSRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 102 SLDFYAKWNTGELVSRVMNDIQ-----------TLQATLFTGFVTLIPHSLlllglmgyifWLNWQLSLLTLVALPLIVQ 170
Cdd:PRK10789   83 HPEFYLRHRTGDLMARATNDVDrvvfaagegvlTLVDSLVMGCAVLIVMST----------QISWQLTLLALLPMPVMAI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 171 VIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVI----A 246
Cdd:PRK10789  153 MIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTIyiaiG 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 247 LLQTIAVVGIVWFggreIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLDVKPSIADlpGAKK 326
Cdd:PRK10789  233 MANLLAIGGGSWM----VVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVVKD--GSEP 306

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 327 LPRINGEINFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLES 404
Cdd:PRK10789  307 VPEGRGELDVNIRQFTYPQTDhpALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDS 386

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 405 LRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAI 484
Cdd:PRK10789  387 WRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARAL 466

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 485 LRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDGLYKYL 564
Cdd:PRK10789  467 LLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDM 546


                  ....
gi 1277238834 565 YAIQ 568
Cdd:PRK10789  547 YRYQ 550
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 334-568 1.06e-98

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: 299.40  E-value: 1.06e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAV 411
Cdd:cd03252     1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRIL 491
Cdd:cd03252    81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 492 ILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDGLYKYLYAIQ 568
Cdd:cd03252   161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 7-565 1.89e-95

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: 306.67  E-value: 1.89e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   7 LLKFIKPYYSQ--IIGGTICTALVTsttLLIAPLVGYIFQLIED-----KNMFLLNLSALGMIGLFVLKGLFQYGQEYLS 79
Cdd:TIGR01193 144 LLKFIPLITRQkkLIVNIVIAAIIV---TLISIAGSYYLQKIIDtyiphKMMGTLGIISIGLIIAYIIQQILSYIQIFLL 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  80 YFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSR---VMNDIQTLQATLFTGFVTLipHSLLLLGLmgYIFWLNWQ 156
Cdd:TIGR01193 221 NVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRftdASSIIDALASTILSLFLDM--WILVIVGL--FLVRQNML 296

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 157 LSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQ 236
Cdd:TIGR01193 297 LFLLSLLSIPVYAVIIILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQK 376

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 237 ILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLDVKP 316
Cdd:TIGR01193 377 ADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEVYLVDS 456

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 317 SIADLPGAKKLPRINGEINFENISFAYE-NEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQ 395
Cdd:TIGR01193 457 EFINKKKRTELNNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF 536

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 396 DIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYG-RPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGE 474
Cdd:TIGR01193 537 SLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQ 616

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 475 RQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERlMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQEL 554
Cdd:TIGR01193 617 KQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDEL 695

                         570
                  ....*....|.
gi 1277238834 555 LQKDGLYKYLY 565
Cdd:TIGR01193 696 LDRNGFYASLI 706
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
 18-308 7.71e-95

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: 291.63  E-value: 7.71e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  18 IIGGTICTALVTSTTLLIAPLVGYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYE 96
Cdd:cd18552     1 LALAILGMILVAATTAALAWLLKPLLdDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  97 HLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFA 176
Cdd:cd18552    81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 177 KEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGI 256
Cdd:cd18552   161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 257 VWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18552   241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
 2-564 2.84e-93

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: 297.57  E-value: 2.84e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   2 KLYARLLKFIKPYYSQIigGTICTALVTSTTLLIAP--LVGYIFQLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEylS 79
Cdd:TIGR01192   5 QVYVRALSYLNVHKNRV--LLIVIANITLAAITIAEpiLFGRIIDAISSKSDVLPTLALWAGFGVFNTIAYVLVARE--A 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  80 YFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSL 159
Cdd:TIGR01192  81 DRLAHGRRATLLTEAFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 160 LTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKsfdismravqILA 239
Cdd:TIGR01192 161 VLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAETSALKQFTNN----------LLS 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 240 TQNPVI----------ALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIF 309
Cdd:TIGR01192 231 AQYPVLdwwalasglnRMASTISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIGRLDQMSGFITQIFEARAKLEDFF 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 310 EVLDVKPSIADLPGAKKLPRINGEINFENISFAYEN-EEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSG 388
Cdd:TIGR01192 311 DLEDSVFQREEPADAPELPNVKGAVEFRHITFEFANsSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVG 390

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 389 RILVDGQDIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGS 468
Cdd:TIGR01192 391 QILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGN 470

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 469 RLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEI 548
Cdd:TIGR01192 471 RLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEK 550

                         570
                  ....*....|....*.
gi 1277238834 549 GSHQELLQKDGLYKYL 564
Cdd:TIGR01192 551 GSFQELIQKDGRFYKL 566
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 57-540 3.81e-92

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: 292.65  E-value: 3.81e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  57 SALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQAtLFTGF-VT 135
Cdd:TIGR02857  46 ALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGELATLALEGVEALDG-YFARYlPQ 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 136 LIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKE 215
Cdd:TIGR02857 125 LVLAVIVPLAILAAVFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKA 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 216 ELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLpqlisfATALGIMT------DPGN 289
Cdd:TIGR02857 205 QAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFATLSVALVAVYIGFRLLAGDLDL------ATGLFVLLlapefyLPLR 278

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 290 TLSKAYSIIQQGMASTKRIFEVLDVKPSI----ADLPGAKKLPringeINFENISFAYENE-EVLQNINLKVKPGEIIAL 364
Cdd:TIGR02857 279 QLGAQYHARADGVAAAEALFAVLDAAPRPlagkAPVTAAPASS-----LEFSGVSVAYPGRrPALRPVSFTVPPGERVAL 353

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 365 VGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAK 444
Cdd:TIGR02857 354 VGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALE 433

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 445 FANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFII 524
Cdd:TIGR02857 434 RAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLV 513

                         490
                  ....*....|....*.
gi 1277238834 525 AHRLYAVEHANRIVVI 540
Cdd:TIGR02857 514 THRLALAALADRIVVL 529
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 21-564 1.32e-91

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: 296.47  E-value: 1.32e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  21 GTICTALVTSTTLLIAPLVGYIFQ-------LIEDKNMFLLNLsALGMIGLFVLKGLFQYGQeyLSYFVAQRIIVDLR-- 91
Cdd:TIGR03796 154 GALLYLLLAGLLLVLPGLVIPAFSqifvdeiLVQGRQDWLRPL-LLGMGLTALLQGVLTWLQ--LYYLRRLEIKLAVGms 230

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  92 NQVYEHLQDLSLDFYAKWNTGELVSRV-MND-----IQTLQATLFTGFVTLIPHSLLLlglmgyiFWLNWQLSLLTLVAL 165
Cdd:TIGR03796 231 ARFLWHILRLPVRFFAQRHAGDIASRVqLNDqvaefLSGQLATTALDAVMLVFYALLM-------LLYDPVLTLIGIAFA 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 166 PLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSfdisMRAVQILATQNPVI 245
Cdd:TIGR03796 304 AINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSRWAGYQAKL----LNAQQELGVLTQIL 379

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 246 ----ALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLD------VK 315
Cdd:TIGR03796 380 gvlpTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPVNNLVGFGGTLQELEGDLNRLDDVLRnpvdplLE 459

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 316 PSIADLPGAKKLPRINGEINFENISFAYE--NEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVD 393
Cdd:TIGR03796 460 EPEGSAATSEPPRRLSGYVELRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFD 539

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 394 GQDIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGG 473
Cdd:TIGR03796 540 GIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGG 619

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 474 ERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERlmKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQE 553
Cdd:TIGR03796 620 QRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEE 697

                         570
                  ....*....|.
gi 1277238834 554 LLQKDGLYKYL 564
Cdd:TIGR03796 698 LWAVGGAYARL 708
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
 18-308 6.26e-87

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: 271.35  E-value: 6.26e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  18 IIGGTICTALVTSTTLLIAPLVGYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYE 96
Cdd:cd07346     1 LLLALLLLLLATALGLALPLLTKLLIdDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  97 HLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFA 176
Cdd:cd07346    81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 177 KEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGI 256
Cdd:cd07346   161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 257 VWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd07346   241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 334-544 1.44e-86

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: 265.79  E-value: 1.44e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENE--EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAV 411
Cdd:cd03228     1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEIALFSGTIKDNIaygrpnaseaeiieaakfanihdfinslpkkyetqvaergsrLSGGERQRVAIARAILRDPRIL 491
Cdd:cd03228    81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 492 ILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQ 544
Cdd:cd03228   119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 332-545 1.74e-83

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: 259.44  E-value: 1.74e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 332 GEINFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQI 409
Cdd:cd03245     1 GRIEFRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPR 489
Cdd:cd03245    81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 490 ILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQI 545
Cdd:cd03245   161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 21-568 3.48e-83

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 273.37  E-value: 3.48e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  21 GTICTALVTSTTLLIAPLVGYIfqlIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQD 100
Cdd:TIGR03797 145 GLLGTLLGMLVPIATGILIGTA---IPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVLRLETRMDASLQAAVWDRLLR 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 101 LSLDFYAKWNTGELVSRVM--NDIQ-----TLQATLFTGFVtliphSLLLLGLMgyiFWLNWQLSLLTLVALPLIVQVIR 173
Cdd:TIGR03797 222 LPVSFFRQYSTGDLASRAMgiSQIRrilsgSTLTTLLSGIF-----ALLNLGLM---FYYSWKLALVAVALALVAIAVTL 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 174 IFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQI---LATQNPVIALLQT 250
Cdd:TIGR03797 294 VLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQRIenlLTVFNAVLPVLTS 373

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 251 IAvvgIVWFGGREIISGSLSLPQLISFATALGI----MTDPGNTLSKAYSIIQQgmasTKRIFEVLDVKPSIAdlpGAKK 326
Cdd:TIGR03797 374 AA---LFAAAISLLGGAGLSLGSFLAFNTAFGSfsgaVTQLSNTLISILAVIPL----WERAKPILEALPEVD---EAKT 443

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 327 LP-RINGEINFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLE 403
Cdd:TIGR03797 444 DPgKLSGAIEVDRVTFRYRPDGplILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQ 523

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 404 SLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEaEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARA 483
Cdd:TIGR03797 524 AVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLD-EAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARA 602

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 484 ILRDPRILILDEATSSLDAETESLIRDALERLmkGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDGLYKY 563
Cdd:TIGR03797 603 LVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQ 680


                  ....*
gi 1277238834 564 LYAIQ 568
Cdd:TIGR03797 681 LARRQ 685
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 54-528 6.40e-82

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: 266.15  E-value: 6.40e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  54 LNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGF 133
Cdd:TIGR02868  52 LSVAAVAVRAFGIGRAVFRYLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVI 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 134 VTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVI-RIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAM 212
Cdd:TIGR02868 132 VPAGVALVVGAAAVAAIAVLSVPAALILAAGLLLAGFVApLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGA 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 213 EKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFA-TALGImTDPGNTL 291
Cdd:TIGR02868 212 LPAALAQVEEADRELTRAERRAAAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVlLPLAA-FEAFAAL 290

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 292 SKAYSIIQQGMASTKRIFEVLDVKPSIAD--LPGAKKLPRINGEINFENISFAYE-NEEVLQNINLKVKPGEIIALVGRT 368
Cdd:TIGR02868 291 PAAAQQLTRVRAAAERIVEVLDAAGPVAEgsAPAAGAVGLGKPTLELRDLSAGYPgAPPVLDGVSLDLPPGERVAILGPS 370

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 369 GAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANI 448
Cdd:TIGR02868 371 GSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGL 450

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 449 HDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRL 528
Cdd:TIGR02868 451 ADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 85-565 1.01e-81

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 266.69  E-value: 1.01e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  85 RIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQaTLFTGFVTLIPHSLLLLGLMgYIF--WLNWQLSLL-- 160
Cdd:PRK11160   90 RVLTHLRVFTFSKLLPLSPAGLARYRQGDLLNRLVADVDTLD-HLYLRLISPLVAALVVILVL-TIGlsFFDLTLALTlg 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 161 -TLVALPLIVQVIriFAKEIREISEGVQQKAAD----ITSHLQetiSQVKtVKSFAMEKEELAKFKGKTEKSFDISMRAV 235
Cdd:PRK11160  168 gILLLLLLLLPLL--FYRLGKKPGQDLTHLRAQyrvqLTEWLQ---GQAE-LTLFGAEDRYRQQLEQTEQQWLAAQRRQA 241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 236 QILATQNPVIALLQTIAVVGIVWFGGREIisGSLSLPQ----LISFAT-----ALGimtdPgntLSKAYSIIQQGMASTK 306
Cdd:PRK11160  242 NLTGLSQALMILANGLTVVLMLWLAAGGV--GGNAQPGaliaLFVFAAlaafeALM----P---VAGAFQHLGQVIASAR 312

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 307 RIFEVLDVKPSIaDLPGAKKLPRINGEINFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYD 384
Cdd:PRK11160  313 RINEITEQKPEV-TFPTTSTAAADQVSLTLNNVSFTYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD 391

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 385 PTSGRILVDGQDIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSlPKKYETQVA 464
Cdd:PRK11160  392 PQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLG 470

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 465 ERGSRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQ 544
Cdd:PRK11160  471 EGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQ 550

                         490       500
                  ....*....|....*....|.
gi 1277238834 545 ILEIGSHQELLQKDGLYKYLY 565
Cdd:PRK11160  551 IIEQGTHQELLAQQGRYYQLK 571
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 330-545 7.54e-81

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: 253.16  E-value: 7.54e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 330 INGEINFENISFAYENE---EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLR 406
Cdd:cd03248     8 LKGIVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 407 KQIAVVPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILR 486
Cdd:cd03248    88 SKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIR 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 487 DPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQI 545
Cdd:cd03248   168 NPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 332-550 1.77e-79

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: 249.33  E-value: 1.77e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 332 GEINFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQI 409
Cdd:cd03244     1 GDIEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFSGTIKDNIA-YGRpnASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDP 488
Cdd:cd03244    81 SIIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 489 RILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGS 550
Cdd:cd03244   159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
6-568 2.31e-77

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 255.80  E-value: 2.31e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   6 RLLKFIKPYYSQIIGGTICTALVTSTTLLIAPLVGY-IFQLIEDKNMFLLNLSALGM--IGLFVLKGLFQYGQEYLSYFV 82
Cdd:PRK10790   13 RLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYfIDNMVAKGNLPLGLVAGLAAayVGLQLLAAGLHYAQSLLFNRA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  83 AQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQaTLFTGFVTLIPHSLLLLGLMGY-IFWLNWQLSLLT 161
Cdd:PRK10790   93 AVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIR-DLYVTVVATVLRSAALIGAMLVaMFSLDWRMALVA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 162 LVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEkeelAKFKGK-TEKSFDISMRAVQILAT 240
Cdd:PRK10790  172 IMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQQ----ARFGERmGEASRSHYMARMQTLRL 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 241 QN----PVIALLQTIAVVG-IVWFGGREiiSGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLDvk 315
Cdd:PRK10790  248 DGfllrPLLSLFSALILCGlLMLFGFSA--SGTIEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMD-- 323

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 316 pSIADLPGAKKLPRINGEINFENISFAYENEE-VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDG 394
Cdd:PRK10790  324 -GPRQQYGNDDRPLQSGRIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDG 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 395 QDIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYGRpNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGE 474
Cdd:PRK10790  403 RPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQ 481

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 475 RQRVAIARAILRDPRILILDEATSSLDAETESLIRDALeRLMKGRTTFI-IAHRLYAVEHANRIVVIDNKQILEIGSHQE 553
Cdd:PRK10790  482 KQLLALARVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVvIAHRLSTIVEADTILVLHRGQAVEQGTHQQ 560

                         570
                  ....*....|....*
gi 1277238834 554 LLQKDGLYKYLYAIQ 568
Cdd:PRK10790  561 LLAAQGRYWQMYQLQ 575
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 53-557 2.02e-73

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: 244.66  E-value: 2.02e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  53 LLNLSALgMIGLFVLKGLFqygqEYLSYFVAQRI--IVD--LRNQVYEHLQDLSLDfyakwNTGELVSRVMNDIQTLQAT 128
Cdd:COG4618    59 LLMLTLL-ALGLYAVMGLL----DAVRSRILVRVgaRLDrrLGPRVFDAAFRAALR-----GGGGAAAQALRDLDTLRQF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 129 LfTGFVTL----IPHSLLLLGLmgyIFWLNWQLSLLTLVALplIVQVIRIFAKEI--REISEGVQQKAADITSHLQETIS 202
Cdd:COG4618   129 L-TGPGLFalfdLPWAPIFLAV---LFLFHPLLGLLALVGA--LVLVALALLNERltRKPLKEANEAAIRANAFAEAALR 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 203 QVKTVKSFAMEKEELAKFKGKTEKSFDISMRA---VQILATQNPVIALLQTIAVVGIvwfGGREIISGSLSLpqlisfat 279
Cdd:COG4618   203 NAEVIEAMGMLPALRRRWQRANARALALQARAsdrAGGFSALSKFLRLLLQSAVLGL---GAYLVIQGEITP-------- 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 280 alGIMTdpgntlskAYSII------------------QQGMASTKRIFEVLDvkpSIADLPGAKKLPRINGEINFENISF 341
Cdd:COG4618   272 --GAMI--------AASILmgralapieqaiggwkqfVSARQAYRRLNELLA---AVPAEPERMPLPRPKGRLSVENLTV 338

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 342 AYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEIALF 419
Cdd:COG4618   339 VPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELF 418

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 420 SGTIKDNIAygR-PNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRILILDEATS 498
Cdd:COG4618   419 DGTIAENIA--RfGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNS 496

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 499 SLDAETESLIRDALERL-MKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQK 557
Cdd:COG4618   497 NLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 21-308 1.04e-71

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: 231.60  E-value: 1.04e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  21 GTICTALVTSTTLLIAPLVGYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQ 99
Cdd:cd18576     1 GLILLLLSSAIGLVFPLLAGQLIdAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 100 DLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAKEI 179
Cdd:cd18576    81 RLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 180 REISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWF 259
Cdd:cd18576   161 RKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWY 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1277238834 260 GGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18576   241 GGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 50-308 2.66e-70

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: 228.55  E-value: 2.66e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  50 NMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATL 129
Cdd:cd18564    49 PLALLLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 130 FTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKS 209
Cdd:cd18564   129 VSGVLPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQA 208

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 210 FAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGN 289
Cdd:cd18564   209 FGREEHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVR 288

                         250
                  ....*....|....*....
gi 1277238834 290 TLSKAYSIIQQGMASTKRI 308
Cdd:cd18564   289 DLAKLTGRIAKASASAERV 307
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
 17-308 9.24e-69

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: 223.88  E-value: 9.24e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  17 QIIGGTICTALVTSTTLLIAPLVGY-IFQLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVY 95
Cdd:cd18545     1 KLLLALLLMLLSTAASLAGPYLIKIaIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  96 EHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIF 175
Cdd:cd18545    81 SHLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 176 AKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVG 255
Cdd:cd18545   161 RRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTAL 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 256 IVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18545   241 VYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
 19-308 6.95e-68

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: 221.54  E-value: 6.95e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  19 IGGTICTALVTSTTLLIAPLVGYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEH 97
Cdd:cd18542     2 LLAILALLLATALNLLIPLLIRRIIdSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  98 LQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAK 177
Cdd:cd18542    82 LQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 178 EIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIV 257
Cdd:cd18542   162 KVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVL 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 258 WFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18542   242 WVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 33-557 2.85e-66

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 224.92  E-value: 2.85e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  33 LLIAPLvgYIFQL----IEDKNMFLLNLSALGMIGLFVLKGLFqygqEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAK 108
Cdd:TIGR01842  22 MLAPPL--YMLQVydrvLTSGSVPTLLMLTVLALGLYLFLGLL----DALRSFVLVRIGEKLDGALNQPIFAASFSATLR 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 109 WNTGElVSRVMNDIQTLQ-----ATLFTGFVtlIPHSLLLLGLmgyIFWLNWQLSLLTLVALPLIVQVI----RIFAKEI 179
Cdd:TIGR01842  96 RGSGD-GLQALRDLDQLRqfltgPGLFAFFD--APWMPIYLLV---CFLLHPWIGILALGGAVVLVGLAllnnRATKKPL 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 180 REISEGVQQKaadiTSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWF 259
Cdd:TIGR01842 170 KEATEASIRA----NNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGL 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 260 GGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLDVKPSIADlpgAKKLPRINGEINFENI 339
Cdd:TIGR01842 246 GAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSRDP---AMPLPEPEGHLSVENV 322

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 340 SFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEIA 417
Cdd:TIGR01842 323 TIVPPGGKkpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVE 402

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 418 LFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRILILDEAT 497
Cdd:TIGR01842 403 LFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPN 482

                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 498 SSLDAETESLIRDALERLMK-GRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQK 557
Cdd:TIGR01842 483 SNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 18-308 3.24e-65

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


Pssm-ID: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 214.68  E-value: 3.24e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  18 IIGGTICTALVTSTTLLIAPLVGYI-----FQLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRN 92
Cdd:cd18563     1 LILGFLLMLLGTALGLVPPYLTKILiddvlIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  93 QVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVI 172
Cdd:cd18563    81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 173 RIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIA 252
Cdd:cd18563   161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 253 VVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18563   241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSAERI 296
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 18-308 2.20e-63

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


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 209.70  E-value: 2.20e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  18 IIGGTICTALVTSTTLLIAPLVGYIFQLIEDKNMFL--LNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVY 95
Cdd:cd18778     1 LILTLLCALLSTLLGLVPPWLIRELVDLVTIGSKSLglLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  96 EHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIF 175
Cdd:cd18778    81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 176 AKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVG 255
Cdd:cd18778   161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 256 IVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18778   241 VLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAERV 293
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
 18-308 7.76e-63

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: 208.40  E-value: 7.76e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  18 IIGGTICTALVTSTTLLIAPLVGYI---FQLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQV 94
Cdd:cd18544     1 FILALLLLLLATALELLGPLLIKRAiddYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  95 YEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRI 174
Cdd:cd18544    81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 175 FAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVV 254
Cdd:cd18544   161 FRKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 255 GIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18544   241 LVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASAERI 294
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
 18-308 1.05e-61

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: 205.34  E-value: 1.05e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  18 IIGGTICTALVTSTTLLIAPLVGYIFQLIEDKN--MFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVY 95
Cdd:cd18541     1 YLLGILFLILVDLLQLLIPRIIGRAIDALTAGTltASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  96 EHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIF 175
Cdd:cd18541    81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 176 AKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVG 255
Cdd:cd18541   161 GKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLI 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 256 IVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18541   241 VLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 8-544 1.26e-60

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 217.97  E-value: 1.26e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834    8 LKFIKPYYSQIIGGTICTALVTSTTLliaPLVGYIFQLIEdKNMFLLNlSALGMIGLFVLKGLFQYGQEYLSYF----VA 83
Cdd:PTZ00265    51 FKCLPASHRKLLGVSFVCATISGGTL---PFFVSVFGVIM-KNMNLGE-NVNDIIFSLVLIGIFQFILSFISSFcmdvVT 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   84 QRIIVDLRnqvYEHLQDLsldFY--AKWNTGELVSRVMNDI----QTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQL 157
Cdd:PTZ00265   126 TKILKTLK---LEFLKSV---FYqdGQFHDNNPGSKLTSDLdfylEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARL 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  158 SLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKgKTEKSFDISMRAVQI 237
Cdd:PTZ00265   200 TLCITCVFPLIYICGVICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFN-LSEKLYSKYILKANF 278

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  238 LATQNpvIALLQTIAVVGIV---WFGGREIISGSLSLPQLISFATALGIMTDPGNTLSK-AYSII-------QQGMASTK 306
Cdd:PTZ00265   279 MESLH--IGMINGFILASYAfgfWYGTRIIISDLSNQQPNNDFHGGSVISILLGVLISMfMLTIIlpniteyMKSLEATN 356

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  307 RIFEVLDVKPSIADLPGAKKLPRINgEINFENISFAYENE---EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFY 383
Cdd:PTZ00265   357 SLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYDTRkdvEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLY 435

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  384 DPTSGRILV-DGQDIKTAKLESLRKQIAVVPQEIALFSGTIKDNIAYG-------------------------------- 430
Cdd:PTZ00265   436 DPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdlealsnyynedgndsqenknkrnscr 515

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  431 ----------------------RPN---ASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAIL 485
Cdd:PTZ00265   516 akcagdlndmsnttdsneliemRKNyqtIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAII 595

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277238834  486 RDPRILILDEATSSLDAETESLIRDALERLmKG---RTTFIIAHRLYAVEHANRIVVIDNKQ 544
Cdd:PTZ00265   596 RNPKILILDEATSSLDNKSEYLVQKTINNL-KGnenRITIIIAHRLSTIRYANTIFVLSNRE 656
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 333-566 2.13e-60

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 210.47  E-value: 2.13e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 333 EINFENIS-FAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYdPTSGRILVDGQDIKTAKLESLRKQIAV 411
Cdd:PRK11174  349 TIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSW 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRIL 491
Cdd:PRK11174  428 VGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLL 507

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 492 ILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDGLYKYLYA 566
Cdd:PRK11174  508 LLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLA 582
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 332-550 5.58e-59

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: 195.32  E-value: 5.58e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 332 GEINFENISFAY--ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQI 409
Cdd:cd03369     5 GEIEVENLSVRYapDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFSGTIKDNI-AYGRpnASEAEIIEAAKfanihdfinslpkkyetqVAERGSRLSGGERQRVAIARAILRDP 488
Cdd:cd03369    85 TIIPQDPTLFSGTIRSNLdPFDE--YSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRP 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 489 RILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGS 550
Cdd:cd03369   145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 334-557 5.34e-57

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: 191.01  E-value: 5.34e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENE-EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVV 412
Cdd:COG1122     1 IELENLSFSYPGGtPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 PQ--EIALFSGTIKDNIAYGRPNA--SEAEII----EAAKFANIHDFINSLPkkyetqvaergSRLSGGERQRVAIARAI 484
Cdd:COG1122    81 FQnpDDQLFAPTVEEDVAFGPENLglPREEIRerveEALELVGLEHLADRPP-----------HELSGGQKQRVAIAGVL 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 485 LRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIA-HRL-YAVEHANRIVVIDNKQILEIGSHQELLQK 557
Cdd:COG1122   150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLdLVAELADRVIVLDDGRIVADGTPREVFSD 224
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
 21-308 1.35e-55

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: 189.31  E-value: 1.35e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  21 GTICTALVTSTTLLIAPLVGYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHL- 98
Cdd:cd18557     1 GLLFLLISSAAQLLLPYLIGRLIdTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  99 -QDLSldFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAK 177
Cdd:cd18557    81 rQEIA--FFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 178 EIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIV 257
Cdd:cd18557   159 YIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 258 WFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18557   239 WYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 334-545 1.70e-54

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: 182.03  E-value: 1.70e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAV 411
Cdd:cd03246     1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEIALFSGTIKDNIaygrpnaseaeiieaakfanihdfinslpkkyetqvaergsrLSGGERQRVAIARAILRDPRIL 491
Cdd:cd03246    81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 492 ILDEATSSLDAETESLIRDALERL-MKGRTTFIIAHRLYAVEHANRIVVIDNKQI 545
Cdd:cd03246   119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
 18-308 3.79e-54

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: 185.33  E-value: 3.79e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  18 IIGGTICTALVTSTTLLIAPLVGYIFQLIEDKNmfLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEH 97
Cdd:cd18551     1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGG--SSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  98 LQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAK 177
Cdd:cd18551    79 LLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 178 EIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIV 257
Cdd:cd18551   159 RIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVL 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 258 WFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18551   239 GVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 334-549 2.37e-53

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: 179.43  E-value: 2.37e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKlESLRKQIAV 411
Cdd:cd03247     1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEIALFSGTIKDNIaygrpnaseaeiieaakfanihdfinslpkkyetqvaerGSRLSGGERQRVAIARAILRDPRIL 491
Cdd:cd03247    80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 492 ILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIG 549
Cdd:cd03247   121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 54-561 3.90e-53

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: 195.93  E-value: 3.90e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   54 LNLSALGMIGlfVLKGLFQYGQEYL----SYFVAQRIIVDLRNQVYEHLQDlsldFYAKWNTGELVSRVMNDIQTLQatl 129
Cdd:TIGR00957 1006 LRLSVYGALG--ILQGFAVFGYSMAvsigGIQASRVLHQDLLHNKLRSPMS----FFERTPSGNLVNRFSKELDTVD--- 1076

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  130 ftgfvTLIPHSLLLL-----GLMGYIFWLNWQLSLLTLVALPLIVQ---VIRIFAKEIREISEGVQQKAADITSHLQETI 201
Cdd:TIGR00957 1077 -----SMIPPVIKMFmgslfNVIGALIVILLATPIAAVIIPPLGLLyffVQRFYVASSRQLKRLESVSRSPVYSHFNETL 1151

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  202 SQVKTVKSFamekEELAKFKGKTEKSFDISMRAVQILATQNPVIALlqTIAVVG--IVWFGGREIISGSLSL-PQLISFA 278
Cdd:TIGR00957 1152 LGVSVIRAF----EEQERFIHQSDLKVDENQKAYYPSIVANRWLAV--RLECVGncIVLFAALFAVISRHSLsAGLVGLS 1225

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  279 TALGI-MTDPGNTLSKAYSIIQQGMASTKRIFEVLDVKPS----IADLPGAKKLPRInGEINFENISFAYEN--EEVLQN 351
Cdd:TIGR00957 1226 VSYSLqVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEapwqIQETAPPSGWPPR-GRVEFRNYCLRYREdlDLVLRH 1304

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  352 INLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEIALFSGTIKDNI-AYG 430
Cdd:TIGR00957 1305 INVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdPFS 1384

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  431 RpnASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRD 510
Cdd:TIGR00957 1385 Q--YSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQS 1462

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1277238834  511 ALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDGLY 561
Cdd:TIGR00957 1463 TIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
 18-308 5.63e-53

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: 182.30  E-value: 5.63e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  18 IIGGTICTALVTSTTLLIAPLVGYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYE 96
Cdd:cd18543     1 LILALLAALLATLAGLAIPLLTRRAIdGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  97 HLQDLSLDFYAKWNTGELVSRVMNDIQTLQAtlFTGFV-TLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIF 175
Cdd:cd18543    81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQR--FLAFGpFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 176 AKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVG 255
Cdd:cd18543   159 RRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 256 IVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18543   239 VLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
336-545 1.04e-52

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 178.86  E-value: 1.04e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 336 FENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQE 415
Cdd:COG4619     3 LEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQE 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 416 IALFSGTIKDNIAYGRPNASEAEIIEAAK--FANIHdfinsLPKKY-ETQVaergSRLSGGERQRVAIARAILRDPRILI 492
Cdd:COG4619    83 PALWGGTVRDNLPFPFQLRERKFDRERALelLERLG-----LPPDIlDKPV----ERLSGGERQRLALIRALLLQPDVLL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 493 LDEATSSLDAET----ESLIRDALERlmKGRTTFIIAH-RLYAVEHANRIVVIDNKQI 545
Cdd:COG4619   154 LDEPTSALDPENtrrvEELLREYLAE--EGRAVLWVSHdPEQIERVADRVLTLEAGRL 209
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
334-557 5.61e-52

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 177.56  E-value: 5.61e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLEsLRKQIAVVP 413
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNI-----AYGRPNA-SEAEIIEAAKFANIHDFINSLPKKYetqvaergsrlSGGERQRVAIARAILR 486
Cdd:COG1131    80 QEPALYPDlTVRENLrffarLYGLPRKeARERIDELLELFGLTDAADRKVGTL-----------SGGMKQRLGLALALLH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 487 DPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIA-HRLYAVEH-ANRIVVIDNKQILEIGSHQELLQK 557
Cdd:COG1131   149 DPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 33-562 6.35e-51

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 189.08  E-value: 6.35e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   33 LLIAPLVGYIF---QLIEDKNMFLLNLSALGmIGLFVLKGLfqygQEYLSYFVAQRIIVDLRNQVYEHL--QDLSLDFYA 107
Cdd:PTZ00265   846 LLYAKYVSTLFdfaNLEANSNKYSLYILVIA-IAMFISETL----KNYYNNVIGEKVEKTMKRRLFENIlyQEISFFDQD 920

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  108 KWNTGELVSRVMNDIQTLQATL------FTGFVTLiphsLLLLGLMGYIFwlnwqLSLLTLVALPLIVQVIRIFAKEIR- 180
Cdd:PTZ00265   921 KHAPGLLSAHINRDVHLLKTGLvnniviFTHFIVL----FLVSMVMSFYF-----CPIVAAVLTGTYFIFMRVFAIRARl 991

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  181 EISEGVQQKAADITSH-----------------LQETISQVKTVKSFAMEKeelaKFKGKTEKSFDISMRAVQILATQNP 243
Cdd:PTZ00265   992 TANKDVEKKEINQPGTvfaynsddeifkdpsflIQEAFYNMNTVIIYGLED----YFCNLIEKAIDYSNKGQKRKTLVNS 1067

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  244 VIALLQTIAVVGI----VWFGGREIISGSLslpQLISFATALGIMTDPGNTLSKAYSIiQQGMASTKRIFEV---LDVKP 316
Cdd:PTZ00265  1068 MLWGFSQSAQLFInsfaYWFGSFLIRRGTI---LVDDFMKSLFTFLFTGSYAGKLMSL-KGDSENAKLSFEKyypLIIRK 1143

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  317 SIADL--PGAKKLPR---INGEINFENISFAY---ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYD---- 384
Cdd:PTZ00265  1144 SNIDVrdNGGIRIKNkndIKGKIEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlknd 1223

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  385 --------------------------------------------------PTSGRILVDGQDIKTAKLESLRKQIAVVPQ 414
Cdd:PTZ00265  1224 hhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQ 1303

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  415 EIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRILILD 494
Cdd:PTZ00265  1304 EPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLD 1383

                          570       580       590       600       610       620       630
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834  495 EATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEHANRIVVIDNKQ-----ILEIGSHQELLQ-KDGLYK 562
Cdd:PTZ00265  1384 EATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFNNPDrtgsfVQAHGTHEELLSvQDGVYK 1459
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 334-558 8.21e-51

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: 174.78  E-value: 8.21e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKT---AKLESLRKQIA 410
Cdd:COG1127     6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlseKELYELRRRIG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 411 VVPQEIALFSG-TIKDNIAYG---RPNASEAEIIEAAKFA----NIHDFINSLPkkyetqvaergSRLSGGERQRVAIAR 482
Cdd:COG1127    86 MLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVLEKlelvGLPGAADKMP-----------SELSGGMRKRVALAR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 483 AILRDPRILILDEATSSLD----AETESLIRDALERLmkGRTTFIIAHRL---YAVehANRIVVIDNKQILEIGSHQELL 555
Cdd:COG1127   155 ALALDPEILLYDEPTAGLDpitsAVIDELIRELRDEL--GLTSVVVTHDLdsaFAI--ADRVAVLADGKIIAEGTPEELL 230


                  ...
gi 1277238834 556 QKD 558
Cdd:COG1127   231 ASD 233
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 334-558 1.52e-50

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: 174.46  E-value: 1.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVP 413
Cdd:COG1120     2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QE-IALFSGTIKDNIAYGR---------PNASEAEIIEAA-KFANIHDFinslpkkyetqvAERG-SRLSGGERQRVAIA 481
Cdd:COG1120    82 QEpPAPFGLTVRELVALGRyphlglfgrPSAEDREAVEEAlERTGLEHL------------ADRPvDELSGGERQRVLIA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 482 RAILRDPRILILDEATSSLD----AETESLIRDALERlmKGRTTFIIAHRLY-AVEHANRIVVIDNKQILEIGSHQELLQ 556
Cdd:COG1120   150 RALAQEPPLLLLDEPTSHLDlahqLEVLELLRRLARE--RGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVLT 227


                  ..
gi 1277238834 557 KD 558
Cdd:COG1120   228 PE 229
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 19-308 1.92e-50

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


Pssm-ID: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 175.75  E-value: 1.92e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  19 IGGTICTALVTSTTLLIAPLvgyIFQLIED-----KNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQ 93
Cdd:cd18550     1 LALVLLLILLSALLGLLPPL---LLREIIDdalpqGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  94 VYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIR 173
Cdd:cd18550    78 LYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 174 IFAKEIREISEGVQQKAADITSHLQET--ISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTI 251
Cdd:cd18550   158 RVGRRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAI 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 252 AVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18550   238 GPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLALFERI 294
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 336-544 1.86e-49

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: 170.34  E-value: 1.86e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 336 FENISFAYEN--EEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVP 413
Cdd:cd03225     2 LKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 Q--EIALFSGTIKDNIAYGRPNA--SEAEIIEAAKFA----NIHDFINSLPkkyetqvaergSRLSGGERQRVAIARAIL 485
Cdd:cd03225    82 QnpDDQFFGPTVEEEVAFGLENLglPEEEIEERVEEAlelvGLEGLRDRSP-----------FTLSGGQKQRVAIAGVLA 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 486 RDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIA-HRL-YAVEHANRIVVIDNKQ 544
Cdd:cd03225   151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLdLLLELADRVIVLEDGK 211
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 334-560 5.43e-49

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 169.88  E-value: 5.43e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAkleslRKQIAVVP 413
Cdd:COG1121     7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIAL---FSGTIKDNIAYG---------RPNASEAEIIEAA-KFANIHDFINslpkkyeTQVAErgsrLSGGERQRVAI 480
Cdd:COG1121    82 QRAEVdwdFPITVRDVVLMGrygrrglfrRPSRADREAVDEAlERVGLEDLAD-------RPIGE----LSGGQQQRVLL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 481 ARAILRDPRILILDEATSSLDAETESLIRDALERL-MKGRTTFIIAHRLYAV-EHANRIVVIdNKQILEIGSHQELLQKD 558
Cdd:COG1121   151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPPEEVLTPE 229


                  ..
gi 1277238834 559 GL 560
Cdd:COG1121   230 NL 231
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
 18-308 2.69e-48

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: 169.59  E-value: 2.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  18 IIGGTICTALVTSTTLLIAPLVGY-IFQLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYE 96
Cdd:cd18546     1 LALALLLVVVDTAASLAGPLLVRYgIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  97 HLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFA 176
Cdd:cd18546    81 HLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWFR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 177 KEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGI 256
Cdd:cd18546   161 RRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAV 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 257 VWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18546   241 LLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQVFDSYQQARAALEKI 292
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
 18-308 2.76e-48

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: 169.89  E-value: 2.76e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  18 IIGGTICTALVTSTTLLIAPLVGYIFQLIEDK-------NMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDL 90
Cdd:cd18547     1 LILVIILAIISTLLSVLGPYLLGKAIDLIIEGlgggggvDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  91 RNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQ 170
Cdd:cd18547    81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 171 VIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQT 250
Cdd:cd18547   161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 251 IAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18547   241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAERV 298
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 334-573 2.82e-48

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


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 168.11  E-value: 2.82e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLEsLRKQIAVVP 413
Cdd:COG4555     2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNI-----AYGRPNASEAEIIEA-AKFANIHDFINslpKKYETqvaergsrLSGGERQRVAIARAILR 486
Cdd:COG4555    81 DERGLYDRlTVRENIryfaeLYGLFDEELKKRIEElIELLGLEEFLD---RRVGE--------LSTGMKKKVALARALVH 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 487 DPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIA-HRLYAVEH-ANRIVVIDNKQILEIGSHQELLQK---DGLY 561
Cdd:COG4555   150 DPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEigeENLE 229

                         250
                  ....*....|..
gi 1277238834 562 KYLYAIQFNNKA 573
Cdd:COG4555   230 DAFVALIGSEEG 241
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
334-547 3.62e-48

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 167.15  E-value: 3.62e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENE-EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQD---IKTAKLESLRKQI 409
Cdd:COG2884     2 IRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDlsrLKRREIPYLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFSG-TIKDNIAY-----GRPNAS-EAEIIEAAKFANIHDFINSLPkkyetqvaergSRLSGGERQRVAIAR 482
Cdd:COG2884    82 GVVFQDFRLLPDrTVYENVALplrvtGKSRKEiRRRVREVLDLVGLSDKAKALP-----------HELSGGEQQRVAIAR 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 483 AILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIA-HRLYAVEHAN-RIVVIDNKQILE 547
Cdd:COG2884   151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPkRVLELEDGRLVR 217
PLN03232 PLN03232
ABC transporter C family member; Provisional
 105-559 9.47e-48

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 179.79  E-value: 9.47e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  105 FYAKWNTGELVSRVMNDIQTLQ---ATLFTGFVTLIPHSLLLLGLMGYIFwlnwQLSLLTLVALPLIVQVIRIFAKEI-R 180
Cdd:PLN03232  1000 FFHTNPTGRVINRFSKDIGDIDrnvANLMNMFMNQLWQLLSTFALIGTVS----TISLWAIMPLLILFYAAYLYYQSTsR 1075

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  181 EISEGVQQKAADITSHLQETISQVKTVKSFAmEKEELAKFKGKtekSFDISMRAVQILATQNPVIAL-LQTIAVVgIVWF 259
Cdd:PLN03232  1076 EVRRLDSVTRSPIYAQFGEALNGLSSIRAYK-AYDRMAKINGK---SMDNNIRFTLANTSSNRWLTIrLETLGGV-MIWL 1150

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  260 GGREIISGSLSLPQLISFATALGIM-------TDPGNTLSKAYSIIQQGMASTKRIFEVLDVKPSIADLPGAKKLPR--- 329
Cdd:PLN03232  1151 TATFAVLRNGNAENQAGFASTMGLLlsytlniTTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIIENNRPVSgwp 1230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  330 INGEINFENISFAYENE--EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRK 407
Cdd:PLN03232  1231 SRGSIKFEDVHLRYRPGlpPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  408 QIAVVPQEIALFSGTIKDNI-AYGRPNasEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILR 486
Cdd:PLN03232  1311 VLSIIPQSPVLFSGTVRFNIdPFSEHN--DADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLR 1388

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277238834  487 DPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDG 559
Cdd:PLN03232  1389 RSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
 27-308 1.45e-47

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


Pssm-ID: 350019 [Multi-domain]  Cd Length: 289  Bit Score: 167.66  E-value: 1.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  27 LVTSTTLLiapLVGYIFQLIEDK-----NMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDL 101
Cdd:cd18575     6 LIAAAATL---ALGQGLRLLIDQgfaagNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 102 SLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAKEIRE 181
Cdd:cd18575    83 SPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 182 ISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGG 261
Cdd:cd18575   163 LSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGA 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 262 REIISGSLSLPQLISF-------ATALGimtdpgnTLSKAYSIIQQGMASTKRI 308
Cdd:cd18575   243 HDVLAGRMSAGELSQFvfyavlaAGSVG-------ALSEVWGDLQRAAGAAERL 289
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 349-498 1.69e-47

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: 162.82  E-value: 1.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEIALFSG-TIKDNI 427
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 428 AYGRP------NASEAEIIEAAKFANIHDFINSLpkkyetqVAERGSRLSGGERQRVAIARAILRDPRILILDEATS 498
Cdd:pfam00005  81 RLGLLlkglskREKDARAEEALEKLGLGDLADRP-------VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
 18-287 3.19e-47

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: 166.28  E-value: 3.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  18 IIGGTICTALVTSTTLLIAPLVGYIFQLIEDKNM---FLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQV 94
Cdd:pfam00664   1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDpetQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  95 YEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRI 174
Cdd:pfam00664  81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 175 FAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVV 254
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1277238834 255 GIVWFGGREIISGSLSLPQLISFATALGIMTDP 287
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGP 273
PLN03130 PLN03130
ABC transporter C family member; Provisional
 332-559 4.32e-47

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 178.01  E-value: 4.32e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  332 GEINFENISFAYENE--EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQI 409
Cdd:PLN03130  1236 GSIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  410 AVVPQEIALFSGTIKDNI-AYGRPNasEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDP 488
Cdd:PLN03130  1316 GIIPQAPVLFSGTVRFNLdPFNEHN--DADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRS 1393

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834  489 RILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDG 559
Cdd:PLN03130  1394 KILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 334-554 5.19e-47

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: 164.28  E-value: 5.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYD-----PTSGRILVDGQDIKT--AKLESLR 406
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDldVDVLELR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 407 KQIAVVPQEIALFSGTIKDNIAYG------RPNASEAEIIEAA-KFANIHDfinslpkkyetQVAER--GSRLSGGERQR 477
Cdd:cd03260    81 RRVGMVFQKPNPFPGSIYDNVAYGlrlhgiKLKEELDERVEEAlRKAALWD-----------EVKDRlhALGLSGGQQQR 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 478 VAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIGSHQEL 554
Cdd:cd03260   150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 332-554 7.42e-47

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 167.56  E-value: 7.42e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 332 GEINFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLtsllLR----FYDPTSGRILVDGQDIktAKLESLRK 407
Cdd:COG3839     2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTL----LRmiagLEDPTSGEILIGGRDV--TDLPPKDR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 408 QIAVVPQEIALF-SGTIKDNIAYG---RpNASEAEI----IEAAKFANIHDFINSLPKKyetqvaergsrLSGGERQRVA 479
Cdd:COG3839    76 NIAMVFQSYALYpHMTVYENIAFPlklR-KVPKAEIdrrvREAAELLGLEDLLDRKPKQ-----------LSGGQRQRVA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 480 IARAILRDPRILILDEATSSLDA----ETESLIRDALERLmkgRTTFIIahrlyaVEH--------ANRIVVIDNKQILE 547
Cdd:COG3839   144 LGRALVREPKVFLLDEPLSNLDAklrvEMRAEIKRLHRRL---GTTTIY------VTHdqveamtlADRIAVMNDGRIQQ 214


                  ....*..
gi 1277238834 548 IGSHQEL 554
Cdd:COG3839   215 VGTPEEL 221
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 334-543 1.09e-46

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: 163.03  E-value: 1.09e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENE----EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAkleslRKQI 409
Cdd:cd03293     1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFS-GTIKDNIAYG-----RPNASEAEIIEAA-KFANIHDFINSLPKkyetqvaergsRLSGGERQRVAIAR 482
Cdd:cd03293    76 GYVFQQDALLPwLTVLDNVALGlelqgVPKAEARERAEELlELVGLSGFENAYPH-----------QLSGGMRQRVALAR 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 483 AILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLY-AVEHANRIVVIDNK 543
Cdd:cd03293   145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSAR 208
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 334-542 1.38e-46

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: 162.25  E-value: 1.38e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE-----VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQdiktakleslrkq 408
Cdd:cd03250     1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 409 IAVVPQEIALFSGTIKDNIAYGRPNASE--AEIIEAAKFANihDfINSLPKKYETQVAERGSRLSGGERQRVAIARAILR 486
Cdd:cd03250    68 IAYVSQEPWIQNGTIRENILFGKPFDEEryEKVIKACALEP--D-LEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 487 DPRILILDEATSSLDAETES-LIRDAL-ERLMKGRTTFIIAHRLYAVEHANRIVVIDN 542
Cdd:cd03250   145 DADIYLLDDPLSAVDAHVGRhIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDN 202
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 334-558 2.20e-46

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


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 162.67  E-value: 2.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI---KTAKLESLRKQIA 410
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglSEAELYRLRRRMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 411 VVPQEIALFSG-TIKDNIAYG---RPNASEAEIIEAAK----FANIHDFINSLPkkyetqvaergSRLSGGERQRVAIAR 482
Cdd:cd03261    81 MLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLekleAVGLRGAEDLYP-----------AELSGGMKKRVALAR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 483 AILRDPRILILDEATSSLD----AETESLIRDALERLmkGRTTFIIAH---RLYAVehANRIVVIDNKQILEIGSHQELL 555
Cdd:cd03261   150 ALALDPELLLYDEPTAGLDpiasGVIDDLIRSLKKEL--GLTSIMVTHdldTAFAI--ADRIAVLYDGKIVAEGTPEELR 225


                  ...
gi 1277238834 556 QKD 558
Cdd:cd03261   226 ASD 228
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 334-556 8.99e-46

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


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 161.51  E-value: 8.99e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAY----ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQI 409
Cdd:COG1124     2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALfS----GTIKDNIA-----YGRPNAsEAEIIEAAKFANIH-DFINSLPkkyetqvaergSRLSGGERQRVA 479
Cdd:COG1124    82 QMVFQDPYA-SlhprHTVDRILAeplriHGLPDR-EERIAELLEQVGLPpSFLDRYP-----------HQLSGGQRQRVA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 480 IARAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIGSHQELLQ 556
Cdd:COG1124   149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
 23-308 1.02e-45

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: 162.71  E-value: 1.02e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  23 ICTALVTSTTLLIAP-LVGY-IFQLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHL-- 98
Cdd:cd18572     2 FVFLVVAALSELAIPhYTGAvIDAVVADGSREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLlr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  99 QDLSldFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAKE 178
Cdd:cd18572    82 QDIA--FFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 179 IREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVW 258
Cdd:cd18572   160 YRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLF 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1277238834 259 FGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18572   240 YGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 336-543 4.04e-45

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: 158.47  E-value: 4.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 336 FENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQdiktaKLESLRKQIAVVPQE 415
Cdd:cd03235     2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK-----PLEKERKRIGYVPQR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 416 IAL---FSGTIKDNIAYGR---------PNASEAEIIEAA-KFANIHDFINSlpkkyetQVAErgsrLSGGERQRVAIAR 482
Cdd:cd03235    77 RSIdrdFPISVRDVVLMGLyghkglfrrLSKADKAKVDEAlERVGLSELADR-------QIGE----LSGGQQQRVLLAR 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 483 AILRDPRILILDEATSSLDAETESLIRDALERL-MKGRTTFIIAHRLYAV-EHANRIVVIDNK 543
Cdd:cd03235   146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRT 208
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
 15-308 4.15e-45

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: 161.07  E-value: 4.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  15 YSQIIGGTICTALVTSTTLLIAPLVGYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQ 93
Cdd:cd18570     1 KKLLILILLLSLLITLLGIAGSFFFQILIdDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  94 VYEHLQDLSLDFYAKWNTGELVSRvMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIR 173
Cdd:cd18570    81 YFKHLLKLPLSFFETRKTGEIISR-FNDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIIL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 174 IFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAV 253
Cdd:cd18570   160 LFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGS 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 254 VGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18570   240 LLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 334-549 9.74e-45

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


Pssm-ID: 213224 [Multi-domain]  Cd Length: 228  Bit Score: 158.05  E-value: 9.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENE----EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI---KTAKLESLR 406
Cdd:cd03257     2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklSRRLRKIRR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 407 KQIAVVPQEI--AL-FSGTIKDNIA------YGRPNASEAEIIEAAKFANIH---DFINSLPkkyetqvaergSRLSGGE 474
Cdd:cd03257    82 KEIQMVFQDPmsSLnPRMTIGEQIAeplrihGKLSKKEARKEAVLLLLVGVGlpeEVLNRYP-----------HELSGGQ 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 475 RQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERL--MKGRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIG 549
Cdd:cd03257   151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLqeELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 312-556 1.19e-44

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


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 165.46  E-value: 1.19e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 312 LDVKPSIADLPGAKKLPRINGE--INFENISFAYENEE-----VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYD 384
Cdd:COG1123   237 LAAVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLR 316

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 385 PTSGRILVDGQDIKTAK---LESLRKQIAVVPQ--EIALFSG-TIKDNIA-----YGRPNASEAE--IIEAAKFANIH-D 450
Cdd:COG1123   317 PTSGSILFDGKDLTKLSrrsLRELRRRVQMVFQdpYSSLNPRmTVGDIIAeplrlHGLLSRAERRerVAELLERVGLPpD 396

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 451 FINSLPkkyetqvaergSRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERL--MKGRTTFIIAHRL 528
Cdd:COG1123   397 LADRYP-----------HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqrELGLTYLFISHDL 465

                         250       260
                  ....*....|....*....|....*....
gi 1277238834 529 YAVEH-ANRIVVIDNKQILEIGSHQELLQ 556
Cdd:COG1123   466 AVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 336-549 1.45e-44

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: 157.30  E-value: 1.45e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 336 FENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIktAKLESLRKQIAVVPQE 415
Cdd:cd03259     3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV--TGVPPERRNIGMVFQD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 416 IALFSG-TIKDNIAYG-----RPNASEAE-IIEAAKFANIHDFINSLPkkyetqvaergSRLSGGERQRVAIARAILRDP 488
Cdd:cd03259    81 YALFPHlTVAENIAFGlklrgVPKAEIRArVRELLELVGLEGLLNRYP-----------HELSGGQQQRVALARALAREP 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 489 RILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLY-AVEHANRIVVIDNKQILEIG 549
Cdd:cd03259   150 SLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
 23-307 2.28e-44

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: 159.15  E-value: 2.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  23 ICTALVTSTTLLIAPLVGYIFQ-LIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDL 101
Cdd:cd18549     9 FCAVLIAALDLVFPLIVRYIIDdLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 102 SLDFYAKWNTGELVSRVMNDIQTLQA-------TLFTGFVTLIphsllllGLMGYIFWLNWQLSLLTLVALPLIVQVIRI 174
Cdd:cd18549    89 SFSFFDNNKTGQLMSRITNDLFDISElahhgpeDLFISIITII-------GSFIILLTINVPLTLIVFALLPLMIIFTIY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 175 FAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVV 254
Cdd:cd18549   162 FNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFLESKKKAYKAMAYFFSGMNFFTNLLNL 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 255 GIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKR 307
Cdd:cd18549   242 VVLVAGGYFIIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGMAGFER 294
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 334-555 2.66e-44

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: 156.97  E-value: 2.66e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYEN----EEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKT---AKLESLR 406
Cdd:cd03258     2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgKELRKAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 407 KQIAVVPQEIALFSG-TIKDNIAYgrP----NASEAEIIEAA----KFANIHDFINSLPkkyetqvaergSRLSGGERQR 477
Cdd:cd03258    82 RRIGMIFQHFNLLSSrTVFENVAL--PleiaGVPKAEIEERVlellELVGLEDKADAYP-----------AQLSGGQKQR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 478 VAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAV-EHANRIVVIDNKQILEIGSHQEL 554
Cdd:cd03258   149 VGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVkRICDRVAVMEKGEVVEEGTVEEV 228


                  .
gi 1277238834 555 L 555
Cdd:cd03258   229 F 229
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 334-560 6.80e-44

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: 157.21  E-value: 6.80e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAK-LESLRKQIA 410
Cdd:TIGR04520   1 IEVENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnLWEIRKKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 411 VVPQ--EIALFSGTIKDNIAYGRPNA--SEAEII----EAAKFANIHDFINSLPkkyetqvaergSRLSGGERQRVAIAR 482
Cdd:TIGR04520  81 MVFQnpDNQFVGATVEDDVAFGLENLgvPREEMRkrvdEALKLVGMEDFRDREP-----------HLLSGGQKQRVAIAG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 483 AILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEHANRIVVIDNKQILEIG------SHQEL 554
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGtpreifSQVEL 229


                  ....*.
gi 1277238834 555 LQKDGL 560
Cdd:TIGR04520 230 LKEIGL 235
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
334-547 6.91e-44

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 155.59  E-value: 6.91e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE----VLQNINLKVKPGEIIALVGRTGAGKSTL---TSLLLRfydPTSGRILVDGQDIKT---AKLE 403
Cdd:COG1136     5 LELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLlniLGGLDR---PTSGEVLIDGQDISSlseRELA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 404 SLRKQ-IAVVPQEIALFSG-TIKDNIA----YGRPNASEAE--IIEAAKFANIHDFINSLPkkyetqvaergSRLSGGER 475
Cdd:COG1136    82 RLRRRhIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRerARELLERVGLGDRLDHRP-----------SQLSGGQQ 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 476 QRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEHANRIVVIDNKQILE 547
Cdd:COG1136   151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 334-548 9.06e-44

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 156.40  E-value: 9.06e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENE----EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIktaklESLRKQI 409
Cdd:COG1116     8 LELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPDR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFs-gTIKDNIAYGRPNA--SEAEIIEAAKFA----NIHDFINSLPKkyetqvaergsRLSGGERQRVAIAR 482
Cdd:COG1116    83 GVVFQEPALLpwlTVLDNVALGLELRgvPKAERRERARELlelvGLAGFEDAYPH-----------QLSGGMRQRVAIAR 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 483 AILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLY-AVEHANRIVVIDNK--QILEI 548
Cdd:COG1116   152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHDVDeAVFLADRVVVLSARpgRIVEE 222
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 334-545 1.35e-43

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: 152.94  E-value: 1.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKlESLRKQIAVVP 413
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP-EEVKRRIGYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIaygrpnaseaeiieaakfanihdfinslpkkyetqvaergsRLSGGERQRVAIARAILRDPRILI 492
Cdd:cd03230    80 EEPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLI 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 493 LDEATSSLDAETESLIRDALERLMK-GRTTFIIAHRLYAVEH-ANRIVVIDNKQI 545
Cdd:cd03230   119 LDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 336-542 8.98e-43

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: 150.47  E-value: 8.98e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 336 FENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQe 415
Cdd:cd00267     2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 416 ialfsgtikdniaygrpnaseaeiieaakfanihdfinslpkkyetqvaergsrLSGGERQRVAIARAILRDPRILILDE 495
Cdd:cd00267    81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1277238834 496 ATSSLDAETESLIRDALERLM-KGRTTFIIAHRL-YAVEHANRIVVIDN 542
Cdd:cd00267   107 PTSGLDPASRERLLELLRELAeEGRTVIIVTHDPeLAELAADRVIVLKD 155
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 337-549 1.10e-42

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: 151.05  E-value: 1.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEI 416
Cdd:cd03214     3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQAL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 417 ALFsgtikdniaygrpnaseaeiieaakfaNIHDFinslpkkyetqvAERG-SRLSGGERQRVAIARAILRDPRILILDE 495
Cdd:cd03214    83 ELL---------------------------GLAHL------------ADRPfNELSGGERQRVLLARALAQEPPILLLDE 123

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 496 ATSSLDAETESLIRDALERLMK--GRTTFIIAHRL-YAVEHANRIVVIDNKQILEIG 549
Cdd:cd03214   124 PTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 330-564 1.10e-42

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: 153.53  E-value: 1.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 330 INGEINFENISFAYEN--EEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRK 407
Cdd:cd03288    16 LGGEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 408 QIAVVPQEIALFSGTIKDNIAYGRpNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRD 487
Cdd:cd03288    96 RLSIILQDPILFSGSIRFNLDPEC-KCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 488 PRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELL-QKDGLYKYL 564
Cdd:cd03288   175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASL 252
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 334-545 1.33e-42

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: 151.87  E-value: 1.33e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENE----EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKT---AKLESLR 406
Cdd:cd03255     1 IELKNLSKTYGGGgekvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlseKELAAFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 407 -KQIAVVPQEIALFSG-TIKDNIAY-----GRPNAS-EAEIIEAAKFANIHDFINSLPkkyetqvaergSRLSGGERQRV 478
Cdd:cd03255    81 rRHIGFVFQSFNLLPDlTALENVELplllaGVPKKErRERAEELLERVGLGDRLNHYP-----------SELSGGQQQRV 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 479 AIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGR-TTFIIA-HRLYAVEHANRIVVIDNKQI 545
Cdd:cd03255   150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAgTTIVVVtHDPELAEYADRIIELRDGKI 218
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 334-554 3.42e-42

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 154.87  E-value: 3.42e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLtsllLR----FYDPTSGRILVDGQDIktAKLESLRKQI 409
Cdd:COG3842     6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTL----LRmiagFETPDSGRILLDGRDV--TGLPPEKRNV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFSG-TIKDNIAYG--RPNASEAEII----EAAKFANIHDFINSLPkkyetqvaergSRLSGGERQRVAIAR 482
Cdd:COG3842    80 GMVFQDYALFPHlTVAENVAFGlrMRGVPKAEIRarvaELLELVGLEGLADRYP-----------HQLSGGQQQRVALAR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 483 AILRDPRILILDEATSSLDA----ETESLIRDALERLmkgRTTFIIA-HRLY-AVEHANRIVVIDNKQILEIGSHQEL 554
Cdd:COG3842   149 ALAPEPRVLLLDEPLSALDAklreEMREELRRLQREL---GITFIYVtHDQEeALALADRIAVMNDGRIEQVGTPEEI 223
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 337-557 4.12e-42

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: 151.33  E-value: 4.12e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYeNEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLEslRKQIAVVPQEI 416
Cdd:cd03299     4 ENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 417 ALFSG-TIKDNIAYG-------RPNAsEAEIIEAAKFANIHDFINSLPKkyetqvaergsRLSGGERQRVAIARAILRDP 488
Cdd:cd03299    81 ALFPHmTVYKNIAYGlkkrkvdKKEI-ERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALVVNP 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 489 RILILDEATSSLDAETESLIRDALERLMK-GRTTFI-IAHRLY-AVEHANRIVVIDNKQILEIGSHQELLQK 557
Cdd:cd03299   149 KILLLDEPFSALDVRTKEKLREELKKIRKeFGVTVLhVTHDFEeAWALADKVAIMLNGKLIQVGKPEEVFKK 220
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 334-556 1.40e-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: 156.99  E-value: 1.40e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPT---SGRILVDGQDIKTAKLESLRKQ 408
Cdd:COG1123     5 LEVRDLSVRYPGGDvpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 409 IAVVPQE--IALFSGTIKDNIAYG------RPNASEAEIIEAAKFANIHDFINSLPkkyetqvaergSRLSGGERQRVAI 480
Cdd:COG1123    85 IGMVFQDpmTQLNPVTVGDQIAEAlenlglSRAEARARVLELLEAVGLERRLDRYP-----------HQLSGGQRQRVAI 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 481 ARAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAV-EHANRIVVIDNKQILEIGSHQELLQ 556
Cdd:COG1123   154 AMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
334-558 4.73e-41

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 148.36  E-value: 4.73e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVlqNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIkTAKLESLRKqIAVVP 413
Cdd:COG3840     2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERP-VSMLF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIAYG-----RPNASE-AEIIEAAKFANIHDFINSLPkkyetqvaergSRLSGGERQRVAIARAILR 486
Cdd:COG3840    78 QENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALARCLVR 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 487 DPRILILDEATSSLD----AETESLIRD-ALERlmkGRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIGSHQELLQKD 558
Cdd:COG3840   147 KRPILLLDEPFSALDpalrQEMLDLVDElCRER---GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 334-555 5.04e-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: 148.22  E-value: 5.04e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI--KTAKLESLRKQIAV 411
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEIALFSG-TIKDNIAYGrP----NASEAEIIEAAKFA----NIHDFINSLPkkyetqvaergSRLSGGERQRVAIAR 482
Cdd:COG1126    82 VFQQFNLFPHlTVLENVTLA-PikvkKMSKAEAEERAMELlervGLADKADAYP-----------AQLSGGQQQRVAIAR 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 483 AILRDPRILILDEATSSLDAEtesLIRDALErLMK-----GRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQELL 555
Cdd:COG1126   150 ALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMRdlakeGMTMVVVTHEMgFAREVADRVVFMDGGRIVEEGPPEEFF 224
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 334-542 8.06e-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: 145.79  E-value: 8.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLES--LRKQIAV 411
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEIALFSG-TIKDNIAYGrpnaseaeiieaakfanihdfinslpkkyetqvaergsrLSGGERQRVAIARAILRDPRI 490
Cdd:cd03229    81 VFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDV 121

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 491 LILDEATSSLDAETESLIRDALERL--MKGRTTFIIAHRL-YAVEHANRIVVIDN 542
Cdd:cd03229   122 LLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLdEAARLADRVVVLRD 176
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 23-308 1.36e-40

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


Pssm-ID: 349984 [Multi-domain]  Cd Length: 295  Bit Score: 149.17  E-value: 1.36e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  23 ICTALVTSTTLLIAPLV-GY-IFQLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQD 100
Cdd:cd18540     8 IILMLLVALLDAVFPLLtKYaIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 101 LSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAKEIR 180
Cdd:cd18540    88 LSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKIL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 181 EISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFG 260
Cdd:cd18540   168 KAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALVLWYG 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1277238834 261 GREIISGSLSLPQLISFAT-ALGIMtDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18540   248 GILVLAGAITIGTLVAFISyATQFF-EPIQQLARVLAELQSAQASAERV 295
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
334-550 6.54e-40

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 148.30  E-value: 6.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENIS--FAYENEEV--LQNINLKVKPGEIIALVGRTGAGKSTLT---SLLLRfydPTSGRILVDGQDIKT---AKLE 403
Cdd:COG1135     2 IELENLSktFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLER---PTSGSVLVDGVDLTAlseRELR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 404 SLRKQIAVVPQEIALFSG-TIKDNIAYgrP----NASEAEIIEAAK----FANIHDFINSLPkkyetqvaergSRLSGGE 474
Cdd:COG1135    79 AARRKIGMIFQHFNLLSSrTVAENVAL--PleiaGVPKAEIRKRVAelleLVGLSDKADAYP-----------SQLSGGQ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 475 RQRVAIARAILRDPRILILDEATSSLDAE-TES---LIRDALERLmkGRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIG 549
Cdd:COG1135   146 KQRVGIARALANNPKVLLCDEATSALDPEtTRSildLLKDINREL--GLTIVLITHEMDVVRRiCDRVAVLENGRIVEQG 223


                  .
gi 1277238834 550 S 550
Cdd:COG1135   224 P 224
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 334-549 8.91e-40

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: 144.32  E-value: 8.91e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIktAKLESLRKQIAVVP 413
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV--TDLPPKDRDIAMVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIAYG------RPNASEAEIIEAAKFANIHDFINSLPKkyetqvaergsRLSGGERQRVAIARAILR 486
Cdd:cd03301    79 QNYALYPHmTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVR 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 487 DPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAH-RLYAVEHANRIVVIDNKQILEIG 549
Cdd:cd03301   148 EPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
 18-308 9.10e-40

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: 146.77  E-value: 9.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  18 IIGGTICTALVTSTTLLIAPLVGYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYE 96
Cdd:cd18548     1 AILAPLFKLLEVLLELLLPTLMADIIdEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  97 HLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFA 176
Cdd:cd18548    81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 177 KEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGI 256
Cdd:cd18548   161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 257 VWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18548   241 LWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 334-545 1.49e-39

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: 143.44  E-value: 1.49e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI--KTAKLESLRKQIAV 411
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEIALFSG-TIKDNIAYG---RPNASEAEIIEAAKFA----NIHDFINSLPkkyetqvaergSRLSGGERQRVAIARA 483
Cdd:cd03262    81 VFQQFNLFPHlTVLENITLApikVKGMSKAEAEERALELlekvGLADKADAYP-----------AQLSGGQQQRVAIARA 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 484 ILRDPRILILDEATSSLDAEtesLIRDALErLMK-----GRTTFIIAHRL-YAVEHANRIVVIDNKQI 545
Cdd:cd03262   150 LAMNPKVMLFDEPTSALDPE---LVGEVLD-VMKdlaeeGMTMVVVTHEMgFAREVADRVIFMDDGRI 213
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 333-556 1.96e-39

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 147.22  E-value: 1.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 333 EINFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLtsllLR----FYDPTSGRILVDGQDIKTAkLESLRKQ 408
Cdd:COG1118     2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTL----LRiiagLETPDSGRIVLNGRDLFTN-LPPRERR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 409 IAVVPQEIALFSG-TIKDNIAYG---RPnASEAEI----------IEAAKFANihdfinslpkKYETQvaergsrLSGGE 474
Cdd:COG1118    77 VGFVFQHYALFPHmTVAENIAFGlrvRP-PSKAEIrarveellelVQLEGLAD----------RYPSQ-------LSGGQ 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 475 RQRVAIARAILRDPRILILDEATSSLDAEteslIRDALERLMK------GRTTFIIAH-RLYAVEHANRIVVIDNKQILE 547
Cdd:COG1118   139 RQRVALARALAVEPEVLLLDEPFGALDAK----VRKELRRWLRrlhdelGGTTVFVTHdQEEALELADRVVVMNQGRIEQ 214


                  ....*....
gi 1277238834 548 IGSHQELLQ 556
Cdd:COG1118   215 VGTPDEVYD 223
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
 51-308 3.06e-39

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


Pssm-ID: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 145.79  E-value: 3.06e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  51 MFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLF 130
Cdd:cd18565    50 RGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLD 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 131 TGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSF 210
Cdd:cd18565   130 DGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAF 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 211 AMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISG------SLSLPQLISFATALGIM 284
Cdd:cd18565   210 TAEDFERERVADASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVLDGpplftgTLTVGTLVTFLFYTQRL 289

                         250       260
                  ....*....|....*....|....
gi 1277238834 285 TDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18565   290 LWPLTRLGDLIDQYQRAMASAKRV 313
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 334-540 5.20e-39

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 143.27  E-value: 5.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENE-EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI---KTAKLESLRKQI 409
Cdd:COG3638     3 LELRNLSKRYPGGtPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalRGRALRRLRRRI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFSG-TIKDNIAYGR-----------PNASEAEIIEA---------AKFANihdfinslpkkyetqvaERGS 468
Cdd:COG3638    83 GMIFQQFNLVPRlSVLTNVLAGRlgrtstwrsllGLFPPEDRERAlealervglADKAY-----------------QRAD 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 469 RLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRL-YAVEHANRIVVI 540
Cdd:COG3638   146 QLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVdLARRYADRIIGL 220
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 334-554 2.96e-38

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: 140.78  E-value: 2.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYEN-EEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI---KTAKLESLRKQI 409
Cdd:cd03256     1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklKGKALRQLRRQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFSG-TIKDNIAYGRPNA-----------SEAEIIEAAKF---ANIHDFINSlpkkyetqvaeRGSRLSGGE 474
Cdd:cd03256    81 GMIFQQFNLIERlSVLENVLSGRLGRrstwrslfglfPKEEKQRALAAlerVGLLDKAYQ-----------RADQLSGGQ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 475 RQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERL--MKGRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSH 551
Cdd:cd03256   150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVdLAREYADRIVGLKDGRIVFDGPP 229


                  ...
gi 1277238834 552 QEL 554
Cdd:cd03256   230 AEL 232
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 349-557 6.74e-38

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: 140.86  E-value: 6.74e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESL----RKQIAVVPQEIALFSG-TI 423
Cdd:cd03294    40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 424 KDNIAYG------RPNASEAEIIEAAKFANIHDFINSLPKKyetqvaergsrLSGGERQRVAIARAILRDPRILILDEAT 497
Cdd:cd03294   120 LENVAFGlevqgvPRAEREERAAEALELVGLEGWEHKYPDE-----------LSGGMQQRVGLARALAVDPDILLMDEAF 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 498 SSLDaeteSLIR----DALERLMK--GRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQELLQK 557
Cdd:cd03294   189 SALD----PLIRremqDELLRLQAelQKTIVFITHDLdEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 334-555 1.44e-37

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: 138.97  E-value: 1.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE-VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVV 412
Cdd:cd03295     1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 PQEIALFSG-TIKDNIA-------YGRPNAsEAEIIEAAKFANIHdfinslPKKYetqvAER-GSRLSGGERQRVAIARA 483
Cdd:cd03295    81 IQQIGLFPHmTVEENIAlvpkllkWPKEKI-RERADELLALVGLD------PAEF----ADRyPHELSGGQQQRVGVARA 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 484 ILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLY-AVEHANRIVVIDNKQILEIGSHQELL 555
Cdd:cd03295   150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDeAFRLADRIAIMKNGEIVQVGTPDEIL 224
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 333-554 2.99e-37

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: 138.24  E-value: 2.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 333 EINFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIktAKLESLRKQIAVV 412
Cdd:cd03296     2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA--TDVPVQERNVGFV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 PQEIALFSG-TIKDNIAYG---RPNA---SEAEIieAAKFANIHDFI--NSLPKKYETQvaergsrLSGGERQRVAIARA 483
Cdd:cd03296    80 FQHYALFRHmTVFDNVAFGlrvKPRSerpPEAEI--RAKVHELLKLVqlDWLADRYPAQ-------LSGGQRQRVALARA 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 484 ILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAH-RLYAVEHANRIVVIDNKQILEIGSHQEL 554
Cdd:cd03296   151 LAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHdQEEALEVADRVVVMNKGRIEQVGTPDEV 224
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
 27-308 4.10e-37

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


Pssm-ID: 350053 [Multi-domain]  Cd Length: 295  Bit Score: 139.31  E-value: 4.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  27 LVTSTTLLIAPLvgYIFQLIE----------DKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYE 96
Cdd:cd18780     6 LVSSGTNLALPY--FFGQVIDavtnhsgsggEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  97 HLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFA 176
Cdd:cd18780    84 AIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 177 KEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGI 256
Cdd:cd18780   164 KYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLV 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 257 VWFGGREIISGSLSLPQLISF-------ATALGImtdpgntLSKAYSIIQQGMASTKRI 308
Cdd:cd18780   244 LWYGGRLVIDGELTTGLLTSFllytltvAMSFAF-------LSSLYGDFMQAVGASVRV 295
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 337-556 6.01e-37

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: 136.80  E-value: 6.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLES-LRKQIAVVPQE 415
Cdd:cd03224     4 ENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 416 IALFSG-TIKDNI---AYGRPNASEAEIIEA--AKFANIHDFINSlpkkyetqvaeRGSRLSGGERQRVAIARAILRDPR 489
Cdd:cd03224    84 RRIFPElTVEENLllgAYARRRAKRKARLERvyELFPRLKERRKQ-----------LAGTLSGGEQQMLAIARALMSRPK 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 490 ILILDEATSSLDAETESLIRDALERLMKGRTTFII----AHRlyAVEHANRIVVIDNKQILEIGSHQELLQ 556
Cdd:cd03224   153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLveqnARF--ALEIADRAYVLERGRVVLEGTAAELLA 221
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
348-540 2.67e-36

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 141.69  E-value: 2.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQ--DIKTAKlESLRKQIAVVPQEIALFSG-TIK 424
Cdd:COG1129    19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvRFRSPR-DAQAAGIAIIHQELNLVPNlSVA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 425 DNIAYGRPNAS-----EAEIIEAAKfanihDFINSLpkKYETQVAERGSRLSGGERQRVAIARAILRDPRILILDEATSS 499
Cdd:COG1129    98 ENIFLGREPRRgglidWRAMRRRAR-----ELLARL--GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTAS 170

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1277238834 500 L-DAETESLIRdALERLM-KGRTTFIIAHRLYAV-EHANRIVVI 540
Cdd:COG1129   171 LtEREVERLFR-IIRRLKaQGVAIIYISHRLDEVfEIADRVTVL 213
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 334-554 2.86e-36

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: 135.06  E-value: 2.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIktAKLESLRKQIAVVP 413
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIAYG------RPNASEAEIIEAAKFANIHDFINSLPkkyetqvaergSRLSGGERQRVAIARAILR 486
Cdd:cd03300    79 QNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLVQLEGYANRKP-----------SQLSGGQQQRVAIARALVN 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 487 DPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAH-RLYAVEHANRIVVIDNKQILEIGSHQEL 554
Cdd:cd03300   148 EPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHdQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 337-545 4.70e-36

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: 133.54  E-value: 4.70e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAY-ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKlesLRKQIAVVPQE 415
Cdd:cd03226     3 ENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 416 I--ALFSGTIKDNIAYGRPNASEA-EIIEAA-KFANIHDFINSLPKKyetqvaergsrLSGGERQRVAIARAILRDPRIL 491
Cdd:cd03226    80 VdyQLFTDSVREELLLGLKELDAGnEQAETVlKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGKDLL 148

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 492 ILDEATSSLDAETESLIRDALERLMK-GRTTFIIAHRL-YAVEHANRIVVIDNKQI 545
Cdd:cd03226   149 IFDEPTSGLDYKNMERVGELIRELAAqGKAVIVITHDYeFLAKVCDRVLLLANGAI 204
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 337-542 1.04e-35

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: 131.40  E-value: 1.04e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTA-KLESLRKQIAVVPQe 415
Cdd:cd03216     4 RGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDARRAGIAMVYQ- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 416 ialfsgtikdniaygrpnaseaeiieaakfanihdfinslpkkyetqvaergsrLSGGERQRVAIARAILRDPRILILDE 495
Cdd:cd03216    83 ------------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1277238834 496 ATSSL-DAETESLIrDALERLMK-GRTTFIIAHRLYAV-EHANRIVVIDN 542
Cdd:cd03216   109 PTAALtPAEVERLF-KVIRRLRAqGVAVIFISHRLDEVfEIADRVTVLRD 157
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 334-549 8.86e-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: 130.61  E-value: 8.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEV-LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI---KTAKLESLRKQI 409
Cdd:cd03292     1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlRGRAIPYLRRKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFSG-TIKDNIA------YGRPNASEAEIIEAAKFANIHDFINSLPkkyetqvaergSRLSGGERQRVAIAR 482
Cdd:cd03292    81 GVVFQDFRLLPDrNVYENVAfalevtGVPPREIRKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIAR 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 483 AILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAhrlyavEHANRIVVIDNKQILEIG 549
Cdd:cd03292   150 AIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA------THAKELVDTTRHRVIALE 210
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
334-556 1.29e-34

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 132.06  E-value: 1.29e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAV 411
Cdd:PRK13635    6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEI-ALFSG-TIKDNIAYGRPN--ASEAEIIE----AAKFANIHDFINSLPkkyetqvaergSRLSGGERQRVAIARA 483
Cdd:PRK13635   86 VFQNPdNQFVGaTVQDDVAFGLENigVPREEMVErvdqALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 484 ILRDPRILILDEATSSLD----AETESLIRDALErlmKGRTTFI-IAHRLYAVEHANRIVVIDNKQILEIGSHQELLQ 556
Cdd:PRK13635  155 LALQPDIIILDEATSMLDprgrREVLETVRQLKE---QKGITVLsITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 334-555 1.76e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 131.27  E-value: 1.76e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAV 411
Cdd:PRK13632    8 IKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEI-ALFSG-TIKDNIAYG------RPNASEAEIIEAAKFANIHDFINSLPKKyetqvaergsrLSGGERQRVAIARA 483
Cdd:PRK13632   88 IFQNPdNQFIGaTVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIASV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 484 ILRDPRILILDEATSSLDAETESLIRDALERLMKGRT-TFI-IAHRLYAVEHANRIVVIDNKQILEIGSHQELL 555
Cdd:PRK13632  157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 334-550 2.18e-34

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 133.00  E-value: 2.18e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENE----EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI---KTAKLESLR 406
Cdd:PRK11153    2 IELKNISKVFPQGgrtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalSEKELRKAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 407 KQIAVVPQEIALFSG-TIKDNIAYgrP----NASEAEI-------IEAAKFANIHDfinslpkKYETQvaergsrLSGGE 474
Cdd:PRK11153   82 RQIGMIFQHFNLLSSrTVFDNVAL--PlelaGTPKAEIkarvtelLELVGLSDKAD-------RYPAQ-------LSGGQ 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 475 RQRVAIARAILRDPRILILDEATSSLDAETE----SLIRDALERLmkGRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIG 549
Cdd:PRK11153  146 KQRVAIARALASNPKVLLCDEATSALDPATTrsilELLKDINREL--GLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223


                  .
gi 1277238834 550 S 550
Cdd:PRK11153  224 T 224
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 332-562 2.36e-34

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: 131.13  E-value: 2.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 332 GEINFENISFAYEN--EEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDpTSGRILVDGQDIKTAKLESLRKQI 409
Cdd:cd03289     1 GQMTVKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFSGTIKDNI-AYGRpnASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDP 488
Cdd:cd03289    80 GVIPQKVFIFSGTFRKNLdPYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 489 RILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDGLYK 562
Cdd:cd03289   158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFK 231
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 337-564 3.02e-34

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: 129.72  E-value: 3.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESL-RKQIAVVPQE 415
Cdd:COG0410     7 ENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 416 IALFSG-TIKDNI---AYGRPNASE-AEIIEA--AKFANIHDFINSlpkkyetqvaeRGSRLSGGERQRVAIARAILRDP 488
Cdd:COG0410    87 RRIFPSlTVEENLllgAYARRDRAEvRADLERvyELFPRLKERRRQ-----------RAGTLSGGEQQMLAIGRALMSRP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 489 RILILDEAtssldaeTESL-------IRDALERLMKGRTTFII----AHRlyAVEHANRIVVIDNKQILEIGSHQELLQK 557
Cdd:COG0410   156 KLLLLDEP-------SLGLapliveeIFEIIRRLNREGVTILLveqnARF--ALEIADRAYVLERGRIVLEGTAAELLAD 226


                  ....*...
gi 1277238834 558 DGLYK-YL 564
Cdd:COG0410   227 PEVREaYL 234
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 338-556 4.35e-34

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: 131.71  E-value: 4.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 338 NISFAYENEEV--LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDP---TSGRILVDGQDIKTAKLESLR----KQ 408
Cdd:COG0444     8 KVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRkirgRE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 409 IAVVPQE--IAL---FsgTIKDNIA-------YGRPNASEAEIIEAAKFANIHDfinslpkkyetqVAERGSR----LSG 472
Cdd:COG0444    88 IQMIFQDpmTSLnpvM--TVGDQIAeplrihgGLSKAEARERAIELLERVGLPD------------PERRLDRypheLSG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 473 GERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGR-TTFI-IAHRLYAVEH-ANRIVVIDNKQILEIG 549
Cdd:COG0444   154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELgLAILfITHDLGVVAEiADRVAVMYAGRIVEEG 233


                  ....*..
gi 1277238834 550 SHQELLQ 556
Cdd:COG0444   234 PVEELFE 240
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
337-558 6.01e-34

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 129.47  E-value: 6.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEI 416
Cdd:COG4559     5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 417 AL-FSGTIKDNIAYGR-----PNASEAEIIEAAkfanIHdfinslpkkyETQVAERGSR----LSGGERQRVAIARAIL- 485
Cdd:COG4559    85 SLaFPFTVEEVVALGRaphgsSAAQDRQIVREA----LA----------LVGLAHLAGRsyqtLSGGEQQRVQLARVLAq 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 486 ------RDPRILILDEATSSLD----AETESLIRDALERlmkGRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQEL 554
Cdd:COG4559   151 lwepvdGGPRWLFLDEPTSALDlahqHAVLRLARQLARR---GGGVVAVLHDLnLAAQYADRILLLHQGRLVAQGTPEEV 227


                  ....
gi 1277238834 555 LQKD 558
Cdd:COG4559   228 LTDE 231
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 108-562 7.00e-34

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: 137.73  E-value: 7.00e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  108 KWNTGELVSRVMNDIQTLQATLFTGFVTLIPhslLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAKEIReISEGVQ 187
Cdd:TIGR01271  978 TMKAGRILNRFTKDMAIIDDMLPLTLFDFIQ---LTLIVLGAIFVVSVLQPYIFIAAIPVAVIFIMLRAYFLR-TSQQLK 1053

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  188 QKAAD----ITSHLQETISQVKTVKSFAMEkeelAKFKGKTEKSFDIS-------MRAVQILATQNPVIALLQTIAVVGI 256
Cdd:TIGR01271 1054 QLESEarspIFSHLITSLKGLWTIRAFGRQ----SYFETLFHKALNLHtanwflyLSTLRWFQMRIDIIFVFFFIAVTFI 1129

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  257 VwFGGREIISGSLSlpqlISFATALGIMTdpgnTLSKAY--SIIQQG-MASTKRIFEVLDVKPS---------------- 317
Cdd:TIGR01271 1130 A-IGTNQDGEGEVG----IILTLAMNILS----TLQWAVnsSIDVDGlMRSVSRVFKFIDLPQEeprpsggggkyqlstv 1200

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  318 -IADLPGAKKLPRINGEINFENISFAY--ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDpTSGRILVDG 394
Cdd:TIGR01271 1201 lVIENPHAQKCWPSGGQMDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG 1279

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  395 QDIKTAKLESLRKQIAVVPQEIALFSGTIKDNI-AYGRpnASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGG 473
Cdd:TIGR01271 1280 VSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLdPYEQ--WSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNG 1357

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  474 ERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQE 553
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQK 1437


                   ....*....
gi 1277238834  554 LLQKDGLYK 562
Cdd:TIGR01271 1438 LLNETSLFK 1446
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
334-556 7.79e-34

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 128.67  E-value: 7.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIK--TAKLESLRKQIAV 411
Cdd:PRK09493    2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEIALFSG-TIKDNIAYGrP----NASEAEIIEAAKfanihdfinSLPKKyeTQVAERG----SRLSGGERQRVAIAR 482
Cdd:PRK09493   82 VFQQFYLFPHlTALENVMFG-PlrvrGASKEEAEKQAR---------ELLAK--VGLAERAhhypSELSGGQQQRVAIAR 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 483 AILRDPRILILDEATSSLDAEteslIRDALERLMK-----GRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQELLQ 556
Cdd:PRK09493  150 ALAVKPKLMLFDEPTSALDPE----LRHEVLKVMQdlaeeGMTMVIVTHEIgFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
 27-308 1.67e-33

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: 129.17  E-value: 1.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  27 LVTSTTLLIAP-----LVGYIFQLIEDKNMFLLNLS--ALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHL- 98
Cdd:cd18573     6 LVSSAVTMSVPfaigkLIDVASKESGDIEIFGLSLKtfALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSIl 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  99 -QDLSldFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAK 177
Cdd:cd18573    86 rQDAA--FFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGR 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 178 EIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIV 257
Cdd:cd18573   164 YVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVL 243

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 258 WFGGREIISGSLSLPQLISFA-----TALGIMtdpgnTLSKAYSIIQQGMASTKRI 308
Cdd:cd18573   244 YYGGSLVASGELTVGDLTSFLmyavyVGSSVS-----GLSSFYSELMKGLGASSRL 294
cbiO PRK13637
energy-coupling factor transporter ATPase;
334-560 2.46e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 128.63  E-value: 2.46e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYeNE------EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI--KTAKLESL 405
Cdd:PRK13637    3 IKIENLTHIY-MEgtpfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 406 RKQIAVVPQ--EIALFSGTIKDNIAYGRPN--ASEAEIIEAAKFAnihdfINSLPKKYETQVAERGSRLSGGERQRVAIA 481
Cdd:PRK13637   82 RKKVGLVFQypEYQLFEETIEKDIAFGPINlgLSEEEIENRVKRA-----MNIVGLDYEDYKDKSPFELSGGQKRRVAIA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 482 RAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAV-EHANRIVVIDNKQILEIGSHQEL---- 554
Cdd:PRK13637  157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREVfkev 236


                  ....*...
gi 1277238834 555 --LQKDGL 560
Cdd:PRK13637  237 etLESIGL 244
PLN03232 PLN03232
ABC transporter C family member; Provisional
 158-564 2.56e-33

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 136.26  E-value: 2.56e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  158 SLLTLVALPLIVQVIRifaKEIREISEGVQQKAADItSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDIsMRAVQI 237
Cdd:PLN03232   447 SLILFLLIPLQTLIVR---KMRKLTKEGLQWTDKRV-GIINEILASMDTVKCYAWEKSFESRIQGIRNEELSW-FRKAQL 521

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  238 LATQNPVIaLLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRIFEVLDVKPS 317
Cdd:PLN03232   522 LSAFNSFI-LNSIPVVVTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSEER 600

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  318 IAdlpgAKKLPRING--EINFENISFAYE---NEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILV 392
Cdd:PLN03232   601 IL----AQNPPLQPGapAISIKNGYFSWDsktSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV 676

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  393 dgqdiktaklesLRKQIAVVPQEIALFSGTIKDNIAYGRPNASE--AEIIEAAKFAniHDfINSLPKKYETQVAERGSRL 470
Cdd:PLN03232   677 ------------IRGSVAYVPQVSWIFNATVRENILFGSDFESEryWRAIDVTALQ--HD-LDLLPGRDLTEIGERGVNI 741

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  471 SGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDA-LERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIG 549
Cdd:PLN03232   742 SGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEG 821

                          410
                   ....*....|....*
gi 1277238834  550 SHQELLQKDGLYKYL 564
Cdd:PLN03232   822 TFAELSKSGSLFKKL 836
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 334-539 3.63e-33

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: 125.67  E-value: 3.63e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKlESLRKQIAVVP 413
Cdd:COG4133     3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAYLG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIA-----YGRPnASEAEIIEAAKFANIHDFINSLPKKyetqvaergsrLSGGERQRVAIARAILRD 487
Cdd:COG4133    82 HADGLKPElTVRENLRfwaalYGLR-ADREAIDEALEAVGLAGLADLPVRQ-----------LSAGQKRRVALARLLLSP 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 488 PRILILDEATSSLDAETESLIRDALERLMKGRTTFIIA-HRLYAVEHANRIVV 539
Cdd:COG4133   150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 112-561 4.03e-33

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 135.46  E-value: 4.03e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  112 GELVSRVMNDIQTLQAtlFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVA-LPLIVQVIRIFAKEIREIsEGVQQKA 190
Cdd:TIGR00957  415 GEIVNLMSVDAQRFMD--LATYINMIWSAPLQVILALYFLWLNLGPSVLAGVAvMVLMVPLNAVMAMKTKTY-QVAHMKS 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  191 ADITSHL-QETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQ------NPVIALLQTIAVvgIVWFGGRE 263
Cdd:TIGR00957  492 KDNRIKLmNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGtftwvcTPFLVALITFAV--YVTVDENN 569

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  264 IISGSLSLPQLISFatalGIMTDPGNTLSKAYSIIQQGMASTKRIFEVL---DVKPSIADLPGAKklPRINGEINFENIS 340
Cdd:TIGR00957  570 ILDAEKAFVSLALF----NILRFPLNILPMVISSIVQASVSLKRLRIFLsheELEPDSIERRTIK--PGEGNSITVHNAT 643

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  341 FAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQdiktakleslrkqIAVVPQEIAL 418
Cdd:TIGR00957  644 FTWARDLppTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWI 710

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  419 FSGTIKDNIAYGR---PNASEAEIIEAAKFANIHdfinSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRILILDE 495
Cdd:TIGR00957  711 QNDSLRENILFGKalnEKYYQQVLEACALLPDLE----ILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDD 786

                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834  496 ATSSLDAETESLIRDAL---ERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDGLY 561
Cdd:TIGR00957  787 PLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 337-524 5.95e-33

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 126.69  E-value: 5.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYD--P---TSGRILVDGQDI--KTAKLESLRKQI 409
Cdd:COG1117    15 RNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELRRRV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFSGTIKDNIAYG------RPNASEAEIIEAA-KFANIHDfinslpkkyetQVAER----GSRLSGGERQRV 478
Cdd:COG1117    95 GMVFQKPNPFPKSIYDNVAYGlrlhgiKSKSELDEIVEESlRKAALWD-----------EVKDRlkksALGLSGGQQQRL 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1277238834 479 AIARAILRDPRILILDEATSSLDAETESLIRDALERLmKGRTTFII 524
Cdd:COG1117   164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILEL-KKDYTIVI 208
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
334-554 6.95e-33

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 129.05  E-value: 6.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIktAKLESLRKQIAVVP 413
Cdd:PRK10851    3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV--SRLHARDRKVGFVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIAYG--------RPNASEA--------EIIEAAKFANihdfinslpkKYETQvaergsrLSGGERQ 476
Cdd:PRK10851   81 QHYALFRHmTVFDNIAFGltvlprreRPNAAAIkakvtqllEMVQLAHLAD----------RYPAQ-------LSGGQKQ 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 477 RVAIARAILRDPRILILDEATSSLDAETESLIRDALERL---MKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQE 553
Cdd:PRK10851  144 RVALARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLheeLKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQ 223


                  .
gi 1277238834 554 L 554
Cdd:PRK10851  224 V 224
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 334-549 9.05e-33

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: 125.00  E-value: 9.05e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGeIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKtAKLESLRKQIAVVP 413
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIGYLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIAY-----GRPNA-SEAEIIEAAKFANIHDFINslpkkyetqvaERGSRLSGGERQRVAIARAILR 486
Cdd:cd03264    79 QEFGVYPNfTVREFLDYiawlkGIPSKeVKARVDEVLELVNLGDRAK-----------KKIGSLSGGMRRRVGIAQALVG 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 487 DPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVE-HANRIVVIDNKQILEIG 549
Cdd:cd03264   148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
334-553 9.12e-33

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 129.30  E-value: 9.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIktAKLESLRKQIAVVP 413
Cdd:PRK09452   15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI--THVPAENRHVNTVF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIAYG-----RPNAS-EAEIIEAAKFANIHDFINSLPKkyetqvaergsRLSGGERQRVAIARAILR 486
Cdd:PRK09452   93 QSYALFPHmTVFENVAFGlrmqkTPAAEiTPRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVN 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 487 DPRILILDEATSSLDAETESLIRDALERLMK--GrTTFI-IAH-RLYAVEHANRIVVIDNKQILEIGSHQE 553
Cdd:PRK09452  162 KPKVLLLDESLSALDYKLRKQMQNELKALQRklG-ITFVfVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
PLN03130 PLN03130
ABC transporter C family member; Provisional
 158-564 1.57e-32

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 133.71  E-value: 1.57e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  158 SLLTLVALPLIVQVIrifaKEIREIS-EGVQQKAADItSHLQETISQVKTVKSFAMEKEelakFKGKTE--KSFDIS-MR 233
Cdd:PLN03130   447 SLMLVLMFPIQTFII----SKMQKLTkEGLQRTDKRI-GLMNEVLAAMDTVKCYAWENS----FQSKVQtvRDDELSwFR 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  234 AVQILATQNPVIalLQTIAV-VGIVWFGGREIISG---------SLSLPQLISFatalgimtdPGNTLSKAYSIIQQGMA 303
Cdd:PLN03130   518 KAQLLSAFNSFI--LNSIPVlVTVVSFGVFTLLGGdltparaftSLSLFAVLRF---------PLFMLPNLITQAVNANV 586

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  304 STKRIFEVLDVKPSI--ADLPGAKKLPringEINFENISFAYENE---EVLQNINLKVKPGEIIALVGRTGAGKSTLTSL 378
Cdd:PLN03130   587 SLKRLEELLLAEERVllPNPPLEPGLP----AISIKNGYFSWDSKaerPTLSNINLDVPVGSLVAIVGSTGEGKTSLISA 662

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  379 LLRFYDPTSGRILVdgqdiktaklesLRKQIAVVPQEIALFSGTIKDNIAYGRP-NASEAE-IIEAAKFAniHDfINSLP 456
Cdd:PLN03130   663 MLGELPPRSDASVV------------IRGTVAYVPQVSWIFNATVRDNILFGSPfDPERYErAIDVTALQ--HD-LDLLP 727

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  457 KKYETQVAERGSRLSGGERQRVAIARAILRDPRILILDEATSSLDAET-----ESLIRDALerlmKGRTTFIIAHRLYAV 531
Cdd:PLN03130   728 GGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVgrqvfDKCIKDEL----RGKTRVLVTNQLHFL 803

                          410       420       430
                   ....*....|....*....|....*....|...
gi 1277238834  532 EHANRIVVIDNKQILEIGSHQELLQKDGLYKYL 564
Cdd:PLN03130   804 SQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
ABC_6TM_Sav1866_like cd18554
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...
 14-308 4.22e-32

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: 125.61  E-value: 4.22e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  14 YYSQIIGGTICTALVTSTTLLIAPLVGYIFQ---LIEDKNMFLLNLSALGMIGLF-VLKGLFQYGQEYLSYFVAQRIIVD 89
Cdd:cd18554     1 IIITIVIGLVRFGIPLLLPLILKYIVDDVIQgssLTLDEKVYKLFTIIGIMFFIFlILRPPVEYYRQYFAQWIANKILYD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  90 LRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIV 169
Cdd:cd18554    81 IRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 170 QVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQ 249
Cdd:cd18554   161 LAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTIT 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 250 TIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18554   241 DLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 334-560 4.86e-32

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 124.04  E-value: 4.86e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVP 413
Cdd:COG4604     2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIAYGR-------PNASEAEIIEAA-KFANIHDFINslpkKYETQvaergsrLSGGERQRVAIARAI 484
Cdd:COG4604    82 QENHINSRlTVRELVAFGRfpyskgrLTAEDREIIDEAiAYLDLEDLAD----RYLDE-------LSGGQRQRAFIAMVL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 485 LRDPRILILDEATSSLD----AETESLIRDALERLmkGRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQELLQKDG 559
Cdd:COG4604   151 AQDTDYVLLDEPLNNLDmkhsVQMMKLLRRLADEL--GKTVVIVLHDInFASCYADHIVAMKDGRVVAQGTPEEIITPEV 228


                  .
gi 1277238834 560 L 560
Cdd:COG4604   229 L 229
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 337-558 4.94e-32

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 124.11  E-value: 4.94e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEI 416
Cdd:PRK13548    6 RNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHS 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 417 AL-FSGTIKDNIAYGR-----PNASEAEIIEAAkfanIHdfinslpkkyETQVAERGSR----LSGGERQRVAIARAILR 486
Cdd:PRK13548   86 SLsFPFTVEEVVAMGRaphglSRAEDDALVAAA----LA----------QVDLAHLAGRdypqLSGGEQQRVQLARVLAQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 487 ------DPRILILDEATSSLD-AETESLIRDALERLMKGRTTFI-IAHRL-YAVEHANRIVVIDNKQILEIGSHQELLQK 557
Cdd:PRK13548  152 lwepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAHERGLAVIvVLHDLnLAARYADRIVLLHQGRLVADGTPAEVLTP 231


                  .
gi 1277238834 558 D 558
Cdd:PRK13548  232 E 232
PTZ00243 PTZ00243
ABC transporter; Provisional
 332-554 5.28e-32

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 132.21  E-value: 5.28e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  332 GEINFENISFAYEN--EEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQI 409
Cdd:PTZ00243  1307 GSLVFEGVQMRYREglPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  410 AVVPQEIALFSGTIKDNIaygRP--NASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAIL-R 486
Cdd:PTZ00243  1387 SMIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLkK 1463

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834  487 DPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQEL 554
Cdd:PTZ00243  1464 GSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 348-554 7.18e-32

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: 122.61  E-value: 7.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTaKLESLRKQIAVVPQEIALFSG-TIKDN 426
Cdd:cd03263    17 AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFDElTVREH 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 427 IAY-----GRPNASEAEIIEAAkfanIHDFinSLPKKYETQVaergSRLSGGERQRVAIARAILRDPRILILDEATSSLD 501
Cdd:cd03263    96 LRFyarlkGLPKSEIKEEVELL----LRVL--GLTDKANKRA----RTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLD 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 502 AETESLIRDALERLMKGRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIGSHQEL 554
Cdd:cd03263   166 PASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
 34-308 9.84e-32

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: 124.21  E-value: 9.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  34 LIAPLVGYIF--QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNT 111
Cdd:cd18568    19 LALPLFTQIIldRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASRKV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 112 GELVSRVmNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAA 191
Cdd:cd18568    99 GDIITRF-QENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 192 DITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSL 271
Cdd:cd18568   178 EQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVISGQLTI 257

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1277238834 272 PQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18568   258 GQLVAFNMLFGSVINPLLALVGLWDELQETRISVERL 294
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 349-540 1.34e-31

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 128.22  E-value: 1.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQ--DIKTAKlESLRKQIAVVPQEIALFSG-TIKD 425
Cdd:COG3845    21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPR-DAIALGIGMVHQHFMLVPNlTVAE 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 426 NIAYGRPNASEAEI-IEAAKfANIHDFInslpKKYETQV--AERGSRLSGGERQRVAIARAILRDPRILILDEATSSL-D 501
Cdd:COG3845   100 NIVLGLEPTKGGRLdRKAAR-ARIRELS----ERYGLDVdpDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtP 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1277238834 502 AETESLIRdALERLMK-GRTTFIIAHRLYAV-EHANRIVVI 540
Cdd:COG3845   175 QEADELFE-ILRRLAAeGKSIIFITHKLREVmAIADRVTVL 214
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 334-554 2.00e-31

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: 121.32  E-value: 2.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIkTAKLESLRKQIAVVP 413
Cdd:cd03265     1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREPREVRRRIGIVF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIA-----YGRPNASEAE-IIEAAKFANIHDFINSLPKKYetqvaergsrlSGGERQRVAIARAILR 486
Cdd:cd03265    80 QDLSVDDElTGWENLYiharlYGVPGAERRErIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 487 DPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQEL 554
Cdd:cd03265   149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMeEAEQLCDRVAIIDHGRIIAEGTPEEL 219
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 1-495 2.41e-31

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: 127.99  E-value: 2.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   1 MKLYARLLKfikPYYSQIIGGTICTALV-TSTTLLIAplvgYIFQLIEDKNMFLLNLsALGMIGLFVLKGLFQYGQEYLS 79
Cdd:COG4615     1 MNLLRLLLR---ESRWLLLLALLLGLLSgLANAGLIA----LINQALNATGAALARL-LLLFAGLLVLLLLSRLASQLLL 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  80 YFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLqATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSL 159
Cdd:COG4615    73 TRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAYLAWLSPPLFL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 160 LTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVK-----SFAMEKEELakfKGKTEKSFDISMRA 234
Cdd:COG4615   152 LTLVLLGLGVAGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKlnrrrRRAFFDEDL---QPTAERYRDLRIRA 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 235 VQILATQNPVIALLqTIAVVGIVWFGGREIisGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI---FEV 311
Cdd:COG4615   229 DTIFALANNWGNLL-FFALIGLILFLLPAL--GWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIeelELA 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 312 LDVKPSIADLPGAKKLPRINGEINFENISFAYENEE-----VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPT 386
Cdd:COG4615   306 LAAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPE 385

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 387 SGRILVDGQDIKTAKLESLRKQIAVVPQEIALFSGTikdniaYGRPNASEAEIIEA--AKFanihdfinslpkKYETQVA 464
Cdd:COG4615   386 SGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDGEADPARAREllERL------------ELDHKVS 447

                         490       500       510
                  ....*....|....*....|....*....|....*.
gi 1277238834 465 ERGSR-----LSGGERQRVAIARAILRDPRILILDE 495
Cdd:COG4615   448 VEDGRfsttdLSQGQRKRLALLVALLEDRPILVFDE 483
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 348-546 1.44e-30

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: 119.46  E-value: 1.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIkTAKLESLRKQ--IAVVPQEIALFSG-TIK 424
Cdd:cd03219    15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI-TGLPPHEIARlgIGRTFQIPRLFPElTVL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 425 DNIAYG------------RPNASEAEIIEAAkfANIHDFINsLPKKYETQVAErgsrLSGGERQRVAIARAILRDPRILI 492
Cdd:cd03219    94 ENVMVAaqartgsglllaRARREEREARERA--EELLERVG-LADLADRPAGE----LSYGQQRRLEIARALATDPKLLL 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 493 LDEATSSL-DAETESLIrDALERL-MKGRTTFIIAHRLYAV-EHANRIVVIDNKQIL 546
Cdd:cd03219   167 LDEPAAGLnPEETEELA-ELIRELrERGITVLLVEHDMDVVmSLADRVTVLDQGRVI 222
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 349-554 1.66e-30

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 121.76  E-value: 1.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI---KTAKLESLRKQIAVVPQEialfsgtikd 425
Cdd:COG4608    34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDItglSGRELRPLRRRMQMVFQD---------- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 426 niaygrPNAS------EAEII-EAAKFANIHDfinslPKKYETQVAE----------RGSR----LSGGERQRVAIARAI 484
Cdd:COG4608   104 ------PYASlnprmtVGDIIaEPLRIHGLAS-----KAERRERVAEllelvglrpeHADRypheFSGGQRQRIGIARAL 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 485 LRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIGSHQEL 554
Cdd:COG4608   173 ALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 334-540 2.13e-30

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: 118.62  E-value: 2.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE----VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKqI 409
Cdd:cd03266     2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR-L 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFSG-TIKDNIAY-GR-----PNASEAEIIEAAKFANIHDFINslpkkyetqvaERGSRLSGGERQRVAIAR 482
Cdd:cd03266    81 GFVSDSTGLYDRlTARENLEYfAGlyglkGDELTARLEELADRLGMEELLD-----------RRVGGFSTGMRQKVAIAR 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 483 AILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIA-HRLYAVEH-ANRIVVI 540
Cdd:cd03266   150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVL 209
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
 34-308 2.24e-30

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: 120.68  E-value: 2.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  34 LIAPLvgyIFQLIEDK-----NMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAK 108
Cdd:cd18588    19 LVTPL---FFQVIIDKvlvhrSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFES 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 109 WNTGELVSRV--MNDI-QTLQATLFTGFVTLIpHSLLLLGLMgyiFWLNWQLSLLTLVALPLIVQVIRIFAKEIREISEG 185
Cdd:cd18588    96 RQVGDTVARVreLESIrQFLTGSALTLVLDLV-FSVVFLAVM---FYYSPTLTLIVLASLPLYALLSLLVTPILRRRLEE 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 186 VQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREII 265
Cdd:cd18588   172 KFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLVM 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1277238834 266 SGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18588   252 DGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQAKVSVERL 294
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 351-555 9.94e-30

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: 9.94e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 351 NINLKVKPGEIIALVGRTGAGKSTLTSL---LLRfydPTSGRILVDG---QDikTAKLESL---RKQIAVVPQEIALFSG 421
Cdd:COG4148    17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGevlQD--SARGIFLpphRRRIGYVFQEARLFPH 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 422 -TIKDNIAYGRPNASEAEiiEAAKFANIHDF--INSLpkkyetqvAERG-SRLSGGERQRVAIARAILRDPRILILDEAT 497
Cdd:COG4148    92 lSVRGNLLYGRKRAPRAE--RRISFDEVVELlgIGHL--------LDRRpATLSGGERQRVAIGRALLSSPRLLLMDEPL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 498 SSLDAETESLIRDALERLmkgRTTF-----IIAHRLYAVEH-ANRIVVIDNKQILEIGSHQELL 555
Cdd:COG4148   162 AALDLARKAEILPYLERL---RDELdipilYVSHSLDEVARlADHVVLLEQGRVVASGPLAEVL 222
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
338-554 8.55e-29

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 118.01  E-value: 8.55e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 338 NISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIktAKLESLRKQIAVVPQEIA 417
Cdd:PRK11607   24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL--SHVPPYQRPINMMFQSYA 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 418 LFSG-TIKDNIAYG--RPNASEAEII----EAAKFANIHDFINSLPKKyetqvaergsrLSGGERQRVAIARAILRDPRI 490
Cdd:PRK11607  102 LFPHmTVEQNIAFGlkQDKLPKAEIAsrvnEMLGLVHMQEFAKRKPHQ-----------LSGGQRQRVALARSLAKRPKL 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 491 LILDEATSSLDAETESLIR----DALERLmkGRTTFIIAH-RLYAVEHANRIVVIDNKQILEIGSHQEL 554
Cdd:PRK11607  171 LLLDEPMGALDKKLRDRMQlevvDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
334-556 8.59e-29

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 114.29  E-value: 8.59e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVlqNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDiKTAKLESlRKQIAVVP 413
Cdd:PRK10771    2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPS-RRPVSMLF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIAYG-----RPNASEAEIIEA-AKFANIHDFINSLPkkyetqvaergSRLSGGERQRVAIARAILR 486
Cdd:PRK10771   78 QENNLFSHlTVAQNIGLGlnpglKLNAAQREKLHAiARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVR 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 487 DPRILILDEATSSLD----AETESLIRDALERlmKGRTTFIIAHRLY-AVEHANRIVVIDNKQILEIGSHQELLQ 556
Cdd:PRK10771  147 EQPILLLDEPFSALDpalrQEMLTLVSQVCQE--RQLTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 331-541 8.88e-29

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 120.68  E-value: 8.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 331 NGEINFENISFAYENEEVL-QNINLKVKPGEIIALVGRTGAGKSTLtsllLR----FYDPTSGRILV-DGQDIktakles 404
Cdd:COG4178   360 DGALALEDLTLRTPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTL----LRaiagLWPYGSGRIARpAGARV------- 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 405 lrkqiAVVPQEIALFSGTIKDNIAYgrPNA----SEAEIIEAAKFANIHDFINSLpkkyeTQVAERGSRLSGGERQRVAI 480
Cdd:COG4178   429 -----LFLPQRPYLPLGTLREALLY--PATaeafSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAF 496

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 481 ARAILRDPRILILDEATSSLDAETESLIRDALERLMKGrTTFI-IAHRLYAVEHANRIVVID 541
Cdd:COG4178   497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPG-TTVIsVGHRSTLAAFHDRVLELT 557
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 348-546 1.05e-28

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


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 114.75  E-value: 1.05e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESL-RKQIAVVPQEIALFSG-TIKD 425
Cdd:COG0411    19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPElTVLE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 426 NIA-----------------YGRPNASEAEIIEAA----KFANIHDFINslpkkyetqvaERGSRLSGGERQRVAIARAI 484
Cdd:COG0411    99 NVLvaaharlgrgllaallrLPRARREEREARERAeellERVGLADRAD-----------EPAGNLSYGQQRRLEIARAL 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 485 LRDPRILILDEATSSL-DAETESLIrDALERLMK--GRTTFIIAHRLYAV-EHANRIVVIDNKQIL 546
Cdd:COG0411   168 ATEPKLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVmGLADRIVVLDFGRVI 232
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 334-528 1.06e-28

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


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 114.41  E-value: 1.06e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSG---RILvdGQDIKTAKLESLRKQIA 410
Cdd:COG1119     4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGGEDVWELRKRIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 411 VVPQEIAL---------------FSGTIkdniayGRPNASEAEIIEAA----KFANIHDFINslpKKYETqvaergsrLS 471
Cdd:COG1119    82 LVSPALQLrfprdetvldvvlsgFFDSI------GLYREPTDEQRERArellELLGLAHLAD---RPFGT--------LS 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 472 GGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK-GRTTFI-IAHRL 528
Cdd:COG1119   145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVlVTHHV 203
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 336-545 1.80e-28

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 119.01  E-value: 1.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 336 FENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQdiktakleslrKQIAVVPQE 415
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 416 IALFSG-TIKDNI----------------AYGRPNASEAEIIEAA----KFANIHDFinslpkKYETQVAE--------- 465
Cdd:COG0488    70 PPLDDDlTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAelqeEFEALGGW------EAEARAEEilsglgfpe 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 466 -----RGSRLSGGERQRVAIARAILRDPRILILDEATSSLDAETesliRDALERLMKGR--TTFIIAH-R--LYAVehAN 535
Cdd:COG0488   144 edldrPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEFLKNYpgTVLVVSHdRyfLDRV--AT 217

                         250
                  ....*....|
gi 1277238834 536 RIVVIDNKQI 545
Cdd:COG0488   218 RILELDRGKL 227
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 343-547 2.22e-28

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: 112.31  E-value: 2.22e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 343 YENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKtaKLESLRKQIAVVPQEIALFSG- 421
Cdd:cd03268    10 YGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRRIGALIEAPGFYPNl 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 422 TIKDNI-----AYGRPNASEAEIIEAAKFANIHDfinslpkkyetqvaERGSRLSGGERQRVAIARAILRDPRILILDEA 496
Cdd:cd03268    88 TARENLrllarLLGIRKKRIDEVLDVVGLKDSAK--------------KKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 497 TSSLDAETESLIRDALERLMK-GRTTFIIAHRLYAVEH-ANRIVVIDNKQILE 547
Cdd:cd03268   154 TNGLDPDGIKELRELILSLRDqGITVLISSHLLSEIQKvADRIGIINKGKLIE 206
cbiO PRK13644
energy-coupling factor transporter ATPase;
334-564 2.44e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 114.31  E-value: 2.44e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAY-ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI-KTAKLESLRKQIAV 411
Cdd:PRK13644    2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgDFSKLQGIRKLVGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQ--EIALFSGTIKDNIAYGRPNASEAEIieaakfanihdfinSLPKKYETQVAERG---------SRLSGGERQRVAI 480
Cdd:PRK13644   82 VFQnpETQFVGRTVEEDLAFGPENLCLPPI--------------EIRKRVDRALAEIGlekyrhrspKTLSGGQGQCVAL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 481 ARAILRDPRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDG 559
Cdd:PRK13644  148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227


                  ....*
gi 1277238834 560 LyKYL 564
Cdd:PRK13644  228 L-QTL 231
cbiO PRK13650
energy-coupling factor transporter ATPase;
334-554 3.12e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 114.06  E-value: 3.12e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE---VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIA 410
Cdd:PRK13650    5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 411 VVPQ--EIALFSGTIKDNIAYGRPNAS------EAEIIEAAKFANIHDFINSLPkkyetqvaergSRLSGGERQRVAIAR 482
Cdd:PRK13650   85 MVFQnpDNQFVGATVEDDVAFGLENKGipheemKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 483 AILRDPRILILDEATSSLDAETE-SLIRDALE-RLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQEL 554
Cdd:PRK13650  154 AVAMRPKIIILDEATSMLDPEGRlELIKTIKGiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 338-554 3.15e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 114.02  E-value: 3.15e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 338 NISFAY-ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLtslLLRF---YDPTSGRILVDGQDIKTAK--LESLRKQIAV 411
Cdd:PRK13639    6 DLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTL---FLHFngiLKPTSGEVLIKGEPIKYDKksLLEVRKTVGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQ--EIALFSGTIKDNIAYGRPNAS------EAEIIEAAKFANIHDFINSLPKkyetqvaergsRLSGGERQRVAIARA 483
Cdd:PRK13639   83 VFQnpDDQLFAPTVEEDVAFGPLNLGlskeevEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIAGI 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 484 ILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIA-HRLYAVE-HANRIVVIDNKQILEIGSHQEL 554
Cdd:PRK13639  152 LAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPvYADKVYVMSDGKIIKEGTPKEV 224
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
317-554 9.39e-28

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 114.16  E-value: 9.39e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 317 SIADLPGAKKlpriNGEINFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQD 396
Cdd:PRK13536   29 AKASIPGSMS----TVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 397 IKtAKLESLRKQIAVVPQEIAL-FSGTIKDN-IAYGRPNASEAEIIEAAkFANIHDFINsLPKKYETQVAErgsrLSGGE 474
Cdd:PRK13536  105 VP-ARARLARARIGVVPQFDNLdLEFTVRENlLVFGRYFGMSTREIEAV-IPSLLEFAR-LESKADARVSD----LSGGM 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 475 RQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAH----------RLYAVEHANRIV----- 538
Cdd:PRK13536  178 KRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHfmeeaerlcdRLCVLEAGRKIAegrph 257

                         250       260
                  ....*....|....*....|..
gi 1277238834 539 -VIDNK---QILEI--GSHQEL 554
Cdd:PRK13536  258 aLIDEHigcQVIEIygGDPHEL 279
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
337-556 9.73e-28

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 112.03  E-value: 9.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEI 416
Cdd:PRK11231    6 ENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHH 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 417 ALFSG-TIKDNIAYGRP---------NASEAEIIEAAkfanihdfinsLPKKYETQVAERG-SRLSGGERQRVAIARAIL 485
Cdd:PRK11231   86 LTPEGiTVRELVAYGRSpwlslwgrlSAEDNARVNQA-----------MEQTRINHLADRRlTDLSGGQRQRAFLAMVLA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 486 RDPRILILDEATSSLD----AETESLIRdalERLMKGRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQELLQ 556
Cdd:PRK11231  155 QDTPVVLLDEPTTYLDinhqVELMRLMR---ELNTQGKTVVTVLHDLnQASRYCDHLVVLANGHVMAQGTPEEVMT 227
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 333-527 1.15e-27

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: 109.95  E-value: 1.15e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 333 EINFENISFAYEN------EEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLL--LRFYDPTSGRILVDGQDIktaKLES 404
Cdd:cd03213     3 TLSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 405 LRKQIAVVPQEIALFSG-TIKDNIAYgrpnaseaeiieAAKFanihdfinslpkkyetqvaeRGsrLSGGERQRVAIARA 483
Cdd:cd03213    80 FRKIIGYVPQDDILHPTlTVRETLMF------------AAKL--------------------RG--LSGGERKRVSIALE 125

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1277238834 484 ILRDPRILILDEATSSLDAETESLIRDALERLMK-GRTTFIIAHR 527
Cdd:cd03213   126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQ 170
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 334-545 1.52e-27

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: 110.28  E-value: 1.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYEneEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAklESLRKQIAVVP 413
Cdd:cd03298     1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA--PPADRPVSMLF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIAYGRP-----NASEAEIIE-AAKFANIHDFINSLPKKyetqvaergsrLSGGERQRVAIARAILR 486
Cdd:cd03298    77 QENNLFAHlTVEQNVGLGLSpglklTAEDRQAIEvALARVGLAGLEKRLPGE-----------LSGGERQRVALARVLVR 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 487 DPRILILDEATSSLDaeteSLIRDALERLM------KGRTTFIIAHRLYAVEH-ANRIVVIDNKQI 545
Cdd:cd03298   146 DKPVLLLDEPFAALD----PALRAEMLDLVldlhaeTKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
cbiO PRK13640
energy-coupling factor transporter ATPase;
331-560 1.72e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 112.20  E-value: 1.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 331 NGEINFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSL---LLRFYDPTSGRILVDGQDIKTAKLESL 405
Cdd:PRK13640    3 DNIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLingLLLPDDNPNSKITVDGITLTAKTVWDI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 406 RKQIAVVPQ--EIALFSGTIKDNIAYGRPNA----SEAEIIEAAKFANIH--DFINSLPkkyetqvaergSRLSGGERQR 477
Cdd:PRK13640   83 REKVGIVFQnpDNQFVGATVGDDVAFGLENRavprPEMIKIVRDVLADVGmlDYIDSEP-----------ANLSGGQKQR 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 478 VAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEHANRIVVIDNKQIL------EIG 549
Cdd:PRK13640  152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLaqgspvEIF 231

                         250
                  ....*....|.
gi 1277238834 550 SHQELLQKDGL 560
Cdd:PRK13640  232 SKVEMLKEIGL 242
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 334-547 2.02e-27

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 115.93  E-value: 2.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVdGQDIKtakleslrkqIAVVP 413
Cdd:COG0488   316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGYFD 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG--TIKDNIAYGRPNASEAEIIE-AAKFanihDFInslPKKYETQVaergSRLSGGERQRVAIARAILRDPRI 490
Cdd:COG0488   385 QHQEELDPdkTVLDELRDGAPGGTEQEVRGyLGRF----LFS---GDDAFKPV----GVLSGGEKARLALAKLLLSPPNV 453

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 491 LILDEATSSLDAETesliRDALERLM---KGrTTFIIAHRLYAVEH-ANRIVVIDNKQILE 547
Cdd:COG0488   454 LLLDEPTNHLDIET----LEALEEALddfPG-TVLLVSHDRYFLDRvATRILEFEDGGVRE 509
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
 8-318 2.54e-27

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: 112.55  E-value: 2.54e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   8 LKFIKPYYSQIIGGTICTALVTSTTlliaPLVGYIF-QLIE-------DKNMFLLNLSALGMIGLFVLKGLFQYGQEYLS 79
Cdd:cd18578     1 LKLNKPEWPLLLLGLIGAIIAGAVF----PVFAILFsKLISvfslpddDELRSEANFWALMFLVLAIVAGIAYFLQGYLF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  80 YFVAQRIIVDLRNQVYEHL--QDLSldFY--AKWNTGELVSRVMNDIQTLQ-------ATLFTGFVTLIphsllllglMG 148
Cdd:cd18578    77 GIAGERLTRRLRKLAFRAIlrQDIA--WFddPENSTGALTSRLSTDASDVRglvgdrlGLILQAIVTLV---------AG 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 149 YI--FWLNWQLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEK 226
Cdd:cd18578   146 LIiaFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEE 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 227 SFDISMRAVQIlatQNPVIALLQTI--AVVGIV-WFGGREIISGSLSLPQL--ISFATALGIMTdPGNTLSKAYSiIQQG 301
Cdd:cd18578   226 PLKKGLRRALI---SGLGFGLSQSLtfFAYALAfWYGGRLVANGEYTFEQFfiVFMALIFGAQS-AGQAFSFAPD-IAKA 300

                         330
                  ....*....|....*..
gi 1277238834 302 MASTKRIFEVLDVKPSI 318
Cdd:cd18578   301 KAAAARIFRLLDRKPEI 317
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
338-557 2.79e-27

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 112.89  E-value: 2.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 338 NISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLEslRKQIAVVPQEIA 417
Cdd:PRK11432   11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 418 LFSG-TIKDNIAYG-----RPNASEAE-IIEAAKFANIHDFINslpkKYETQVaergsrlSGGERQRVAIARAILRDPRI 490
Cdd:PRK11432   89 LFPHmSLGENVGYGlkmlgVPKEERKQrVKEALELVDLAGFED----RYVDQI-------SGGQQQRVALARALILKPKV 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 491 LILDEATSSLDAETESLIRDALERLMK--GRTTFIIAH---RLYAVehANRIVVIDNKQILEIGSHQELLQK 557
Cdd:PRK11432  158 LLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHdqsEAFAV--SDTVIVMNKGKIMQIGSPQELYRQ 227
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 337-545 2.93e-27

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 110.54  E-value: 2.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDgqdikTAKLESLRKQIAVVPQEI 416
Cdd:PRK11247   16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG-----TAPLAEAREDTRLMFQDA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 417 ALFS-GTIKDNIAYG-----RPNASEAeiIEAAKFANihdfinslpkkyetQVAERGSRLSGGERQRVAIARAILRDPRI 490
Cdd:PRK11247   91 RLLPwKKVIDNVGLGlkgqwRDAALQA--LAAVGLAD--------------RANEWPAALSGGQKQRVALARALIHRPGL 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 491 LILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLY-AVEHANRIVVIDNKQI 545
Cdd:PRK11247  155 LLLDEPLGALDALTRIEMQDLIESLWQqhGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 337-563 7.38e-27

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 110.58  E-value: 7.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKleslRKQIAVVPQEI 416
Cdd:COG4152     5 KGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 417 ALFSG-TIKDNIAY-GR-PNASEAEIIEAA-----KFaNIHDFINslpKKYETqvaergsrLSGGERQRVAIARAILRDP 488
Cdd:COG4152    81 GLYPKmKVGEQLVYlARlKGLSKAEAKRRAdewleRL-GLGDRAN---KKVEE--------LSKGNQQKVQLIAALLHDP 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 489 RILILDEATSSLDAETESLIRDALERLM-KGRTtfII--AHRLYAVE-HANRIVVIDNKQILEIGSHQELLQKDGLYKY 563
Cdd:COG4152   149 ELLILDEPFSGLDPVNVELLKDVIRELAaKGTT--VIfsSHQMELVEeLCDRIVIINKGRKVLSGSVDEIRRQFGRNTL 225
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
348-547 7.67e-27

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 109.78  E-value: 7.67e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI---KTAKLESLRKQIAVVPQeialfsgtik 424
Cdd:PRK10419   27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklNRAQRKAFRRDIQMVFQ---------- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 425 DNIAYGRPNASEAEII-----------EAAKFANIHDFINS--LPkkyETQVAERGSRLSGGERQRVAIARAILRDPRIL 491
Cdd:PRK10419   97 DSISAVNPRKTVREIIreplrhllsldKAERLARASEMLRAvdLD---DSVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 492 ILDEATSSLDAETESLIRDALERLMKGRTT--FIIAHRLYAVEH-ANRIVVIDNKQILE 547
Cdd:PRK10419  174 ILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLRLVERfCQRVMVMDNGQIVE 232
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 337-564 8.16e-27

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 108.77  E-value: 8.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESL-RKQIAVVPQE 415
Cdd:TIGR03410   4 SNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 416 IALFSG-TIKDNIAYG---RPnASEAEIIEA--AKFANIHDFINslpkkyetqvaERGSRLSGGERQRVAIARAILRDPR 489
Cdd:TIGR03410  84 REIFPRlTVEENLLTGlaaLP-RRSRKIPDEiyELFPVLKEMLG-----------RRGGDLSGGQQQQLAIARALVTRPK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 490 ILILDEATS----SLDAETESLIRDAleRLMKGRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQElLQKDGLYKYL 564
Cdd:TIGR03410 152 LLLLDEPTEgiqpSIIKDIGRVIRRL--RAEGGMAILLVEQYLdFARELADRYYVMERGRVVASGAGDE-LDEDKVRRYL 228
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 337-538 8.38e-27

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 108.65  E-value: 8.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEI 416
Cdd:PRK10247   11 QNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTP 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 417 ALFSGTIKDNIAYG---RPNASEAEIIEA--AKFAnihdfinsLPkkyETQVAERGSRLSGGERQRVAIARAILRDPRIL 491
Cdd:PRK10247   91 TLFGDTVYDNLIFPwqiRNQQPDPAIFLDdlERFA--------LP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1277238834 492 ILDEATSSLDAETESLIRDALERLMKGRTTFII--AHRLYAVEHANRIV 538
Cdd:PRK10247  160 LLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVI 208
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 337-510 8.53e-27

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 107.95  E-value: 8.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDP---TSGRILVDGQDIktAKLESLRKQIAVVP 413
Cdd:COG4136     5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL--TALPAEQRRIGILF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIAYGRP-----NASEAEIIEAAKFANIHDFINSLPkkyetqvAErgsrLSGGERQRVAIARAILRD 487
Cdd:COG4136    83 QDDLLFPHlSVGENLAFALPptigrAQRRARVEQALEEAGLAGFADRDP-------AT----LSGGQRARVALLRALLAE 151

                         170       180
                  ....*....|....*....|...
gi 1277238834 488 PRILILDEATSSLDAETESLIRD 510
Cdd:COG4136   152 PRALLLDEPFSKLDAALRAQFRE 174
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 334-555 9.10e-27

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 109.07  E-value: 9.10e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAK--------LESL 405
Cdd:PRK11264    4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqkglIRQL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 406 RKQIAVVPQEIALFSG-TIKDNIAYGrPNASEAEIIEAAKfanihdfinSLPKKYETQVAERGS------RLSGGERQRV 478
Cdd:PRK11264   84 RQHVGFVFQNFNLFPHrTVLENIIEG-PVIVKGEPKEEAT---------ARARELLAKVGLAGKetsyprRLSGGQQQRV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 479 AIARAILRDPRILILDEATSSLD----AETESLIRDALErlmKGRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQE 553
Cdd:PRK11264  154 AIARALAMRPEVILFDEPTSALDpelvGEVLNTIRQLAQ---EKRTMVIVTHEMsFARDVADRAIFMDQGRIVEQGPAKA 230


                  ..
gi 1277238834 554 LL 555
Cdd:PRK11264  231 LF 232
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 333-557 1.43e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 109.72  E-value: 1.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 333 EINFENISFAYE-----NEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI----KTAKLE 403
Cdd:PRK13634    2 DITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 404 SLRKQIAVVPQ--EIALFSGTIKDNIAYGRPN--ASEAEIIEAAKfanihDFIN--SLPKKYETQvaergS--RLSGGER 475
Cdd:PRK13634   82 PLRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAR-----EMIElvGLPEELLAR-----SpfELSGGQM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 476 QRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLM--KGRTTFIIAHRLY-AVEHANRIVVIDNKQILEIGSHQ 552
Cdd:PRK13634  152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEdAARYADQIVVMHKGTVFLQGTPR 231


                  ....*
gi 1277238834 553 ELLQK 557
Cdd:PRK13634  232 EIFAD 236
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
342-540 2.10e-26

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 106.16  E-value: 2.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 342 AYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGqdiktakleslRKQIAVVPQEIAL--- 418
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRSEVpds 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 419 FSGTIKDNIAYG---------RPNASEAEIIEAAKFA-NIHDFINSlpkkyetQVAErgsrLSGGERQRVAIARAILRDP 488
Cdd:NF040873   70 LPLTVRDLVAMGrwarrglwrRLTRDDRAAVDDALERvGLADLAGR-------QLGE----LSGGQRQRALLAQGLAQEA 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 489 RILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLYAVEHANRIVVI 540
Cdd:NF040873  139 DLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
333-551 2.27e-26

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 107.79  E-value: 2.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 333 EINFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDG------QDIKTAKLESLR 406
Cdd:COG4161     2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 407 KQIAVVPQEIALFSG-TIKDNIAYGRPN----ASEAEIIEAAKFAN---IHDFINSLPkkyetqvaergSRLSGGERQRV 478
Cdd:COG4161    82 QKVGMVFQQYNLWPHlTVMENLIEAPCKvlglSKEQAREKAMKLLArlrLTDKADRFP-----------LHLSGGQQQRV 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 479 AIARAILRDPRILILDEATSSLDAETESLIRDALERLMK-GRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSH 551
Cdd:COG4161   151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVeFARKVASQVVYMEKGRIIEQGDA 225
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 348-547 2.29e-26

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 108.35  E-value: 2.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIktAKLEslRKQIAVVPQEIALfsgTIKDNI 427
Cdd:TIGR02769  26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDL--YQLD--RKQRRAFRRDVQL---VFQDSP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 428 AYGRPNASEAEII-----------EAAKFANIHDFINSLpkKYETQVAERGSR-LSGGERQRVAIARAILRDPRILILDE 495
Cdd:TIGR02769  99 SAVNPRMTVRQIIgeplrhltsldESEQKARIAELLDMV--GLRSEDADKLPRqLSGGQLQRINIARALAVKPKLIVLDE 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 496 ATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEH-ANRIVVIDNKQILE 547
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVE 231
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
 19-308 2.29e-26

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


Pssm-ID: 350018 [Multi-domain]  Cd Length: 295  Bit Score: 109.17  E-value: 2.29e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  19 IGGTICTALV-TSTTLLIAPLVGYIFQLIED---KNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQV 94
Cdd:cd18574     2 VLSALAAALVnIQIPLLLGDLVNVISRSLKEtngDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  95 YEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATlFTGFVTLIPHSL-LLLGLMGYIFWLNWQLSLLTLVALPLIVQVIR 173
Cdd:cd18574    82 FSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSS-FKQCVSQGLRSVtQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 174 IFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKsfdiSMRAVQILATQnpvIALLQTIA- 252
Cdd:cd18574   161 LYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEK----AAKLNEKLGLG---IGIFQGLSn 233

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 253 ------VVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18574   234 lalngiVLGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 334-560 2.65e-26

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 111.09  E-value: 2.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVP 413
Cdd:PRK09536    4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIAL-FSGTIKDNIAYGR-PNASEAEIIEAAKFANIHDFINslpKKYETQVAERG-SRLSGGERQRVAIARAILRDPRI 490
Cdd:PRK09536   84 QDTSLsFEFDVRQVVEMGRtPHRSRFDTWTETDRAAVERAME---RTGVAQFADRPvTSLSGGERQRVLLARALAQATPV 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 491 LILDEATSSLD----AETESLIRDALErlmKGRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQELLQKDGL 560
Cdd:PRK09536  161 LLLDEPTASLDinhqVRTLELVRRLVD---DGKTAVAAIHDLdLAARYCDELVLLADGRVRAAGPPADVLTADTL 232
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 348-544 3.42e-26

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: 106.75  E-value: 3.42e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILV--DGQDIKTAKLE-----SLRKQ-IA-------VV 412
Cdd:COG4778    26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASpreilALRRRtIGyvsqflrVI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 PQEIALfsgtikDNIAygRP----NASEAEIIEAAKfanihDFINSLpkkyetQVAERGSRL-----SGGERQRVAIARA 483
Cdd:COG4778   106 PRVSAL------DVVA--EPllerGVDREEARARAR-----ELLARL------NLPERLWDLppatfSGGEQQRVNIARG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 484 ILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFI-IAHRLYAVEH-ANRIVVIDNKQ 544
Cdd:COG4778   167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPFS 229
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 347-547 3.90e-26

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


Pssm-ID: 443338 [Multi-domain]  Cd Length: 233  Bit Score: 106.75  E-value: 3.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 347 EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKT------AKLesLRKQIAVVPQEIALFS 420
Cdd:COG4181    26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldedarARL--RARHVGFVFQSFQLLP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 421 G-TIKDNIAY-----GRPNASE--AEIIEAAKfanihdfinslpkkyetqVAERG----SRLSGGERQRVAIARAILRDP 488
Cdd:COG4181   104 TlTALENVMLplelaGRRDARAraRALLERVG------------------LGHRLdhypAQLSGGEQQRVALARAFATEP 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 489 RILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEHANRIVVIDNKQILE 547
Cdd:COG4181   166 AILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 349-556 4.88e-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: 112.09  E-value: 4.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFyDPTSGRILVDGQDI---KTAKLESLRKQIAVVPQEIalFSG---- 421
Cdd:COG4172   302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLdglSRRALRPLRRRMQVVFQDP--FGSlspr 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 422 -TIKDNIAYG----RPNASEAE----IIEA-------AKFAN--IHDFinslpkkyetqvaergsrlSGGERQRVAIARA 483
Cdd:COG4172   379 mTVGQIIAEGlrvhGPGLSAAErrarVAEAleevgldPAARHryPHEF-------------------SGGQRQRIAIARA 439

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 484 ILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIGSHQELLQ 556
Cdd:COG4172   440 LILEPKLLVLDEPTSALDVSVQAQILDLLRDLQRehGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 334-557 5.66e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 107.53  E-value: 5.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE--VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAV 411
Cdd:PRK13648    8 IVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQ--EIALFSGTIKDNIAYGRPNAS------EAEIIEAAKFANIHDFINSLPKKyetqvaergsrLSGGERQRVAIARA 483
Cdd:PRK13648   88 VFQnpDNQFVGSIVKYDVAFGLENHAvpydemHRRVSEALKQVDMLERADYEPNA-----------LSGGQKQRVAIAGV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 484 ILRDPRILILDEATSSLDAETESLIRDALERLM--KGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQK 557
Cdd:PRK13648  157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKseHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 349-549 7.33e-26

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


Pssm-ID: 213264 [Multi-domain]  Cd Length: 214  Bit Score: 105.45  E-value: 7.33e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVK---PGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI----KTAKLESLRKQIAVVPQEIALFSG 421
Cdd:cd03297    10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYALFPH 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 422 -TIKDNIAYGRPNASEAEI-IEAAKFANIHDfINSLPKKYETQvaergsrLSGGERQRVAIARAILRDPRILILDEATSS 499
Cdd:cd03297    90 lNVRENLAFGLKRKRNREDrISVDELLDLLG-LDHLLNRYPAQ-------LSGGEKQRVALARALAAQPELLLLDEPFSA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 500 LDAETESLIRDALERLMK--GRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIG 549
Cdd:cd03297   162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
 18-308 7.57e-26

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350021 [Multi-domain]  Cd Length: 300  Bit Score: 107.56  E-value: 7.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  18 IIGGTICTALVTSTTLLIAPLVGYIFQLI-------EDKNMFL--LNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIV 88
Cdd:cd18577     1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFtdfgsgeSSPDEFLddVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  89 DLRNQVYEHL--QDLSldFYAKWNTGELVSRVMNDIQTLQ-------ATLFTGFVTLIphSLLLLGlmgyiFWLNWQLSL 159
Cdd:cd18577    81 RIRKRYLKALlrQDIA--WFDKNGAGELTSRLTSDTNLIQdgigeklGLLIQSLSTFI--AGFIIA-----FIYSWKLTL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 160 LTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILA 239
Cdd:cd18577   152 VLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSG 231

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 240 TQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLIS--FATALGIMtdpgnTLSKA---YSIIQQGMASTKRI 308
Cdd:cd18577   232 LGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTvfFAVLIGAF-----SLGQIapnLQAFAKARAAAAKI 300
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 337-556 1.06e-25

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: 105.70  E-value: 1.06e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKL-ESLRKQIAVVPQE 415
Cdd:cd03218     4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 416 IALFSG-TIKDNI--AYGRPNASEAEIIEAAKfANIHDF-INSLPKKyetqvaeRGSRLSGGERQRVAIARAILRDPRIL 491
Cdd:cd03218    84 ASIFRKlTVEENIlaVLEIRGLSKKEREEKLE-ELLEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFL 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 492 ILDEATSSLDAETESLIRDALERLM-KG----------RTTFIIAHRLYavehanrivVIDNKQILEIGSHQELLQ 556
Cdd:cd03218   156 LLDEPFAGVDPIAVQDIQKIIKILKdRGigvlitdhnvRETLSITDRAY---------IIYEGKVLAEGTPEEIAA 222
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
334-560 1.15e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 106.71  E-value: 1.15e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEE------VLQNINLKVKPGEIIALVGRTGAGKSTLT----SLLLrfydPTSGRILVDGQDIKTAK-L 402
Cdd:PRK13633    5 IKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAkhmnALLI----PSEGKVYVDGLDTSDEEnL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 403 ESLRKQIAVVPQ--EIALFSGTIKDNIAYGRPNAS-EAEII-----EAAKFANIHDFinslpKKYETQVaergsrLSGGE 474
Cdd:PRK13633   81 WDIRNKAGMVFQnpDNQIVATIVEEDVAFGPENLGiPPEEIrervdESLKKVGMYEY-----RRHAPHL------LSGGQ 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 475 RQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEHANRIVVIDNKQIL------ 546
Cdd:PRK13633  150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVmegtpk 229

                         250
                  ....*....|....
gi 1277238834 547 EIGSHQELLQKDGL 560
Cdd:PRK13633  230 EIFKEVEMMKKIGL 243
cbiO PRK13645
energy-coupling factor transporter ATPase;
331-568 1.42e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 106.63  E-value: 1.42e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 331 NGEINFENISFAYENE-----EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI-----KTA 400
Cdd:PRK13645    4 SKDIILDNVSYTYAKKtpfefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 401 KLESLRKQIAVVPQ--EIALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFInSLPKKYetqvAERGS-RLSGGERQR 477
Cdd:PRK13645   84 EVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPEDY----VKRSPfELSGGQKRR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 478 VAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAV-EHANRIVVIDNKQILEIG----- 549
Cdd:PRK13645  159 VALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfei 238

                         250       260
                  ....*....|....*....|....*
gi 1277238834 550 -SHQELLQK-----DGLYKYLYAIQ 568
Cdd:PRK13645  239 fSNQELLTKieidpPKLYQLMYKLK 263
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 331-554 1.65e-25

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: 106.48  E-value: 1.65e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 331 NGEINFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGqdiktakleslrkQIA 410
Cdd:cd03291    35 SDDNNLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RIS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 411 VVPQEIALFSGTIKDNIAYGRpNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRI 490
Cdd:cd03291   102 FSSQFSWIMPGTIKENIIFGV-SYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADL 180

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 491 LILDEATSSLDAETESLIRDA-LERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQEL 554
Cdd:cd03291   181 YLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
334-546 1.94e-25

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 104.96  E-value: 1.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI---KTAKLesLRKQIA 410
Cdd:PRK11614    6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDItdwQTAKI--MREAVA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 411 VVPQEIALFSG-TIKDNIAYGRPNASEAEIIEaaKFANIHDFinsLPKKYETQvAERGSRLSGGERQRVAIARAILRDPR 489
Cdd:PRK11614   84 IVPEGRRVFSRmTVEENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERR-IQRAGTMSGGEQQMLAIGRALMSQPR 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 490 ILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRL-YAVEHANRIVVIDNKQIL 546
Cdd:PRK11614  158 LLLLDEPSLGLAPIIIQQIFDTIEQLReQGMTIFLVEQNAnQALKLADRGYVLENGHVV 216
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
 12-308 2.25e-25

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: 106.14  E-value: 2.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  12 KPYYSQIIGGTICTALVTsttlLIAPLvgyIFQLIEDK-----NMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRI 86
Cdd:cd18782     1 RRALIEVLALSFVVQLLG----LANPL---LFQVIIDKvlvqqDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  87 IVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVmNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALP 166
Cdd:cd18782    74 DLELGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 167 LIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIA 246
Cdd:cd18782   153 LQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQ 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 247 LLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18782   233 FLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQELRVSLERL 294
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 330-558 2.36e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 105.59  E-value: 2.36e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 330 INGEINFENISFAYEN-EEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQ 408
Cdd:PRK13647    1 MDNIIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 409 IAVVPQEI--ALFSGTIKDNIAYGRPNA--SEAEII----EAAKFANIHDFINSLPKkyetqvaergsRLSGGERQRVAI 480
Cdd:PRK13647   81 VGLVFQDPddQVFSSTVWDDVAFGPVNMglDKDEVErrveEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 481 ARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIA-HRL-YAVEHANRIVVIDNKQILEIGSHQELLQKD 558
Cdd:PRK13647  150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVdLAAEWADQVIVLKEGRVLAEGDKSLLTDED 229
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
338-554 2.89e-25

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 107.42  E-value: 2.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 338 NISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQ---DIKTAKleslrKQIAVVPQ 414
Cdd:PRK11000    8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKrmnDVPPAE-----RGVGMVFQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 415 EIALFSG-TIKDNIAYGR--PNASEAEII----EAAKFANIHDFINSLPKKyetqvaergsrLSGGERQRVAIARAILRD 487
Cdd:PRK11000   83 SYALYPHlSVAENMSFGLklAGAKKEEINqrvnQVAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLVAE 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 488 PRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAH-RLYAVEHANRIVVIDNKQILEIGSHQEL 554
Cdd:PRK11000  152 PSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 337-537 2.97e-25

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 104.86  E-value: 2.97e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYD-----PTSGRILVDGQDIKTAKLES--LRKQI 409
Cdd:PRK14239    9 SDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRKEI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFSGTIKDNIAYG-RPNA-SEAEIIEAA-----KFANIHDFINSlpKKYETQVAergsrLSGGERQRVAIAR 482
Cdd:PRK14239   89 GMVFQQPNPFPMSIYENVVYGlRLKGiKDKQVLDEAvekslKGASIWDEVKD--RLHDSALG-----LSGGQQQRVCIAR 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 483 AILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLyavEHANRI 537
Cdd:PRK14239  162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSM---QQASRI 213
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 352-555 3.18e-25

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: 107.12  E-value: 3.18e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 352 INLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAK----LESLRKQIAVVPQEIALFSG-TIKDN 426
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRkgifLPPEKRRIGYVFQEARLFPHlSVRGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 427 IAYGR-------PNASEAEIIEaakFANIHDFINSLPkkyetqvaergSRLSGGERQRVAIARAILRDPRILILDEATSS 499
Cdd:TIGR02142  96 LRYGMkrarpseRRISFERVIE---LLGIGHLLGRLP-----------GRLSGGEKQRVAIGRALLSSPRLLLMDEPLAA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 500 LDAETESLIRDALERLMK--GRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIGSHQELL 555
Cdd:TIGR02142 162 LDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVW 220
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
334-557 3.81e-25

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 106.85  E-value: 3.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENE-EVLQNINLKVKPGEIIALVGRTGAGKSTLtsllLRFY----DPTSGRILVDGQDIKTakLESLRKQ 408
Cdd:PRK11650    4 LKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTL----LRMVagleRITSGEIWIGGRVVNE--LEPADRD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 409 IAVVPQEIALFSG-TIKDNIAYGRPNA--SEAEI----IEAAKFANIHDFINSLPKKyetqvaergsrLSGGERQRVAIA 481
Cdd:PRK11650   78 IAMVFQNYALYPHmSVRENMAYGLKIRgmPKAEIeervAEAARILELEPLLDRKPRE-----------LSGGQRQRVAMG 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 482 RAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAH-RLYAVEHANRIVVIDNKQILEIGSHQELLQK 557
Cdd:PRK11650  147 RAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVAEQIGTPVEVYEK 225
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
334-539 4.00e-25

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 104.56  E-value: 4.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYEN----EEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESlrkqi 409
Cdd:COG4525     4 LTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR----- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALFSG-TIKDNIAYGrpnaseaeiieaAKFAnihdfinSLPKKYETQVAER----------GSR----LSGGE 474
Cdd:COG4525    79 GVVFQKDALLPWlNVLDNVAFG------------LRLR-------GVPKAERRARAEEllalvgladfARRriwqLSGGM 139

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 475 RQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHrlyAVEHA----NRIVV 539
Cdd:COG4525   140 RQRVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITH---SVEEAlflaTRLVV 207
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 334-531 6.26e-25

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 104.35  E-value: 6.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTS-----GRILVDGQDI--KTAKLESLR 406
Cdd:PRK14258    8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRLR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 407 KQIAVVPQEIALFSGTIKDNIAYG------RPNASEAEIIEAA-KFANIHDFInslpkkyETQVAERGSRLSGGERQRVA 479
Cdd:PRK14258   88 RQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESAlKDADLWDEI-------KHKIHKSALDLSGGQQQRLC 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 480 IARAILRDPRILILDEATSSLDA----ETESLIRDAleRLMKGRTTFIIAHRLYAV 531
Cdd:PRK14258  161 IARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSL--RLRSELTMVIVSHNLHQV 214
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 58-571 7.28e-25

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: 110.00  E-value: 7.28e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834   58 ALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATL-FTGFVTL 136
Cdd:TIGR01271  125 ALGLCLLFIVRTLLLHPAIFGLHHLGMQMRIALFSLIYKKTLKLSSRVLDKISTGQLVSLLSNNLNKFDEGLaLAHFVWI 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  137 IPHSLLLLglMGYIFWLnwqLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHL---QETISQVKTVKSF--- 210
Cdd:TIGR01271  205 APLQVILL--MGLIWEL---LEVNGFCGLGFLILLALFQACLGQKMMPYRDKRAGKISERLaitSEIIENIQSVKAYcwe 279

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  211 -AMEK-------------EELAKFKGKTEKSFDISMRAVQILATQNpvIALLQTIAVVGIVWFGGREII---SGSLSLPQ 273
Cdd:TIGR01271  280 eAMEKiiknirqdelkltRKIAYLRYFYSSAFFFSGFFVVFLSVVP--YALIKGIILRRIFTTISYCIVlrmTVTRQFPG 357

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  274 LI-SFATALGIMTDPGNTLSK-AYSIIQQGMASTKriFEVLDVKPS----IADL-------PGAKKLPRINGEINFENis 340
Cdd:TIGR01271  358 AIqTWYDSLGAITKIQDFLCKeEYKTLEYNLTTTE--VEMVNVTASwdegIGELfekikqnNKARKQPNGDDGLFFSN-- 433

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  341 FAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQdiktakleslrkqIAVVPQEIALFS 420
Cdd:TIGR01271  434 FSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMP 500

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  421 GTIKDNIAYGRpNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRILILDEATSSL 500
Cdd:TIGR01271  501 GTIKDNIIFGL-SYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHL 579

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834  501 DAETESLIRDA-LERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQEL--LQKDGLYKYLYAIQFNN 571
Cdd:TIGR01271  580 DVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELqaKRPDFSSLLLGLEAFDN 653
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
349-555 8.00e-25

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 106.66  E-value: 8.00e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQD---IKTAKL-ESLRKQIAVVPQEIALFSG-TI 423
Cdd:PRK10070   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDiakISDAELrEVRRKKIAMVFQSFALMPHmTV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 424 KDNIAYGRPNAS------EAEIIEAAKFANIHDFINSLPKKyetqvaergsrLSGGERQRVAIARAILRDPRILILDEAT 497
Cdd:PRK10070  124 LDNTAFGMELAGinaeerREKALDALRQVGLENYAHSYPDE-----------LSGGMRQRVGLARALAINPDILLMDEAF 192

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 498 SSLDAETESLIRDALERLMKG--RTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQELL 555
Cdd:PRK10070  193 SALDPLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
cbiO PRK13649
energy-coupling factor transporter ATPase;
334-557 1.64e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 103.29  E-value: 1.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYE-----NEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI----KTAKLES 404
Cdd:PRK13649    3 INLQNVSYTYQagtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 405 LRKQIAVVPQ--EIALFSGTIKDNIAYGRPN----ASEAEIIEAAKFANI---HDFINSLPkkYEtqvaergsrLSGGER 475
Cdd:PRK13649   83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQNfgvsQEEAEALAREKLALVgisESLFEKNP--FE---------LSGGQM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 476 QRVAIARAILRDPRILILDEATSSLDAETESLIRDALERL-MKGRTTFIIAHRLYAV-EHANRIVVIDNKQILEIGSHQE 553
Cdd:PRK13649  152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKD 231


                  ....
gi 1277238834 554 LLQK 557
Cdd:PRK13649  232 IFQD 235
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 349-548 1.73e-24

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: 102.16  E-value: 1.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLrkqiaVVPQEIALFSG-TIKDNI 427
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPWlTVRENI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 428 AYG----RPNASEAE---IIEAakfaniHDFINSLpkkyeTQVAE-RGSRLSGGERQRVAIARAILRDPRILILDEATSS 499
Cdd:TIGR01184  76 ALAvdrvLPDLSKSErraIVEE------HIALVGL-----TEAADkRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 500 LDAETESLIRdalERLMK-----GRTTFIIAHRL-YAVEHANRIVVIDN------KQILEI 548
Cdd:TIGR01184 145 LDALTRGNLQ---EELMQiweehRVTVLMVTHDVdEALLLSDRVVMLTNgpaaniGQILEV 202
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 348-550 1.92e-24

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 102.47  E-value: 1.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGqdiktaKLESLrkqIAV----VPQeialFSGti 423
Cdd:COG1134    41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------RVSAL---LELgagfHPE----LTG-- 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 424 KDNI-----AYGRP----NASEAEIIEaakFANIHDFINsLP-KKYetqvaergsrlSGGERQRVAIARAILRDPRILIL 493
Cdd:COG1134   106 RENIylngrLLGLSrkeiDEKFDEIVE---FAELGDFID-QPvKTY-----------SSGMRARLAFAVATAVDPDILLV 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 494 DEATSSLDAETESLIRDALERLMK-GRTTFIIAHRLYAV-EHANRIVVIDNKQILEIGS 550
Cdd:COG1134   171 DEVLAVGDAAFQKKCLARIRELREsGRTVIFVSHSMGAVrRLCDRAIWLEKGRLVMDGD 229
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 348-545 2.26e-24

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 102.47  E-value: 2.26e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIkTAKLESLR-KQIAVVPQEIAL---FSGTI 423
Cdd:COG1101    21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKRaKYIGRVFQDPMMgtaPSMTI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 424 KDN--IAYGR----------PNASEAEIIEAAKfanihDFINSLPKKYETQVaerGSrLSGGERQRVAIARAILRDPRIL 491
Cdd:COG1101   100 EENlaLAYRRgkrrglrrglTKKRRELFRELLA-----TLGLGLENRLDTKV---GL-LSGGQRQALSLLMATLTKPKLL 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 492 ILDEATSSLDAETESLIRDALERLMKGR--TTFIIAHRL-YAVEHANRIVVIDNKQI 545
Cdd:COG1101   171 LLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMeQALDYGNRLIMMHEGRI 227
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
 26-277 2.48e-24

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


Pssm-ID: 350011 [Multi-domain]  Cd Length: 294  Bit Score: 103.31  E-value: 2.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  26 ALVTSTTLLIAPlvgYIFQLIED-----KNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQD 100
Cdd:cd18567    11 SLALELFALASP---LYLQLVIDevivsGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 101 LSLDFYAKWNTGELVSRVmNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALpLIVQVIRIFA-KEI 179
Cdd:cd18567    88 LPLSYFEKRHLGDIVSRF-GSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAV-ALYALLRLALyPPL 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 180 REISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWF 259
Cdd:cd18567   166 RRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYL 245

                         250
                  ....*....|....*...
gi 1277238834 260 GGREIISGSLSLPQLISF 277
Cdd:cd18567   246 GALLVLDGEFTVGMLFAF 263
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
 23-308 2.82e-24

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: 102.97  E-value: 2.82e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  23 ICTALVTSTTLLIAPLVGYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDL 101
Cdd:cd18555     9 LLSLLLQLLTLLIPILTQYVIdNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 102 SLDFYAKWNTGELVSRvMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAKEIRE 181
Cdd:cd18555    89 PYSFFENRSSGDLLFR-ANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 182 ISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGG 261
Cdd:cd18555   168 LNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIAPLLILWIGA 247

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1277238834 262 REIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18555   248 YLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFILLKSYLERL 294
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
334-558 3.10e-24

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 103.35  E-value: 3.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESlRKQIAVVP 413
Cdd:PRK13537    8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGVVP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIAL---FsgTIKDNI-AYGRPNASEAEIIEAA-----KFANihdfinsLPKKYETQVAErgsrLSGGERQRVAIARAI 484
Cdd:PRK13537   87 QFDNLdpdF--TVRENLlVFGRYFGLSAAAARALvppllEFAK-------LENKADAKVGE----LSGGMKRRLTLARAL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 485 LRDPRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIGSHQELLQKD 558
Cdd:PRK13537  154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIESE 229
PTZ00243 PTZ00243
ABC transporter; Provisional
 341-572 4.23e-24

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 107.56  E-value: 4.23e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  341 FAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDgqdiktakleslrKQIAVVPQEIALFS 420
Cdd:PTZ00243   668 FELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMN 734

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  421 GTIKDNIAYGRPNaSEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRILILDEATSSL 500
Cdd:PTZ00243   735 ATVRGNILFFDEE-DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277238834  501 DAET-ESLIRDALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELLQKDgLYKYLYAIQFNNK 572
Cdd:PTZ00243   814 DAHVgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS-LYATLAAELKENK 885
cbiO PRK13641
energy-coupling factor transporter ATPase;
334-560 5.43e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 102.21  E-value: 5.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQ-----NINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIK----TAKLES 404
Cdd:PRK13641    3 IKFENVDYIYSPGTPMEkkgldNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 405 LRKQIAVVPQ--EIALFSGTIKDNIAYGRPN--ASEAEIIEAA-----KFANIHDFINSLPkkYEtqvaergsrLSGGER 475
Cdd:PRK13641   83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDEAKEKAlkwlkKVGLSEDLISKSP--FE---------LSGGQM 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 476 QRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK-GRTTFIIAHRLYAV-EHANRIVVIDNKQIL------E 547
Cdd:PRK13641  152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKaGHTVILVTHNMDDVaEYADDVLVLEHGKLIkhaspkE 231

                         250
                  ....*....|...
gi 1277238834 548 IGSHQELLQKDGL 560
Cdd:PRK13641  232 IFSDKEWLKKHYL 244
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 334-560 7.29e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 101.42  E-value: 7.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYE-NEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVV 412
Cdd:PRK13652    4 IETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 PQ--EIALFSGTIKDNIAYGRPN------ASEAEIIEAAKFANIHDFINSLPKkyetqvaergsRLSGGERQRVAIARAI 484
Cdd:PRK13652   84 FQnpDDQIFSPTVEQDIAFGPINlgldeeTVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVI 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 485 LRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAV-EHANRIVVIDNKQILEIGSHQELLQKDGL 560
Cdd:PRK13652  153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 337-557 1.06e-23

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 100.14  E-value: 1.06e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRF--YDPTSGRILVDGQDIKTAKL-ESLRKQIAVV- 412
Cdd:COG0396     4 KNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPdERARAGIFLAf 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 --PQEI-----ALFSGTIKDNIAYGRPNASE--AEIIEAAKFANI-HDFINSlpkkyetQVAErGsrLSGGERQRVAIAR 482
Cdd:COG0396    84 qyPVEIpgvsvSNFLRTALNARRGEELSAREflKLLKEKMKELGLdEDFLDR-------YVNE-G--FSGGEKKRNEILQ 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 483 AILRDPRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAH--RLYAVEHANRIVVIDNKQILEIGSHqELLQK 557
Cdd:COG0396   154 MLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGK-ELALE 230
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
336-528 1.07e-23

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 104.61  E-value: 1.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 336 FENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIK-TAKLESLRKQIAVVPQ 414
Cdd:PRK11288    7 FDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGVAIIYQ 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 415 EIALFsgtikdniaygrPNASEAEIIEAAKFANIHDFINSLPKKYET--QVAERG---------SRLSGGERQRVAIARA 483
Cdd:PRK11288   87 ELHLV------------PEMTVAENLYLGQLPHKGGIVNRRLLNYEAreQLEHLGvdidpdtplKYLSIGQRQMVEIAKA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1277238834 484 ILRDPRILILDEATSSLDA-ETESLIRDALERLMKGRTTFIIAHRL 528
Cdd:PRK11288  155 LARNARVIAFDEPTSSLSArEIEQLFRVIRELRAEGRVILYVSHRM 200
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 334-557 1.58e-23

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: 104.11  E-value: 1.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLL--LRFYDPTSGRIL-------------------- 391
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIyhvalcekcgyverpskvge 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 392 -------------VDGQDIKTAKLESLRKQIAVVPQE-IALFSG-TIKDNIAYGRPNAsEAEIIEAAKFAniHDFINSLp 456
Cdd:TIGR03269  81 pcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRtFALYGDdTVLDNVLEALEEI-GYEGKEAVGRA--VDLIEMV- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 457 kKYETQVAERGSRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEH- 533
Cdd:TIGR03269 157 -QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDl 235

                         250       260
                  ....*....|....*....|....
gi 1277238834 534 ANRIVVIDNKQILEIGSHQELLQK 557
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAV 259
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
337-567 1.60e-23

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 100.25  E-value: 1.60e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEI 416
Cdd:PRK10575   15 RNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 417 ALFSG-TIKDNIAYGR-P---------NASEAEIIEAAKFANIHDFINSLPKKyetqvaergsrLSGGERQRVAIARAIL 485
Cdd:PRK10575   95 PAAEGmTVRELVAIGRyPwhgalgrfgAADREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIAMLVA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 486 RDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIA--HRL-YAVEHANRIVVIDNKQILEIGSHQELLQKDGLYK 562
Cdd:PRK10575  164 QDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDInMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQ 243


                  ....*
gi 1277238834 563 yLYAI 567
Cdd:PRK10575  244 -IYGI 247
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 337-557 1.80e-23

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: 98.37  E-value: 1.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRF--YDPTSGRILVDGQDIKTAKL-ESLRKQIAVVP 413
Cdd:cd03217     4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPeERARLGIFLAF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSGTikdniaygrpnaseaeiieaakfaNIHDFINSLPKKyetqvaergsrLSGGERQRVAIARAILRDPRILIL 493
Cdd:cd03217    84 QYPPEIPGV------------------------KNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAIL 128

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 494 DEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLYAVEH--ANRIVVIDNKQILEIGShQELLQK 557
Cdd:cd03217   129 DEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDYikPDRVHVLYDGRIVKSGD-KELALE 194
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 334-544 2.99e-23

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: 95.59  E-value: 2.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVdGQDIKtakleslrkqIAVVP 413
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IGYFE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QeialfsgtikdniaygrpnaseaeiieaakfanihdfinslpkkyetqvaergsrLSGGERQRVAIARAILRDPRILIL 493
Cdd:cd03221    70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 494 DEATSSLDAETesliRDALERLMKG--RTTFIIAHRLYAVEH-ANRIVVIDNKQ 544
Cdd:cd03221    95 DEPTNHLDLES----IEALEEALKEypGTVILVSHDRYFLDQvATKIIELEDGK 144
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 338-540 4.01e-23

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 102.82  E-value: 4.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 338 NISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQdiKTAKLESLRKQ---IAVVPQ 414
Cdd:PRK15439   16 SISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGN--PCARLTPAKAHqlgIYLVPQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 415 EIALFSG-TIKDNIAYGRPNASEAEiieaakfanihdfinslpKKYETQVAERGSRLS---------GGERQRVAIARAI 484
Cdd:PRK15439   94 EPLLFPNlSVKENILFGLPKRQASM------------------QKMKQLLAALGCQLDldssagsleVADRQIVEILRGL 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 485 LRDPRILILDEATSSLD-AETESLIRDALERLMKGRTTFIIAHRLYAV-EHANRIVVI 540
Cdd:PRK15439  156 MRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVM 213
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 349-542 4.22e-23

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: 97.79  E-value: 4.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESL----RKQIAVVPQEIALFSGTIK 424
Cdd:cd03290    17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAAQKPWLLNATVE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 425 DNIAYGRP-NASEAEIIEAAkfANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRDPRILILDEATSSLDAE 503
Cdd:cd03290    97 ENITFGSPfNKQRYKAVTDA--CSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1277238834 504 -TESLIRDALERLMKG--RTTFIIAHRLYAVEHANRIVVIDN 542
Cdd:cd03290   175 lSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKD 216
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 349-545 4.79e-23

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 102.70  E-value: 4.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYdPT---SGRILVDGQDIKTAKL-ESLRKQIAVVPQEIALFSG-TI 423
Cdd:PRK13549   21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIrDTERAGIAIIHQELALVKElSV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 424 KDNI-------AYGRPNaSEAEIIEAAK-FANIHDFINslpkkyetqVAERGSRLSGGERQRVAIARAILRDPRILILDE 495
Cdd:PRK13549  100 LENIflgneitPGGIMD-YDAMYLRAQKlLAQLKLDIN---------PATPVGNLGLGQQQLVEIAKALNKQARLLILDE 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 496 ATSSL-DAETESL---IRDaLERlmKGRTTFIIAHRLYAVEH-ANRIVVI-DNKQI 545
Cdd:PRK13549  170 PTASLtESETAVLldiIRD-LKA--HGIACIYISHKLNEVKAiSDTICVIrDGRHI 222
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 334-545 5.97e-23

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: 96.97  E-value: 5.97e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKleslRKQIAVVP 413
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIAY-----GRPNAseaeiiEAAKfaNIHDFINSLP-KKYETQVAErgsRLSGGERQRVAIARAILR 486
Cdd:cd03269    77 EERGLYPKmKVIDQLVYlaqlkGLKKE------EARR--RIDEWLERLElSEYANKRVE---ELSKGNQQKVQFIAAVIH 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 487 DPRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLYAVEH-ANRIVVIDNKQI 545
Cdd:cd03269   146 DPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRA 206
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 334-552 7.21e-23

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 97.78  E-value: 7.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDG------QDIKTAKLESLRK 407
Cdd:PRK11124    3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRELRR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 408 QIAVVPQEIALFSG-TIKDNIaygrpnaseaeiIEA-------AKFANIHDFINSLPKKYETQVAERGS-RLSGGERQRV 478
Cdd:PRK11124   83 NVGMVFQQYNLWPHlTVQQNL------------IEApcrvlglSKDQALARAEKLLERLRLKPYADRFPlHLSGGQQQRV 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 479 AIARAILRDPRILILDEATSSLDAETESLIRDALERLMK-GRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQ 552
Cdd:PRK11124  151 AIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVeVARKTASRVVYMENGHIVEQGDAS 226
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
334-531 9.59e-23

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 96.87  E-value: 9.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAY-ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI---KTAKLESLRKQI 409
Cdd:PRK10908    2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALF-SGTIKDNIAYgrpnaseAEIIEAAKFANIH-------DFINSLPKKYETQVaergsRLSGGERQRVAIA 481
Cdd:PRK10908   82 GMIFQDHHLLmDRTVYDNVAI-------PLIIAGASGDDIRrrvsaalDKVGLLDKAKNFPI-----QLSGGEQQRVGIA 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 482 RAILRDPRILILDEATSSLD-AETESLIR--DALER-----LMKGRTTFIIAHRLYAV 531
Cdd:PRK10908  150 RAVVNKPAVLLADEPTGNLDdALSEGILRlfEEFNRvgvtvLMATHDIGLISRRSYRM 207
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 334-555 1.11e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 97.29  E-value: 1.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYD-----PTSGRILVDGQDIKTAKLESLRKQ 408
Cdd:PRK14247    4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 409 IAVV---PQEIALFSgtIKDNIAYG----RPNASEAEIIEAAKFAnihdfinsLPK-KYETQVAER----GSRLSGGERQ 476
Cdd:PRK14247   84 VQMVfqiPNPIPNLS--IFENVALGlklnRLVKSKKELQERVRWA--------LEKaQLWDEVKDRldapAGKLSGGQQQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 477 RVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAH-RLYAVEHANRIVVIDNKQILEIGSHQELL 555
Cdd:PRK14247  154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVF 233
cbiO PRK13642
energy-coupling factor transporter ATPase;
330-555 1.32e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 97.86  E-value: 1.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 330 INGEINFENISFAYENEEVLQNIN---LKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLR 406
Cdd:PRK13642    1 MNKILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 407 KQIAVVPQ--EIALFSGTIKDNIAYGRPNAS--EAEII----EAAKFANIHDFINSLPkkyetqvaergSRLSGGERQRV 478
Cdd:PRK13642   81 RKIGMVFQnpDNQFVGATVEDDVAFGMENQGipREEMIkrvdEALLAVNMLDFKTREP-----------ARLSGGQKQRV 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 479 AIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGR--TTFIIAHRLYAVEHANRIVVIDNKQILEIGSHQELL 555
Cdd:PRK13642  150 AVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 349-569 1.77e-22

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 96.83  E-value: 1.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYdPTSGRILVDGQDIKTAKLESLRKQIAVVPQE------------I 416
Cdd:COG4138    12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQqsppfampvfqyL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 417 ALfsgtikdniaYGRPNASEAEIIEAakFANIHDFINsLPKKYETQVaergSRLSGGERQRVAIARAILR-------DPR 489
Cdd:COG4138    91 AL----------HQPAGASSEAVEQL--LAQLAEALG-LEDKLSRPL----TQLSGGEWQRVRLAAVLLQvwptinpEGQ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 490 ILILDEATSSLDAETESlirdALERLMK-----GRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQELLQKDGLYKy 563
Cdd:COG4138   154 LLLLDEPMNSLDVAQQA----ALDRLLRelcqqGITVVMSSHDLnHTLRHADRVWLLKQGKLVASGETAEVMTPENLSE- 228


                  ....*.
gi 1277238834 564 LYAIQF 569
Cdd:COG4138   229 VFGVKF 234
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 348-524 2.81e-22

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: 95.42  E-value: 2.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLL---LRFYDPTSGRILVDGQDIKTAKLeslRKQIAVVPQEIALFSG-TI 423
Cdd:cd03234    22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRKPDQF---QKCVAYVRQDDILLPGlTV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 424 KDNIAYgrpnaseaeiieAAKFANIHDFINSLPKKYETQVAER--------GSR---LSGGERQRVAIARAILRDPRILI 492
Cdd:cd03234    99 RETLTY------------TAILRLPRKSSDAIRKKRVEDVLLRdlaltrigGNLvkgISGGERRRVSIAVQLLWDPKVLI 166

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1277238834 493 LDEATSSLDAETESLIRDALERLMKGRTTFII 524
Cdd:cd03234   167 LDEPTSGLDSFTALNLVSTLSQLARRNRIVIL 198
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
 81-308 3.00e-22

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: 97.00  E-value: 3.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  81 FVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLL 160
Cdd:cd18784    62 LAMARLNIRIRNLLFRSIVSQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLV 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 161 TLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILAT 240
Cdd:cd18784   142 TLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGG 221

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 241 QNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18784   222 YVWSNELTELALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 348-549 3.51e-22

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: 95.29  E-value: 3.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQdiktakleslrkqiaVVPQeIALFSG-----T 422
Cdd:cd03220    37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR---------------VSSL-LGLGGGfnpelT 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 423 IKDNIA-----YGRPNAS----EAEIIEaakFANIHDFINSLPKKYetqvaergsrlSGGERQRVAIARAILRDPRILIL 493
Cdd:cd03220   101 GRENIYlngrlLGLSRKEidekIDEIIE---FSELGDFIDLPVKTY-----------SSGMKARLAFAIATALEPDILLI 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 494 DEATSSLDAETESLIRDALERLMKGRTTFIIA-HRLYAV-EHANRIVVIDNKQILEIG 549
Cdd:cd03220   167 DEVLAVGDAAFQEKCQRRLRELLKQGKTVILVsHDPSSIkRLCDRALVLEKGKIRFDG 224
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 337-556 4.61e-22

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 95.10  E-value: 4.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLtslllrFY------DPTSGRILVDGQDI------KTAkles 404
Cdd:COG1137     7 ENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDIthlpmhKRA---- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 405 lRKQIAVVPQEIALFSG-TIKDNIA-----YGRPNASEAEIIEAAkfanIHDF-INSLPKKyetqvaeRGSRLSGGERQR 477
Cdd:COG1137    77 -RLGIGYLPQEASIFRKlTVEDNILavlelRKLSKKEREERLEEL----LEEFgITHLRKS-------KAYSLSGGERRR 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 478 VAIARAILRDPRILILDEATSSLD----AETESLIRDALERlmkG----------RTTFIIAHRLYavehanrivVIDNK 543
Cdd:COG1137   145 VEIARALATNPKFILLDEPFAGVDpiavADIQKIIRHLKER---GigvlitdhnvRETLGICDRAY---------IISEG 212

                         250
                  ....*....|...
gi 1277238834 544 QILEIGSHQELLQ 556
Cdd:COG1137   213 KVLAEGTPEEILN 225
cbiO PRK13643
energy-coupling factor transporter ATPase;
334-557 5.65e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 96.34  E-value: 5.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYE-----NEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRI----LVDGQDIKTAKLES 404
Cdd:PRK13643    2 IKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 405 LRKQIAVVPQ--EIALFSGTIKDNIAYGRPN----ASEAEIIEAAKFANIhdfinSLPKKYETQVAergSRLSGGERQRV 478
Cdd:PRK13643   82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNfgipKEKAEKIAAEKLEMV-----GLADEFWEKSP---FELSGGQMRRV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 479 AIARAILRDPRILILDEATSSLDAETESLIRDALERLMK-GRTTFIIAHRLYAV-EHANRIVVIDNKQILEIGSHQELLQ 556
Cdd:PRK13643  154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVFQ 233


                  .
gi 1277238834 557 K 557
Cdd:PRK13643  234 E 234
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
347-536 6.98e-22

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 94.50  E-value: 6.98e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 347 EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIK----TAKLESLRKQIAVVPQeialFSGT 422
Cdd:PRK11629   23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssAAKAELRNQKLGFIYQ----FHHL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 423 IKDNIAYgrPNASEAEIIEAAKFANIHDFINSLPKK--YETQVAERGSRLSGGERQRVAIARAILRDPRILILDEATSSL 500
Cdd:PRK11629   99 LPDFTAL--ENVAMPLLIGKKKPAEINSRALEMLAAvgLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1277238834 501 DAETESLIRDALERL--MKGRTTFIIAHRLYAVEHANR 536
Cdd:PRK11629  177 DARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSR 214
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
 78-277 7.78e-22

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: 96.00  E-value: 7.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  78 LSYFVAQRIIVDLRNQVYEHLQDL--------SLDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIPHSLLLLGLMGY 149
Cdd:cd18589    51 VSEFVCDLIYNITMSRIHSRLQGLvfaavlrqEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIF 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 150 IFWLNWQLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFD 229
Cdd:cd18589   131 MLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYR 210

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1277238834 230 ISMRAVqILATQNPVIALLQTIAV-VGIVWFGGREIISGSLSLPQLISF 277
Cdd:cd18589   211 LNKKEA-AAYAVSMWTSSFSGLALkVGILYYGGQLVTAGTVSSGDLVTF 258
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
334-526 1.06e-21

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 94.77  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESlrkqiAVVP 413
Cdd:PRK11248    2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFS-GTIKDNIAYGRPNA--SEAEIIEAAKFANIHDFINSLPKKYETQvaergsrLSGGERQRVAIARAILRDPRI 490
Cdd:PRK11248   77 QNEGLLPwRNVQDNVAFGLQLAgvEKMQRLEIAHQMLKKVGLEGAEKRYIWQ-------LSGGQRQRVGIARALAANPQL 149

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1277238834 491 LILDEATSSLDAETESLIRDALERLMK--GRTTFIIAH 526
Cdd:PRK11248  150 LLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH 187
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 333-555 1.14e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 95.92  E-value: 1.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 333 EINFENISFAYENE-----EVLQNINLKVKPGEIIALVGRTGAGKST----LTSLLLrfydPTSGRILVDGQDIKTAK-- 401
Cdd:PRK13651    2 QIKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTfiehLNALLL----PDTGTIEWIFKDEKNKKkt 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 402 ----------------------LESLRKQIAVVPQ--EIALFSGTIKDNIAYGrPNASEAEIIEAAKFANIHDFINSLPK 457
Cdd:PRK13651   78 kekekvleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG-PVSMGVSKEEAKKRAAKYIELVGLDE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 458 KYetqvAERGS-RLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK-GRTTFIIAHRL-YAVEHA 534
Cdd:PRK13651  157 SY----LQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLdNVLEWT 232

                         250       260
                  ....*....|....*....|.
gi 1277238834 535 NRIVVIDNKQILEIGSHQELL 555
Cdd:PRK13651  233 KRTIFFKDGKIIKDGDTYDIL 253
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 312-558 1.37e-21

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 98.51  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 312 LDVKPSIADLPGAKKLPRINgEINFENISFAYENEEV-LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRI 390
Cdd:PRK10522  302 LALAPYKAEFPRPQAFPDWQ-TLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 391 LVDGQDIKTAKLESLRKQIAVVPQEIALFSGTIKDniaygRPNASEAEIIEAakfanihdFINSLPKKYETQVAE---RG 467
Cdd:PRK10522  381 LLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGP-----EGKPANPALVEK--------WLERLKMAHKLELEDgriSN 447

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 468 SRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEHANRIVVIDNKQI 545
Cdd:PRK10522  448 LKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHDDHYFIHADRLLEMRNGQL 527

                         250
                  ....*....|....
gi 1277238834 546 LEI-GSHQELLQKD 558
Cdd:PRK10522  528 SELtGEERDAASRD 541
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 334-531 1.46e-21

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 94.03  E-value: 1.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQdiktaklesLRkqIAVVP 413
Cdd:PRK09544    5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG---TIKDNIAYgRPNASEAEIIEAAKFANIHDFINSLPKKyetqvaergsrLSGGERQRVAIARAILRDPRI 490
Cdd:PRK09544   74 QKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQL 141

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1277238834 491 LILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAV 531
Cdd:PRK09544  142 LVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLV 184
ABC_6TM_AarD_CydDC_like cd18561
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...
 25-308 4.04e-21

Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).


Pssm-ID: 350005 [Multi-domain]  Cd Length: 289  Bit Score: 93.88  E-value: 4.04e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  25 TALVTSTTLLIAPLVGYIFQLIEDKNMFLLnlsALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLD 104
Cdd:cd18561     9 TALYIAQAWLLARALARIFAGGPWEDIMPP---LAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 105 FYAKWNTGELVSRVMNDIQTLQATlftgFVTLIPHSLL----LLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAKEIR 180
Cdd:cd18561    86 YLEGERTGELQTTVVDGVEALEAY----YGRYLPQLLVallgPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 181 EISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFG 260
Cdd:cd18561   162 DTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLSSGIMGLATALGTALALGVG 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1277238834 261 GREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18561   242 ALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAADSI 289
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 334-558 4.26e-21

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 92.65  E-value: 4.26e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKL-ESLRKQIAVV 412
Cdd:PRK10895    4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 PQEIALFSG-----------TIKDNIAYGRPNASEAEIIEAAKFANIHDFInslpkkyetqvaerGSRLSGGERQRVAIA 481
Cdd:PRK10895   84 PQEASIFRRlsvydnlmavlQIRDDLSAEQREDRANELMEEFHIEHLRDSM--------------GQSLSGGERRRVEIA 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 482 RAILRDPRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLY-AVEHANRIVVIDNKQILEIGSHQELLQKD 558
Cdd:PRK10895  150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVReTLAVCERAYIVSQGHLIAHGTPTEILQDE 228
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 343-546 5.55e-21

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: 92.01  E-value: 5.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 343 YENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLEsLRKQIAVV---------- 412
Cdd:cd03267    31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKK-FLRRIGVVfgqktqlwwd 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 --PQEIALFSGTIKDnIAYGRPNASEAEIIEAAKFANIHDfinslpkkyeTQVaergSRLSGGERQRVAIARAILRDPRI 490
Cdd:cd03267   110 lpVIDSFYLLAAIYD-LPPARFKKRLDELSELLDLEELLD----------TPV----RQLSLGQRMRAEIAAALLHEPEI 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 491 LILDEATSSLDAETESLIRDALERLMKGRTTFII--AHRLYAVEH-ANRIVVIDNKQIL 546
Cdd:cd03267   175 LFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLltSHYMKDIEAlARRVLVIDKGRLL 233
ABC_6TM_PrtD_LapB_HlyB_like cd18783
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
 42-277 6.06e-21

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


Pssm-ID: 350056 [Multi-domain]  Cd Length: 294  Bit Score: 93.35  E-value: 6.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  42 IFQLIEDK-----NMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVS 116
Cdd:cd18783    24 FFQIVIDKvlvhqSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFERTPAGVLTK 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 117 RvMNDIQTLQATLfTG--FVTLIpHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADIT 194
Cdd:cd18783   104 H-MQQIERIRQFL-TGqlFGTLL-DATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQ 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 195 SHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQL 274
Cdd:cd18783   181 AFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLVFAGSLTVGAL 260


                  ...
gi 1277238834 275 ISF 277
Cdd:cd18783   261 IAF 263
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 334-543 9.45e-21

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: 89.52  E-value: 9.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVL-QNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRIlvdgqdIKTAkleslRKQIAVV 412
Cdd:cd03223     1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI------GMPE-----GEDLLFL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 PQEIALFSGTIKDNIAYgrpnaseaeiieaakfanihdfinslPkkyetqvaeRGSRLSGGERQRVAIARAILRDPRILI 492
Cdd:cd03223    70 PQRPYLPLGTLREQLIY--------------------------P---------WDDVLSGGEQQRLAFARLLLHKPKFVF 114

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 493 LDEATSSLDAETESLIRDALERLMkgrTTFI-IAHRLYAVEHANRIVVIDNK 543
Cdd:cd03223   115 LDEATSALDEESEDRLYQLLKELG---ITVIsVGHRPSLWKFHDRVLDLDGE 163
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
331-555 9.76e-21

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 91.95  E-value: 9.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 331 NGEINFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAK--------- 401
Cdd:PRK10619    3 ENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRdkdgqlkva 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 402 ----LESLRKQIAVVPQEIALFSG-TIKDNIAYGRPNA---SEAEIIE-AAKFANIHDFINSLPKKYETQvaergsrLSG 472
Cdd:PRK10619   83 dknqLRLLRTRLTMVFQHFNLWSHmTVLENVMEAPIQVlglSKQEARErAVKYLAKVGIDERAQGKYPVH-------LSG 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 473 GERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIGS 550
Cdd:PRK10619  156 GQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGA 235


                  ....*
gi 1277238834 551 HQELL 555
Cdd:PRK10619  236 PEQLF 240
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 347-555 1.22e-20

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: 95.52  E-value: 1.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 347 EVLQNINLKVKPGEIIALVGRTGAGKStLTSL-LLRFYDP----TSGRILVDGQDIKTAKLESLRK----QIAVVPQE-- 415
Cdd:COG4172    24 EAVKGVSFDIAAGETLALVGESGSGKS-VTALsILRLLPDpaahPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEpm 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 416 IAL---FsgTIKDNIAYG-------RPNASEAEIIEAAKFANIHDfinslPkkyETQVAERGSRLSGGERQRVAIARAIL 485
Cdd:COG4172   103 TSLnplH--TIGKQIAEVlrlhrglSGAAARARALELLERVGIPD-----P---ERRLDAYPHQLSGGQRQRVMIAMALA 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 486 RDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIGSHQELL 555
Cdd:COG4172   173 NEPDLLIADEPTTALDVTVQAQILDLLKDLQRelGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAELF 245
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 324-537 1.89e-20

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 91.38  E-value: 1.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 324 AKKLPRINGEINFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYD--PT---SGRILVDGQDIK 398
Cdd:PRK14243    1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 399 TAKLE--SLRKQIAVVPQEIALFSGTIKDNIAYG-RPNASEA---EIIEAA-KFANIHDfinslpkKYETQVAERGSRLS 471
Cdd:PRK14243   81 APDVDpvEVRRRIGMVFQKPNPFPKSIYDNIAYGaRINGYKGdmdELVERSlRQAALWD-------EVKDKLKQSGLSLS 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 472 GGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLyavEHANRI 537
Cdd:PRK14243  154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM---QQAARV 216
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 343-564 2.56e-20

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 92.07  E-value: 2.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 343 YENEEVLQNINLKVKPGEIIALVGRTGAGKST----LTSLLLrfydPTSGRILVDGQDIkTAKLESLRKQIAVV------ 412
Cdd:COG4586    32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTtikmLTGILV----PTSGEVRVLGYVP-FKRRKEFARRIGVVfgqrsq 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 ------PQEIALFSGTIkdniaYGRPNAS-EAEIIEAAKFANIHDFINslpkkyeTQVaeRgsRLSGGERQRVAIARAIL 485
Cdd:COG4586   107 lwwdlpAIDSFRLLKAI-----YRIPDAEyKKRLDELVELLDLGELLD-------TPV--R--QLSLGQRMRCELAAALL 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 486 RDPRILILDEATSSLDAETESLIRDALERLMKGR-TTFIIA-HRLYAVEH-ANRIVVIDNKQILEIGSHQELLQKDGLYK 562
Cdd:COG4586   171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYK 250


                  ..
gi 1277238834 563 YL 564
Cdd:COG4586   251 TI 252
cbiO PRK13646
energy-coupling factor transporter ATPase;
334-558 5.41e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 90.61  E-value: 5.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYEN-----EEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI----KTAKLES 404
Cdd:PRK13646    3 IRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 405 LRKQIAVVPQ--EIALFSGTIKDNIAYGrPNASEAEIIEAAKFAniHDFINSLpkKYETQVAERGS-RLSGGERQRVAIA 481
Cdd:PRK13646   83 VRKRIGMVFQfpESQLFEDTVEREIIFG-PKNFKMNLDEVKNYA--HRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAIV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 482 RAILRDPRILILDEATSSLDAETESLIRDALERLM--KGRTTFIIAHRLYAV-EHANRIVVIDNKQILEIGSHQELLQKD 558
Cdd:PRK13646  158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDK 237
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
 49-308 7.05e-20

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: 90.33  E-value: 7.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  49 KNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRvMNDIQTLQaT 128
Cdd:cd18566    36 ESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLER-LNSLEQIR-E 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 129 LFTG--FVTLI--PHSLLLLGLMGYIFWLnwqLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQV 204
Cdd:cd18566   114 FLTGqaLLALLdlPFVLIFLGLIWYLGGK---LVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGI 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 205 KTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIM 284
Cdd:cd18566   191 HTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIACTMLSGRV 270

                         250       260
                  ....*....|....*....|....
gi 1277238834 285 TDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18566   271 LQPLQRAFGLWTRFQQVRVAVRRL 294
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 334-557 7.87e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 89.91  E-value: 7.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAY-ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAK--LESLRKQIA 410
Cdd:PRK13636    6 LKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkgLMKLRESVG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 411 VVPQ--EIALFSGTIKDNIAYGRPNAS--EAEIIEAAKFANIHDFINSLPKKyETQVaergsrLSGGERQRVAIARAILR 486
Cdd:PRK13636   86 MVFQdpDNQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKDK-PTHC------LSFGQKKRVAIAGVLVM 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 487 DPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVE-HANRIVVIDNKQILEIGSHQELLQK 557
Cdd:PRK13636  159 EPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAE 232
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 348-545 8.28e-20

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: 87.10  E-value: 8.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAK-LESLRKQIAVVP---QEIALFSG-T 422
Cdd:cd03215    15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPedrKREGLVLDlS 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 423 IKDNIAygrpnaseaeiieaakfanihdfINSLpkkyetqvaergsrLSGGERQRVAIARAILRDPRILILDEATSSLDA 502
Cdd:cd03215    95 VAENIA-----------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1277238834 503 ETESLIRDALERL-MKGRTTFIIAHRL-YAVEHANRIVVIDNKQI 545
Cdd:cd03215   138 GAKAEIYRLIRELaDAGKAVLLISSELdELLGLCDRILVMYEGRI 182
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 338-555 8.47e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 89.34  E-value: 8.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 338 NISFAY---ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRF---YDP---TSGRILVDGQDIKTAKLESLRKQ 408
Cdd:PRK14246   12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 409 IAVVPQEIALFSG-TIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSRLSGGERQRVAIARAILRD 487
Cdd:PRK14246   92 VGMVFQQPNPFPHlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALK 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 488 PRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIGSHQELL 555
Cdd:PRK14246  172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 348-561 2.91e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 88.75  E-value: 2.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTS----LLLRFYDPTSGRILVDGQDI------------KTAKLESLRKQIAV 411
Cdd:PRK13631   41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIKSKYGTIQVGDIYIGDKKnnhelitnpyskKIKNFKELRRRVSM 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQ--EIALFSGTIKDNIAYGrPNASEAEIIEAAKFANIHdfINSLPKKYEtqVAERGS-RLSGGERQRVAIARAILRDP 488
Cdd:PRK13631  121 VFQfpEYQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFY--LNKMGLDDS--YLERSPfGLSGGQKRRVAIAGILAIQP 195

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 489 RILILDEATSSLDAETES----LIRDALErlmKGRTTFIIAHRLYAV-EHANRIVVIDNKQILEIGSHQELLQKDGLY 561
Cdd:PRK13631  196 EILIFDEPTAGLDPKGEHemmqLILDAKA---NNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHII 270
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 354-543 9.58e-19

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: 85.92  E-value: 9.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 354 LKVKPG-----EIIALVGRTGAGKSTLTSLLlrfydptSGRILVDGQDIktaklESLRKQIAVVPQEI-ALFSGTI---- 423
Cdd:cd03237    15 LEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDI-----EIELDTVSYKPQYIkADYEGTVrdll 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 424 --KDNIAYGRPNAsEAEIIEAAKFANIhdfinslpkkYETQVAErgsrLSGGERQRVAIARAILRDPRILILDEATSSLD 501
Cdd:cd03237    83 ssITKDFYTHPYF-KTEIAKPLQIEQI----------LDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1277238834 502 AETESLIRDALERLM--KGRTTFIIAHRLYAVEH-ANRIVVIDNK 543
Cdd:cd03237   148 VEQRLMASKVIRRFAenNEKTAFVVEHDIIMIDYlADRLIVFEGE 192
ABC_6TM_T1SS_like cd18779
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ...
 21-279 1.20e-18

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of 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: 350052 [Multi-domain]  Cd Length: 294  Bit Score: 86.45  E-value: 1.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  21 GTICTALVTSTTL----LIAPLV-GYIF-QLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQV 94
Cdd:cd18779     2 GLLGQILLASLLLqllgLALPLLtGVLVdRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  95 YEHLQDLSLDFYAKWNTGELVSRVmNDIQTLQATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRI 174
Cdd:cd18779    82 LEHLLRLPYRFFQQRSTGDLLMRL-SSNATIRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 175 FAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVV 254
Cdd:cd18779   161 TRRRVRELMARELAAQAEAQSYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPL 240

                         250       260
                  ....*....|....*....|....*
gi 1277238834 255 GIVWFGGREIISGSLSLPQLISFAT 279
Cdd:cd18779   241 VLLWVGAWQVLDGQLSLGTMLALNA 265
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
338-560 1.34e-18

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 86.21  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 338 NISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAK--LESLRKQIAVVPQ- 414
Cdd:PRK13638    6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKrgLLALRQQVATVFQd 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 415 -EIALFSGTIKDNIAYGRPN--ASEAEII----EAAKFANIHDFinslpKKYETQVaergsrLSGGERQRVAIARAILRD 487
Cdd:PRK13638   86 pEQQIFYTDIDSDIAFSLRNlgVPEAEITrrvdEALTLVDAQHF-----RHQPIQC------LSHGQKKRVAIAGALVLQ 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 488 PRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLYAV-EHANRIVVIDNKQIL------EIGSHQELLQKDG 559
Cdd:PRK13638  155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIyEISDAVYVLRQGQILthgapgEVFACTEAMEQAG 234


                  .
gi 1277238834 560 L 560
Cdd:PRK13638  235 L 235
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 352-562 1.57e-18

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 87.07  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 352 INLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI---KTAKLESLRKQIAVVPQEiALFS----GTIK 424
Cdd:PRK15079   40 VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmKDDEWRAVRSDIQMIFQD-PLASlnprMTIG 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 425 DNIA-----YgRPNASEAEIIE-----AAKFANIHDFINSLPKKYetqvaergsrlSGGERQRVAIARAILRDPRILILD 494
Cdd:PRK15079  119 EIIAeplrtY-HPKLSRQEVKDrvkamMLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILEPKLIICD 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 495 EATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEH-ANRIVVidnkqiLEIGSHQELLQKDGLYK 562
Cdd:PRK15079  187 EPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLV------MYLGHAVELGTYDEVYH 251
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 351-555 1.67e-18

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 88.71  E-value: 1.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 351 NINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVD-GQD-IKTAKLESL-----RKQIAVVPQEIALFS-GT 422
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwVDMTKPGPDgrgraKRYIGILHQEYDLYPhRT 381

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 423 IKDNIAygrpNASEAEI-IEAAKFANIHDFINS-LPKKYETQVAER-GSRLSGGERQRVAIARAILRDPRILILDEATSS 499
Cdd:TIGR03269 382 VLDNLT----EAIGLELpDELARMKAVITLKMVgFDEEKAEEILDKyPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 500 LDAETEsliRDALERLMKGR-----TTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQELL 555
Cdd:TIGR03269 458 MDPITK---VDVTHSILKAReemeqTFIIVSHDMdFVLDVCDRAALMRDGKIVKIGDPEEIV 516
GguA NF040905
sugar ABC transporter ATP-binding protein;
349-540 1.72e-18

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 88.69  E-value: 1.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYdPT---SGRILVDGQ-----DIKtaklESLRKQIAVVPQEIALFS 420
Cdd:NF040905   17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcrfkDIR----DSEALGIVIIHQELALIP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 421 G-TIKDNIAYGRPNAS------EAEIIEAAKfanihdfinsLPKKY------ETQVAERGSrlsgGERQRVAIARAILRD 487
Cdd:NF040905   92 YlSIAENIFLGNERAKrgvidwNETNRRARE----------LLAKVgldespDTLVTDIGV----GKQQLVEIAKALSKD 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 488 PRILILDEATSSL-DAETESLIRDALERLMKGRTTFIIAHRLYAVEH-ANRIVVI 540
Cdd:NF040905  158 VKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVL 212
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
337-546 1.95e-18

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 89.01  E-value: 1.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAY----ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESL----RKQ 408
Cdd:PRK10535    8 KDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREH 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 409 IAVVPQEIALFSG-TIKDNIAYgrpNASEAEIIEAAKFANIHDFINSLpkKYETQVAERGSRLSGGERQRVAIARAILRD 487
Cdd:PRK10535   88 FGFIFQRYHLLSHlTAAQNVEV---PAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 488 PRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLYAVEHANRIVVIDNKQIL 546
Cdd:PRK10535  163 GQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 348-554 2.10e-18

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 88.61  E-value: 2.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYdPTSGRILVDGQDIKT---AKLESLRKQIAVVPQeialfsgtik 424
Cdd:PRK15134  301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNlnrRQLLPVRHRIQVVFQ---------- 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 425 DNIAYGRPNASEAEIIEAAkfANIHDFINSlPKKYETQV----AERG----------SRLSGGERQRVAIARAILRDPRI 490
Cdd:PRK15134  370 DPNSSLNPRLNVLQIIEEG--LRVHQPTLS-AAQREQQViavmEEVGldpetrhrypAEFSGGQRQRIAIARALILKPSL 446

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 491 LILDEATSSLDAETESLIRDALERLM-KGRTTFI-IAHRLYAVEH-ANRIVVIDNKQILEIGSHQEL 554
Cdd:PRK15134  447 IILDEPTSSLDKTVQAQILALLKSLQqKHQLAYLfISHDLHVVRAlCHQVIVLRQGEVVEQGDCERV 513
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 345-525 2.32e-18

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 83.77  E-value: 2.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 345 NEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIktaKLESLRKQIAVVPQEIALFSG-TI 423
Cdd:PRK13539   14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLGHRNAMKPAlTV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 424 KDNIAYGRP--NASEAEIIEAAKFANIHDFINsLPKKYetqvaergsrLSGGERQRVAIARAILRDPRILILDEATSSLD 501
Cdd:PRK13539   91 AENLEFWAAflGGEELDIAAALEAVGLAPLAH-LPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALD 159

                         170       180
                  ....*....|....*....|....
gi 1277238834 502 AETESLIRDALERLMKGRTTFIIA 525
Cdd:PRK13539  160 AAAVALFAELIRAHLAQGGIVIAA 183
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 349-549 2.61e-18

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 88.37  E-value: 2.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKT---AKLESLRKQIAVVPQE-IALFS--GT 422
Cdd:PRK10261  340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspGKLQALRRDIQFIFQDpYASLDprQT 419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 423 IKDNI-----AYGRPNASEAeiieAAKFANIHDFINSLPK---KYETQvaergsrLSGGERQRVAIARAILRDPRILILD 494
Cdd:PRK10261  420 VGDSImeplrVHGLLPGKAA----AARVAWLLERVGLLPEhawRYPHE-------FSGGQRQRICIARALALNPKVIIAD 488

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1277238834 495 EATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIG 549
Cdd:PRK10261  489 EAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 337-555 2.65e-18

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 88.22  E-value: 2.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENE----EVLQNINLKVKPGEIIALVGRTGAGKS-TLTSLLLRFYDP----TSGRILVDGQDIKTAKLESLRK 407
Cdd:PRK15134    9 ENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRG 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 408 ----QIAVVPQE------------------IALFSGTikdniaygRPNASEAEIIEAAKFANIHDFINSLpKKYETQvae 465
Cdd:PRK15134   89 vrgnKIAMIFQEpmvslnplhtlekqlyevLSLHRGM--------RREAARGEILNCLDRVGIRQAAKRL-TDYPHQ--- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 466 rgsrLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAVEH-ANRIVVIDN 542
Cdd:PRK15134  157 ----LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQN 232

                         250
                  ....*....|...
gi 1277238834 543 KQILEIGSHQELL 555
Cdd:PRK15134  233 GRCVEQNRAATLF 245
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
334-561 2.69e-18

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 87.92  E-value: 2.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIK--TAKLeSLRKQIAV 411
Cdd:PRK09700    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKL-AAQLGIGI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEIALFSG-TIKDNIAYGRPNASE---AEIIEAAKF---ANIHDFINSLPKKYETQVAErgsrLSGGERQRVAIARAI 484
Cdd:PRK09700   85 IYQELSVIDElTVLENLYIGRHLTKKvcgVNIIDWREMrvrAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 485 LRDPRILILDEATSSL-DAETESL--IRDALERlmKGRTTFIIAHRLyavehanrivvidnKQILEIGSHQELLqKDGLY 561
Cdd:PRK09700  161 MLDAKVIIMDEPTSSLtNKEVDYLflIMNQLRK--EGTAIVYISHKL--------------AEIRRICDRYTVM-KDGSS 223
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 349-539 3.94e-18

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 85.79  E-value: 3.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIK---TAKLESLRKQIAVVPQEialfsgtikd 425
Cdd:PRK11308   31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQN---------- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 426 niAYG--RPNASEAEIIEAAKFANihdfiNSLPKkyetqvAERGSR---------------------LSGGERQRVAIAR 482
Cdd:PRK11308  101 --PYGslNPRKKVGQILEEPLLIN-----TSLSA------AERREKalammakvglrpehydryphmFSGGQRQRIAIAR 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 483 AILRDPRILILDEATSSLD----AETESLIRDaLERLMKGRTTFiIAHRLYAVEH-ANRIVV 539
Cdd:PRK11308  168 ALMLDPDVVVADEPVSALDvsvqAQVLNLMMD-LQQELGLSYVF-ISHDLSVVEHiADEVMV 227
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 338-544 5.08e-18

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: 87.19  E-value: 5.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 338 NISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFY--DPTSGRILVDGQDIKTAKL-ESLRKQIAVVPQ 414
Cdd:TIGR02633   6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIrDTERAGIVIIHQ 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 415 EIALFSG-TIKDNIAYGRPNASEAEIIE-AAKFANIHDFINSLpKKYETQVAERGSRLSGGERQRVAIARAILRDPRILI 492
Cdd:TIGR02633  86 ELTLVPElSVAENIFLGNEITLPGGRMAyNAMYLRAKNLLREL-QLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLI 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 493 LDEATSSL-DAETESL---IRDaLERlmKGRTTFIIAHRLYAVEH-ANRIVVIDNKQ 544
Cdd:TIGR02633 165 LDEPSSSLtEKETEILldiIRD-LKA--HGVACVYISHKLNEVKAvCDTICVIRDGQ 218
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
334-573 7.17e-18

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 83.52  E-value: 7.17e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLL--LRFYDPTSG-RILVDGQDIKTA-----KLESL 405
Cdd:PRK09984    5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsgLITGDKSAGsHIELLGRTVQREgrlarDIRKS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 406 RKQIAVVPQEIALFSG-TIKDNIAYGRPNASEAEIIEAAKFANIH--DFINSLPKKYETQVA-ERGSRLSGGERQRVAIA 481
Cdd:PRK09984   85 RANTGYIFQQFNLVNRlSVLENVLIGALGSTPFWRTCFSWFTREQkqRALQALTRVGMVHFAhQRVSTLSGGQQQRVAIA 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 482 RAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQELLQK- 557
Cdd:PRK09984  165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVdYALRYCERIVALRQGHVFYDGSSQQFDNEr 244

                         250
                  ....*....|....*..
gi 1277238834 558 -DGLYKYLYAIQFNNKA 573
Cdd:PRK09984  245 fDHLYRSINRVEENAKA 261
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
334-531 1.23e-17

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 83.39  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYEN-EEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLrkqIAVV 412
Cdd:PRK15056    7 IVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 PQEIAL---FSGTIKDNIAYGR---------PNASEAEIIEAAkFANIhdfiNSLPKKYEtQVAErgsrLSGGERQRVAI 480
Cdd:PRK15056   84 PQSEEVdwsFPVLVEDVVMMGRyghmgwlrrAKKRDRQIVTAA-LARV----DMVEFRHR-QIGE----LSGGQKKRVFL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 481 ARAILRDPRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLYAV 531
Cdd:PRK15056  154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSV 205
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 334-556 1.64e-17

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 82.44  E-value: 1.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISfAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDP----TSGRILVDGQDIKTAKLESlrKQI 409
Cdd:PRK10418    5 IELRNIA-LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALRG--RKI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQE--------IALFSGTIKDNIAYGRP--NASEAEIIEAAKFANIHDFINSLPkkYEtqvaergsrLSGGERQRVA 479
Cdd:PRK10418   82 ATIMQNprsafnplHTMHTHARETCLALGKPadDATLTAALEAVGLENAARVLKLYP--FE---------MSGGMLQRMM 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 480 IARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRT--TFIIAHRLYAVEH-ANRIVVIDNKQILEIGSHQELLQ 556
Cdd:PRK10418  151 IALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETLFN 230
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 332-510 1.75e-17

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 85.77  E-value: 1.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 332 GEINF--ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDgqdiktAKLEslrkqI 409
Cdd:PRK11147  316 GKIVFemENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG------TKLE-----V 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 410 AVVPQEIALF--SGTIKDNIAYGRpnaSEAEI--IEAAKFANIHDFINSlPKKYETQVaergSRLSGGERQRVAIARAIL 485
Cdd:PRK11147  385 AYFDQHRAELdpEKTVMDNLAEGK---QEVMVngRPRHVLGYLQDFLFH-PKRAMTPV----KALSGGERNRLLLARLFL 456

                         170       180
                  ....*....|....*....|....*....
gi 1277238834 486 RDPRILILDEATSSLDAET----ESLIRD 510
Cdd:PRK11147  457 KPSNLLILDEPTNDLDVETlellEELLDS 485
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
334-554 1.87e-17

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 82.51  E-value: 1.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKT---AKLESLRKQIA 410
Cdd:PRK11831    8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrSRLYTVRKRMS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 411 VVPQEIALFSG-TIKDNIAYgrPNASEAEIIEAAkfanIHdfiNSLPKKYETqVAERG------SRLSGGERQRVAIARA 483
Cdd:PRK11831   88 MLFQSGALFTDmNVFDNVAY--PLREHTQLPAPL----LH---STVMMKLEA-VGLRGaaklmpSELSGGMARRAALARA 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 484 ILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLYAV-EHANRIVVIDNKQILEIGSHQEL 554
Cdd:PRK11831  158 IALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVlSIADHAYIVADKKIVAHGSAQAL 231
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 334-556 1.95e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 82.20  E-value: 1.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYD-----PTSGRILVDGQDIKTAKLESL--R 406
Cdd:PRK14267    5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 407 KQIAVVPQEIALFSG-TIKDNIAYG-------RPNASEAEIIE-----AAKFANIHDFINSLPkkyetqvaergSRLSGG 473
Cdd:PRK14267   85 REVGMVFQYPNPFPHlTIYDNVAIGvklnglvKSKKELDERVEwalkkAALWDEVKDRLNDYP-----------SNLSGG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 474 ERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHR-LYAVEHANRIVVIDNKQILEIGSHQ 552
Cdd:PRK14267  154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTR 233


                  ....
gi 1277238834 553 ELLQ 556
Cdd:PRK14267  234 KVFE 237
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
 56-277 2.03e-17

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: 82.77  E-value: 2.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  56 LSALGMIGLFVL-KGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIqTLQATLFTGFV 134
Cdd:cd18590    36 TSAIGLMCLFSLgSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDT-TLMSRSVALNA 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 135 TLIPHSLL-LLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAME 213
Cdd:cd18590   115 NVLLRSLVkTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAE 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 214 KEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISF 277
Cdd:cd18590   195 EEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSF 258
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
337-568 2.54e-17

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 81.96  E-value: 2.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIK------TAKLESLRKQIA 410
Cdd:PRK10253   11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQhyaskeVARRIGLLAQNA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 411 VVPQEIalfsgTIKDNIAYGR-PNA---------SEAEIIEAAKFANIHDFINslpKKYETqvaergsrLSGGERQRVAI 480
Cdd:PRK10253   91 TTPGDI-----TVQELVARGRyPHQplftrwrkeDEEAVTKAMQATGITHLAD---QSVDT--------LSGGQRQRAWI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 481 ARAILRDPRILILDEATSSLDAETESLIRDALERL--MKGRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQELLQK 557
Cdd:PRK10253  155 AMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIVTA 234

                         250
                  ....*....|.
gi 1277238834 558 DgLYKYLYAIQ 568
Cdd:PRK10253  235 E-LIERIYGLR 244
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 349-548 2.58e-17

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 85.06  E-value: 2.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIK-TAKLESLRKQIAVVPQEIALFSG-TIKDN 426
Cdd:PRK10762   20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEAGIGIIHQELNLIPQlTIAEN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 427 IAYGRPNASEAEIIEAAK-FANIHDFINSLPKKYETQvaERGSRLSGGERQRVAIARAILRDPRILILDEATSSL-DAET 504
Cdd:PRK10762  100 IFLGREFVNRFGRIDWKKmYAEADKLLARLNLRFSSD--KLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTET 177

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1277238834 505 ESLIRDALERLMKGRTTFIIAHRLyavehanrivvidnKQILEI 548
Cdd:PRK10762  178 ESLFRVIRELKSQGRGIVYISHRL--------------KEIFEI 207
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 351-554 2.69e-17

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 81.96  E-value: 2.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 351 NINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI------KTAKLESLR--------KQIAV----- 411
Cdd:PRK11300   23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpghQIARMGVVRtfqhvrlfREMTVienll 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQ----EIALFSGTIKdNIAYGRpnaSEAEIIEAAKFAnihdfinsLPKKYETQVAER-GSRLSGGERQRVAIARAILR 486
Cdd:PRK11300  103 VAQhqqlKTGLFSGLLK-TPAFRR---AESEALDRAATW--------LERVGLLEHANRqAGNLAYGQQRRLEIARCMVT 170

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 487 DPRILILDEATSSLD-AETESLirDALERLMK---GRTTFIIAHRLYAV-EHANRIVVIDNKQILEIGSHQEL 554
Cdd:PRK11300  171 QPEILMLDEPAAGLNpKETKEL--DELIAELRnehNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEI 241
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
333-550 5.17e-17

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 82.61  E-value: 5.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 333 EINFEnisfayeneEVLQNINLKVK---PGE-IIALVGRTGAGKSTLTSLLLRFYDPTSGRI------LVDGQdiKTAKL 402
Cdd:PRK11144    3 ELNFK---------QQLGDLCLTVNltlPAQgITAIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvLFDAE--KGICL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 403 ESLRKQIAVVPQEIALFSG-TIKDNIAYGRPNASEAEiieaakFANIHDF--INSLPKKYEtqvaergSRLSGGERQRVA 479
Cdd:PRK11144   72 PPEKRRIGYVFQDARLFPHyKVRGNLRYGMAKSMVAQ------FDKIVALlgIEPLLDRYP-------GSLSGGEKQRVA 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 480 IARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFII--AHRLYAVEH-ANRIVVIDNKQILEIGS 550
Cdd:PRK11144  139 IGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILyvSHSLDEILRlADRVVVLEQGKVKAFGP 212
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
347-555 5.79e-17

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 81.04  E-value: 5.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 347 EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQ--EIALfsgtik 424
Cdd:COG4167    27 EAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQdpNTSL------ 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 425 dniaygRPNASEAEIIEAakfanihdfinslPKKYETQV--AERGSR---------------------LSGGERQRVAIA 481
Cdd:COG4167   101 ------NPRLNIGQILEE-------------PLRLNTDLtaEEREERifatlrlvgllpehanfyphmLSSGQKQRVALA 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 482 RAILRDPRILILDEATSSLDAETES-LIRDALERLMKGRTTFI-IAHRLYAVEH-ANRIVVIDNKQILEIGSHQELL 555
Cdd:COG4167   162 RALILQPKIIIADEALAALDMSVRSqIINLMLELQEKLGISYIyVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVF 238
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
347-497 6.74e-17

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 83.53  E-value: 6.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 347 EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQ--DIKTAKlESLRKQIAVVP---QEIALFSG 421
Cdd:COG1129   266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPR-DAIRAGIAYVPedrKGEGLVLD 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 422 -TIKDNIAYGRPNA-------SEAEIIEAAKfanihDFINSL---PKKYETQVaergSRLSGGERQRVAIARAILRDPRI 490
Cdd:COG1129   345 lSIRENITLASLDRlsrggllDRRRERALAE-----EYIKRLrikTPSPEQPV----GNLSGGNQQKVVLAKWLATDPKV 415


                  ....*..
gi 1277238834 491 LILDEAT 497
Cdd:COG1129   416 LILDEPT 422
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 337-500 6.79e-17

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 83.63  E-value: 6.79e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDI--KTAKlESLRKQIAVVPQ 414
Cdd:PRK10982    2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSK-EALENGISMVHQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 415 EIALF-SGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQvaERGSRLSGGERQRVAIARAILRDPRILIL 493
Cdd:PRK10982   81 ELNLVlQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIM 158


                  ....*..
gi 1277238834 494 DEATSSL 500
Cdd:PRK10982  159 DEPTSSL 165
ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 cd18560
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ...
 57-308 1.03e-16

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: 80.73  E-value: 1.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  57 SALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVsRVMN-DIQTLQATLFTGFVT 135
Cdd:cd18560    40 LILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSLDWHLSKKTGEVV-RIMDrGTESANTLLSYLVFY 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 136 LIPhSLLLLGLMGYIFWL--NWQLSLLTLVALPL--IVQV-IRIFAKEIREISEGVQQKAADITShlqETISQVKTVKSF 210
Cdd:cd18560   119 LVP-TLLELIVVSVVFAFhfGAWLALIVFLSVLLygVFTIkVTEWRTKFRRAANKKDNEAHDIAV---DSLLNFETVKYF 194

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 211 AMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNT 290
Cdd:cd18560   195 TNEKYEVDRYGEAVKEYQKSSVKVQASLSLLNVGQQLIIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNF 274

                         250
                  ....*....|....*...
gi 1277238834 291 LSKAYSIIQQGMASTKRI 308
Cdd:cd18560   275 LGTIYRMIIQSLTDMENL 292
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 352-540 1.36e-16

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: 83.91  E-value: 1.36e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  352 INLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTaKLESLRKQIAVVPQEIALFSG-TIKDNIAY- 429
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHILFy 1027

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  430 ----GRpNASEAEIIEAAKFAN--IHDFINslpkkyetqvaERGSRLSGGERQRVAIARAILRDPRILILDEATSSLDAE 503
Cdd:TIGR01257 1028 aqlkGR-SWEEAQLEMEAMLEDtgLHHKRN-----------EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1277238834  504 TESLIRDALERLMKGRTTFIIAHRLYAVE-HANRIVVI 540
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAII 1133
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 348-524 1.58e-16

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 79.05  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLE---SLR-KQIAVVPQEIALF-SGT 422
Cdd:PRK10584   25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSFMLIpTLN 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 423 IKDNIAY------GRPNASEAEIIEAAKFANIHDFINSLPkkyetqvaergSRLSGGERQRVAIARAILRDPRILILDEA 496
Cdd:PRK10584  105 ALENVELpallrgESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173

                         170       180
                  ....*....|....*....|....*...
gi 1277238834 497 TSSLDAETESLIRDALERLMKGRTTFII 524
Cdd:PRK10584  174 TGNLDRQTGDKIADLLFSLNREHGTTLI 201
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
 337-549 1.59e-16

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


Pssm-ID: 273907 [Multi-domain]  Cd Length: 243  Bit Score: 79.23  E-value: 1.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLL--RFYDPTSGRILVDGQDIKTAKL-ESLRKQIAVVP 413
Cdd:TIGR01978   4 KDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghPSYEVTSGTILFKGQDLLELEPdERARAGLFLAF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 Q---EIalfsgtikdniaygrPNASEAEIIEAAKFA----------NIHDFINSLPKKYET--QVAERGSR-----LSGG 473
Cdd:TIGR01978  84 QypeEI---------------PGVSNLEFLRSALNArrsargeeplDLLDFEKLLKEKLALldMDEEFLNRsvnegFSGG 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 474 ERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAH--RLYAVEHANRIVVIDNKQILEIG 549
Cdd:TIGR01978 149 EKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLRePDRSFLIITHyqRLLNYIKPDYVHVLLDGRIVKSG 227
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 347-556 1.77e-16

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 82.79  E-value: 1.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 347 EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLrFYDPT----SGRILVDGQDIKTAKLeslrKQIAVVPQEIALFSGT 422
Cdd:TIGR00955  39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKEM----RAISAYVQQDDLFIPT 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 423 I--------------KDNIAYGRPNASEAEIIEAAKFANIHDFInslpkkyeTQVAERGSRLSGGERQRVAIARAILRDP 488
Cdd:TIGR00955 114 LtvrehlmfqahlrmPRRVTKKEKRERVDEVLQALGLRKCANTR--------IGVPGRVKGLSGGERKRLAFASELLTDP 185

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 489 RILILDEATSSLDAETESLIRDALERL-MKGRTTFIIAH----RLYavEHANRIVVIDNKQILEIGSHQELLQ 556
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHqpssELF--ELFDKIILMAEGRVAYLGSPDQAVP 256
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
356-541 1.88e-16

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 82.55  E-value: 1.88e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 356 VKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILvdgQDIKtakleslrkqIAVVPQEI-ALFSGTIKDNIAygrpna 434
Cdd:PRK13409  362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---PELK----------ISYKPQYIkPDYDGTVEDLLR------ 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 435 SEAEIIEAAKFanIHDFIN--SLPKKYETQVAErgsrLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDAL 512
Cdd:PRK13409  423 SITDDLGSSYY--KSEIIKplQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAI 496

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1277238834 513 ERLMKGR--TTFIIAHRLYAVEH-ANRIVVID 541
Cdd:PRK13409  497 RRIAEEReaTALVVDHDIYMIDYiSDRLMVFE 528
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
348-557 2.87e-16

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 79.95  E-value: 2.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDP----TSGRILVDGQDIktAKLeSLRKQIAVVPQEIALF---- 419
Cdd:COG4170    22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDL--LKL-SPRERRKIIGREIAMIfqep 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 420 ------SGTIKDNIA------------YGRPNASEAEIIEAAKFANI--HDFI-NSLPkkYEtqvaergsrLSGGERQRV 478
Cdd:COG4170    99 sscldpSAKIGDQLIeaipswtfkgkwWQRFKWRKKRAIELLHRVGIkdHKDImNSYP--HE---------LTEGECQKV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 479 AIARAILRDPRILILDEATSSLDAETESLIRDALERL--MKGRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIGSHQELL 555
Cdd:COG4170   168 MIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnqLQGTSILLISHDLESISQwADTITVLYCGQTVESGPTEQIL 247


                  ..
gi 1277238834 556 QK 557
Cdd:COG4170   248 KS 249
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 355-541 8.25e-16

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: 80.60  E-value: 8.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 355 KVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRIlvdGQDIKtakleslrkqIAVVPQEI-ALFSGTIKDNI--AYGR 431
Cdd:COG1245   362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLK----------ISYKPQYIsPDYDGTVEEFLrsANTD 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 432 PNAS---EAEIIEAAkfanihdfinSLPKKYETQVAErgsrLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLI 508
Cdd:COG1245   429 DFGSsyyKTEIIKPL----------GLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1277238834 509 RDALERLM--KGRTTFIIAHRLYAVEH-ANRIVVID 541
Cdd:COG1245   495 AKAIRRFAenRGKTAMVVDHDIYLIDYiSDRLMVFE 530
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 347-512 1.17e-15

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 79.69  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 347 EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQ-IAVVPQE------IALF 419
Cdd:COG3845   272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDrlgrglVPDM 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 420 SgtIKDNIA---YGRPNASEAEIIeaaKFANIHDFINSLPKKY-------ETQVaergSRLSGGERQRVAIARAILRDPR 489
Cdd:COG3845   352 S--VAENLIlgrYRRPPFSRGGFL---DRKAIRAFAEELIEEFdvrtpgpDTPA----RSLSGGNQQKVILARELSRDPK 422

                         170       180
                  ....*....|....*....|...
gi 1277238834 490 ILILDEATSSLDAETESLIRDAL 512
Cdd:COG3845   423 LLIAAQPTRGLDVGAIEFIHQRL 445
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 334-541 1.41e-15

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 79.99  E-value: 1.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLlrfydptSGRILVD------GQDIKTAKLEslrk 407
Cdd:PRK11147    4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdgriiyEQDLIVARLQ---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 408 QIAvvPQEIAlfsGTIKDNIAYGRPNASEA---------------------------EIIEAA---KFAN-IHDFINSLP 456
Cdd:PRK11147   73 QDP--PRNVE---GTVYDFVAEGIEEQAEYlkryhdishlvetdpseknlnelaklqEQLDHHnlwQLENrINEVLAQLG 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 457 KKYETQVAErgsrLSGGERQRVAIARAILRDPRILILDEATSSLDAETeslIrDALERLMK---GRTTFIIAHRLYAVEH 533
Cdd:PRK11147  148 LDPDAALSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---I-EWLEGFLKtfqGSIIFISHDRSFIRNM 219


                  ....*...
gi 1277238834 534 ANRIVVID 541
Cdd:PRK11147  220 ATRIVDLD 227
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 338-555 3.01e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 76.29  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 338 NISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSG-----RILVDGQDIKTAK-LESLRKQIAV 411
Cdd:PRK14271   26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRdVLEFRRRVGM 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 VPQEIALFSGTIKDNIAYG-RPN----------ASEAEIIEAAKFANIHDFINSLPkkyetqvaergSRLSGGERQRVAI 480
Cdd:PRK14271  106 LFQRPNPFPMSIMDNVLAGvRAHklvprkefrgVAQARLTEVGLWDAVKDRLSDSP-----------FRLSGGQQQLLCL 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 481 ARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQELL 555
Cdd:PRK14271  175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEGPTEQLF 250
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 337-564 4.33e-15

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 75.45  E-value: 4.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRF--YDPTSGRILVDGQDIKTAKLEsLRKQIAVV-- 412
Cdd:CHL00131   11 KNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIFla 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 ---PQEIALFSGTIKDNIAYGRP----NASEAEIIEAAKFAN-IHDFINSLPKKYETQVAErgsRLSGGERQRVAIARAI 484
Cdd:CHL00131   90 fqyPIEIPGVSNADFLRLAYNSKrkfqGLPELDPLEFLEIINeKLKLVGMDPSFLSRNVNE---GFSGGEKKRNEILQMA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 485 LRDPRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAH--RLYAVEHANRIVVIDNKQILEIGSHQ--ELLQKDG 559
Cdd:CHL00131  167 LLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKKG 246


                  ....*
gi 1277238834 560 lYKYL 564
Cdd:CHL00131  247 -YDWL 250
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 356-569 5.09e-15

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 74.97  E-value: 5.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 356 VKPGEIIALVGRTGAGKSTLTS----LLlrfydPTSGRILVDGQDIKTAKLESLRKQIAVVPQEI-ALFSGTIKDNIAYG 430
Cdd:PRK03695   19 VRAGEILHLVGPNGAGKSTLLArmagLL-----PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQtPPFAMPVFQYLTLH 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 431 RPNASEAEIIEAAkfanIHDFINS--LPKKYETQVaergSRLSGGERQRVAIARAILR-DPRI------LILDEATSSLD 501
Cdd:PRK03695   94 QPDKTRTEAVASA----LNEVAEAlgLDDKLGRSV----NQLSGGEWQRVRLAAVVLQvWPDInpagqlLLLDEPMNSLD 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 502 AETESlirdALERLMK-----GRTTFIIAHRL-YAVEHANRIVVIDNKQILEIGSHQELLQKDGLYKyLYAIQF 569
Cdd:PRK03695  166 VAQQA----ALDRLLSelcqqGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQ-VFGVNF 234
hmuV PRK13547
heme ABC transporter ATP-binding protein;
334-558 6.11e-15

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 75.25  E-value: 6.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLL-RFYDP-------TSGRILVDGQDIKTAKLESL 405
Cdd:PRK13547    2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGgaprgarVTGDVTLNGEPLAAIDAPRL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 406 RKQIAVVPQEI-ALFSGTIKDNIAYGR-PNASEA--------EIIEAAkfanihdfinsLPKKYETQVAERG-SRLSGGE 474
Cdd:PRK13547   82 ARLRAVLPQAAqPAFAFSAREIVLLGRyPHARRAgalthrdgEIAWQA-----------LALAGATALVGRDvTTLSGGE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 475 RQRVAIARAI---------LRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRL-YAVEHANRIVVIDN 542
Cdd:PRK13547  151 LARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPnLAARHADRIAMLAD 230

                         250
                  ....*....|....*.
gi 1277238834 543 KQILEIGSHQELLQKD 558
Cdd:PRK13547  231 GAIVAHGAPADVLTPA 246
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 334-520 2.31e-14

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: 71.89  E-value: 2.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISF----AYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLL-LRFYDPT-SGRILVDGQDIKtaklESLRK 407
Cdd:cd03232     4 LTWKNLNYtvpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRPLD----KNFQR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 408 QIAVVPQEIALFsgtikdniaygrpnaSEAEIIEAAKF-ANIhdfinslpkkyetqvaeRGsrLSGGERQRVAIARAILR 486
Cdd:cd03232    80 STGYVEQQDVHS---------------PNLTVREALRFsALL-----------------RG--LSVEQRKRLTIGVELAA 125

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1277238834 487 DPRILILDEATSSLDAETESLIRDALERL-MKGRT 520
Cdd:cd03232   126 KPSILFLDEPTSGLDSQAAYNIVRFLKKLaDSGQA 160
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 348-527 3.47e-14

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 71.91  E-value: 3.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFY--DPTSGRILVDGQDIktakleslrkqiavvPQEialfsGTIKD 425
Cdd:COG2401    45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----ASLID 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 426 NIAYGRPNASEAEIIEAAKFANIHDFInslpKKYetqvaergSRLSGGERQRVAIARAILRDPRILILDEATSSLDAETE 505
Cdd:COG2401   105 AIGRKGDFKDAVELLNAVGLSDAVLWL----RRF--------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172

                         170       180
                  ....*....|....*....|....
gi 1277238834 506 SLIRDALERLM-KGRTTFIIA-HR 527
Cdd:COG2401   173 KRVARNLQKLArRAGITLVVAtHH 196
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 337-549 5.58e-14

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 72.27  E-value: 5.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESL---------RK 407
Cdd:PRK11701   10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaerrrllRT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 408 QIAVVPQE------IALFSGTikdNIA----------YGRPNASEAEIIEAAKFANihDFINSLPKKYetqvaergsrlS 471
Cdd:PRK11701   90 EWGFVHQHprdglrMQVSAGG---NIGerlmavgarhYGDIRATAGDWLERVEIDA--ARIDDLPTTF-----------S 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 472 GGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK--GRTTFIIAHRLyAVEH--ANRIVVIDNKQILE 547
Cdd:PRK11701  154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDL-AVARllAHRLLVMKQGRVVE 232


                  ..
gi 1277238834 548 IG 549
Cdd:PRK11701  233 SG 234
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 334-527 2.69e-13

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 68.82  E-value: 2.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTaKLESLRKQIAVVP 413
Cdd:PRK13540    2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QEIALFSG-TIKDNIAYGRPNASEA----EIIEAAKFANIHDFINSLpkkyetqvaergsrLSGGERQRVAIARAILRDP 488
Cdd:PRK13540   81 HRSGINPYlTLRENCLYDIHFSPGAvgitELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKA 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1277238834 489 RILILDEATSSLDAET-ESLIRDALERLMKGRTTFIIAHR 527
Cdd:PRK13540  147 KLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQ 186
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 313-560 3.35e-13

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 72.23  E-value: 3.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 313 DVKPSIADLP-----GAKKLPRINGEInfENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTS 387
Cdd:PRK15064  296 EVKPSSRQNPfirfeQDKKLHRNALEV--ENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDS 373

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 388 GRilvdgqdIKTAKleslRKQIAVVPQ--------EIALFS-----GTIKDNI-----AYGRPNASEAEIIEAAKFanih 449
Cdd:PRK15064  374 GT-------VKWSE----NANIGYYAQdhaydfenDLTLFDwmsqwRQEGDDEqavrgTLGRLLFSQDDIKKSVKV---- 438

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 450 dfinslpkkyetqvaergsrLSGGERQRVAIARAILRDPRILILDEATSSLDAET-ESLiRDALErLMKGRTTFIIAHRL 528
Cdd:PRK15064  439 --------------------LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESiESL-NMALE-KYEGTLIFVSHDRE 496

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1277238834 529 YAVEHANRIVVIDNKQILEI-GSHQELLQKDGL 560
Cdd:PRK15064  497 FVSSLATRIIEITPDGVVDFsGTYEEYLRSQGI 529
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 334-554 6.34e-13

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 70.16  E-value: 6.34e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEV----LQNINLKVKPGEIIALVGRTGAGKStLTSLLLRFYDPTSGRILVD-----GQDIKTAKlES 404
Cdd:PRK11022    4 LNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKS-VSSLAIMGLIDYPGRVMAEklefnGQDLQRIS-EK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 405 LRKQIavVPQEIALFsgtIKDNIAYGRPNASEA-EIIEAAKfanIHDFINSLPKKYE-----TQVA--ERGSR------- 469
Cdd:PRK11022   82 ERRNL--VGAEVAMI---FQDPMTSLNPCYTVGfQIMEAIK---VHQGGNKKTRRQRaidllNQVGipDPASRldvyphq 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 470 LSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTT--FIIAHRLYAV-EHANRIVVIDNKQIL 546
Cdd:PRK11022  154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMalVLITHDLALVaEAAHKIIVMYAGQVV 233


                  ....*...
gi 1277238834 547 EIGSHQEL 554
Cdd:PRK11022  234 ETGKAHDI 241
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 351-501 7.96e-13

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 70.73  E-value: 7.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 351 NINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYD-PTSGRILVDGQDIKT-AKLESLRKQIAVVPQE-----IALFSGtI 423
Cdd:PRK13549  280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIrNPQQAIAQGIAMVPEDrkrdgIVPVMG-V 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 424 KDNI---AYGRpNASEAEIIEAAKFANIHDFINSLpkKYETQVAE-RGSRLSGGERQRVAIARAILRDPRILILDEATSS 499
Cdd:PRK13549  359 GKNItlaALDR-FTGGSRIDDAAELKTILESIQRL--KVKTASPElAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRG 435


                  ..
gi 1277238834 500 LD 501
Cdd:PRK13549  436 ID 437
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
341-555 1.72e-12

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 67.89  E-value: 1.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 341 FAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQEIA--- 417
Cdd:PRK15112   21 FRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStsl 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 418 --------LFSGTIKDNIAYgRPNASEAEIIEAAKFANI-HDFINSLPKKyetqvaergsrLSGGERQRVAIARAILRDP 488
Cdd:PRK15112  101 nprqrisqILDFPLRLNTDL-EPEQREKQIIETLRQVGLlPDHASYYPHM-----------LAPGQKQRLGLARALILRP 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 489 RILILDEATSSLDAETES-LIRDALERLMKGRTTFI-IAHRLYAVEH-ANRIVVIDNKQILEIGSHQELL 555
Cdd:PRK15112  169 KVIIADEALASLDMSMRSqLINLMLELQEKQGISYIyVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVL 238
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 345-529 1.81e-12

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 69.96  E-value: 1.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 345 NEEVLQNINLKVKPGEIIALVGRTGAGKSTLTslllrfydptsgRIL--VDGQDIKTAKLESLRKqIAVVPQEIAL-FSG 421
Cdd:TIGR03719  17 KKEILKDISLSFFPGAKIGVLGLNGAGKSTLL------------RIMagVDKDFNGEARPQPGIK-VGYLPQEPQLdPTK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 422 TIKDNI-------------------AYGRPNAS-------EAEIIEAAKFANIHDFINSL---------PKKyETQVAEr 466
Cdd:TIGR03719  84 TVRENVeegvaeikdaldrfneisaKYAEPDADfdklaaeQAELQEIIDAADAWDLDSQLeiamdalrcPPW-DADVTK- 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 467 gsrLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLmKGrTTFIIAHRLY 529
Cdd:TIGR03719 162 ---LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTHDRY 219
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 328-526 1.99e-12

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 69.58  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 328 PRINGE-INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVdGQDIKTAKLESLR 406
Cdd:TIGR03719 316 PRLGDKvIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLAYVDQSR 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 407 KQIA---VVPQEIAlfSGTikdniaygrpnaseaEIIEAAKFAnihdfINSlpKKYETQVAERGS-------RLSGGERQ 476
Cdd:TIGR03719 395 DALDpnkTVWEEIS--GGL---------------DIIKLGKRE-----IPS--RAYVGRFNFKGSdqqkkvgQLSGGERN 450

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1277238834 477 RVAIARAILRDPRILILDEATSSLDAETESLIRDALERLmkGRTTFIIAH 526
Cdd:TIGR03719 451 RVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISH 498
ABC_6TM_ATM1_ABCB7 cd18582
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...
 70-275 2.28e-12

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: 67.91  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  70 LFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGEL---VSRVMNDIQTLqatLFTGFVTLIPhSLLLLGL 146
Cdd:cd18582    53 LFNELRDALFARVSQRAVRRLALRVFRHLHSLSLRFHLSRKTGALsraIERGTRGIEFL---LRFLLFNILP-TILELLL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 147 MGYIFWLN--WQLSLLTLVALPLIVQVIRIFAKEIREISEgvQQKAADI--TSHLQETISQVKTVKSFAMEKEELAKFKG 222
Cdd:cd18582   129 VCGILWYLygWSYALITLVTVALYVAFTIKVTEWRTKFRR--EMNEADNeaNAKAVDSLLNYETVKYFNNEEYEAERYDK 206

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 223 KTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLI 275
Cdd:cd18582   207 ALAKYEKAAVKSQTSLALLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDFV 259
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 347-545 2.46e-12

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 69.31  E-value: 2.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 347 EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAK-LESLRKQIAVVP---QEIALF-SG 421
Cdd:PRK15439  277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPedrQSSGLYlDA 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 422 TIKDNI---AYGRPNASEAEIIEAAKFANIHDFINSlpKKYETQVAERgsRLSGGERQRVAIARAILRDPRILILDEATS 498
Cdd:PRK15439  357 PLAWNVcalTHNRRGFWIKPARENAVLERYRRALNI--KFNHAEQAAR--TLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1277238834 499 SLDAETESLIRDALERLMKGRTTFI-IAHRLYAVEH-ANRIVVIDNKQI 545
Cdd:PRK15439  433 GVDVSARNDIYQLIRSIAAQNVAVLfISSDLEEIEQmADRVLVMHQGEI 481
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 284-527 2.75e-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: 69.39  E-value: 2.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 284 MTDPGNTLSKAYSIIQQGMASTKRIFEVLDV----------KPSIAD-------------LPGAKKLPRINGEINFENIS 340
Cdd:TIGR00954 379 AADALGRLMLAGRDMTRLAGFTARVDTLLQVlddvksgnfkRPRVEEiesgreggrnsnlVPGRGIVEYQDNGIKFENIP 458

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 341 FAYENEEVL-QNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGqdiktakleslRKQIAVVPQEIALF 419
Cdd:TIGR00954 459 LVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMT 527

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 420 SGTIKDNIAY-------GRPNASEAEIIEAAKFANIHDFInslpkKYE---TQVAERGSRLSGGERQRVAIARAILRDPR 489
Cdd:TIGR00954 528 LGTLRDQIIYpdssedmKRRGLSDKDLEQILDNVQLTHIL-----EREggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQ 602

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1277238834 490 ILILDEATSSLDAETESLIRDALERlmKGRTTFIIAHR 527
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHR 638
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 347-520 3.74e-12

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: 65.75  E-value: 3.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 347 EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLL---LRFYDPTSGRILVDGQDIKTAKlESLRKQIAVVPQEIALFsgti 423
Cdd:cd03233    21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYKEFA-EKYPGEIIYVSEEDVHF---- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 424 kdniaygrPNASEAEIIEAAKFANIHDFInslpkkyetqvaeRGsrLSGGERQRVAIARAILRDPRILILDEATSSLDAE 503
Cdd:cd03233    96 --------PTLTVRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152

                         170
                  ....*....|....*..
gi 1277238834 504 TeslirdALERLMKGRT 520
Cdd:cd03233   153 T------ALEILKCIRT 163
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 334-538 3.87e-12

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 66.35  E-value: 3.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLL--RFYDPTSGRILVDGQDIKTAKLESlRKQIAV 411
Cdd:PRK09580    2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPED-RAGEGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 412 V-----PQEIALFSGTIKDNIAYgrpNA----SEAEIIEAAKFAnihDFIN------SLPKKYETQVAERGsrLSGGERQ 476
Cdd:PRK09580   81 FmafqyPVEIPGVSNQFFLQTAL---NAvrsyRGQEPLDRFDFQ---DLMEekiallKMPEDLLTRSVNVG--FSGGEKK 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 477 RVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFIIahrlyaVEHANRIV 538
Cdd:PRK09580  153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFII------VTHYQRIL 208
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 337-512 5.03e-12

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: 65.21  E-value: 5.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKlESLRKQIAVVPQEI 416
Cdd:cd03231     4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR-DSIARGLLYLGHAP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 417 ALFSG-TIKDNIAYGRPNASEAEIIEAAKFANIHDFiNSLPKKYetqvaergsrLSGGERQRVAIARAILRDPRILILDE 495
Cdd:cd03231    83 GIKTTlSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDE 151

                         170
                  ....*....|....*..
gi 1277238834 496 ATSSLDAETESLIRDAL 512
Cdd:cd03231   152 PTTALDKAGVARFAEAM 168
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 338-556 5.75e-12

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 68.34  E-value: 5.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 338 NISFAYENEEV--LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSG-------------RILVDGQDIKTAKL 402
Cdd:PRK10261   19 NIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGlvqcdkmllrrrsRQVIELSEQSAAQM 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 403 ESLR-KQIAVVPQE-------IALFSGTIKDNIAYGRPNASEAEIIEAAKFANIHDFINSlpkkyETQVAERGSRLSGGE 474
Cdd:PRK10261   99 RHVRgADMAMIFQEpmtslnpVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEA-----QTILSRYPHQLSGGM 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 475 RQRVAIARAILRDPRILILDEATSSLD----AETESLIRdALERLMKGRTTFIIAHRLYAVEHANRIVVIDNKQILEIGS 550
Cdd:PRK10261  174 RQRVMIAMALSCRPAVLIADEPTTALDvtiqAQILQLIK-VLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252


                  ....*.
gi 1277238834 551 HQELLQ 556
Cdd:PRK10261  253 VEQIFH 258
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 334-508 1.09e-11

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 67.50  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRI-LVDGqdIKTA-----KLESLRk 407
Cdd:PRK10636  313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKG--IKLGyfaqhQLEFLR- 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 408 qiavvPQEIALfsgtikDNIAYGRPNASEAEiieaakfanIHDFINSLPKKYEtQVAERGSRLSGGERQRVAIARAILRD 487
Cdd:PRK10636  390 -----ADESPL------QHLARLAPQELEQK---------LRDYLGGFGFQGD-KVTEETRRFSGGEKARLVLALIVWQR 448

                         170       180
                  ....*....|....*....|....*.
gi 1277238834 488 PRILILDEATSSLD-----AETESLI 508
Cdd:PRK10636  449 PNLLLLDEPTNHLDldmrqALTEALI 474
ABC_6TM_LapB_like cd18587
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ...
 79-275 1.20e-11

Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.


Pssm-ID: 350031  Cd Length: 293  Bit Score: 65.54  E-value: 1.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  79 SYFV---AQRIIVDLRNQVYEHLQDLSLDFYAKwNTGELVSRvMNDIQTLQ-----ATLfTGFVTLiPHSLLLLGLmgyI 150
Cdd:cd18587    63 AYFIdvaGKRADVILSSRLFERVLGLRLEARPA-SVGSFANN-LREFESVRdfftsATL-TALIDL-PFVLLFLAV---I 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 151 FWLNWQLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDI 230
Cdd:cd18587   136 ALIGGPLALVPLVAIPLVLLYGLLLQKPLRRLVEESMRESAQKNALLVESLSGLETIKALGAEGRMQRRWEEAVAALARS 215

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1277238834 231 SMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLI 275
Cdd:cd18587   216 SLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLISDGELTMGGLI 260
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
329-563 4.72e-11

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 65.19  E-value: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 329 RINGEINFE--NISfAYENEEVlQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIK-TAKLESL 405
Cdd:PRK09700  259 NLAHETVFEvrNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISpRSPLDAV 336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 406 RKQIAVVPQ---EIALFSG-TIKDNIAYGRPnaseaeiIEAAKFANIHDFINSlpkKYETQVAERG-------------- 467
Cdd:PRK09700  337 KKGMAYITEsrrDNGFFPNfSIAQNMAISRS-------LKDGGYKGAMGLFHE---VDEQRTAENQrellalkchsvnqn 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 468 -SRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRL---YAVehANRIVVIDN 542
Cdd:PRK09700  407 iTELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELpeiITV--CDRIAVFCE 484

                         250       260
                  ....*....|....*....|.
gi 1277238834 543 KQILEIGSHQELLQKDGLYKY 563
Cdd:PRK09700  485 GRLTQILTNRDDMSEEEIMAW 505
PLN03211 PLN03211
ABC transporter G-25; Provisional
 344-527 6.23e-11

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 65.29  E-value: 6.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 344 ENEEVLQNINLKVKPGEIIALVGRTGAGKST-LTSLLLRFYDPT-SGRILVDGQDIKTAKLeslrKQIAVVPQeialfsg 421
Cdd:PLN03211   79 QERTILNGVTGMASPGEILAVLGPSGSGKSTlLNALAGRIQGNNfTGTILANNRKPTKQIL----KRTGFVTQ------- 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 422 tikDNIAYGRPNASEAEIieaakFANIHDFINSLPKKYETQVAE---------------------RGsrLSGGERQRVAI 480
Cdd:PLN03211  148 ---DDILYPHLTVRETLV-----FCSLLRLPKSLTKQEKILVAEsviselgltkcentiignsfiRG--ISGGERKRVSI 217

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1277238834 481 ARAILRDPRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHR 527
Cdd:PLN03211  218 AHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAqKGKTIVTSMHQ 265
ABC_6TM_PrtD_like cd18586
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ...
 50-306 6.65e-11

Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides


Pssm-ID: 350030 [Multi-domain]  Cd Length: 291  Bit Score: 63.39  E-value: 6.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  50 NMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQATL 129
Cdd:cd18586    37 SLSTLLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELPLESRPSGYWQQLLRDLDTLRNFLTGPS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 130 FTGFVTLiPHSLLLLGLmgyIFWLNWQLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKS 209
Cdd:cd18586   117 LFAFFDL-PWAPLFLAV---IFLIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 210 FAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISfatalgimtdpGN 289
Cdd:cd18586   193 LGMLGNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGELTIGALIA-----------AS 261

                         250
                  ....*....|....*...
gi 1277238834 290 TLS-KAYSIIQQGMASTK 306
Cdd:cd18586   262 ILSgRALAPIDQLVGAWK 279
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 349-532 8.65e-11

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 64.53  E-value: 8.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVPQ-EI-ALFSGTIKDN 426
Cdd:PRK13545   40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENiELkGLMMGLTKEK 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 427 IAYGRPnaseaEIIEaakFANIHDFINSLPKKYetqvaergsrlSGGERQRVAIARAILRDPRILILDEATSSLDaetES 506
Cdd:PRK13545  120 IKEIIP-----EIIE---FADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGD---QT 177

                         170       180       190
                  ....*....|....*....|....*....|
gi 1277238834 507 LIRDALERL----MKGRTTFIIAHRLYAVE 532
Cdd:PRK13545  178 FTKKCLDKMnefkEQGKTIFFISHSLSQVK 207
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
350-514 1.06e-10

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 61.36  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 350 QNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKlESLRKQIavvpqeiaLFSG---TIKD- 425
Cdd:PRK13538   18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQR-DEYHQDL--------LYLGhqpGIKTe 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 426 -----NIAY---GRPNASEAEIIEAAKFANIHDFINsLPKKYetqvaergsrLSGGERQRVAIARAILRDPRILILDEAT 497
Cdd:PRK13538   89 ltaleNLRFyqrLHGPGDDEALWEALAQVGLAGFED-VPVRQ----------LSAGQQRRVALARLWLTRAPLWILDEPF 157

                         170       180
                  ....*....|....*....|.
gi 1277238834 498 SSLD----AETESLIRDALER 514
Cdd:PRK13538  158 TAIDkqgvARLEALLAQHAEQ 178
ABC_6TM_AarD_CydD cd18584
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ...
 22-168 1.95e-10

Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).


Pssm-ID: 350028 [Multi-domain]  Cd Length: 290  Bit Score: 62.04  E-value: 1.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  22 TICTALVTSTTLLIAPLVGYIFQ--LIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQ 99
Cdd:cd18584     2 VLLGLLAALLIIAQAWLLARIIAgvFLEGAGLAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARLL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 100 DLSLDFYAKWNTGELVSRVMNDIQTLQAtLFTGF------VTLIPhsLLLLglmGYIFWLNWQLSLLTLVALPLI 168
Cdd:cd18584    82 ALGPALLRRQSSGELATLLTEGVDALDG-YFARYlpqlvlAAIVP--LLIL---VAVFPLDWVSALILLVTAPLI 150
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
351-526 3.28e-10

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 63.22  E-value: 3.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 351 NINLKVKPGEIIALVGRTGAGKST----LTSLLlrfyDPTSGRIL-----VDGQDIKTakleslRKQIAVVPQEIALFSG 421
Cdd:NF033858  284 HVSFRIRRGEIFGFLGSNGCGKSTtmkmLTGLL----PASEGEAWlfgqpVDAGDIAT------RRRVGYMSQAFSLYGE 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 422 -TIKDNIA-----YGRPNASEAEIIE--AAKFaNIHDFINSLPkkyetqvaergSRLSGGERQRVAIARAILRDPRILIL 493
Cdd:NF033858  354 lTVRQNLElharlFHLPAAEIAARVAemLERF-DLADVADALP-----------DSLPLGIRQRLSLAVAVIHKPELLIL 421

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1277238834 494 DEATSSLD--AetesliRDALERLM------KGRTTFIIAH 526
Cdd:NF033858  422 DEPTSGVDpvA------RDMFWRLLielsreDGVTIFISTH 456
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 345-504 5.12e-10

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 62.06  E-value: 5.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 345 NEEVLQNINLKVKPGEIIALVGRTGAGKSTLTslllrfydptsgRIL--VDGQDIKTAKLESLRKqIAVVPQEIAL-FSG 421
Cdd:PRK11819   19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLL------------RIMagVDKEFEGEARPAPGIK-VGYLPQEPQLdPEK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 422 TIKDNI-------------------AYGRPNA-SEA---------EIIEAAkfaNIHDfINS----------LPKKyETQ 462
Cdd:PRK11819   86 TVRENVeegvaevkaaldrfneiyaAYAEPDAdFDAlaaeqgelqEIIDAA---DAWD-LDSqleiamdalrCPPW-DAK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1277238834 463 VaergSRLSGGERQRVAIARAILRDPRILILDEATSSLDAET 504
Cdd:PRK11819  161 V----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 358-519 6.60e-10

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: 57.77  E-value: 6.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  358 PGEIIALVGRTGAGKSTLTSLLLRFYDPTSGR-ILVDGQDIKTAKLESLRKQIavvpqeialfsgtikdniaygrpnase 436
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLLII--------------------------- 53

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  437 aeiieaakfanihdfinslpkkyetqVAERGSRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLM 516
Cdd:smart00382  54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRL 107


                   ...
gi 1277238834  517 KGR 519
Cdd:smart00382 108 LLL 110
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
356-528 7.78e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 61.36  E-value: 7.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 356 VKPGEIIALVGRTGAGKSTLTSLLlrfydptSGRIL-----VDGQDIKTAKLESLR-------------KQIAVV--PQE 415
Cdd:PRK13409   96 PKEGKVTGILGPNGIGKTTAVKIL-------SGELIpnlgdYEEEPSWDEVLKRFRgtelqnyfkklynGEIKVVhkPQY 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 416 IAL----FSGTIKDNIAygrpNASEAEII-EAAKFANIHdfiNSLPKKYETqvaergsrLSGGERQRVAIARAILRDPRI 490
Cdd:PRK13409  169 VDLipkvFKGKVRELLK----KVDERGKLdEVVERLGLE---NILDRDISE--------LSGGELQRVAIAAALLRDADF 233

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1277238834 491 LILDEATSSLDAETESLIRDALERLMKGRTTFIIAHRL 528
Cdd:PRK13409  234 YFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 357-528 8.35e-10

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: 8.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 357 KPGEIIALVGRTGAGKSTLTSLL--------------------LRFYdptSGRILVDG-QDIKTAKLESLRK--QIAVVP 413
Cdd:COG1245    97 KKGKVTGILGPNGIGKSTALKILsgelkpnlgdydeepswdevLKRF---RGTELQDYfKKLANGEIKVAHKpqYVDLIP 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 414 QeiaLFSGTIKDNIAygrpNASE----AEIIEAAKFANIHDfinslpkkyetqvaERGSRLSGGERQRVAIARAILRDPR 489
Cdd:COG1245   174 K---VFKGTVRELLE----KVDErgklDELAEKLGLENILD--------------RDISELSGGELQRVAIAAALLRDAD 232

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1277238834 490 ILILDEATSSLD----AETESLIRDALErlmKGRTTFIIAHRL 528
Cdd:COG1245   233 FYFFDEPSSYLDiyqrLNVARLIRELAE---EGKYVLVVEHDL 272
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 351-501 8.86e-10

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: 61.38  E-value: 8.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 351 NINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPT-SGRILVDGQ--DIKTAkLESLRKQIAVVPQEIALfSGTIKD-- 425
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNP-AQAIRAGIAMVPEDRKR-HGIVPIlg 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 426 ---NIAYGRPN--ASEAEIIEAAKFANIHDFINSLPKKYETQVAERGsRLSGGERQRVAIARAILRDPRILILDEATSSL 500
Cdd:TIGR02633 356 vgkNITLSVLKsfCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434


                  .
gi 1277238834 501 D 501
Cdd:TIGR02633 435 D 435
ABC_6TM_CydC cd18585
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ...
 35-309 9.30e-10

Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).


Pssm-ID: 350029 [Multi-domain]  Cd Length: 290  Bit Score: 59.80  E-value: 9.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  35 IAPLVGYIFqliedkNMFLLnlsALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGEL 114
Cdd:cd18585    24 LAGLAAPTF------NYFTP---AAGVRGFAITRTAGRYGERLVSHDATFRLLSNLRVWFYRKLEPLAPARLQKYRSGDL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 115 VSRVMNDIQTLQAT---LFTGFVTLIphsLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIR-IFAKEIREISEGVQQKA 190
Cdd:cd18585    95 LNRIVADIDTLDNLylrVLSPPVVAL---LVILATILFLAFFSPALALILLAGLLLAGVVIPlLFYRLGKKIGQQLVQLR 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 191 ADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLS 270
Cdd:cd18585   172 AELRTELVDGLQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGAPLVQNGALD 251

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1277238834 271 LPQLISFatALGIMT--DPGNTLSKAYSIIQQGMASTKRIF 309
Cdd:cd18585   252 GALLAML--VFAVLAsfEAVAPLPLAFQYLGETRAAARRLF 290
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
352-539 1.15e-09

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 60.70  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 352 INLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQ--DIKTAKlESLRKQIAVVPQE------IALFSgtI 423
Cdd:PRK11288  272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPR-DAIRAGIMLCPEDrkaegiIPVHS--V 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 424 KDNIAYG-RPNASEAE-IIEAAKFANIHD-FINSLPKKyeTQVAERGSR-LSGGERQRVAIARAILRDPRILILDEATSS 499
Cdd:PRK11288  349 ADNINISaRRHHLRAGcLINNRWEAENADrFIRSLNIK--TPSREQLIMnLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1277238834 500 LDAETESLIRDALERLMK-GRTTFIIAHRLYAVEH-ANRIVV 539
Cdd:PRK11288  427 IDVGAKHEIYNVIYELAAqGVAVLFVSSDLPEVLGvADRIVV 468
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
349-557 1.22e-09

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 59.44  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 349 LQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKQIAVVP--QEIALFSGTIKDN 426
Cdd:PRK13546   40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIEniEFKMLCMGFKRKE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 427 IAYGRPnaseaEIIEaakFANIHDFINSLPKKYetqvaergsrlSGGERQRVAIARAILRDPRILILDEATSSLDAE-TE 505
Cdd:PRK13546  120 IKAMTP-----KIIE---FSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGDQTfAQ 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 506 SLIRDALERLMKGRTTFIIAHRLYAV-EHANRIVVIDNKQILEIGSHQELLQK 557
Cdd:PRK13546  181 KCLDKIYEFKEQNKTIFFVSHNLGQVrQFCTKIAWIEGGKLKDYGELDDVLPK 233
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 328-513 1.48e-09

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 60.52  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 328 PRINGE-INFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVdGQDIKTAKLESLR 406
Cdd:PRK11819  318 PRLGDKvIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKLAYVDQSR 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 407 KQIA---VVPQEIalfSGtikdniaygrpnasEAEIIEAAKFAnihdfINSlpKKYETQVAERGS-------RLSGGERQ 476
Cdd:PRK11819  397 DALDpnkTVWEEI---SG--------------GLDIIKVGNRE-----IPS--RAYVGRFNFKGGdqqkkvgVLSGGERN 452

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1277238834 477 RVAIARAILRDPRILILDEATSSLDAETESLIRDALE 513
Cdd:PRK11819  453 RLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 351-554 2.64e-09

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 58.97  E-value: 2.64e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 351 NINLKVKPGEIIALVGRTGAGKS-TLTSL--LLRFYDPTSGRILVDGQDI---KTAKLESLR-KQIAVVPQE-------- 415
Cdd:PRK09473   34 DLNFSLRAGETLGIVGESGSGKSqTAFALmgLLAANGRIGGSATFNGREIlnlPEKELNKLRaEQISMIFQDpmtslnpy 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 416 ----------IALFSGtikdniaYGRPNASEAEI--IEAAKFANIHDFINSLPKKYetqvaergsrlSGGERQRVAIARA 483
Cdd:PRK09473  114 mrvgeqlmevLMLHKG-------MSKAEAFEESVrmLDAVKMPEARKRMKMYPHEF-----------SGGMRQRVMIAMA 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 484 ILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFI--IAHRLYAVEH-ANRIVVIDNKQILEIGSHQEL 554
Cdd:PRK09473  176 LLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIimITHDLGVVAGiCDKVLVMYAGRTMEYGNARDV 249
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 351-501 2.94e-09

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 59.63  E-value: 2.94e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 351 NINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAK-LESLRKQIAVVPQEI---ALFSG-TIKD 425
Cdd:PRK10762  270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLANGIVYISEDRkrdGLVLGmSVKE 349

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 426 NI---AYGRPNASEAEIIEAAKFANIHDFINSLPKKYETQVAERGSrLSGGERQRVAIARAILRDPRILILDEATSSLD 501
Cdd:PRK10762  350 NMsltALRYFSRAGGSLKHADEQQAVSDFIRLFNIKTPSMEQAIGL-LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 356-541 3.50e-09

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 57.76  E-value: 3.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 356 VKPGEIIALVGRTGAGKST--------LTSLLLRFYDPTSGRILVDG------QDIKTAKLESLRKqIAVVPQEIalfsg 421
Cdd:cd03236    23 PREGQVLGLVGPNGIGKSTalkilagkLKPNLGKFDDPPDWDEILDEfrgselQNYFTKLLEGDVK-VIVKPQYV----- 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 422 tikDNIaygrPNASEAEIIEAAKFANIHDFINSLPKKYE-TQVAERG-SRLSGGERQRVAIARAILRDPRILILDEATSS 499
Cdd:cd03236    97 ---DLI----PKAVKGKVGELLKKKDERGKLDELVDQLElRHVLDRNiDQLSGGELQRVAIAAALARDADFYFFDEPSSY 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1277238834 500 LDaeteslIRdalERLMKGRttfiIAHRLyaVEHANRIVVID 541
Cdd:cd03236   170 LD------IK---QRLNAAR----LIREL--AEDDNYVLVVE 196
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 348-556 7.28e-09

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 58.97  E-value: 7.28e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  348 VLQNINLKVKPGEIIALVGRTGAGKSTL----TSLLLRFYDPTSGRILVDGQDiktakLESLRKQ-----IAVVPQEIAL 418
Cdd:TIGR00956   76 ILKPMDGLIKPGELTVVLGRPGSGCSTLlktiASNTDGFHIGVEGVITYDGIT-----PEEIKKHyrgdvVYNAETDVHF 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  419 FSGTIKDNIAYG--------RP-NASEAEIieAAKFANIHDFINSLPKKYETQVAE---RGsrLSGGERQRVAIARAILR 486
Cdd:TIGR00956  151 PHLTVGETLDFAarcktpqnRPdGVSREEY--AKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLG 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  487 DPRILILDEATSSLDAETeslirdALE--RLMKGRTTFIIAHRLYAVEHA--------NRIVVIDNKQILEIGSHQELLQ 556
Cdd:TIGR00956  227 GAKIQCWDNATRGLDSAT------ALEfiRALKTSANILDTTPLVAIYQCsqdayelfDKVIVLYEGYQIYFGPADKAKQ 300
PLN03073 PLN03073
ABC transporter F family; Provisional
 316-522 8.32e-09

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 58.33  E-value: 8.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 316 PSIADLPGAKKlpringeINFENISFAYENEEVL-QNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRIL--- 391
Cdd:PLN03073  498 PTPDDRPGPPI-------ISFSDASFGYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFrsa 570

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 392 -----------VDGQDIKTAKLESLRKQIAVVPQE---IALFSGTIKDNIAygrpnaseaeiieaakfanihdfinsLPK 457
Cdd:PLN03073  571 kvrmavfsqhhVDGLDLSSNPLLYMMRCFPGVPEQklrAHLGSFGVTGNLA--------------------------LQP 624

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 458 KYEtqvaergsrLSGGERQRVAIARAILRDPRILILDEATSSLDAeteslirDALERLMKGRTTF 522
Cdd:PLN03073  625 MYT---------LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL-------DAVEALIQGLVLF 673
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 356-559 1.63e-08

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: 57.72  E-value: 1.63e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  356 VKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTaKLESLRKQIAVVPQEIA---LFSGtiKDNI-AYGR 431
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAiddLLTG--REHLyLYAR 2038

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  432 PNASEAEIIEAAKFANIHDFINSLpkkYETQVAergSRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDA 511
Cdd:TIGR01257 2039 LRGVPAEEIEKVANWSIQSLGLSL---YADRLA---GTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1277238834  512 LERLMK-GRTTFIIAHRLYAVEH-ANRIVVIDNKQILEIGSHQELLQKDG 559
Cdd:TIGR01257 2113 IVSIIReGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 356-541 2.82e-08

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: 53.73  E-value: 2.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 356 VKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDgqdiktakleslRKQIAVVPQEIalfsgtikdniaygrpnas 435
Cdd:cd03222    22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD------------GITPVYKPQYI------------------- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 436 eaeiieaakfanihdfinslpkkyetqvaergsRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERL 515
Cdd:cd03222    71 ---------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117

                         170       180
                  ....*....|....*....|....*....
gi 1277238834 516 -MKG-RTTFIIAHRLYAVEH-ANRIVVID 541
Cdd:cd03222   118 sEEGkKTALVVEHDLAVLDYlSDRIHVFE 146
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
470-555 2.99e-08

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 55.58  E-value: 2.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 470 LSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMKGRTTFI--IAHRLYAVEH-ANRIVVIDNKQIL 546
Cdd:PRK15093  159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLSQwADKINVLYCGQTV 238


                  ....*....
gi 1277238834 547 EIGSHQELL 555
Cdd:PRK15093  239 ETAPSKELV 247
ABC_6TM_NHLM_bacteriocin cd18569
Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ...
 59-308 4.18e-08

Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350013 [Multi-domain]  Cd Length: 294  Bit Score: 54.79  E-value: 4.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  59 LGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVM-ND------IQTLqATLFT 131
Cdd:cd18569    46 LGMALTALLQGLLTWLQQYYLLRLETKLALSSSSRFFWHVLRLPVEFFSQRYAGDIASRVQsNDrvanllSGQL-ATTVL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 132 GFVTLIphslLLLGLMgyiFWLNWQLSLLTLVALPLIVQVIRIFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFA 211
Cdd:cd18569   125 NLVMAV----FYALLM---LQYDVPLTLIGIAIALLNLLVLRLVSRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASG 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 212 MEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTL 291
Cdd:cd18569   198 AESDFFSRWAGYQAKVLNAQQELGRTNQLLGALPTLLSALTNAAILGLGGLLVMDGALTIGMLVAFQSLMASFLAPVNSL 277

                         250
                  ....*....|....*..
gi 1277238834 292 SKAYSIIQQGMASTKRI 308
Cdd:cd18569   278 VGLGGTLQEMRGDMERL 294
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 344-504 4.25e-08

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 56.27  E-value: 4.25e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  344 ENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDP---TSGRILVDGQDIKtaklESLRKQIAVVPQE-IALF 419
Cdd:TIGR00956  774 EKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLD----SSFQRSIGYVQQQdLHLP 849

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  420 SGTIKDNI---AYGR-PNaseaEIIEAAKFANIHDFINSLP-KKY-ETQVAERGSRLSGGERQRVAIARAILRDPRILI- 492
Cdd:TIGR00956  850 TSTVRESLrfsAYLRqPK----SVSKSEKMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLf 925

                          170
                   ....*....|..
gi 1277238834  493 LDEATSSLDAET 504
Cdd:TIGR00956  926 LDEPTSGLDSQT 937
GguA NF040905
sugar ABC transporter ATP-binding protein;
348-501 1.97e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 53.64  E-value: 1.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLT-SLLLRFYDP-TSGRILVDGQDIKTAKL-ESLRKQIAVVPQ---EIAL-FS 420
Cdd:NF040905  275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKEVDVSTVsDAIDAGLAYVTEdrkGYGLnLI 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 421 GTIKDNI-AYGRPNASEAEII---EAAKFANihDFINSLPKKYETqVAERGSRLSGGERQRVAIARAILRDPRILILDEA 496
Cdd:NF040905  355 DDIKRNItLANLGKVSRRGVIdenEEIKVAE--EYRKKMNIKTPS-VFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEP 431


                  ....*
gi 1277238834 497 TSSLD 501
Cdd:NF040905  432 TRGID 436
ABC_6TM_ABCC_D1 cd18579
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ...
 23-308 2.30e-07

Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350023 [Multi-domain]  Cd Length: 289  Bit Score: 52.49  E-value: 2.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  23 ICTALVTSTTLLIAPLVGYiFQLIEDKNMFLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLS 102
Cdd:cd18579     8 LEDLLSLAQPLLLGLLISY-LSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRKALRLS 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 103 LDFYAKWNTGELVSRVMNDIQTLQATLFTGFVTLIphSLLLLGLMGYIFW--LNWQlSLLTLVALPLIVQVIRIFAKEIR 180
Cdd:cd18579    87 SSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWS--APLQIIVALYLLYrlLGWA-ALAGLGVLLLLIPLQAFLAKLIS 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 181 EISEGVQQKAADITSHLQETISQVKTVKSFAMEK-----------EELAKFKGKteksfdISMRAVQILATQ-NPVIALL 248
Cdd:cd18579   164 KLRKKLMKATDERVKLTNEILSGIKVIKLYAWEKpflkrieelrkKELKALRKF------GYLRALNSFLFFsTPVLVSL 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 249 QTIAVvgIVWFGgreiisGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGMASTKRI 308
Cdd:cd18579   238 ATFAT--YVLLG------NPLTAAKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
339-530 2.45e-07

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 51.77  E-value: 2.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 339 ISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLEslrKQIAVVPQEIAL 418
Cdd:PRK13543   17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS---RFMAYLGHLPGL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 419 fsgtikdniaygRPNASEAEiieaakfaNIHdFINSL--------PKKYETQVAERG------SRLSGGERQRVAIARAI 484
Cdd:PRK13543   94 ------------KADLSTLE--------NLH-FLCGLhgrrakqmPGSALAIVGLAGyedtlvRQLSAGQKKRLALARLW 152

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1277238834 485 LRDPRILILDEATSSLDAETESLIRDALE-RLMKGRTTFIIAHRLYA 530
Cdd:PRK13543  153 LSPAPLWLLDEPYANLDLEGITLVNRMISaHLRGGGAALVTTHGAYA 199
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 345-561 2.48e-07

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 53.58  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 345 NEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAK-LESLRKQIAVVPQE------IA 417
Cdd:PRK10982  260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEErrstgiYA 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 418 LFSGTIKDNIAYGRPNASEAEIIEAAKF-ANIHDFINSLPKKYETQVAERGSrLSGGERQRVAIARAILRDPRILILDEA 496
Cdd:PRK10982  340 YLDIGFNSLISNIRNYKNKVGLLDNSRMkSDTQWVIDSMRVKTPGHRTQIGS-LSGGNQQKVIIGRWLLTQPEILMLDEP 418

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 497 TSSLDA----ETESLIrdaLERLMKGRTTFIIAH---RLYAVehANRIVVIDNKQILEI-----GSHQELLQKDGLY 561
Cdd:PRK10982  419 TRGIDVgakfEIYQLI---AELAKKDKGIIIISSempELLGI--TDRILVMSNGLVAGIvdtktTTQNEILRLASLH 490
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 333-556 3.51e-07

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 53.09  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 333 EINFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDGQDIKTAKLESLRKqiaVV 412
Cdd:PRK10938    3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK---LV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 PQEIA-----LFSGTIKDniaYGRpnaSEAEIIEAakfaNIHDfiNSLPKKYETQ------VAERGSRLSGGERQRVAIA 481
Cdd:PRK10938   80 SDEWQrnntdMLSPGEDD---TGR---TTAEIIQD----EVKD--PARCEQLAQQfgitalLDRRFKYLSTGETRKTLLC 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 482 RAILRDPRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLYAV-EHANRIVVIDNKQILEIGSHQELLQ 556
Cdd:PRK10938  148 QALMSEPDLLILDEPFDGLDVASRQQLAELLASLHqSGITLVLVLNRFDEIpDFVQFAGVLADCTLAETGEREEILQ 224
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
 28-275 4.11e-07

Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.


Pssm-ID: 350002 [Multi-domain]  Cd Length: 312  Bit Score: 51.89  E-value: 4.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  28 VTSTTLLIAPLVGYIFQLIEDKNMFLLNLSALGMIGLFVLkglfqYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYA 107
Cdd:cd18558    37 ITGNSSGLNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITA-----YIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 108 KWNTGELVSRVMNDIQTLQ--------------ATLFTGFVtliphsllllglMGYIFwlNWQLSLLTLVALPLIVQVIR 173
Cdd:cd18558   112 VNDTGELNTRLADDVSKINegigdkigvifqniATFGTGFI------------IGFIR--GWKLTLVILAISPVLGLSAV 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 174 IFAKEIREISEGVQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEKSFDISMRAVQILATQNPVIALLQTIAV 253
Cdd:cd18558   178 VWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASY 257

                         250       260
                  ....*....|....*....|..
gi 1277238834 254 VGIVWFGGREIISGSLSLPQLI 275
Cdd:cd18558   258 ALAFWYGTYLVTQQEYSIGEVL 279
ABC_6TM_NdvA_beta-glucan_exporter_like cd18562
Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar ...
 92-277 5.13e-07

Six-transmembrane helical domain of the cyclic beta-glucan ABC transporter NdvA, and similar proteins; This group represents the six-transmembrane domain of NdvA, an ATP-dependent exporter of cyclic beta glucans, and similar proteins. NdvA is required for nodulation of legume roots and is involved in beta-(1,2)-glucan export to the periplasm. NdvA mutants in Brucella abortus and Sinorhizobium meliloti have been shown to exhibit decreased virulence in mice and inhibit intracellular multiplication in HeLa cells. These results suggest that cyclic beta-(1,2)-glucan is required to transport into the periplasmatic space to function as a virulence factor. 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: 350006 [Multi-domain]  Cd Length: 289  Bit Score: 51.47  E-value: 5.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  92 NQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLqATLFTGF-----VTLIphSLLLLGLMGyiFWLNWQLSLLtLVALP 166
Cdd:cd18562    73 ASYFEHVITLPLSFHSQRGSGRLLRIMLRGTDAL-FGLWLGFfrehlAALV--SLIVLLPVA--LWMNWRLALL-LVVLA 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 167 LIVQVIRIFAkeIREISEG---VQQKAADITSHLQETISQVKTVKSFAMEKEELAKFKGKTEksfdismravQILATQNP 243
Cdd:cd18562   147 AVYAALNRLV--MRRTKAGqaaVEEHHSALSGRVGDVIGNVTVVQSYTRLAAETSALRGITR----------RLLAAQYP 214

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1277238834 244 VI---ALL-------QTIAVVGIVWFGGREIISGSLSLPQLISF 277
Cdd:cd18562   215 VLnwwALAsvltraaSTLTMVAIFALGAWLVQRGELTVGEIVSF 258
ABC_6TM_AarD_CydDC_like cd18781
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine ...
 32-177 5.45e-07

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; This subgroup belongs to the ABC_6TM_AarD_CydDC_like subgroup of the ABC_6TM exporter family. The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs). 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: 350054 [Multi-domain]  Cd Length: 290  Bit Score: 51.38  E-value: 5.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  32 TLLIAPLVGYIFQLIEDKNmfLLNLSALGMIGLFVLKGLFQYGQEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNT 111
Cdd:cd18781    16 VFSIANLLQKLLEGKLTTA--SLLIVLGILAIAIIVRFICTRLASRASYRASADVKKTLREKIYDKLLRLGPSYQEKVST 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834 112 GELVSRVMNDIQTLQaTLFTGFVTLIPHSLLL-LGLMGYIFWLNWQLSLLTLVALPLI------VQVI--RIFAK 177
Cdd:cd18781    94 AEVVQLSVEGVEQLE-IYFGRYLPQFFYSMLApLTLFVVLAPINWKAALVLLICVPLIpisiiaVQKIakKLLSK 167
PLN03073 PLN03073
ABC transporter F family; Provisional
 333-501 8.23e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 52.17  E-value: 8.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 333 EINFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKST-LTSLLLRFYD--PTSGRIL-----VDGQDI------- 397
Cdd:PLN03073  177 DIHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTfLRYMAMHAIDgiPKNCQILhveqeVVGDDTtalqcvl 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 398 -----KTAKLE---SLRKQIAVVPQEIALFSGTIKDNIAYGRPNASEA--------EIIEA----AKFANIhdfINSLPK 457
Cdd:PLN03073  257 ntdieRTQLLEeeaQLVAQQRELEFETETGKGKGANKDGVDKDAVSQRleeiykrlELIDAytaeARAASI---LAGLSF 333

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1277238834 458 KYETQVaERGSRLSGGERQRVAIARAILRDPRILILDEATSSLD 501
Cdd:PLN03073  334 TPEMQV-KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
ABC_6TM_HMT1 cd18583
Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...
 62-307 9.00e-07

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: 50.60  E-value: 9.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  62 IGLFVLKGLFQYG------QEYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVsRVMNDIQTLQATLFTGFVT 135
Cdd:cd18583    38 IGLYVLLRFLQSGgglgllRSWLWIPVEQYSYRALSTAAFNHVMNLSMDFHDSKKSGEVL-KAIEQGSSINDLLEQILFQ 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 136 LIPHSLLLLGLMGYIFWL-NWQLSLLTLValpliVQVIRIFAkEIReISEGVQQKAADIT-------SHLQETISQVKTV 207
Cdd:cd18583   117 IVPMIIDLVIAIVYLYYLfDPYMGLIVAV-----VMVLYVWS-TIK-LTSWRTKLRRDMIdadreerSILTESLLNWETV 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 208 KSFAMEKEELAKFKG------KTEKSFDISMRAVQilATQNpviaLLQTIAVVGIVWFGGREIISGSLSLPQLISFATAL 281
Cdd:cd18583   190 KYFNREPYEKERYREavknyqKAERKYLFSLNLLN--AVQS----LILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYW 263

                         250       260
                  ....*....|....*....|....*.
gi 1277238834 282 GIMTDPGNTLSKAYSIIQQGMASTKR 307
Cdd:cd18583   264 AQLSGPLNFFATLYRSIQSDLIDAER 289
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
461-559 3.40e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 49.35  E-value: 3.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 461 TQVAERGS-RLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK-GRTTFIIAHRLYAVEH-ANRI 537
Cdd:NF000106  135 TEAAGRAAaKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQlAHEL 214

                          90       100
                  ....*....|....*....|..
gi 1277238834 538 VVIDNKQILEIGSHQELLQKDG 559
Cdd:NF000106  215 TVIDRGRVIADGKVDELKTKVG 236
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
337-559 3.98e-06

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 49.74  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 337 ENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLL-----LRfydptSGRILVDGQDIKTAK-LESLRKQIA 410
Cdd:NF033858    5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIagarkIQ-----QGRVEVLGGDMADARhRRAVCPRIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 411 VVPQeialfsG---------TIKDNIAY-GR---PNASE--AEIIEAAKFANIHDFinslpkkyetqvAER-GSRLSGGE 474
Cdd:NF033858   80 YMPQ------GlgknlyptlSVFENLDFfGRlfgQDAAErrRRIDELLRATGLAPF------------ADRpAGKLSGGM 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 475 RQRVAIARAILRDPRILILDEATSSLDaeteSLIR----DALERLMKGRT--TFIIAhRLYaVEHANR---IVVIDNKQI 545
Cdd:NF033858  142 KQKLGLCCALIHDPDLLILDEPTTGVD----PLSRrqfwELIDRIRAERPgmSVLVA-TAY-MEEAERfdwLVAMDAGRV 215

                         250
                  ....*....|....
gi 1277238834 546 LEIGSHQELLQKDG 559
Cdd:NF033858  216 LATGTPAELLARTG 229
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 338-526 1.20e-05

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 47.96  E-value: 1.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 338 NISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILVDgQDIKTAKL-------ESLR---- 406
Cdd:PRK15064    6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD-PNERLGKLrqdqfafEEFTvldt 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 407 -----KQIAVVPQEialfsgtiKDNIaYGRPNASEAEIIEAA----KFAnihdfinslpkKYETQVAER--GSRLSG--- 472
Cdd:PRK15064   85 vimghTELWEVKQE--------RDRI-YALPEMSEEDGMKVAdlevKFA-----------EMDGYTAEAraGELLLGvgi 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 473 --------------GERQRVAIARAILRDPRILILDEATSSLDAETeslIRdALERLMKGR--TTFIIAH 526
Cdd:PRK15064  145 peeqhyglmsevapGWKLRVLLAQALFSNPDILLLDEPTNNLDINT---IR-WLEDVLNERnsTMIIISH 210
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 334-508 1.33e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 46.02  E-value: 1.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 334 INFENISFAYENEeVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRFYDPTSGRILvdgqdIKTAKLESLRKQ-IAVV 412
Cdd:PRK13541    2 LSLHQLQFNIEQK-NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIY-----YKNCNINNIAKPyCTYI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 413 PQEIAL-FSGTIKDNIAYGRPNASEAEIIEAAkfanIHDFinslpkKYETQVAERGSRLSGGERQRVAIARAILRDPRIL 491
Cdd:PRK13541   76 GHNLGLkLEMTVFENLKFWSEIYNSAETLYAA----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLW 145

                         170
                  ....*....|....*..
gi 1277238834 492 ILDEATSSLDAETESLI 508
Cdd:PRK13541  146 LLDEVETNLSKENRDLL 162
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 319-528 1.78e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 47.32  E-value: 1.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 319 ADLPGAK-KLPRINGEINFENISFAYENEEVLQNINLKVKPGEIIALVGRTGAGKSTLTSL------------LLRFydp 385
Cdd:PRK10938  245 PDEPSARhALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndLTLF--- 321

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 386 tsGRILVDGQ---DIKtakleslrKQIAVVPQEIAL---FSGTIKDNIAYGRPNA-------SEAEIIEAAKFANIHDFI 452
Cdd:PRK10938  322 --GRRRGSGEtiwDIK--------KHIGYVSSSLHLdyrVSTSVRNVILSGFFDSigiyqavSDRQQKLAQQWLDILGID 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 453 NSLPKKyetqvaeRGSRLSGGERQRVAIARAILRDPRILILDEATSSLDAETESLIRDALERLM-KGRTTFI-------- 523
Cdd:PRK10938  392 KRTADA-------PFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETQLLfvshhaed 464


                  ....*....
gi 1277238834 524 ----IAHRL 528
Cdd:PRK10938  465 apacITHRL 473
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 468-538 4.76e-05

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: 44.24  E-value: 4.76e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 468 SRLSGGERQRVAIARAILRDPR--ILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLYAVEHANRIV 538
Cdd:cd03238    86 STLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADWII 159
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
 47-310 8.92e-05

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.


Pssm-ID: 350024 [Multi-domain]  Cd Length: 294  Bit Score: 44.80  E-value: 8.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  47 EDKNMFLLNLSALGMIGLFVLkGLFQYgqeYLSYFVAQRIIVDLRNQVYEHLQDLSLDFYAKWNTGELVSRVMNDIQTLQ 126
Cdd:cd18580    35 SSSGYYLGVYAALLVLASVLL-VLLRW---LLFVLAGLRASRRLHDKLLRSVLRAPMSFFDTTPSGRILNRFSKDIGLID 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 127 ATLFTGFVTLIPHSLLLLGLMGYIFWLNWQLSLLTLVALPLIVQVIRIFAKEIREIS--EGVQQkaADITSHLQETISQV 204
Cdd:cd18580   111 EELPLALLDFLQSLFSVLGSLIVIAIVSPYFLIVLPPLLVVYYLLQRYYLRTSRQLRrlESESR--SPLYSHFSETLSGL 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 205 KTVKSFAMEKEELAKFKGKTeksfDISMRAVQIL-ATQ-------NPVIALLQTIAVVGIVWFggREIISGS---LSLPQ 273
Cdd:cd18580   189 STIRAFGWQERFIEENLRLL----DASQRAFYLLlAVQrwlglrlDLLGALLALVVALLAVLL--RSSISAGlvgLALTY 262

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1277238834 274 LISFATALgimtdpgNTLSKAYSIIQQGMASTKRIFE 310
Cdd:cd18580   263 ALSLTGSL-------QWLVRQWTELETSMVSVERILE 292
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 348-547 1.16e-04

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 45.16  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 348 VLQNINLKVKPGEIIALVGRTGAGKSTLTSLLlrfydptSGRILVDGQDIKTAKLESLrkqiAVVPQEI-ALFSGTIKDN 426
Cdd:PRK10636   16 LLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGNWQL----AWVNQETpALPQPALEYV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 427 IAYGRP-NASEAEIIEAAK------FANIH---DFINSLPKK------------YETQVAERGSRLSGGERQRVAIARAI 484
Cdd:PRK10636   85 IDGDREyRQLEAQLHDANErndghaIATIHgklDAIDAWTIRsraasllhglgfSNEQLERPVSDFSGGWRMRLNLAQAL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1277238834 485 LRDPRILILDEATSSLDAeteslirDA---LERLMKGR--TTFIIAH-RLYAVEHANRIVVIDNKQILE 547
Cdd:PRK10636  165 ICRSDLLLLDEPTNHLDL-------DAviwLEKWLKSYqgTLILISHdRDFLDPIVDKIIHIEQQSLFE 226
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 338-538 1.27e-04

ATP-binding cassette domain I 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: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 43.79  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 338 NISFAYENEevLQNINLKVKPGEIIALVGRTGAGKSTLT----------------SLLLRFYDPTSGRILVDgqdiktaK 401
Cdd:cd03270     2 IVRGAREHN--LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslSAYARQFLGQMDKPDVD-------S 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 402 LESLRKQIAVVPQEIALFS----GTIKDNIAYGRPNASEAEIIEAAKFanihdfINSLPKKYETqVAERGSRLSGGERQR 477
Cdd:cd03270    73 IEGLSPAIAIDQKTTSRNPrstvGTVTEIYDYLRLLFARVGIRERLGF------LVDVGLGYLT-LSRSAPTLSGGEAQR 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1277238834 478 VAIARAI---LrDPRILILDEATSSL-DAETESLIrDALERLM-KGRTTFIIAHRLYAVEHANRIV 538
Cdd:cd03270   146 IRLATQIgsgL-TGVLYVLDEPSIGLhPRDNDRLI-ETLKRLRdLGNTVLVVEHDEDTIRAADHVI 209
ABC_6TM_ABCB6 cd18581
Six-transmembrane helical domain of the ATP-binding cassette subfamily B member 6, ...
 81-302 2.43e-04

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: 43.39  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  81 FVAQRIIVDLrnqvYEHLQDLSLDFYAKWNTGElVSRVM----NDIQT-LQATLFTGFVTLIPhslLLLGLMGYIFWLNW 155
Cdd:cd18581    76 FTTREISVKL----FAHLHSLSLRWHLSRKTGE-VLRVMdrgtSSINSlLSYVLFNIGPTIAD---IIIAIIYFAIAFNP 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 156 QLSLLTLVA----LPLIVQVIRIFAKEIREISE---GVQQKAADitSHLqetisQVKTVKSFAMEKEELAKFKGKTEKSF 228
Cdd:cd18581   148 WFGLIVFVTmalyLILTIIITEWRTKFRREMNKldnEKRAKAVD--SLL-----NFETVKYYNAERFEVERYRRAIDDYQ 220

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1277238834 229 DISMRAVQILATQNPVIALLQTIAVVGIVWFGGREIISGSLSLPQLISFATALGIMTDPGNTLSKAYSIIQQGM 302
Cdd:cd18581   221 VAEWKSNASLNLLNTAQNLIITIGLLAGSLLCAYFVVEGKLTVGDFVLFLTYIIQLYAPLNFFGTYYRMIQQSF 294
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 470-538 2.80e-04

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 43.85  E-value: 2.80e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 470 LSGGERQRVAIARAILRD---PRILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLYAVEHANRIV 538
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVdKGNTVVVIEHNLDVIKTADYII 902
PLN03140 PLN03140
ABC transporter G family member; Provisional
 347-527 2.93e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 44.07  E-value: 2.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  347 EVLQNINLKVKPGEIIALVGRTGAGKSTLTSLLLRfyDPTSGRIlvDGqDIKTAKLESLRKQIAVV-----------PQ- 414
Cdd:PLN03140   894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--EG-DIRISGFPKKQETFARIsgyceqndihsPQv 968

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834  415 ---EIALFSGTIKDNIAYGRPNASE--AEIIEAAKFANIHDFINSLPKKyetqvaergSRLSGGERQRVAIARAILRDPR 489
Cdd:PLN03140   969 tvrESLIYSAFLRLPKEVSKEEKMMfvDEVMELVELDNLKDAIVGLPGV---------TGLSTEQRKRLTIAVELVANPS 1039

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1277238834  490 ILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHR 527
Cdd:PLN03140  1040 IIFMDEPTSGLDARAAAIVMRTVRNTVdTGRTVVCTIHQ 1078
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 470-538 5.84e-04

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


Pssm-ID: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 41.83  E-value: 5.84e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1277238834 470 LSGGERQRVAIARAILRDPR---ILILDEATSSLDAETESLIRDALERLM-KGRTTFIIAHRLYAVEHANRIV 538
Cdd:cd03271   170 LSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKCADWII 242
SbcC_Walker_B pfam13558
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ...
 460-513 6.33e-04

SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.


Pssm-ID: 463921 [Multi-domain]  Cd Length: 90  Bit Score: 39.14  E-value: 6.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 460 ETQVAERGSRLSGGERQRVA-------------IARAILRDPRILILDEATSSLDAETeslIRDALE 513
Cdd:pfam13558  23 EVETYRRSGGLSGGEKQLLAylplaaalaaqygSAEGRPPAPRLVFLDEAFAKLDEEN---IRTALE 86
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
 369-541 2.21e-03

ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 39.94  E-value: 2.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 369 GAGKSTLTSLLLRFYDPTSGRILVDGQDIKtaklesLRKQIavvpqeialfsGTIKDNIAYGRPNASEAEII---EAAKF 445
Cdd:cd03272    66 GSGPSVMSAYVEIIFDNSDNRFPIDKEEVR------LRRTI-----------GLKKDEYFLDKKNVTKNDVMnllESAGF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 446 ANIHDF-------INSLP--KKYETQVAERgsrLSGGERQRVAIAR--AILR-DPR-ILILDEATSSLDAETesliRDAL 512
Cdd:cd03272   129 SRSNPYyivpqgkINSLTnmKQDEQQEMQQ---LSGGQKSLVALALifAIQKcDPApFYLFDEIDAALDAQY----RTAV 201

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1277238834 513 ERLMK---GRTTFII----------AHRLYAVEHANRIVVID 541
Cdd:cd03272   202 ANMIKelsDGAQFITttfrpellevADKFYGVKFRNKVSTID 243
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 465-519 2.27e-03

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


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 39.51  E-value: 2.27e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1277238834 465 ERGsRLSGGERQ------RVAIARAILRDPRILILDEATSSLDAETeslIRDALERLMKGR 519
Cdd:cd03240   112 MRG-RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---IEESLAEIIEER 168
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
361-515 3.07e-03

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 39.22  E-value: 3.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 361 IIALVGRTGAGKST-LTSLLLRFYDPTSGRILVDGQDIKTAKLE---SLRKQIAVVPQEIALFSGTIKDNIAYGRPNASE 436
Cdd:COG0419    25 LNLIVGPNGAGKSTiLEAIRYALYGKARSRSKLRSDLINVGSEEasvELEFEHGGKRYRIERRQGEFAEFLEAKPSERKE 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 437 A--EIIEAAKFANIHDFINSLPKKYETQVAERG-------------------SRLSGGERQRVAIARAILrdpriLILDe 495
Cdd:COG0419   105 AlkRLLGLEIYEELKERLKELEEALESALEELAelqklkqeilaqlsgldpiETLSGGERLRLALADLLS-----LILD- 178

                         170       180
                  ....*....|....*....|
gi 1277238834 496 aTSSLDAETESLIRDALERL 515
Cdd:COG0419   179 -FGSLDEERLERLLDALEEL 197
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 468-538 3.56e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 40.58  E-value: 3.56e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1277238834  468 SRLSGGERQRVAIARAIL---RDPRILILDEATSSLDA-ETESLIRDALERLMKGRTTFIIAHRLYAVEHANRIV 538
Cdd:PRK00635   808 SSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHThDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVL 882
PRK01156 PRK01156
chromosome segregation protein; Provisional
 457-517 4.94e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.88  E-value: 4.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1277238834 457 KKYETQVAERGSRLSGGERQ------RVAIARAILRDPRILILDEATSSLDAETESLIRDALERLMK 517
Cdd:PRK01156  789 TVSRGGMVEGIDSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLK 855
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 340-538 6.02e-03

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 38.21  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 340 SFAyeneevlQNINLKVKPGeIIALVGRTGAGKSTLTSLLlRFydptsgrilVDGQdiKTAKleSLRkqiavvpqeialf 419
Cdd:cd03278    11 SFA-------DKTTIPFPPG-LTAIVGPNGSGKSNIIDAI-RW---------VLGE--QSAK--SLR------------- 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1277238834 420 SGTIKDNIAYG---RPNASEAE-------------IIEAAKfanIHDFINSLPKKyetqvAERGSRLSGGERQRVAIAR- 482
Cdd:cd03278    56 GEKMSDVIFAGsetRKPANFAEvtltfdnsdgrysIISQGD---VSEIIEAPGKK-----VQRLSLLSGGEKALTALALl 127

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1277238834 483 -AILR---DPrILILDEATSSLD-AETESLIRdaLERLMKGRTTFI-IAHRLYAVEHANRIV 538
Cdd:cd03278   128 fAIFRvrpSP-FCVLDEVDAALDdANVERFAR--LLKEFSKETQFIvITHRKGTMEAADRLY 186
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH