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Conserved domains on  [gi|492039060|ref|WP_005728560|]
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ABC transporter ATP-binding protein [Lactobacillus crispatus]

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-572 0e+00

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


:

Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 553.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   1 MENFKIILPYLKRYKKDVVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFA 79
Cdd:COG1132    6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRiIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  80 AKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWW 159
Cdd:COG1132   86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 160 APVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFS 239
Cdd:COG1132  166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 240 AIMPAFQMIAYTVIALIVYLIGKNITAHPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRIREVLETEPDVK 319
Cdd:COG1132  246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 320 FVESG-SVAPLSGSVEFDHVSFTYPdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI 398
Cdd:COG1132  326 DPPGAvPLPPVRGEIEFENVSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 399 KDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQR 478
Cdd:COG1132  405 RDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKT 558
Cdd:COG1132  485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
                        570
                 ....*....|....
gi 492039060 559 SLVYQEIFKTQKGK 572
Cdd:COG1132  565 GGLYARLYRLQFGE 578
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-572 0e+00

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 553.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   1 MENFKIILPYLKRYKKDVVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFA 79
Cdd:COG1132    6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRiIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  80 AKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWW 159
Cdd:COG1132   86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 160 APVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFS 239
Cdd:COG1132  166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 240 AIMPAFQMIAYTVIALIVYLIGKNITAHPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRIREVLETEPDVK 319
Cdd:COG1132  246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 320 FVESG-SVAPLSGSVEFDHVSFTYPdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI 398
Cdd:COG1132  326 DPPGAvPLPPVRGEIEFENVSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 399 KDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQR 478
Cdd:COG1132  405 RDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKT 558
Cdd:COG1132  485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
                        570
                 ....*....|....
gi 492039060 559 SLVYQEIFKTQKGK 572
Cdd:COG1132  565 GGLYARLYRLQFGE 578
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
4-569 1.67e-114

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: 352.10  E-value: 1.67e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060    4 FKIILPYLKRYKKDVVCAIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLsdgiWLVVLGIIAI-----ISGIFNVYF 78
Cdd:TIGR02203   2 FRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVL----WWVPLVVIGLavlrgICSFVSTYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   79 AAKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFW 158
Cdd:TIGR02203  78 LSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  159 WAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWF 238
Cdd:TIGR02203 158 LIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  239 SAIMPAFQMIAYTVIALIVYLIGknitaHPSDIAVVSP--FVNYvltllFTIMIAGMT-LMQFSRANISLGR-------I 308
Cdd:TIGR02203 238 SISSPITQLIASLALAVVLFIAL-----FQAQAGSLTAgdFTAF-----ITAMIALIRpLKSLTNVNAPMQRglaaaesL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  309 REVLETEPDVkfvESGSVAP--LSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP 386
Cdd:TIGR02203 308 FTLLDSPPEK---DTGTRAIerARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEP 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  387 TKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGN-AQAKLHELQRAANMAQASEFIERYNDSFDHEVE 465
Cdd:TIGR02203 385 DSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  466 ERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGK 545
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
                         570       580
                  ....*....|....*....|....
gi 492039060  546 LVAQGTHEELLKTSLVYQEIFKTQ 569
Cdd:TIGR02203 545 IVERGTHNELLARNGLYAQLHNMQ 568
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
333-566 2.54e-90

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: 277.96  E-value: 2.54e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:cd03251    1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03251   81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIF 566
Cdd:cd03251  161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
162-556 6.66e-88

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 283.39  E-value: 6.66e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 162 VVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNI-VIGYWfsA 240
Cdd:PRK13657 163 VVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMpVLSWW--A 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 241 IMPAFQMIAYTVIALIVYLIGknITAHPSDIAVVSPFVNYVLtlLFTIMIAGMTLMQ--FSRANISLGRIREVLETEPDV 318
Cdd:PRK13657 241 LASVLNRAASTITMLAILVLG--AALVQKGQLRVGEVVAFVG--FATLLIGRLDQVVafINQVFMAAPKLEEFFEVEDAV 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 319 KFVE----SGSVAPLSGSVEFDHVSFTYpDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIG 394
Cdd:PRK13657 317 PDVRdppgAIDLGRVKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILID 395
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 395 GQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGG 474
Cdd:PRK13657 396 GTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGG 475
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 475 QKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEE 554
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDE 555

                 ..
gi 492039060 555 LL 556
Cdd:PRK13657 556 LV 557
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
350-499 1.36e-40

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: 144.33  E-value: 1.36e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSG-TIASNL 428
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060  429 RQGnaqAKLHELQRAANMAQASEFIERYNDSF--DHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:pfam00005  81 RLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
345-555 1.55e-09

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 59.75  E-value: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAqLIARLYDPTKGKvKIGGQNIKDVTEAALRKTVSF----VLQRAVLF 420
Cdd:NF000106  24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR-RPWRF*TWCANRRALRRTIG*hrpvR*GRRESF 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SGTiaSNLRQgnaQAKLHELQRAANMAQASEFIERYndSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:NF000106 102 SGR--ENLYM---IGR*LDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTG 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 501 LDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEEL 555
Cdd:NF000106 175 LDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqlAHELTVIDRGRVIADGKVDEL 231
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
352-502 2.12e-08

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 57.06  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 352 DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIkDVTEAALRKTVSFVLQRAVLFSG-TIASNLrq 430
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAGDIATRRRVGYMSQAFSLYGElTVRQNL-- 360
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 431 gNAQAKLHELQRAANMAQASEFIERyndsFD--HEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:NF033858 361 -ELHARLFHLPAAEIAARVAEMLER----FDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
333-556 1.08e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 55.13  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIA---RLYDptkGKVKI-GGqnikDVTEAALRK 408
Cdd:NF033858   2 ARLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgarKIQQ---GRVEVlGG----DMADARHRR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 409 TVS----FVLQravlfsG---------TIASNLR-------QGNAQ--AKLHELQRAANMAqasEFIERyndsfdhevee 466
Cdd:NF033858  73 AVCpriaYMPQ------GlgknlyptlSVFENLDffgrlfgQDAAErrRRIDELLRATGLA---PFADR----------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 467 RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESekKVQ-----QALEHELPDtttfiiaekiVSVINA------ 535
Cdd:NF033858 133 PAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS--RRQfweliDRIRAERPG----------MSVLVAtaymee 200
                        250       260
                 ....*....|....*....|....*
gi 492039060 536 ----DTILVLDDGKLVAQGTHEELL 556
Cdd:NF033858 201 aerfDWLVAMDAGRVLATGTPAELL 225
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
359-514 1.26e-07

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: 51.22  E-value: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   359 PGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVK-IGGQNIKDVTEAALRKTVsfvlqravlfsgtiasnlrqgnaqakl 437
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLII--------------------------- 53
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060   438 helqraanmaqasefieryndsfdheVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALE 514
Cdd:smart00382  54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104
GguA NF040905
sugar ABC transporter ATP-binding protein;
350-547 2.23e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 53.64  E-value: 2.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPT---KGKVKIGGQ-----NIKDvTEAalrKTVSFVLQRAVLFS 421
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcrfkDIRD-SEA---LGIVIIHQELALIP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 G-TIASNLRQGNAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:NF040905  92 YlSIAENIFLGNERAKRGVIDWNETNRRARELLAKVG--LDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492039060 501 L-DAESEKKVQQALEHELPDTTTFIIAEK---IVSVinADTILVLDDGKLV 547
Cdd:NF040905 170 LnEEDSAALLDLLLELKAQGITSIIISHKlneIRRV--ADSITVLRDGRTI 218
GguA NF040905
sugar ABC transporter ATP-binding protein;
350-502 3.47e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.79  E-value: 3.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLA-QLIARLYDP-TKGKVKIGGQ-----NIKDVTEAAL------RKTVSFVLQR 416
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKevdvsTVSDAIDAGLayvtedRKGYGLNLID 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 417 AVLFSGTIASnlrqgnaqakLHELQRAANMAQASEFI--ERYNDSFD---HEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:NF040905 356 DIKRNITLAN----------LGKVSRRGVIDENEEIKvaEEYRKKMNiktPSVFQKVGNLSGGNQQKVVLSKWLFTDPDV 425
                        170
                 ....*....|.
gi 492039060 492 LILDDSTSALD 502
Cdd:NF040905 426 LILDEPTRGID 436
 
Name Accession Description Interval E-value
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
1-572 0e+00

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 553.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   1 MENFKIILPYLKRYKKDVVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFA 79
Cdd:COG1132    6 RKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRiIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  80 AKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWW 159
Cdd:COG1132   86 ARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLAL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 160 APVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFS 239
Cdd:COG1132  166 IVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSA 245
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 240 AIMPAFQMIAYTVIALIVYLIGKNITAHPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRIREVLETEPDVK 319
Cdd:COG1132  246 LFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 320 FVESG-SVAPLSGSVEFDHVSFTYPdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI 398
Cdd:COG1132  326 DPPGAvPLPPVRGEIEFENVSFSYP-GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDI 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 399 KDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQR 478
Cdd:COG1132  405 RDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQR 484
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKT 558
Cdd:COG1132  485 IAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR 564
                        570
                 ....*....|....
gi 492039060 559 SLVYQEIFKTQKGK 572
Cdd:COG1132  565 GGLYARLYRLQFGE 578
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
3-569 1.17e-116

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: 361.84  E-value: 1.17e-116
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   3 NFKIILPYLKRYKKDVVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQavlsdgiWLVVLGIIAIISGIFNV----- 76
Cdd:COG2274  143 GLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVvIDRVLPNQDLS-------TLWVLAIGLLLALLFEGllrll 215
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  77 --YFAAKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRL-----INDMNQVMNMMmqlfmqmlrLPILIVGSFIF 149
Cdd:COG2274  216 rsYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFrdvesIREFLTGSLLT---------ALLDLLFVLIF 286
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 150 CIVII---PRFWWAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQ 226
Cdd:COG2274  287 LIVLFfysPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAK 366
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 227 LNDYNI---VIGYWFSAIMPAFQMIAYTVI-ALIVYL-IGKNITAhPSDIAVVSpFVNYVLTLLFTIMiagMTLMQFSRA 301
Cdd:COG2274  367 YLNARFklrRLSNLLSTLSGLLQQLATVALlWLGAYLvIDGQLTL-GQLIAFNI-LSGRFLAPVAQLI---GLLQRFQDA 441
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 302 NISLGRIREVLETEPDVKFVESGSVAP-LSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLI 380
Cdd:COG2274  442 KIALERLDDILDLPPEREEGRSKLSLPrLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLL 521
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 381 ARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSF 460
Cdd:COG2274  522 LGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGY 601
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 461 DHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILV 540
Cdd:COG2274  602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIV 681
                        570       580
                 ....*....|....*....|....*....
gi 492039060 541 LDDGKLVAQGTHEELLKTSLVYQEIFKTQ 569
Cdd:COG2274  682 LDKGRIVEDGTHEELLARKGLYAELVQQQ 710
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
4-569 1.67e-114

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: 352.10  E-value: 1.67e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060    4 FKIILPYLKRYKKDVVCAIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLsdgiWLVVLGIIAI-----ISGIFNVYF 78
Cdd:TIGR02203   2 FRRLWSYVRPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVL----WWVPLVVIGLavlrgICSFVSTYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   79 AAKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFW 158
Cdd:TIGR02203  78 LSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  159 WAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWF 238
Cdd:TIGR02203 158 LIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAG 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  239 SAIMPAFQMIAYTVIALIVYLIGknitaHPSDIAVVSP--FVNYvltllFTIMIAGMT-LMQFSRANISLGR-------I 308
Cdd:TIGR02203 238 SISSPITQLIASLALAVVLFIAL-----FQAQAGSLTAgdFTAF-----ITAMIALIRpLKSLTNVNAPMQRglaaaesL 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  309 REVLETEPDVkfvESGSVAP--LSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP 386
Cdd:TIGR02203 308 FTLLDSPPEK---DTGTRAIerARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEP 384
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  387 TKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGN-AQAKLHELQRAANMAQASEFIERYNDSFDHEVE 465
Cdd:TIGR02203 385 DSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGRtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIG 464
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  466 ERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGK 545
Cdd:TIGR02203 465 ENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGR 544
                         570       580
                  ....*....|....*....|....
gi 492039060  546 LVAQGTHEELLKTSLVYQEIFKTQ 569
Cdd:TIGR02203 545 IVERGTHNELLARNGLYAQLHNMQ 568
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
3-564 2.06e-94

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: 299.76  E-value: 2.06e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   3 NFKIILPYLKRYKKDVVCAIIAILVSAFSGLyqpklleniqkALMAnqkqavLSdGiWLVVlgIIAIISGIFNVYFAA-- 80
Cdd:COG4987    2 DLLRLLRLLRPHRGRLLLGVLLGLLTLLAGI-----------GLLA------LS-G-WLIA--AAALAPPILNLFVPIvg 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  81 ----KIAQGV----------------VSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNqvmnmmmqlfmqmlRL- 139
Cdd:COG4987   61 vrafAIGRTVfrylerlvshdatlrlLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVD--------------ALd 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 140 --------PILI-VGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVL-----RQMNSLFTKFQEMMDRISNQAQETLQGVR 205
Cdd:COG4987  127 nlylrvllPLLVaLLVILAAVAFLAFFSPALALVLALGLLLAGLLLpllaaRLGRRAGRRLAAARAALRARLTDLLQGAA 206
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 206 VVKSFNQGPQEIKKFDQTSDQLNDYNIVIGyWFSAIMPAFQMIAYTVIALIVYLIGKNITAH----PSDIAVVspfvnyV 281
Cdd:COG4987  207 ELAAYGALDRALARLDAAEARLAAAQRRLA-RLSALAQALLQLAAGLAVVAVLWLAAPLVAAgalsGPLLALL------V 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 282 LTLL-----FTIMIAGMTLMQFSRAniSLGRIREVLETEPDVKFVESGSVAPLSGSVEFDHVSFTYPDGDDPTLKDISFK 356
Cdd:COG4987  280 LAALalfeaLAPLPAAAQHLGRVRA--AARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLT 357
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 357 IKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAK 436
Cdd:COG4987  358 LPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDAT 437
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 437 LHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHE 516
Cdd:COG4987  438 DEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA 517
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*...
gi 492039060 517 LPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQE 564
Cdd:COG4987  518 LAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQ 565
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
10-558 5.33e-91

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: 290.89  E-value: 5.33e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  10 YLKRYKKDVVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQ-KQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVV 87
Cdd:COG4988   11 LARGARRWLALAVLLGLLSGLLIIAQAWLLASlLAGLIIGGApLSALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  88 SDLREDTYAKIQTFSFGNIKKFSAGSLTTRLIndmnqvmnmmmqlfmqmlR------------LPILIVGSFIFCIVIIP 155
Cdd:COG4988   91 RRLRRRLLEKLLALGPAWLRGKSTGELATLLT------------------EgvealdgyfaryLPQLFLAALVPLLILVA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 156 RF---WWAPVVMVA---LIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLND 229
Cdd:COG4988  153 VFpldWLSGLILLVtapLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEASEDFRK 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 230 ynivigywfsAIMP----AFQ------MIAYTVIALI-VY----LIGKNITahpsdiavvspfvnyVLTLLFTIMIAG-- 292
Cdd:COG4988  233 ----------RTMKvlrvAFLssavleFFASLSIALVaVYigfrLLGGSLT---------------LFAALFVLLLAPef 287
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 293 -MTLMQFS-----RANI--SLGRIREVLETEPDVKFVESGSVAPLSG-SVEFDHVSFTYPDGDdPTLKDISFKIKPGQMV 363
Cdd:COG4988  288 fLPLRDLGsfyhaRANGiaAAEKIFALLDAPEPAAPAGTAPLPAAGPpSIELEDVSFSYPGGR-PALDGLSLTIPPGERV 366
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 364 GIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRA 443
Cdd:COG4988  367 ALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAA 446
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 444 ANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTF 523
Cdd:COG4988  447 LEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVI 526
                        570       580       590
                 ....*....|....*....|....*....|....*
gi 492039060 524 IIAEKIVSVINADTILVLDDGKLVAQGTHEELLKT 558
Cdd:COG4988  527 LITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
333-566 2.54e-90

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: 277.96  E-value: 2.54e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:cd03251    1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03251   81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIF 566
Cdd:cd03251  161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKLH 234
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
162-556 6.66e-88

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 283.39  E-value: 6.66e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 162 VVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNI-VIGYWfsA 240
Cdd:PRK13657 163 VVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYNRIEAETQALRDIADNLLAAQMpVLSWW--A 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 241 IMPAFQMIAYTVIALIVYLIGknITAHPSDIAVVSPFVNYVLtlLFTIMIAGMTLMQ--FSRANISLGRIREVLETEPDV 318
Cdd:PRK13657 241 LASVLNRAASTITMLAILVLG--AALVQKGQLRVGEVVAFVG--FATLLIGRLDQVVafINQVFMAAPKLEEFFEVEDAV 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 319 KFVE----SGSVAPLSGSVEFDHVSFTYpDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIG 394
Cdd:PRK13657 317 PDVRdppgAIDLGRVKGAVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILID 395
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 395 GQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGG 474
Cdd:PRK13657 396 GTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGG 475
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 475 QKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEE 554
Cdd:PRK13657 476 ERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDE 555

                 ..
gi 492039060 555 LL 556
Cdd:PRK13657 556 LV 557
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
4-572 1.01e-86

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 280.37  E-value: 1.01e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   4 FKIILPYLKRYKKDVVCAIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLsdgIW--LVVLGIIAI--ISGIFNVYFA 79
Cdd:PRK11176  13 FRRLWPTIAPFKAGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVL---KWmpLVVIGLMILrgITSFISSYCI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  80 AKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFciviipRFW- 158
Cdd:PRK11176  90 SWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIM------MFYy 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 159 -W---------APVVMVALifgfgAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLN 228
Cdd:PRK11176 164 sWqlsliliviAPIVSIAI-----RVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMR 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 229 DYNIVIGYWFSAIMPAFQMIAYTVIALIVYLigkniTAHPSDIAVVSPfvnYVLTLLFTIMIAGMTLM--------QFSR 300
Cdd:PRK11176 239 QQGMKMVSASSISDPIIQLIASLALAFVLYA-----ASFPSVMDTLTA---GTITVVFSSMIALMRPLksltnvnaQFQR 310
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 301 ---ANISLGRIREvLETEPDVKFVEsgsVAPLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLA 377
Cdd:PRK11176 311 gmaACQTLFAILD-LEQEKDEGKRV---IERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIA 386
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 378 QLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQG-NAQAKLHELQRAANMAQASEFIERY 456
Cdd:PRK11176 387 NLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYArTEQYSREQIEEAARMAYAMDFINKM 466
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 457 NDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINAD 536
Cdd:PRK11176 467 DNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKAD 546
                        570       580       590
                 ....*....|....*....|....*....|....*.
gi 492039060 537 TILVLDDGKLVAQGTHEELLKTSLVYQEIFKTQKGK 572
Cdd:PRK11176 547 EILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFGQ 582
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
331-557 6.58e-85

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: 263.70  E-value: 6.58e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 331 GSVEFDHVSFTYpDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTV 410
Cdd:cd03254    1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:cd03254   80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 491 ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLK 557
Cdd:cd03254  160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLA 226
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
303-556 1.36e-82

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: 270.15  E-value: 1.36e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 303 ISLGRIREVLETEPDVKfvESGSVAPLS---GSVEFDHVSFTYpDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQL 379
Cdd:COG5265  327 ADMERMFDLLDQPPEVA--DAPDAPPLVvggGEVRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARL 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 380 IARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDS 459
Cdd:COG5265  404 LFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDG 483
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 460 FDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTIL 539
Cdd:COG5265  484 YDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEIL 563
                        250
                 ....*....|....*..
gi 492039060 540 VLDDGKLVAQGTHEELL 556
Cdd:COG5265  564 VLEAGRIVERGTHAELL 580
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
333-569 8.31e-82

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: 255.93  E-value: 8.31e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDD-PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVS 411
Cdd:cd03249    1 IEFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:cd03249   81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIFKTQ 569
Cdd:cd03249  161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
333-569 1.48e-81

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: 255.23  E-value: 1.48e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:cd03253    1 IEFENVTFAYDPGR-PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03253   80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIFKTQ 569
Cdd:cd03253  160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
18-308 8.56e-79

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: 250.01  E-value: 8.56e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  18 VVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTYA 96
Cdd:cd18548    1 AILAPLFKLLEVLLELLLPTLMADiIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  97 KIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVL 176
Cdd:cd18548   81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 177 RQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIALI 256
Cdd:cd18548  161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 492039060 257 VYLIGKNITAHPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18548  241 LWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASAKRI 292
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
333-545 1.74e-77

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: 242.29  E-value: 1.74e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:cd03228    1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTIASNLrqgnaqaklhelqraanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03228   81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGK 545
Cdd:cd03228  119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
333-569 1.58e-69

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


Pssm-ID: 213219 [Multi-domain]  Cd Length: 237  Bit Score: 224.29  E-value: 1.58e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTY-PDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVS 411
Cdd:cd03252    1 ITFEHVRFRYkPDGPV-ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:cd03252   80 VVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIFKTQ 569
Cdd:cd03252  160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
331-551 3.41e-69

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 222.75  E-value: 3.41e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 331 GSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTV 410
Cdd:cd03244    1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSGTIASNLRQGNaQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:cd03244   81 SIIPQDPVLFSGTIRSNLDPFG-EYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 491 ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGT 551
Cdd:cd03244  160 ILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
331-550 1.72e-68

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: 220.92  E-value: 1.72e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 331 GSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTV 410
Cdd:cd03245    1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:cd03245   81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 491 ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQG 550
Cdd:cd03245  161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
7-562 5.23e-67

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 230.76  E-value: 5.23e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060    7 ILPYLKRYKKDVVCAIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLSDGIWLvvLGIIAIIS--------GIFNVYF 78
Cdd:TIGR00958 152 LLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPALASAIFF--MCLLSIASsvsaglrgGSFNYTM 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   79 AAkiaqgVVSDLREDTYAKI--QTFSFGNIKKfsAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPR 156
Cdd:TIGR00958 230 AR-----INLRIREDLFRSLlrQDLGFFDENK--TGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPR 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  157 FWWAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYN----- 231
Cdd:TIGR00958 303 LTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNkrkal 382
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  232 IVIGY-WFSAIMPAFqmiaytVIALIVYLIGKNITAHPSDIAVVSPFVNYVLTL------LFTIMIAGMTLMQFSRanis 304
Cdd:TIGR00958 383 AYAGYlWTTSVLGML------IQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLgeavrvLSYVYSGMMQAVGASE---- 452
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  305 lgRIREVLETEPDVKfvESGSVAP--LSGSVEFDHVSFTYPD-GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIA 381
Cdd:TIGR00958 453 --KVFEYLDRKPNIP--LTGTLAPlnLEGLIEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ 528
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  382 RLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFD 461
Cdd:TIGR00958 529 NLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYD 608
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  462 HEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHElpDTTTFIIAEKIVSVINADTILVL 541
Cdd:TIGR00958 609 TEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRSRA--SRTVLLIAHRLSTVERADQILVL 686
                         570       580
                  ....*....|....*....|.
gi 492039060  542 DDGKLVAQGTHEELLKTSLVY 562
Cdd:TIGR00958 687 KKGSVVEMGTHKQLMEDQGCY 707
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
184-568 2.57e-65

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: 223.61  E-value: 2.57e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  184 TKFQEMMDRISNqaqetlqgVRVVKSFNQGPQEIKKFDQ-TSDQLNDYNIVIGYWfsAIMPAFQMIAYTVIALIVYLIG- 261
Cdd:TIGR01192 193 NVFKHVSDSISN--------VSVVHSYNRIEAETSALKQfTNNLLSAQYPVLDWW--ALASGLNRMASTISMMCILVIGt 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  262 ---KNITAHPSDIAVVSPFVNYVLTLLfTIMIAGMTLMQFSRAnislgRIREVLETEPDVKFVE----SGSVAPLSGSVE 334
Cdd:TIGR01192 263 vlvIKGELSVGEVIAFIGFANLLIGRL-DQMSGFITQIFEARA-----KLEDFFDLEDSVFQREepadAPELPNVKGAVE 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  335 FDHVSFTYPDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVL 414
Cdd:TIGR01192 337 FRHITFEFANSSQ-GVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVF 415
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  415 QRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILIL 494
Cdd:TIGR01192 416 QDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVL 495
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060  495 DDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIFKT 568
Cdd:TIGR01192 496 DEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLLRR 569
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
324-546 1.06e-64

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: 211.18  E-value: 1.06e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 324 GSVAP--LSGSVEFDHVSFTYPD-GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD 400
Cdd:cd03248    1 GSLAPdhLKGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 401 VTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLS 480
Cdd:cd03248   81 YEHKYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 481 IARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKL 546
Cdd:cd03248  161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
307-556 1.67e-60

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 210.45  E-value: 1.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 307 RIREVLETEPDVKFVESGSVAPLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP 386
Cdd:PRK11160 313 RINEITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP 392
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 387 TKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERyNDSFDHEVEE 466
Cdd:PRK11160 393 QQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGE 471
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 467 RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKL 546
Cdd:PRK11160 472 GGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQI 551
                        250
                 ....*....|
gi 492039060 547 VAQGTHEELL 556
Cdd:PRK11160 552 IEQGTHQELL 561
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
42-541 5.95e-59

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: 205.21  E-value: 5.95e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   42 IQKALMANQKQAVLSDG-------IWLVVLGIIAIISGIFnVYF----AAKIAQGVVSDLREDTYAKIQTFSFGNIKKFS 110
Cdd:TIGR02857  21 AQAWLLARVVDGLISAGeplaellPALGALALVLLLRALL-GWLqeraAARAAAAVKSQLRERLLEAVAALGPRWLQGRP 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  111 AGSLTTRLINDMNQVMNMMMQLfmqmlrLPILI---VGSFIFCIVIIPRFWWAPVVMV---ALIFGFGAYVLRQMNSLFT 184
Cdd:TIGR02857 100 SGELATLALEGVEALDGYFARY------LPQLVlavIVPLAILAAVFPQDWISGLILLltaPLIPIFMILIGWAAQAAAR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  185 KFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIV---IGYWFSAIMPAFQMIAYTVIAliVYlIG 261
Cdd:TIGR02857 174 KQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRvlrIAFLSSAVLELFATLSVALVA--VY-IG 250
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  262 KNITAHPSDIAvvspfvnyvlTLLFTIMIAG---MTLMQFS-----RAN--ISLGRIREVLETEPDVKFVESGSVAPLSG 331
Cdd:TIGR02857 251 FRLLAGDLDLA----------TGLFVLLLAPefyLPLRQLGaqyhaRADgvAAAEALFAVLDAAPRPLAGKAPVTAAPAS 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  332 SVEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVS 411
Cdd:TIGR02857 321 SLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIA 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  412 FVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:TIGR02857 400 WVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 492039060  492 LILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVL 541
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
163-570 6.76e-58

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 203.41  E-value: 6.76e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 163 VMVALIFGFGAyvlrQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIgywfSAIM 242
Cdd:PRK10789 149 VMAIMIKRYGD----QLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRV----ARID 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 243 PAFQMIAYTVIALIVYLI---GKNITAHPS-DIAVVSPFVNYvLTLLFTIMIAgMTLMqFS---RANISLGRIREVLETE 315
Cdd:PRK10789 221 ARFDPTIYIAIGMANLLAiggGSWMVVNGSlTLGQLTSFVMY-LGLMIWPMLA-LAWM-FNiveRGSAAYSRIRAMLAEA 297
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 316 PDVKfVESGSVAPLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGG 395
Cdd:PRK10789 298 PVVK-DGSEPVPEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHD 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 396 QNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQ 475
Cdd:PRK10789 377 IPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQ 456
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 476 KQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK10789 457 KQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQL 536
                        410
                 ....*....|....*
gi 492039060 556 LKTSLVYQEIFKTQK 570
Cdd:PRK10789 537 AQQSGWYRDMYRYQQ 551
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
162-556 3.67e-57

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: 203.65  E-value: 3.67e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  162 VVMVALIFGFGAYVLRQMNslfTKFQEMMDRISNQAQETLQGV---RV----VKSFNQGPQ---EIKKFDQTSDQLNDYN 231
Cdd:TIGR03797 285 ALVAIAVTLVLGLLQVRKE---RRLLELSGKISGLTVQLINGIsklRVagaeNRAFARWAKlfsRQRKLELSAQRIENLL 361
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  232 IVigywFSAIMPAFQMIAytVIALIVYLIGkniTAHPSdiavVSPFVNYvlTLLFTIMIAGMTlmQFSRANISL------ 305
Cdd:TIGR03797 362 TV----FNAVLPVLTSAA--LFAAAISLLG---GAGLS----LGSFLAF--NTAFGSFSGAVT--QLSNTLISIlavipl 424
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  306 -GRIREVLETEPDVkfvESGSVAP--LSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIAR 382
Cdd:TIGR03797 425 wERAKPILEALPEV---DEAKTDPgkLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLG 501
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  383 LYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLrQGNAQAKLHELQRAANMAQASEFIERYNDSFDH 462
Cdd:TIGR03797 502 FETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHT 580
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  463 EVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHElpDTTTFIIAEKIVSVINADTILVLD 542
Cdd:TIGR03797 581 VISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLD 658
                         410
                  ....*....|....
gi 492039060  543 DGKLVAQGTHEELL 556
Cdd:TIGR03797 659 AGRVVQQGTYDELM 672
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
288-557 1.80e-50

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: 182.64  E-value: 1.80e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 288 IMIAGMTLM---------------QFSRANISLGRIREVLETEPDVKfvESGSVAPLSGSVEFDHVSFTYPDGDDPTLKD 352
Cdd:COG4618  273 AMIAASILMgralapieqaiggwkQFVSARQAYRRLNELLAAVPAEP--ERMPLPRPKGRLSVENLTVVPPGSKRPILRG 350
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 353 ISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNL-RQG 431
Cdd:COG4618  351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG 430
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 432 NAQAklHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQ 511
Cdd:COG4618  431 DADP--EKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAA 508
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 492039060 512 ALEHeLPD--TTTFIIAEKiVSVIN-ADTILVLDDGKLVAQGTHEELLK 557
Cdd:COG4618  509 AIRA-LKArgATVVVITHR-PSLLAaVDKLLVLRDGRVQAFGPRDEVLA 555
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
237-525 2.72e-49

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: 178.71  E-value: 2.72e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  237 WFSAIMPAFQMIAYTVIALIVYLIGKNITAH----PSDIAVVspfvnyVLTLL--FTIMIA-GMTLMQFSRANISLGRIR 309
Cdd:TIGR02868 235 AATALGAALTLLAAGLAVLGALWAGGPAVADgrlaPVTLAVL------VLLPLaaFEAFAAlPAAAQQLTRVRAAAERIV 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  310 EVLETEPDVKFVES---GSVAPLSGSVEFDHVSFTYPdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP 386
Cdd:TIGR02868 309 EVLDAAGPVAEGSApaaGAVGLGKPTLELRDLSAGYP-GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  387 TKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEE 466
Cdd:TIGR02868 388 LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGE 467
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060  467 RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFII 525
Cdd:TIGR02868 468 GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLI 526
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
318-555 2.61e-48

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 177.34  E-value: 2.61e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 318 VKFVESGSVAPLSGSVEFDH----------VSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLaqLIARL-YDP 386
Cdd:PRK11174 325 VTFLETPLAHPQQGEKELASndpvtieaedLEILSPDGK-TLAGPLNFTLPAGQRIALVGPSGAGKTSL--LNALLgFLP 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 387 TKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEE 466
Cdd:PRK11174 402 YQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGD 481
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 467 RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKL 546
Cdd:PRK11174 482 QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQI 561

                 ....*....
gi 492039060 547 VAQGTHEEL 555
Cdd:PRK11174 562 VQQGDYAEL 570
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
333-557 5.81e-48

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: 166.74  E-value: 5.81e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:COG1122    1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAV--LFSGTIAS-------NLRQGNAQAKlhelQRAANMAQASEfIERYndsfdhevEERSANF-SGGQKQRLSIA 482
Cdd:COG1122   80 VFQNPDdqLFAPTVEEdvafgpeNLGLPREEIR----ERVEEALELVG-LEHL--------ADRPPHElSGGQKQRVAIA 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 483 RGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDT-TTFIIA----EKIVSVinADTILVLDDGKLVAQGTHEELLK 557
Cdd:COG1122  147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELL-KRLNKEgKTVIIVthdlDLVAEL--ADRVIVLDDGRIVADGTPREVFS 223
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
328-551 6.22e-48

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: 166.05  E-value: 6.22e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 328 PLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALR 407
Cdd:cd03369    2 PEHGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQRAVLFSGTIASNLrqgnaqaklhelqraanmaqasefiERYNDSFDHE------VEERSANFSGGQKQRLSI 481
Cdd:cd03369   82 SSLTIIPQDPTLFSGTIRSNL-------------------------DPFDEYSDEEiygalrVSEGGLNLSQGQRQLLCL 136
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGT 551
Cdd:cd03369  137 ARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
199-566 3.61e-47

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: 175.70  E-value: 3.61e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  199 ETLQGVRVVKSFNQgpqEIKKFDQTSDQLNDY------NIVIGYWFSAIMPAFQMIAYTVI--ALIVYLIGKNITAhpSD 270
Cdd:TIGR01193 339 EDLNGIETIKSLTS---EAERYSKIDSEFGDYlnksfkYQKADQGQQAIKAVTKLILNVVIlwTGAYLVMRGKLTL--GQ 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  271 IAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANIslgRIREVLETepDVKFVESGSVAPLS---GSVEFDHVSFTYPDGDd 347
Cdd:TIGR01193 414 LITFNALLSYFLTPLENIINLQPKLQAARVANN---RLNEVYLV--DSEFINKKKRTELNnlnGDIVINDVSYSYGYGS- 487
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASN 427
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILEN 567
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  428 LRQGNAQ-AKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESE 506
Cdd:TIGR01193 568 LLLGAKEnVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITE 647
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  507 KKVQQALEHeLPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIF 566
Cdd:TIGR01193 648 KKIVNNLLN-LQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
333-566 3.81e-46

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 162.16  E-value: 3.81e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKtVSF 412
Cdd:COG1131    1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IGY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRqgnAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:COG1131   78 VPQEPALYPDlTVRENLR---FFARLYGLPRKEARERIDELLELFG--LTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHELPDTTTFII-------AEKIvsvinADTILVLDDGKLVAQGTHEELLKTSLvyQE 564
Cdd:COG1131  153 LILDEPTSGLDPEARRELWELLRELAAEGKTVLLsthyleeAERL-----CDRVAIIDKGRIVADGTPDELKARLL--ED 225

                 ..
gi 492039060 565 IF 566
Cdd:COG1131  226 VF 227
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
328-569 6.81e-45

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 167.97  E-value: 6.81e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 328 PL-SGSVEFDHVSFTYPDgDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL 406
Cdd:PRK10790 335 PLqSGRIDIDNVSFAYRD-DNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL 413
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 407 RKTVSFVLQRAVLFSGTIASNLRQGNAQAKlHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLI 486
Cdd:PRK10790 414 RQGVAMVQQDPVVLADTFLANVTLGRDISE-EQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLV 492
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 487 AKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEIF 566
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY 572

                 ...
gi 492039060 567 KTQ 569
Cdd:PRK10790 573 QLQ 575
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
141-557 6.91e-45

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: 171.28  E-value: 6.91e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   141 ILIVGSFIFCIVIIPRfwwapVVMVALIFGFGAYVLRQMNSLftkfqEMMDR--ISNQAQETLQGVRVVKSFNqgpqEIK 218
Cdd:TIGR00957 1099 VILLATPIAAVIIPPL-----GLLYFFVQRFYVASSRQLKRL-----ESVSRspVYSHFNETLLGVSVIRAFE----EQE 1164
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   219 KFDQTSDQLNDYN-------IVIGYWFsAIMPAFQMIAYTVIALIVYLIGKnitaHPSDIAVVSPFVNYVLTLLFTI--M 289
Cdd:TIGR00957 1165 RFIHQSDLKVDENqkayypsIVANRWL-AVRLECVGNCIVLFAALFAVISR----HSLSAGLVGLSVSYSLQVTFYLnwL 1239
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   290 IAGMTLMQfsrANI-SLGRIREVLETEPDVKFVESGSVAPLS----GSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVG 364
Cdd:TIGR00957 1240 VRMSSEME---TNIvAVERLKEYSETEKEAPWQIQETAPPSGwpprGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVG 1316
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   365 IVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLrQGNAQAKLHELQRAA 444
Cdd:TIGR00957 1317 IVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL-DPFSQYSDEEVWWAL 1395
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   445 NMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFI 524
Cdd:TIGR00957 1396 ELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLT 1475
                          410       420       430
                   ....*....|....*....|....*....|...
gi 492039060   525 IAEKIVSVINADTILVLDDGKLVAQGTHEELLK 557
Cdd:TIGR00957 1476 IAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQ 1508
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
334-545 2.06e-44

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 156.86  E-value: 2.06e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFV 413
Cdd:cd03225    1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQ--RAVLFSGTIASNLRQG--NAQAKLHELQRAANMAqasefIERYNDSfdhEVEERS-ANFSGGQKQRLSIARGLIAK 488
Cdd:cd03225   81 FQnpDDQFFGPTVEEEVAFGleNLGLPEEEIEERVEEA-----LELVGLE---GLRDRSpFTLSGGQKQRVAIAGVLAMD 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 489 APILILDDSTSALDAESEKKVQQALeHELPDT-TTFIIAEKIVSVIN--ADTILVLDDGK 545
Cdd:cd03225  153 PDILLLDEPTAGLDPAGRRELLELL-KKLKAEgKTIIIVTHDLDLLLelADRVIVLEDGK 211
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
334-546 3.73e-44

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: 154.68  E-value: 3.73e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFV 413
Cdd:cd03246    2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRAVLFSGTIASNLrqgnaqaklhelqraanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKAPILI 493
Cdd:cd03246   82 PQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRILV 119
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492039060 494 LDDSTSALDAESEKKVQQALEH-ELPDTTTFIIAEKIVSVINADTILVLDDGKL 546
Cdd:cd03246  120 LDEPNSHLDVEGERALNQAIAAlKAAGATRIVIAHRPETLASADRILVLEDGRV 173
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
333-550 1.07e-43

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: 153.62  E-value: 1.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVtEAALRKTVSF 412
Cdd:cd03247    1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTIASNLrqgnaqaklhelqraanmaqasefieryndsfdheveerSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03247   80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQG 550
Cdd:cd03247  121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
PLN03130 PLN03130
ABC transporter C family member; Provisional
328-556 2.73e-43

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 166.45  E-value: 2.73e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  328 PLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALR 407
Cdd:PLN03130 1233 PSSGSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLR 1312
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  408 KTVSFVLQRAVLFSGTIASNLRQGNAQ--AKLHE-LQRAanmaQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARG 484
Cdd:PLN03130 1313 KVLGIIPQAPVLFSGTVRFNLDPFNEHndADLWEsLERA----HLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARA 1388
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060  485 LIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELL 556
Cdd:PLN03130 1389 LLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLL 1460
PLN03232 PLN03232
ABC transporter C family member; Provisional
159-556 1.09e-41

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 161.68  E-value: 1.09e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  159 WApvVMVALIFGFGAYVLRQMNSLFTKFQEMMDR--ISNQAQETLQG---VRVVKSFNQGPQEIKKFDQTSDQLNDYNIV 233
Cdd:PLN03232 1054 WA--IMPLLILFYAAYLYYQSTSREVRRLDSVTRspIYAQFGEALNGlssIRAYKAYDRMAKINGKSMDNNIRFTLANTS 1131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  234 IGYWFSAIMPAFQMIAYTVIALIVYLIGKNITAHPSDIAVVSPFVNYvlTLLFTIMIAGMtLMQFSRANISLGRIREV-- 311
Cdd:PLN03232 1132 SNRWLTIRLETLGGVMIWLTATFAVLRNGNAENQAGFASTMGLLLSY--TLNITTLLSGV-LRQASKAENSLNSVERVgn 1208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  312 ---LETE-PDV-KFVESGSVAPLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP 386
Cdd:PLN03232 1209 yidLPSEaTAIiENNRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVEL 1288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  387 TKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLhELQRAANMAQASEFIERYNDSFDHEVEE 466
Cdd:PLN03232 1289 EKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDA-DLWEALERAHIKDVIDRNPFGLDAEVSE 1367
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  467 RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKL 546
Cdd:PLN03232 1368 GGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQV 1447
                         410
                  ....*....|
gi 492039060  547 VAQGTHEELL 556
Cdd:PLN03232 1448 LEYDSPQELL 1457
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
333-555 5.98e-41

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: 147.71  E-value: 5.98e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD-----PTKGKVKIGGQNI--KDVTEAA 405
Cdd:cd03260    1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVLE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 LRKTVSFVLQRAVLFSGTIASNLRQGnaqAKLHELQRAANMAQASEFIERYNDSFDhEVEERSA--NFSGGQKQRLSIAR 483
Cdd:cd03260   79 LRRRVGMVFQKPNPFPGSIYDNVAYG---LRLHGIKLKEELDERVEEALRKAALWD-EVKDRLHalGLSGGQQQRLCLAR 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 484 GLIAKAPILILDDSTSALDAESEKKVQQALeHELPDTTTFII-------AEKIvsvinADTILVLDDGKLVAQGTHEEL 555
Cdd:cd03260  155 ALANEPEVLLLDEPTSALDPISTAKIEELI-AELKKEYTIVIvthnmqqAARV-----ADRTAFLLNGRLVEFGPTEQI 227
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
334-546 1.03e-40

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 146.50  E-value: 1.03e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFV 413
Cdd:COG4619    2 ELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRAVLFSGTIASNLRQGNAQAklhelQRAANMAQASEFIERYNdsFDHEVEERSA-NFSGGQKQRLSIARGLIAKAPIL 492
Cdd:COG4619   80 PQEPALWGGTVRDNLPFPFQLR-----ERKFDRERALELLERLG--LPPDILDKPVeRLSGGERQRLALIRALLLQPDVL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHEL--PDTTTFII------AEKIvsvinADTILVLDDGKL 546
Cdd:COG4619  153 LLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVshdpeqIERV-----ADRVLTLEAGRL 209
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
350-499 1.36e-40

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: 144.33  E-value: 1.36e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSG-TIASNL 428
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060  429 RQGnaqAKLHELQRAANMAQASEFIERYNDSF--DHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:pfam00005  81 RLG---LLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
270-556 1.48e-40

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: 154.29  E-value: 1.48e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 270 DIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRIrEVLETEPDVKFVESGSVAPLsgsVEFDHVSFTYPDGDDPT 349
Cdd:COG1123  202 DLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAAV-PRLGAARGRAAPAAAAAEPL---LEVRNLSKRYPVRGKGG 277
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 ---LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---ALRKTVSFVLQ-------- 415
Cdd:COG1123  278 vraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrELRRRVQMVFQdpysslnp 357
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 -----RAVLFSGTIASNLRQGNAQAKLHELQRAANMaqASEFIERYndsfDHEveersanFSGGQKQRLSIARGLIAKAP 490
Cdd:COG1123  358 rmtvgDIIAEPLRLHGLLSRAERRERVAELLERVGL--PPDLADRY----PHE-------LSGGQRQRVAIARALALEPK 424
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 491 ILILDDSTSALDAESEKKVQQALEH---ELPDTTTFI-----IAEKIvsvinADTILVLDDGKLVAQGTHEELL 556
Cdd:COG1123  425 LLILDEPTSALDVSVQAQILNLLRDlqrELGLTYLFIshdlaVVRYI-----ADRVAVMYDGRIVEDGPTEEVF 493
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
333-556 5.04e-40

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: 152.75  E-value: 5.04e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPT---KGKVKIGGQNIKDVTEAALRKT 409
Cdd:COG1123    5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQ--RAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEF--IERYNDSFDHEveersanFSGGQKQRLSIARGL 485
Cdd:COG1123   85 IGMVFQdpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAvgLERRLDRYPHQ-------LSGGQRQRVAIAMAL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 486 IAKAPILILDDSTSALDAESEKKVQQALEHELPDT-TTFIIAEKIVSVI--NADTILVLDDGKLVAQGTHEELL 556
Cdd:COG1123  158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgTTVLLITHDLGVVaeIADRVVVMDDGRIVEDGPPEEIL 231
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
334-557 6.57e-40

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: 145.39  E-value: 6.57e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKtVSFV 413
Cdd:COG4555    3 EVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRAVLFSG-TIASNLRqgnAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:COG4555   80 PDERGLYDRlTVRENIR---YFAELYGLFDEELKKRIEELIELLG--LEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINA--DTILVLDDGKLVAQGTHEELLK 557
Cdd:COG4555  155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlcDRVVILHKGKVVAQGSLDELRE 221
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
333-557 8.64e-40

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: 146.04  E-value: 8.64e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD---VTEaaLRKT 409
Cdd:TIGR04520   1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDeenLWE--IRKK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  410 VSFVL-----QravlFSGTIAS--------NLrqGNAQAKLHEL-QRAANMAQASEFIeryndsfDHEveerSANFSGGQ 475
Cdd:TIGR04520  79 VGMVFqnpdnQ----FVGATVEddvafgleNL--GVPREEMRKRvDEALKLVGMEDFR-------DRE----PHLLSGGQ 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  476 KQRLSIArGLIAKAP-ILILDDSTSALDAESEKKVQQALE--HELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTH 552
Cdd:TIGR04520 142 KQRVAIA-GVLAMRPdIIILDEATSMLDPKGRKEVLETIRklNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTP 220

                  ....*
gi 492039060  553 EELLK 557
Cdd:TIGR04520 221 REIFS 225
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
3-570 2.65e-39

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 154.42  E-value: 2.65e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060    3 NFKIILPYLKRYKKDVVCAIIAILVSAfsGLYqPKLleniqkALMANQKQAVLSD-----------GIWLVVLGIIAIIS 71
Cdd:PTZ00265  812 NLRIVYREIFSYKKDVTIIALSILVAG--GLY-PVF------ALLYAKYVSTLFDfanleansnkySLYILVIAIAMFIS 882
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   72 GIFNVYFAAKIAQGVVSDLREDTYAKI--QTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLfmqmlrlpILIVGSFI- 148
Cdd:PTZ00265  883 ETLKNYYNNVIGEKVEKTMKRRLFENIlyQEISFFDQDKHAPGLLSAHINRDVHLLKTGLVNN--------IVIFTHFIv 954
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  149 -FCIVIIPRFWWAPVVMVALIFGFGAYVL----------------RQMNS-----LFTKFQEMMDRISNQAQETLQGVRV 206
Cdd:PTZ00265  955 lFLVSMVMSFYFCPIVAAVLTGTYFIFMRvfairarltankdvekKEINQpgtvfAYNSDDEIFKDPSFLIQEAFYNMNT 1034
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  207 VksFNQGPQE-----IKKFDQTSDQLNDYNIVIgywfSAIMPAFQMIAYTVIALIVYLIGKNITAHPSdiAVVSPFVNYV 281
Cdd:PTZ00265 1035 V--IIYGLEDyfcnlIEKAIDYSNKGQKRKTLV----NSMLWGFSQSAQLFINSFAYWFGSFLIRRGT--ILVDDFMKSL 1106
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  282 LTLLFTIMIAG--MTLMQFSR-ANISLGRIREVLETEPDVKFVESGSVA-----PLSGSVEFDHVSFTYPDGDD-PTLKD 352
Cdd:PTZ00265 1107 FTFLFTGSYAGklMSLKGDSEnAKLSFEKYYPLIIRKSNIDVRDNGGIRiknknDIKGKIEIMDVNFRYISRPNvPIYKD 1186
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  353 ISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD----------------------------------------------- 385
Cdd:PTZ00265 1187 LTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggs 1266
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  386 -------PTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYND 458
Cdd:PTZ00265 1267 gedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPN 1346
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  459 SFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALE--HELPDTTTFIIAEKIVSVINAD 536
Cdd:PTZ00265 1347 KYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAHRIASIKRSD 1426
                         650       660       670       680
                  ....*....|....*....|....*....|....*....|
gi 492039060  537 TILVLDD----GKLV-AQGTHEELLKTSL-VYQEIFKTQK 570
Cdd:PTZ00265 1427 KIVVFNNpdrtGSFVqAHGTHEELLSVQDgVYKKYVKLAK 1466
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
18-308 1.14e-38

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: 143.73  E-value: 1.14e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  18 VVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAvlsdgIWLVVLGII--AIISGIFN---VYFAAKIAQGVVSDLR 91
Cdd:cd18542    1 YLLAILALLLATALNLLIPLLIRRiIDSVIGGGLREL-----LWLLALLILgvALLRGVFRylqGYLAEKASQKVAYDLR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  92 EDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGF 171
Cdd:cd18542   76 NDLYDHLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 172 GAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYT 251
Cdd:cd18542  156 SYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGL 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 252 VIALIVYL-----IGKNITahpsdIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18542  236 QIVLVLWVggylvINGEIT-----LGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
333-549 3.16e-38

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 140.56  E-value: 3.16e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL---- 406
Cdd:COG1136    5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELarlr 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 407 RKTVSFVLQRAVLFSG-TIASNLRqgnAQAKLHELQRAANMAQASEFIERYNdsfdheVEERSANF----SGGQKQRLSI 481
Cdd:COG1136   85 RRHIGFVFQFFNLLPElTALENVA---LPLLLAGVSRKERRERARELLERVG------LGDRLDHRpsqlSGGQQQRVAI 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDT--TTFIIA---EKIVSVinADTILVLDDGKLVAQ 549
Cdd:COG1136  156 ARALVNRPKLILADEPTGNLDSKTGEEVLELL-RELNRElgTTIVMVthdPELAAR--ADRVIRLRDGRIVSD 225
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
334-545 1.26e-37

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 136.22  E-value: 1.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDGddPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFV 413
Cdd:cd00267    1 EIENLSFRYGGR--TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQravlfsgtiasnlrqgnaqaklhelqraanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKAPILI 493
Cdd:cd00267   79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492039060 494 LDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGK 545
Cdd:cd00267  104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAElaADRVIVLKDGK 157
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
333-546 2.13e-37

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: 138.01  E-value: 2.13e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL---- 406
Cdd:cd03255    1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 407 RKTVSFVLQRAVLFSG-TIASNLRQGnaqAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGL 485
Cdd:cd03255   81 RRHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLERVG--LGDRLNHYPSELSGGQQQRVAIARAL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 486 IAKAPILILDDSTSALDAESEKKVQQALE--HELPDTTTFI------IAEKivsvinADTILVLDDGKL 546
Cdd:cd03255  156 ANDPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVvthdpeLAEY------ADRIIELRDGKI 218
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
333-550 3.43e-37

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: 137.64  E-value: 3.43e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---ALR 407
Cdd:cd03257    2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIRR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQ---RAVLFSGTIASNLR---QGNAQAKLHELQRAANMAQASEFI--ERYNDSFDHEveersanFSGGQKQRL 479
Cdd:cd03257   82 KEIQMVFQdpmSSLNPRMTIGEQIAeplRIHGKLSKKEARKEAVLLLLVGVGlpEEVLNRYPHE-------LSGGQRQRV 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 480 SIARGLIAKAPILILDDSTSALDAESEKKVQQALE--HELPDTTTFIIAE--KIVSVInADTILVLDDGKLVAQG 550
Cdd:cd03257  155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHdlGVVAKI-ADRVAVMYAGKIVEEG 228
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
333-545 4.26e-37

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: 136.45  E-value: 4.26e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDD---PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGqnikdvteaalrkT 409
Cdd:cd03250    1 ISVEDASFTWDSGEQetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRAVLFSGTIASNLRQGnaqaklhelqraanmaqaSEF-IERYN------------DSFDH----EVEERSANFS 472
Cdd:cd03250   68 IAYVSQEPWIQNGTIRENILFG------------------KPFdEERYEkvikacalepdlEILPDgdltEIGEKGINLS 129
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 473 GGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKV-QQALEHELPDTTTFIIAEKIVSVI-NADTILVLDDGK 545
Cdd:cd03250  130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIfENCILGLLLNNKTRILVTHQLQLLpHADQIVVLDNGR 204
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
333-556 5.96e-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: 137.43  E-value: 5.96e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:cd03295    1 IEFENVTKRYGGGK-KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLrqgNAQAKLHELQRAANMAQASEFIE-------RYNDSFDHEVeersanfSGGQKQRLSIARG 484
Cdd:cd03295   80 VIQQIGLFPHmTVEENI---ALVPKLLKWPKEKIRERADELLAlvgldpaEFADRYPHEL-------SGGQQQRVGVARA 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQA---LEHELPDTTTFI---IAEKIVSvinADTILVLDDGKLVAQGTHEELL 556
Cdd:cd03295  150 LAADPPLLLMDEPFGALDPITRDQLQEEfkrLQQELGKTIVFVthdIDEAFRL---ADRIAIMKNGEIVQVGTPDEIL 224
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
18-308 9.79e-37

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: 138.45  E-value: 9.79e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  18 VVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTYA 96
Cdd:cd07346    1 LLLALLLLLLATALGLALPLLTKLlIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  97 KIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVL 176
Cdd:cd07346   81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 177 RQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIALI 256
Cdd:cd07346  161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 492039060 257 VYLIGKNITAHPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd07346  241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
333-558 1.29e-36

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: 136.86  E-value: 1.29e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDD--PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTV 410
Cdd:COG1124    2 LEVRNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQ------------RAVLfsGTIASNLRQGNAQAKLHELQRAANMAqaSEFIERYndsfDHEVeersanfSGGQKQR 478
Cdd:COG1124   82 QMVFQdpyaslhprhtvDRIL--AEPLRIHGLPDREERIAELLEQVGLP--PSFLDRY----PHQL-------SGGQRQR 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIARGLIAKAPILILDDSTSALDAESEKKVQQAL-----EHELpdttTFIiaekIVS----VIN--ADTILVLDDGKLV 547
Cdd:COG1124  147 VAIARALILEPELLLLDEPTSALDVSVQAEILNLLkdlreERGL----TYL----FVShdlaVVAhlCDRVAVMQNGRIV 218
                        250
                 ....*....|.
gi 492039060 548 AQGTHEELLKT 558
Cdd:COG1124  219 EELTVADLLAG 229
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
333-556 1.81e-36

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: 135.79  E-value: 1.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPD--GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL---R 407
Cdd:cd03258    2 IELKNVSKVFGDtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQRAVLFSG-TIASNLrqgnAQA-KLHELQRAANMAQASEFIERYNDSfdHEVEERSANFSGGQKQRLSIARGL 485
Cdd:cd03258   82 RRIGMIFQHFNLLSSrTVFENV----ALPlEIAGVPKAEIEERVLELLELVGLE--DKADAYPAQLSGGQKQRVGIARAL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 486 IAKAPILILDDSTSALDAESE-------KKVQQALehelpDTTTFIIAEKIvSVIN--ADTILVLDDGKLVAQGTHEELL 556
Cdd:cd03258  156 ANNPKVLLCDEATSALDPETTqsilallRDINREL-----GLTIVLITHEM-EVVKriCDRVAVMEKGEVVEEGTVEEVF 229
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
11-495 2.12e-36

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: 143.01  E-value: 2.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  11 LKRYKKDVVCAIIAILVSAFSGLYqpkLLENIQKALMANQkQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDL 90
Cdd:COG4615    8 LRESRWLLLLALLLGLLSGLANAG---LIALINQALNATG-AALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  91 REDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMqlfmqmlRLPILIVGSFIFCIVIIPRFWWAP----VVMVA 166
Cdd:COG4615   84 RLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFV-------RLPELLQSVALVLGCLAYLAWLSPplflLTLVL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 167 LIFGFGAYVL--RQMNSLFTKFQEMMDRISNQAQETLQGVRVVK-------SFNQgpqeiKKFDQTSDQLNDYNIVIGYW 237
Cdd:COG4615  157 LGLGVAGYRLlvRRARRHLRRAREAEDRLFKHFRALLEGFKELKlnrrrrrAFFD-----EDLQPTAERYRDLRIRADTI 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 238 FSAIMPAFQMIAYTVIALIVYLIGkniTAHPSDIAVVSpfvNYVLTLLFTI----MIAGMTLMqFSRANISLGRIREV-- 311
Cdd:COG4615  232 FALANNWGNLLFFALIGLILFLLP---ALGWADPAVLS---GFVLVLLFLRgplsQLVGALPT-LSRANVALRKIEELel 304
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 312 -LETEPDVKFVESGSVAPLS-GSVEFDHVSFTYPDGDDP---TLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP 386
Cdd:COG4615  305 aLAAAEPAAADAAAPPAPADfQTLELRGVTYRYPGEDGDegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRP 384
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 387 TKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSgtiasnlrqgnaqaKLHELQRAANMAQASEFIERYNdsFDHEVEE 466
Cdd:COG4615  385 ESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD--------------RLLGLDGEADPARARELLERLE--LDHKVSV 448
                        490       500       510
                 ....*....|....*....|....*....|....
gi 492039060 467 RSANF-----SGGQKQRLSIARGLIAKAPILILD 495
Cdd:COG4615  449 EDGRFsttdlSQGQRKRLALLVALLEDRPILVFD 482
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
323-556 2.06e-35

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: 133.88  E-value: 2.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 323 SGSVApLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVT 402
Cdd:cd03288   11 SGLVG-LGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 403 EAALRKTVSFVLQRAVLFSGTIASNLrqgNAQAKLHE--LQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLS 480
Cdd:cd03288   90 LHTLRSRLSIILQDPILFSGSIRFNL---DPECKCTDdrLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFC 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 481 IARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELL 556
Cdd:cd03288  167 LARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLL 242
cbiO PRK13640
energy-coupling factor transporter ATPase;
333-565 3.47e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 133.77  E-value: 3.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP---TKGKVKIGGQNIKDVTEAALRKT 409
Cdd:PRK13640   6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRA--VLFSGTIASNLRQG--NAQAKLHELQRAANMAQASEFIERYNDSfdheveeRSANFSGGQKQRLSIArGL 485
Cdd:PRK13640  86 VGIVFQNPdnQFVGATVGDDVAFGleNRAVPRPEMIKIVRDVLADVGMLDYIDS-------EPANLSGGQKQRVAIA-GI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 486 IAKAP-ILILDDSTSALDAESEKKVQQALEHELPDT--TTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVY 562
Cdd:PRK13640 158 LAVEPkIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEML 237

                 ...
gi 492039060 563 QEI 565
Cdd:PRK13640 238 KEI 240
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
333-565 4.34e-35

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 133.60  E-value: 4.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:PRK13635   6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRA-VLFSGT-----IASNLRqgNAQAKLHELQRAANMAqasefIERYN--DSFDHEveerSANFSGGQKQRLSIArG 484
Cdd:PRK13635  86 VFQNPdNQFVGAtvqddVAFGLE--NIGVPREEMVERVDQA-----LRQVGmeDFLNRE----PHRLSGGQKQRVAIA-G 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 485 LIAKAP-ILILDDSTSALDAESEKKVQQALEH--ELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLV 561
Cdd:PRK13635 154 VLALQPdIIILDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGHM 233

                 ....
gi 492039060 562 YQEI 565
Cdd:PRK13635 234 LQEI 237
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
333-558 5.20e-35

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: 131.86  E-value: 5.20e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---ALRKT 409
Cdd:cd03261    1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRAVLFSG-TIASN----LRQgNAQAKLHELQRaanmaQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARG 484
Cdd:cd03261   79 MGMLFQSGALFDSlTVFENvafpLRE-HTRLSEEEIRE-----IVLEKLEAVG--LRGAEDLYPAELSGGMKKRVALARA 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQALE--HELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEELLKT 558
Cdd:cd03261  151 LALDPELLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRAS 227
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
333-566 8.46e-35

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: 131.70  E-value: 8.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:COG1120    2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVL-FSGTIA----------SNLRQGNAQAKLHELQRAANMAQASEFIERYndsfdheVEErsanFSGGQKQRLSI 481
Cdd:COG1120   80 VPQEPPApFGLTVRelvalgryphLGLFGRPSAEDREAVEEALERTGLEHLADRP-------VDE----LSGGERQRVLI 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQALEHelpdtttfIIAEK---IVSV---IN-----ADTILVLDDGKLVAQG 550
Cdd:COG1120  149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRR--------LARERgrtVVMVlhdLNlaaryADRLVLLKDGRIVAQG 220
                        250
                 ....*....|....*.
gi 492039060 551 THEELLKTSLVyQEIF 566
Cdd:COG1120  221 PPEEVLTPELL-EEVY 235
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
333-550 1.17e-34

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: 130.33  E-value: 1.17e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVteAALRKTVSF 412
Cdd:cd03259    1 LELKGLSKTY--GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPERRNIGM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRQGNAQAKLHELQRAANMAQASEFIEryndsFDHEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:cd03259   77 VFQDYALFPHlTVAENIAFGLKLRGVPKAEIRARVRELLELVG-----LEGLLNRYPHELSGGQQQRVALARALAREPSL 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 492 LILDDSTSALDAesekKVQQALEHELPDT-----TTFIIA----EKIVSVinADTILVLDDGKLVAQG 550
Cdd:cd03259  152 LLLDEPLSALDA----KLREELREELKELqrelgITTIYVthdqEEALAL--ADRIAVMNEGRIVQVG 213
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
336-547 4.01e-33

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 125.83  E-value: 4.01e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYPDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKdvtEAALRKTVSFVLQ 415
Cdd:cd03226    3 ENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 --RAVLFSGTIASNLRQGNAQAklhelqrAANMAQASEFIERYNDSFDHEVEERSanFSGGQKQRLSIARGLIAKAPILI 493
Cdd:cd03226   79 dvDYQLFTDSVREELLLGLKEL-------DAGNEQAETVLKDLDLYALKERHPLS--LSGGQKQRLAIAAALLSGKDLLI 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 494 LDDSTSALDAESEKKVQQALEHELPDTTTFIIA----EKIVSVinADTILVLDDGKLV 547
Cdd:cd03226  150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVIthdyEFLAKV--CDRVLLLANGAIV 205
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
333-556 5.08e-33

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 129.04  E-value: 5.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL---R 407
Cdd:COG1135    2 IELENLSKTFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQRAVLFSG-TIASN----LRqgnaQAKLHELQRAanmAQASEFIERyndsfdheV--EERSANF----SGGQK 476
Cdd:COG1135   82 RKIGMIFQHFNLLSSrTVAENvalpLE----IAGVPKAEIR---KRVAELLEL--------VglSDKADAYpsqlSGGQK 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 477 QRLSIARGLIAKAPILILDDSTSALDaesekkvqqalehelPDTTTFI------IAEK----IV------SVIN--ADTI 538
Cdd:COG1135  147 QRVGIARALANNPKVLLCDEATSALD---------------PETTRSIldllkdINRElgltIVlithemDVVRriCDRV 211
                        250
                 ....*....|....*...
gi 492039060 539 LVLDDGKLVAQGTHEELL 556
Cdd:COG1135  212 AVLENGRIVEQGPVLDVF 229
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
333-557 6.45e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 127.03  E-value: 6.45e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:PRK13632   8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRA-VLFSGT-----IA-----SNLRQGNAQAKLHELQRAANMaqasefieryNDSFDHEveerSANFSGGQKQRLSI 481
Cdd:PRK13632  88 IFQNPdNQFIGAtveddIAfglenKKVPPKKMKDIIDDLAKKVGM----------EDYLDKE----PQNLSGGQKQRVAI 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDTT--TFI-IAEKIVSVINADTILVLDDGKLVAQGTHEELLK 557
Cdd:PRK13632 154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIM-VDLRKTRkkTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEILN 231
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
333-546 8.11e-33

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: 123.66  E-value: 8.11e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKtVSF 412
Cdd:cd03230    1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-IGY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRqgnaqaklhelqraanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKAPI 491
Cdd:cd03230   78 LPEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDPEL 116
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHELPDTTTFII-------AEKIvsvinADTILVLDDGKL 546
Cdd:cd03230  117 LILDEPTSGLDPESRREFWELLRELKKEGKTILLsshileeAERL-----CDRVAILNNGRI 173
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
333-545 8.29e-33

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


Pssm-ID: 213196 [Multi-domain]  Cd Length: 178  Bit Score: 123.84  E-value: 8.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTE--AALRKTV 410
Cdd:cd03229    1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelPPLRRRI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSG-TIASNLRQGnaqaklhelqraanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKA 489
Cdd:cd03229   79 GMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 490 PILILDDSTSALDAESEKKVQQALE--HELPDTTTFIIAEKIVSVIN-ADTILVLDDGK 545
Cdd:cd03229  120 DVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
334-550 1.08e-32

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: 123.70  E-value: 1.08e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFV 413
Cdd:cd03214    1 EVENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQravlfsgtiasnlrqgnaqaklhelqrAANMAQASEFIERYNDSfdheveersanFSGGQKQRLSIARGLIAKAPILI 493
Cdd:cd03214   79 PQ---------------------------ALELLGLAHLADRPFNE-----------LSGGERQRVLLARALAQEPPILL 120
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 494 LDDSTSALDAESEKKVQQALeHELPDTTTFIIaekIVSV--IN-----ADTILVLDDGKLVAQG 550
Cdd:cd03214  121 LDEPTSHLDIAHQIELLELL-RRLARERGKTV---VMVLhdLNlaaryADRVILLKDGRIVAQG 180
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
333-547 1.20e-32

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 124.78  E-value: 1.20e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTE---AALRKT 409
Cdd:COG2884    2 IRFENVSKRYPGGR-EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreiPYLRRR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQ--RaVLFSGTIASNLrqgnAQA-KLHELQRAANMAQASEFIERYN-----DSFDHEVeersanfSGGQKQRLSI 481
Cdd:COG2884   81 IGVVFQdfR-LLPDRTVYENV----ALPlRVTGKSRKEIRRRVREVLDLVGlsdkaKALPHEL-------SGGEQQRVAI 148
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQALEhELPDT-TTFIIA---EKIVSVINAdTILVLDDGKLV 547
Cdd:COG2884  149 ARALVNRPELLLADEPTGNLDPETSWEIMELLE-EINRRgTTVLIAthdLELVDRMPK-RVLELEDGRLV 216
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
333-556 2.83e-32

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 124.43  E-value: 2.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVteaalRKTVSF 412
Cdd:COG1121    7 IELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRA------------VLFSGTIASNLRQGNAQAKLHEL-QRAANMAQASEFIERyndsfdheveeRSANFSGGQKQRL 479
Cdd:COG1121   80 VPQRAevdwdfpitvrdVVLMGRYGRRGLFRRPSRADREAvDEALERVGLEDLADR-----------PIGELSGGQQQRV 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 480 SIARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDTTTFIIaekIVS-----VI-NADTILVLDDGkLVAQGTHE 553
Cdd:COG1121  149 LLARALAQDPDLLLLDEPFAGVDAATEEALYELL-RELRREGKTIL---VVThdlgaVReYFDRVLLLNRG-LVAHGPPE 223

                 ...
gi 492039060 554 ELL 556
Cdd:COG1121  224 EVL 226
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
333-558 6.03e-32

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: 123.55  E-value: 6.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---ALRKT 409
Cdd:COG1127    6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRAVLFSG-TIASN----LRQgnaQAKL--HELQRAANMAQA----SEFIERYndsfdheveerSANFSGGQKQR 478
Cdd:COG1127   84 IGMLFQGGALFDSlTVFENvafpLRE---HTDLseAEIRELVLEKLElvglPGAADKM-----------PSELSGGMRKR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIARGLIAKAPILILDDSTSALDAESEKKVQQ---ALEHELpDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEE 554
Cdd:COG1127  150 VALARALALDPEILLYDEPTAGLDPITSAVIDElirELRDEL-GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228

                 ....
gi 492039060 555 LLKT 558
Cdd:COG1127  229 LLAS 232
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
333-544 1.83e-31

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 122.51  E-value: 1.83e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGqniKDVTEAALRktV 410
Cdd:COG1116    8 LELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG---KPVTGPGPD--R 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFs-gTIASNLRQGnaqAKLHELQRAANMAQASEFIERYN-----DSFDHEVeersanfSGGQKQRLSIARG 484
Cdd:COG1116   83 GVVFQEPALLpwlTVLDNVALG---LELRGVPKAERRERARELLELVGlagfeDAYPHQL-------SGGMRQRVAIARA 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQALE---HELPDTTTFI---IAEkivSVINADTILVLDDG 544
Cdd:COG1116  153 LANDPEVLLMDEPFGALDALTRERLQDELLrlwQETGKTVLFVthdVDE---AVFLADRVVVLSAR 215
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
333-541 2.41e-31

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: 121.04  E-value: 2.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAalrktV 410
Cdd:cd03293    1 LEVRNVSKTYGGGGGAVtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFS-GTIASNLRQGnaqAKLHELQRAANMAQASEFIER-----YNDSFDHEVeersanfSGGQKQRLSIARG 484
Cdd:cd03293   76 GYVFQQDALLPwLTVLDNVALG---LELQGVPKAEARERAEELLELvglsgFENAYPHQL-------SGGMRQRVALARA 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQALE---HELPDTTTFI---IAEkivSVINADTILVL 541
Cdd:cd03293  146 LAVDPDVLLLDEPFSALDALTREQLQEELLdiwRETGKTVLLVthdIDE---AVFLADRVVVL 205
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
333-555 2.42e-31

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 122.09  E-value: 2.42e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRK---T 409
Cdd:COG3638    3 LELRNLSKRYP-GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQ-----------RAVLfSGTIAsnlRQGNAQAKLHeLQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQR 478
Cdd:COG3638   82 IGMIFQqfnlvprlsvlTNVL-AGRLG---RTSTWRSLLG-LFPPEDRERALEALERVG--LADKAYQRADQLSGGQQQR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHelpdtttfiIAE--KIVSVIN----------ADTILVLDDGKL 546
Cdd:COG3638  155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRR---------IARedGITVVVNlhqvdlarryADRIIGLRDGRV 225

                 ....*....
gi 492039060 547 VAQGTHEEL 555
Cdd:COG3638  226 VFDGPPAEL 234
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
198-543 1.55e-30

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 127.84  E-value: 1.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  198 QETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFS---AIMPAFQMIAY-------TVIalivyLIGKNITAH 267
Cdd:PTZ00265  240 EEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESlhiGMINGFILASYafgfwygTRI-----IISDLSNQQ 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  268 PSD----IAVVSPFVNYVLTL-LFTIMIAGMTlmQFSRANISLGRIREVLETEPDVKFVESGSVAPLSGSVEFDHVSFTY 342
Cdd:PTZ00265  315 PNNdfhgGSVISILLGVLISMfMLTIILPNIT--EYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIKKIQFKNVRFHY 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  343 PDGDDPTL-KDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIG-GQNIKDVTEAALRKTVSFVLQRAVLF 420
Cdd:PTZ00265  393 DTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKWWRSKIGVVSQDPLLF 472
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  421 SGTIASNLR---------------------------------------------QGNAQAKLHELQRAANMAQASE---- 451
Cdd:PTZ00265  473 SNSIKNNIKyslyslkdlealsnyynedgndsqenknkrnscrakcagdlndmsNTTDSNELIEMRKNYQTIKDSEvvdv 552
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  452 --------FIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHEL--PDTT 521
Cdd:PTZ00265  553 skkvlihdFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRI 632
                         410       420
                  ....*....|....*....|..
gi 492039060  522 TFIIAEKIVSVINADTILVLDD 543
Cdd:PTZ00265  633 TIIIAHRLSTIRYANTIFVLSN 654
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
333-545 1.95e-30

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: 117.97  E-value: 1.95e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAaLRKTVSF 412
Cdd:COG4133    3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED-YRRRLAY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRqgnAQAKLHelQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:COG4133   80 LGHADGLKPElTVRENLR---FWAALY--GLRADREAIDEALEAVG--LAGLADLPVRQLSAGQKRRVALARLLLSPAPL 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGK 545
Cdd:COG4133  153 WLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDLGDFK 206
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
18-267 4.66e-30

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: 119.45  E-value: 4.66e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  18 VVCAIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLsdgiWLVVLGIIAI-----ISGIFNVYFAAKIAQGVVSDLRE 92
Cdd:cd18552    1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEAL----LLVPLAIIGLfllrgLASYLQTYLMAYVGQRVVRDLRN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  93 DTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFG 172
Cdd:cd18552   77 DLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 173 AYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTV 252
Cdd:cd18552  157 RRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIA 236
                        250
                 ....*....|....*
gi 492039060 253 IALIVYLIGKNITAH 267
Cdd:cd18552  237 IALVLWYGGYQVISG 251
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
331-572 4.73e-30

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: 119.19  E-value: 4.73e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 331 GSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDpTKGKVKIGGQNIKDVTEAALRKTV 410
Cdd:cd03289    1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSGTIASNLrQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:cd03289   80 GVIPQKVFIFSGTFRKNL-DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 491 ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELL-KTSLVYQEIFKTQ 569
Cdd:cd03289  159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLnEKSHFKQAISPSD 238

                 ...
gi 492039060 570 KGK 572
Cdd:cd03289  239 RLK 241
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
331-555 6.81e-30

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 120.56  E-value: 6.81e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 331 GSVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGqniKDVTEAALRK-T 409
Cdd:COG3839    2 ASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVTDLPPKDrN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRAVLF-----SGTIASNLR-QGNAQAKLHE-LQRAANMAQASEFIERyndsfdheveeRSANFSGGQKQRLSIA 482
Cdd:COG3839   77 IAMVFQSYALYphmtvYENIAFPLKlRKVPKAEIDRrVREAAELLGLEDLLDR-----------KPKQLSGGQRQRVALG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 483 RGLIAKAPILILDDSTSALDAE------SE-KKVQQALEhelpdtTTFII-------AEKIvsvinADTILVLDDGKLVA 548
Cdd:COG3839  146 RALVREPKVFLLDEPLSNLDAKlrvemrAEiKRLHRRLG------TTTIYvthdqveAMTL-----ADRIAVMNDGRIQQ 214

                 ....*..
gi 492039060 549 QGTHEEL 555
Cdd:COG3839  215 VGTPEEL 221
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
350-556 1.24e-29

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: 117.74  E-value: 1.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL----RKTVSFVLQRAVLFSG-TI 424
Cdd:cd03294   40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLPHrTV 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 ASNLRQGNAQAKLHELQRAANMAQASEFI--ERYNDSFDHEVeersanfSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:cd03294  120 LENVAFGLEVQGVPRAEREERAAEALELVglEGWEHKYPDEL-------SGGMQQRVGLARALAVDPDILLMDEAFSALD 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 503 AESEKKVQQ---ALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELL 556
Cdd:cd03294  193 PLIRREMQDellRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIL 249
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
332-555 3.84e-29

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 118.66  E-value: 3.84e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVtEAALRKtVS 411
Cdd:COG3842    5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-PPEKRN-VG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSG-TIASN----LR-QGNAQAKLHEL-QRAANMAQASEFIERYndsfDHEVeersanfSGGQKQRLSIARG 484
Cdd:COG3842   81 MVFQDYALFPHlTVAENvafgLRmRGVPKAEIRARvAELLELVGLEGLADRY----PHQL-------SGGQQQRVALARA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 485 LIAKAPILILDDSTSALDAE------SE-KKVQQALEhelpdtTTFIIA----EKIVSVinADTILVLDDGKLVAQGTHE 553
Cdd:COG3842  150 LAPEPRVLLLDEPLSALDAKlreemrEElRRLQRELG------ITFIYVthdqEEALAL--ADRIAVMNDGRIEQVGTPE 221

                 ..
gi 492039060 554 EL 555
Cdd:COG3842  222 EI 223
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
160-568 1.48e-28

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: 121.59  E-value: 1.48e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   160 APVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVK------SFNQGPQEIKKFDQTSDQLNDYNIV 233
Cdd:TIGR00957  462 AGVAVMVLMVPLNAVMAMKTKTYQVAHMKSKDNRIKLMNEILNGIKVLKlyawelAFLDKVEGIRQEELKVLKKSAYLHA 541
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   234 IGYwFSAIMPAFqMIAYTVIALIVYLIGKNItahpsdIAVVSPFVNYVL--TLLFTIMIAGMTLMQFSRANISLGRIREV 311
Cdd:TIGR00957  542 VGT-FTWVCTPF-LVALITFAVYVTVDENNI------LDAEKAFVSLALfnILRFPLNILPMVISSIVQASVSLKRLRIF 613
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   312 L---ETEPDVkfVESGSVAPLSG-SVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPT 387
Cdd:TIGR00957  614 LsheELEPDS--IERRTIKPGEGnSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKV 691
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   388 KGKVKIGGqnikdvteaalrkTVSFVLQRAVLFSGTIASNLRQGNA-QAKLHE--LQRAANMAQasefIERYNDSFDHEV 464
Cdd:TIGR00957  692 EGHVHMKG-------------SVAYVPQQAWIQNDSLRENILFGKAlNEKYYQqvLEACALLPD----LEILPSGDRTEI 754
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   465 EERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQAL---EHELPDTTTFIIAEKIVSVINADTILVL 541
Cdd:TIGR00957  755 GEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVM 834
                          410       420
                   ....*....|....*....|....*..
gi 492039060   542 DDGKLVAQGTHEELLKTSLVYQEIFKT 568
Cdd:TIGR00957  835 SGGKISEMGSYQELLQRDGAFAEFLRT 861
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
332-563 2.03e-28

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: 113.59  E-value: 2.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikDVTEAALRK-TV 410
Cdd:cd03296    2 SIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE---DATDVPVQErNV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSG-TIASNLRQG-------------NAQAKLHELQRaanMAQASEFIERYndsfdheveerSANFSGGQK 476
Cdd:cd03296   77 GFVFQHYALFRHmTVFDNVAFGlrvkprserppeaEIRAKVHELLK---LVQLDWLADRY-----------PAQLSGGQR 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 477 QRLSIARGLIAKAPILILDDSTSALDAESEKKVQ---QALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHE 553
Cdd:cd03296  143 QRVALARALAVEPKVLLLDEPFGALDAKVRKELRrwlRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPD 222
                        250
                 ....*....|...
gi 492039060 554 ELL---KTSLVYQ 563
Cdd:cd03296  223 EVYdhpASPFVYS 235
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
334-550 2.58e-28

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: 112.24  E-value: 2.58e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVteaalRKTVSFV 413
Cdd:cd03235    1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRA-------------VLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERyndsfdheveeRSANFSGGQKQRLS 480
Cdd:cd03235   74 PQRRsidrdfpisvrdvVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADR-----------QIGELSGGQQQRVL 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 481 IARGLIAKAPILILDDSTSALDAESEKKVQQALEhELPDT--TTFIIAEKIVSVIN-ADTILVLdDGKLVAQG 550
Cdd:cd03235  143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR-ELRREgmTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
334-555 3.32e-28

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: 113.05  E-value: 3.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL---RKTV 410
Cdd:cd03256    2 EVENLSKTYPNGK-KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQ-----------RAVLfSGTIA--SNLRQGNAQAKLHELQRAAnmaqasEFIERYNdsFDHEVEERSANFSGGQKQ 477
Cdd:cd03256   81 GMIFQqfnlierlsvlENVL-SGRLGrrSTWRSLFGLFPKEEKQRAL------AALERVG--LLDKAYQRADQLSGGQQQ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 478 RLSIARGLIAKAPILILDDSTSALDAESEKKVQQAL-----EHELpdttTFIIAEKIVSVI--NADTILVLDDGKLVAQG 550
Cdd:cd03256  152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkrinrEEGI----TVIVSLHQVDLAreYADRIVGLKDGRIVFDG 227

                 ....*
gi 492039060 551 THEEL 555
Cdd:cd03256  228 PPAEL 232
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
21-308 8.65e-28

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: 113.28  E-value: 8.65e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  21 AIIAILVSAFSGLYQPKLLENIQKALmanQKQAVLSDGIWLVVLGI--IAIISGIFNV---YFAAKIAQGVVSDLREDTY 95
Cdd:cd18541    4 GILFLILVDLLQLLIPRIIGRAIDAL---TAGTLTASQLLRYALLIllLALLIGIFRFlwrYLIFGASRRIEYDLRNDLF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  96 AKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYV 175
Cdd:cd18541   81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 176 LRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIAL 255
Cdd:cd18541  161 GKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLI 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492039060 256 IVYLIGKNITAHPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18541  241 VLWYGGRLVIRGTITLGDLVAFNSYLGMLIWPMMALGWVINLIQRGAASLKRI 293
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
333-556 9.08e-28

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 111.62  E-value: 9.08e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI--KDVTEAALRKTV 410
Cdd:COG1126    2 IEIENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSG-TIASNLRQgnAQAKLHELQRAANMAQASEFIERYN--DSFDHeveeRSANFSGGQKQRLSIARGLIA 487
Cdd:COG1126   80 GMVFQQFNLFPHlTVLENVTL--APIKVKKMSKAEAEERAMELLERVGlaDKADA----YPAQLSGGQQQRVAIARALAM 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 488 KAPILILDDSTSALDAESEKKVQQALEhELPDT-TTFII-------AEKIvsvinADTILVLDDGKLVAQGTHEELL 556
Cdd:COG1126  154 EPKVMLFDEPTSALDPELVGEVLDVMR-DLAKEgMTMVVvthemgfAREV-----ADRVVFMDGGRIVEEGPPEEFF 224
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
333-555 1.20e-27

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 110.67  E-value: 1.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAlRKTVSF 412
Cdd:cd03263    1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA-RQSLGY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRqgnAQAKLHELQRAANMAQASEFIERYNdSFDHEvEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:cd03263   80 CPQFDALFDElTVREHLR---FYARLKGLPKSEIKEEVELLLRVLG-LTDKA-NKRARTLSGGMKRKLSLAIALIGGPSV 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHELPDTTtfII--------AEKIvsvinADTILVLDDGKLVAQGTHEEL 555
Cdd:cd03263  155 LLLDEPTSGLDPASRRAIWDLILEVRKGRS--IIltthsmdeAEAL-----CDRIAIMSDGKLRCIGSPQEL 219
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
333-550 2.26e-27

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: 109.59  E-value: 2.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdpTLKDISFKIKPGqMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEaALRKTVSF 412
Cdd:cd03264    1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQ-KLRRRIGY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTIAsnLRQGNAQAKLHELQRAANMAQASEFIERYNdSFDHEvEERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03264   77 LPQEFGVYPNFTV--REFLDYIAWLKGIPSKEVKARVDEVLELVN-LGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSIL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 493 ILDDSTSALDAESEKKVQQALEhELPDTTTFIIAEKIVSVI--NADTILVLDDGKLVAQG 550
Cdd:cd03264  153 IVDEPTAGLDPEERIRFRNLLS-ELGEDRIVILSTHIVEDVesLCNQVAVLNKGKLVFEG 211
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
333-546 2.99e-27

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


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 109.54  E-value: 2.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAA--LRKTV 410
Cdd:cd03262    1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSG-TIASNLRQgnAQAKLHELQRAANMAQASEFIERYndSFDHEVEERSANFSGGQKQRLSIARGLIAKA 489
Cdd:cd03262   79 GMVFQQFNLFPHlTVLENITL--APIKVKGMSKAEAEERALELLEKV--GLADKADAYPAQLSGGQQQRVAIARALAMNP 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 490 PILILDDSTSALDAESEKKVQQALEHELPDTTTFII-------AEKIvsvinADTILVLDDGKL 546
Cdd:cd03262  155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVvthemgfAREV-----ADRVIFMDDGRI 213
PLN03232 PLN03232
ABC transporter C family member; Provisional
165-567 2.99e-27

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 117.38  E-value: 2.99e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  165 VALIFG---------FGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVK------SFNQGPQEIKkfdqtSDQLNd 229
Cdd:PLN03232  441 VASLFGslilfllipLQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKcyawekSFESRIQGIR-----NEELS- 514
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  230 ynivigyWF--SAIMPAFQMIAYTVIALIVYLIGKNI-TAHPSDIAVVSPFVNYVL--TLLFTIMIAGMTLMQFSRANIS 304
Cdd:PLN03232  515 -------WFrkAQLLSAFNSFILNSIPVVVTLVSFGVfVLLGGDLTPARAFTSLSLfaVLRSPLNMLPNLLSQVVNANVS 587
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  305 LGRIREVLETEPDVkFVESGSVAPLSGSVEFDHVSFTYPDG-DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIarl 383
Cdd:PLN03232  588 LQRIEELLLSEERI-LAQNPPLQPGAPAISIKNGYFSWDSKtSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM--- 663
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  384 ydptkgkvkIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLRQGnAQAKLHELQRAANMAQASEFIERYNDSFDHE 463
Cdd:PLN03232  664 ---------LGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFG-SDFESERYWRAIDVTALQHDLDLLPGRDLTE 733
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  464 VEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKV-QQALEHELPDTTTFIIAEKIVSVINADTILVLD 542
Cdd:PLN03232  734 IGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVS 813
                         410       420
                  ....*....|....*....|....*
gi 492039060  543 DGKLVAQGTHEELLKTSLVYQEIFK 567
Cdd:PLN03232  814 EGMIKEEGTFAELSKSGSLFKKLME 838
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
106-572 3.04e-27

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 117.32  E-value: 3.04e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   106 IKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSfIFCIVIIPRFWWAPVVMVALIF-GFGAYVLRQMNSLFT 184
Cdd:TIGR01271  976 LNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGA-IFVVSVLQPYIFIAAIPVAVIFiMLRAYFLRTSQQLKQ 1054
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   185 KFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTsdqlndYNIVIGYWFS--AIMPAFQM----------IAYTV 252
Cdd:TIGR01271 1055 LESEARSPIFSHLITSLKGLWTIRAFGRQSYFETLFHKA------LNLHTANWFLylSTLRWFQMridiifvfffIAVTF 1128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   253 IALIVYLIGknitahPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRaniSLGRIREVLETEP---------------D 317
Cdd:TIGR01271 1129 IAIGTNQDG------EGEVGIILTLAMNILSTLQWAVNSSIDVDGLMR---SVSRVFKFIDLPQeeprpsggggkyqlsT 1199
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   318 VKFVESGSVA---PLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDpTKGKVKIG 394
Cdd:TIGR01271 1200 VLVIENPHAQkcwPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQID 1278
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   395 GQNIKDVTEAALRKTVSFVLQRAVLFSGTIASNLrQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGG 474
Cdd:TIGR01271 1279 GVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL-DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNG 1357
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   475 QKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEE 554
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQK 1437
                          490
                   ....*....|....*....
gi 492039060   555 LL-KTSLVYQEIFKTQKGK 572
Cdd:TIGR01271 1438 LLnETSLFKQAMSAADRLK 1456
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
18-288 3.86e-27

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: 110.81  E-value: 3.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   18 VVCAIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLSDGIWLVVLGIIAIISGIFN---VYFAAKIAQGVVSDLREDT 94
Cdd:pfam00664   1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSflqSYLLNHTGERLSRRLRRKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   95 YAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAY 174
Cdd:pfam00664  81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  175 VLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIA 254
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 492039060  255 LIVYLIGKNITAHPSDIAVVSPFVNYVLTLLFTI 288
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
PTZ00243 PTZ00243
ABC transporter; Provisional
325-566 3.88e-27

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 117.19  E-value: 3.88e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  325 SVAP---LSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDV 401
Cdd:PTZ00243 1298 SAAPhpvQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAY 1377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  402 TEAALRKTVSFVLQRAVLFSGTIASNLrQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSI 481
Cdd:PTZ00243 1378 GLRELRRQFSMIPQDPVLFDGTVRQNV-DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCM 1456
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  482 ARGLIAKAPILIL-DDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSl 560
Cdd:PTZ00243 1457 ARALLKKGSGFILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNR- 1535

                  ....*.
gi 492039060  561 vyQEIF 566
Cdd:PTZ00243 1536 --QSIF 1539
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
333-555 9.08e-27

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: 108.48  E-value: 9.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVteAALRKTVSF 412
Cdd:cd03300    1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL--PPHKRPVNT 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRQGNAQAKLHELQRAANMAQASEFI--ERYNDSFDHEVeersanfSGGQKQRLSIARGLIAKA 489
Cdd:cd03300   77 VFQNYALFPHlTVFENIAFGLRLKKLPKAEIKERVAEALDLVqlEGYANRKPSQL-------SGGQQQRVAIARALVNEP 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 490 PILILDDSTSALDAESEKKVQ---QALEHELpdTTTFIIA----EKIVSVinADTILVLDDGKLVAQGTHEEL 555
Cdd:cd03300  150 KVLLLDEPLGALDLKLRKDMQlelKRLQKEL--GITFVFVthdqEEALTM--SDRIAVMNKGKIQQIGTPEEI 218
cbiO PRK13644
energy-coupling factor transporter ATPase;
333-556 1.21e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 109.31  E-value: 1.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTE-AALRKTVS 411
Cdd:PRK13644   2 IRLENVSYSYPDGT-PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRA-VLFSG-TIASNLRQGNAQAKLH--ELQRAANMAQASEFIERYndsfdhevEERS-ANFSGGQKQRLSIArGLI 486
Cdd:PRK13644  81 IVFQNPeTQFVGrTVEEDLAFGPENLCLPpiEIRKRVDRALAEIGLEKY--------RHRSpKTLSGGQGQCVALA-GIL 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 487 AKAP-ILILDDSTSALDAESEKKVQQALE--HELPDTTTFiIAEKIVSVINADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK13644 152 TMEPeCLIFDEVTSMLDPDSGIAVLERIKklHEKGKTIVY-ITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
300-532 1.64e-26

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 113.75  E-value: 1.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 300 RANIS-LGRIREVLETEPDVKFVESGSVAPLSGSVEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQ 378
Cdd:COG4178  329 RATVDrLAGFEEALEAADALPEAASRIETSEDGALALEDLTLRTPDGR-PLLEDLSLSLKPGERLLITGPSGSGKSTLLR 407
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 379 LIARLYDPTKGKVkiggqnikDVTEAAlrkTVSFVLQRAVLFSGTIASNLR--QGNAQAKLHELQRAANMAQASEFIERY 456
Cdd:COG4178  408 AIAGLWPYGSGRI--------ARPAGA---RVLFLPQRPYLPLGTLREALLypATAEAFSDAELREALEAVGLGHLAERL 476
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 457 ndsfdHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTtfiiaekIVSV 532
Cdd:COG4178  477 -----DEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTT-------VISV 540
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
333-550 1.67e-26

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: 107.30  E-value: 1.67e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRktVSF 412
Cdd:cd03268    1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR--IGA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRqgnAQAKLHELQRAANMaqasEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:cd03268   77 LIEAPGFYPNlTARENLR---LLARLLGIRKKRID----EVLDVVG--LKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 492 LILDDSTSALDAESEKKVQQALeHELPDT-TTFIIAEKIVSVIN--ADTILVLDDGKLVAQG 550
Cdd:cd03268  148 LILDEPTNGLDPDGIKELRELI-LSLRDQgITVLISSHLLSEIQkvADRIGIINKGKLIEEG 208
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
337-557 1.68e-26

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: 110.14  E-value: 1.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 337 HVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP---TKGKVKIGGQNIKDVTEAALRK----- 408
Cdd:COG0444    8 KVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKirgre 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 409 ----------------TVSFVLQRAVLFSGtiasNLRQGNAQAKLHELQRAANMAQASEFIERYndsfDHEveersanFS 472
Cdd:COG0444   88 iqmifqdpmtslnpvmTVGDQIAEPLRIHG----GLSKAEARERAIELLERVGLPDPERRLDRY----PHE-------LS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 473 GGQKQRLSIARGLIAKAPILILDDSTSALDAEsekkVQ-QALE------HELpDTTT-FI-----IAEKIvsvinADTIL 539
Cdd:COG0444  153 GGMRQRVMIARALALEPKLLIADEPTTALDVT----IQaQILNllkdlqREL-GLAIlFIthdlgVVAEI-----ADRVA 222
                        250
                 ....*....|....*...
gi 492039060 540 VLDDGKLVAQGTHEELLK 557
Cdd:COG0444  223 VMYAGRIVEEGPVEELFE 240
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
352-502 1.72e-26

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 110.21  E-value: 1.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 352 DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL---RKTVSFVLQ------------- 415
Cdd:COG4608   36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELrplRRRMQMVFQdpyaslnprmtvg 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 RAVLFSGTIASNLRQGNAQAKLHELqraanMAQ---ASEFIERYndsfDHEveersanFSGGQKQRLSIARGLIAKAPIL 492
Cdd:COG4608  116 DIIAEPLRIHGLASKAERRERVAEL-----LELvglRPEHADRY----PHE-------FSGGQRQRIGIARALALNPKLI 179
                        170
                 ....*....|
gi 492039060 493 ILDDSTSALD 502
Cdd:COG4608  180 VCDEPVSALD 189
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
333-555 1.94e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 109.01  E-value: 1.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL--RKTV 410
Cdd:PRK13639   2 LETRDLKYSYPDGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRA--VLFSGTIASNLRQG--NAQAKLHELQRAANMAQASEFIERYNDSFDHeveersaNFSGGQKQRLSIArGLI 486
Cdd:PRK13639  81 GIVFQNPddQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEALKAVGMEGFENKPPH-------HLSGGQKKRVAIA-GIL 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 487 AKAP-ILILDDSTSALDAESEKKVQQALeHELPDT-TTFIIAEKIVSV--INADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK13639 153 AMKPeIIVLDEPTSGLDPMGASQIMKLL-YDLNKEgITIIISTHDVDLvpVYADKVYVMSDGKIIKEGTPKEV 224
PLN03130 PLN03130
ABC transporter C family member; Provisional
164-565 7.12e-26

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 113.29  E-value: 7.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  164 MVALIFGFGAYVLRQMNSLfTK--FQEMMDRISnQAQETLQGVRVVK------SFNQGPQEIKkfdqtSDQLNdynivig 235
Cdd:PLN03130  449 MLVLMFPIQTFIISKMQKL-TKegLQRTDKRIG-LMNEVLAAMDTVKcyawenSFQSKVQTVR-----DDELS------- 514
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  236 yWF--SAIMPAFQM-------IAYTVIALIVY-LIGKNITahPSDiAVVSPFVNYVLTL-LFtiMIAGMtLMQFSRANIS 304
Cdd:PLN03130  515 -WFrkAQLLSAFNSfilnsipVLVTVVSFGVFtLLGGDLT--PAR-AFTSLSLFAVLRFpLF--MLPNL-ITQAVNANVS 587
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  305 LGRIREVLETEPDVkFVESGSVAPLSGSVEFDHVSFTY-PDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARL 383
Cdd:PLN03130  588 LKRLEELLLAEERV-LLPNPPLEPGLPAISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGE 666
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  384 YDPTKGkvkiggqnikdvTEAALRKTVSFVLQRAVLFSGTIASNLRQGnaqaklhelqraanmaqaSEF-IERYNDSFD- 461
Cdd:PLN03130  667 LPPRSD------------ASVVIRGTVAYVPQVSWIFNATVRDNILFG------------------SPFdPERYERAIDv 716
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  462 ---------------HEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKV-QQALEHELPDTTTFII 525
Cdd:PLN03130  717 talqhdldllpggdlTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLV 796
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|
gi 492039060  526 AEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVYQEI 565
Cdd:PLN03130  797 TNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
334-556 7.97e-26

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 105.99  E-value: 7.97e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDgddpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDvTEAALRKtVSFV 413
Cdd:COG3840    3 RLDDLTYRYGD----FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAERP-VSML 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRAVLFSG-TIASNLRQG-NAQAKLHELQRaanmAQASEFIERYNDSfdhEVEER-SANFSGGQKQRLSIARGLIAKAP 490
Cdd:COG3840   77 FQENNLFPHlTVAQNIGLGlRPGLKLTAEQR----AQVEQALERVGLA---GLLDRlPGQLSGGQRQRVALARCLVRKRP 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 491 ILILDDSTSALDaesekkvqQALEHELPDTTTFIIAEKIVSVIN-----------ADTILVLDDGKLVAQGTHEELL 556
Cdd:COG3840  150 ILLLDEPFSALD--------PALRQEMLDLVDELCRERGLTVLMvthdpedaariADRVLLVADGRIAADGPTAALL 218
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
333-551 9.39e-26

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 108.35  E-value: 9.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKT- 409
Cdd:PRK11153   2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 --VSFVLQRAVLFSG-TIASN----LRQGNA-----QAKLHELqraANMAQASEFIERYndsfdheveerSANFSGGQKQ 477
Cdd:PRK11153  82 rqIGMIFQHFNLLSSrTVFDNvalpLELAGTpkaeiKARVTEL---LELVGLSDKADRY-----------PAQLSGGQKQ 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 478 RLSIARGLIAKAPILILDDSTSALDAESEKKVQQALE---HELPDTTTFIIAEkiVSVIN--ADTILVLDDGKLVAQGT 551
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKdinRELGLTIVLITHE--MDVVKriCDRVAVIDAGRLVEQGT 224
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
344-558 9.65e-26

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: 105.88  E-value: 9.65e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 344 DGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGqniKDVTE-AALRKTVSFVLQRAVLFSG 422
Cdd:cd03299    9 DWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG---KDITNlPPEKRDISYVPQNYALFPH 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 -TIASNLRQGNAQAKLHELQRAANMAQASEFIeryndSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSAL 501
Cdd:cd03299   86 mTVYKNIAYGLKKRKVDKKEIERKVLEIAEML-----GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 502 DAESEKKVQQALE--HELPDTTTFIIAEKIVSV-INADTILVLDDGKLVAQGTHEELLKT 558
Cdd:cd03299  161 DVRTKEKLREELKkiRKEFGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPEEVFKK 220
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
332-555 1.10e-25

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 108.63  E-value: 1.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikDVTEAALR-KTV 410
Cdd:PRK10851   2 SIEIANIKKSF--GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT---DVSRLHARdRKV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSG-TIASNLRQG----------NAQAKLHELQRAANMAQASEFIERYndsfdheveerSANFSGGQKQRL 479
Cdd:PRK10851  77 GFVFQHYALFRHmTVFDNIAFGltvlprrerpNAAAIKAKVTQLLEMVQLAHLADRY-----------PAQLSGGQKQRV 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 480 SIARGLIAKAPILILDDSTSALDAESEKKVQ---QALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK10851 146 ALARALAVEPQILLLDEPFGALDAQVRKELRrwlRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
333-565 1.34e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 106.37  E-value: 1.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpDGDDP-TLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVS 411
Cdd:PRK13648   8 IVFKNVSFQY-QSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAV-LFSGTI-----ASNLRqgNAQAKLHELQRAANmaQASEFIERYNDSfDHEVEersaNFSGGQKQRLSIArGL 485
Cdd:PRK13648  87 IVFQNPDnQFVGSIvkydvAFGLE--NHAVPYDEMHRRVS--EALKQVDMLERA-DYEPN----ALSGGQKQRVAIA-GV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 486 IAKAP-ILILDDSTSALDAESEKKVQQALEH--ELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSLVY 562
Cdd:PRK13648 157 LALNPsVIILDEATSMLDPDARQNLLDLVRKvkSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236

                 ...
gi 492039060 563 QEI 565
Cdd:PRK13648 237 TRI 239
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
348-509 1.74e-25

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: 104.82  E-value: 1.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKI--GGQNIkDVTEA------ALRK-TVSFVLQ--R 416
Cdd:COG4778   25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWV-DLAQAspreilALRRrTIGYVSQflR 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 417 AVLFSGTI---ASNLRQgnaqaklHELQRAANMAQASEFIERYNdsfdheVEER-----SANFSGGQKQRLSIARGLIAK 488
Cdd:COG4778  104 VIPRVSALdvvAEPLLE-------RGVDREEARARARELLARLN------LPERlwdlpPATFSGGEQQRVNIARGFIAD 170
                        170       180
                 ....*....|....*....|.
gi 492039060 489 APILILDDSTSALDAESEKKV 509
Cdd:COG4778  171 PPLLLLDEPTASLDAANRAVV 191
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
334-548 2.62e-25

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 110.58  E-value: 2.62e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL----R 407
Cdd:PRK10535   6 ELKDIRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQRAVLFSG-TIASNLRqgnAQAKLHELQRAANMAQASEFIERYndSFDHEVEERSANFSGGQKQRLSIARGLI 486
Cdd:PRK10535  86 EHFGFIFQRYHLLSHlTAAQNVE---VPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 487 AKAPILILDDSTSALDAESEKKVqQALEHELPDT--TTFIIAEKIVSVINADTILVLDDGKLVA 548
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEV-MAILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
333-557 3.41e-25

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 105.49  E-value: 3.41e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdP----TLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---- 404
Cdd:PRK13634   3 ITFQKVEHRYQYKT-PferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklk 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 405 ALRKTVSFVLQ--RAVLFSGTIASNLRQG-------NAQAKlhelqraanmAQASEFIERYndSFDHEVEERSA-NFSGG 474
Cdd:PRK13634  82 PLRKKVGIVFQfpEHQLFEETVEKDICFGpmnfgvsEEDAK----------QKAREMIELV--GLPEELLARSPfELSGG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 475 QKQRLSIArGLIAKAP-ILILDDSTSALDAESEKKVQQALE--HELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQG 550
Cdd:PRK13634 150 QMRRVAIA-GVLAMEPeVLVLDEPTAGLDPKGRKEMMEMFYklHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQG 228

                 ....*..
gi 492039060 551 THEELLK 557
Cdd:PRK13634 229 TPREIFA 235
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
350-556 3.86e-25

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: 109.39  E-value: 3.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLyDPTKGKVKIGGQNIKDVTEAALRKtvsfvLQRA--VLF------- 420
Cdd:COG4172  302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALRP-----LRRRmqVVFqdpfgsl 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 ------SGTIASNLRqgnaqakLHEL-----QRAANMAQA-------SEFIERYndsfDHEveersanFSGGQKQRLSIA 482
Cdd:COG4172  376 sprmtvGQIIAEGLR-------VHGPglsaaERRARVAEAleevgldPAARHRY----PHE-------FSGGQRQRIAIA 437
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 483 RGLIAKAPILILDDSTSALDAESEKKV-------QQalEHELpdTTTFIIAEkiVSVINA--DTILVLDDGKLVAQGTHE 553
Cdd:COG4172  438 RALILEPKLLVLDEPTSALDVSVQAQIldllrdlQR--EHGL--AYLFISHD--LAVVRAlaHRVMVMKDGKVVEQGPTE 511

                 ...
gi 492039060 554 ELL 556
Cdd:COG4172  512 QVF 514
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
332-550 5.43e-25

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: 102.24  E-value: 5.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYPDGDDPT----LKDISFKIKPGQMVGIVGATGAGKSTLAQLIA--RLYDPTKGKVKIGGQNIKDVTeaa 405
Cdd:cd03213    3 TLSFRNLTVTVKSSPSKSgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKRS--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 LRKTVSFVLQRAVLFSG-TIASNLRqgnAQAKLHELqraanmaqasefieryndsfdheveersanfSGGQKQRLSIARG 484
Cdd:cd03213   80 FRKIIGYVPQDDILHPTlTVRETLM---FAAKLRGL-------------------------------SGGERKRVSIALE 125
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFII-----AEKIVSVinADTILVLDDGKLVAQG 550
Cdd:cd03213  126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICsihqpSSEIFEL--FDKLLLLSQGRVIYFG 194
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
336-563 7.88e-25

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 103.66  E-value: 7.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKtvsfvlQ 415
Cdd:COG4559    5 ENLSVRL--GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELAR------R 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 RAVL---------FS-------GTIAsnlrQGNAQAKLHELQRAAnMAQA--SEFIER-YNDsfdheveersanFSGGQK 476
Cdd:COG4559   77 RAVLpqhsslafpFTveevvalGRAP----HGSSAAQDRQIVREA-LALVglAHLAGRsYQT------------LSGGEQ 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 477 QRLSIARGLI-------AKAPILILDDSTSALDaesekkvqqaLEHELpdtTTFII----AEKIVSVI------N----- 534
Cdd:COG4559  140 QRVQLARVLAqlwepvdGGPRWLFLDEPTSALD----------LAHQH---AVLRLarqlARRGGGVVavlhdlNlaaqy 206
                        250       260
                 ....*....|....*....|....*....
gi 492039060 535 ADTILVLDDGKLVAQGTHEELLKTSLVYQ 563
Cdd:COG4559  207 ADRILLLHQGRLVAQGTPEEVLTDELLER 235
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
333-547 1.02e-24

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: 102.33  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVtEAALRKtVSF 412
Cdd:cd03301    1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDL-PPKDRD-IAM 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRQGNAQAKLHE------LQRAANMAQASEFIERYndsfdheveerSANFSGGQKQRLSIARGL 485
Cdd:cd03301   77 VFQNYALYPHmTVYDNIAFGLKLRKVPKdeiderVREVAELLQIEHLLDRK-----------PKQLSGGQRQRVALGRAI 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 486 IAKAPILILDDSTSALDAE------SE-KKVQQALEHelpdTTTFIIAEKIVSVINADTILVLDDGKLV 547
Cdd:cd03301  146 VREPKVFLMDEPLSNLDAKlrvqmrAElKRLQQRLGT----TTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
345-556 1.19e-24

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: 102.13  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDV-TEAALRKTVSFVLQRAVLFSG- 422
Cdd:cd03224   11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpPHERARAGIGYVPEGRRIFPEl 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 TIASNLRQGnAQAKLHElQRAANMAQASEFI----ERYNdsfdheveERSANFSGGQKQRLSIARGLIAKAPILILDDST 498
Cdd:cd03224   91 TVEENLLLG-AYARRRA-KRKARLERVYELFprlkERRK--------QLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 499 SALdaeSEKKVQQALE--HELPDT-TTFIIAEKIVSVI--NADTILVLDDGKLVAQGTHEELL 556
Cdd:cd03224  161 EGL---APKIVEEIFEaiRELRDEgVTILLVEQNARFAleIADRAYVLERGRVVLEGTAAELL 220
cbiO PRK13637
energy-coupling factor transporter ATPase;
332-557 1.33e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 103.97  E-value: 1.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYPDG---DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI--KDVTEAAL 406
Cdd:PRK13637   2 SIKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 407 RKTVSFVLQ--RAVLFSGTIASNLRQGNAQAKLHE------LQRAANMAQASefIERYNDSFDHEVeersanfSGGQKQR 478
Cdd:PRK13637  82 RKKVGLVFQypEYQLFEETIEKDIAFGPINLGLSEeeienrVKRAMNIVGLD--YEDYKDKSPFEL-------SGGQKRR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIArGLIAKAP-ILILDDSTSALDAESEKKV--QQALEHELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEE 554
Cdd:PRK13637 153 VAIA-GVVAMEPkILILDEPTAGLDPKGRDEIlnKIKELHKEYNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPRE 231

                 ...
gi 492039060 555 LLK 557
Cdd:PRK13637 232 VFK 234
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
350-557 1.79e-24

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 102.13  E-value: 1.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL-RKTVSFVLQRAVLFSG-TIASN 427
Cdd:cd03219   16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLEN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 428 LRQGnAQAKLHEL--------QRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:cd03219   96 VMVA-AQARTGSGlllararrEEREARERAEELLERVG--LADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 500 ALDAESEKKVQQALEhELPDT-TTFIIAE---KIVSVInADTILVLDDGKLVAQGTHEELLK 557
Cdd:cd03219  173 GLNPEETEELAELIR-ELRERgITVLLVEhdmDVVMSL-ADRVTVLDQGRVIAEGTPDEVRN 232
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
333-555 1.85e-24

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 102.81  E-value: 1.85e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD--P---TKGKVKIGGQNI--KDVTEAA 405
Cdd:COG1117   12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 LRKTVSFVLQRAVLFSGTIASNLRQGnaqAKLHELQRAANMAqasEFIERyndS------FDhEVEER---SA-NFSGGQ 475
Cdd:COG1117   90 LRRRVGMVFQKPNPFPKSIYDNVAYG---LRLHGIKSKSELD---EIVEE---SlrkaalWD-EVKDRlkkSAlGLSGGQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 476 KQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDTTTFII-------AEKIvsvinADTILVLDDGKLVA 548
Cdd:COG1117  160 QQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELI-LELKKDYTIVIvthnmqqAARV-----SDYTAFFYLGELVE 233

                 ....*..
gi 492039060 549 QGTHEEL 555
Cdd:COG1117  234 FGPTEQI 240
cbiO PRK13641
energy-coupling factor transporter ATPase;
332-559 2.14e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 103.37  E-value: 2.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYPDG---DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---- 404
Cdd:PRK13641   2 SIKFENVDYIYSPGtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlk 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 405 ALRKTVSFVLQ--RAVLFSGTIASNLRQGNAQAKLHElQRAANmaQASEFIERYndSFDHEVEERSA-NFSGGQKQRLSI 481
Cdd:PRK13641  82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE-DEAKE--KALKWLKKV--GLSEDLISKSPfELSGGQMRRVAI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 482 ArGLIAKAP-ILILDDSTSALDAESEKKVQQA-LEHELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK13641 157 A-GVMAYEPeILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSD 235

                 .
gi 492039060 559 S 559
Cdd:PRK13641 236 K 236
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
333-559 2.26e-24

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 102.09  E-value: 2.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD--VTEAALRKTV 410
Cdd:PRK09493   2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQRAVLFSGTIA-SNLRQGNAQAKlhELQRAANMAQASEFIERYNdsfdheVEERSANF----SGGQKQRLSIARGL 485
Cdd:PRK09493  80 GMVFQQFYLFPHLTAlENVMFGPLRVR--GASKEEAEKQARELLAKVG------LAERAHHYpselSGGQQQRVAIARAL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 486 IAKAPILILDDSTSALDAESEK---KVQQALEHElpdTTTFII-------AEKIVSvinadTILVLDDGKLVAQGTHEEL 555
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHevlKVMQDLAEE---GMTMVIvtheigfAEKVAS-----RLIFIDKGRIAEDGDPQVL 223

                 ....
gi 492039060 556 LKTS 559
Cdd:PRK09493 224 IKNP 227
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
333-550 2.67e-24

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


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 101.03  E-value: 2.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTlkDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikDVTEA-ALRKTVS 411
Cdd:cd03298    1 VRLDKIRFSY--GEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTAApPADRPVS 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSG-TIASNLRQG-NAQAKLHELQRAANMAQASEFieryndSFDHEVEERSANFSGGQKQRLSIARGLIAKA 489
Cdd:cd03298   74 MLFQENNLFAHlTVEQNVGLGlSPGLKLTAEDRQAIEVALARV------GLAGLEKRLPGELSGGERQRVALARVLVRDK 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 490 PILILDDSTSALDAesekkvqqALEHELPDTTTFIIAEKIVSVIN-----------ADTILVLDDGKLVAQG 550
Cdd:cd03298  148 PVLLLDEPFAALDP--------ALRAEMLDLVLDLHAETKMTVLMvthqpedakrlAQRVVFLDNGRIAAQG 211
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
350-550 3.32e-24

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: 100.83  E-value: 3.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIK---PGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDvTEAAL-----RKTVSFVLQRAVLFS 421
Cdd:cd03297   10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFD-SRKKInlppqQRKIGLVFQQYALFP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 G-TIASNLRQGnaqakLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:cd03297   89 HlNVRENLAFG-----LKRKRNREDRISVDELLDLLG--LDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 501 LDAESEKKVQQALEH---ELPDTTTFII-----AEKIvsvinADTILVLDDGKLVAQG 550
Cdd:cd03297  162 LDRALRLQLLPELKQikkNLNIPVIFVThdlseAEYL-----ADRIVVMEDGRLQYIG 214
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
323-548 3.33e-24

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: 101.36  E-value: 3.33e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 323 SGSVAPLsgsVEFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD 400
Cdd:COG4181    2 SSSSAPI---IELRGLTKTVGTGAGELtiLKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 401 VTE---AALR-KTVSFVLQRAVLFSGTIAsnLRqgNAQAKLhELQRAAN-MAQASEFIERY--NDSFDHeveeRSANFSG 473
Cdd:COG4181   79 LDEdarARLRaRHVGFVFQSFQLLPTLTA--LE--NVMLPL-ELAGRRDaRARARALLERVglGHRLDH----YPAQLSG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 474 GQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEhELPDT--TTFII-------AEKivsvinADTILVLDDG 544
Cdd:COG4181  150 GEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLF-ELNRErgTTLVLvthdpalAAR------CDRVLRLRAG 222

                 ....
gi 492039060 545 KLVA 548
Cdd:COG4181  223 RLVE 226
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
21-308 3.82e-24

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: 102.85  E-value: 3.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  21 AIIAILVSAFSGLYQPKLLEN-IQKALMANQK--QAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTYAK 97
Cdd:cd18544    4 ALLLLLLATALELLGPLLIKRaIDDYIVPGQGdlQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSH 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  98 IQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVLR 177
Cdd:cd18544   84 IQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLFRK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 178 QMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIALIV 257
Cdd:cd18544  164 KSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVL 243
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492039060 258 YLIGKNITAHPSDIAVVSPFVNYvLTLLFT--IMIAG-MTLMQfsRANISLGRI 308
Cdd:cd18544  244 WYGGGQVLSGAVTLGVLYAFIQY-IQRFFRpiRDLAEkFNILQ--SAMASAERI 294
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
354-556 6.08e-24

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 100.43  E-value: 6.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 354 SFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAalRKTVSFVLQRAVLFSG-TIASNLRQG- 431
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGl 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 432 NAQAKLHELQRAANMAQASE-FIERYNDSFDHEVeersanfSGGQKQRLSIARGLIAKAPILILDDSTSALDAesekkvq 510
Cdd:PRK10771  97 NPGLKLNAAQREKLHAIARQmGIEDLLARLPGQL-------SGGQRQRVALARCLVREQPILLLDEPFSALDP------- 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 511 qALEHELPDTTTFIIAEK-----IVS--VINADTI----LVLDDGKLVAQGTHEELL 556
Cdd:PRK10771 163 -ALRQEMLTLVSQVCQERqltllMVShsLEDAARIaprsLVVADGRIAWDGPTDELL 218
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
350-553 9.59e-24

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: 9.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIA--RLYDPTKGKVKIGGQNIKD--VTEAAlRKTVSFVLQRAVLFSG-TI 424
Cdd:COG0396   16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMghPKYEVTSGSILLDGEDILElsPDERA-RAGIFLAFQYPVEIPGvSV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 ASNLRQGNAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSAN--FSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:COG0396   95 SNFLRTALNARRGEELSAREFLKLLKEKMKELG--LDEDFLDRYVNegFSGGEKKRNEILQMLLLEPKLAILDETDSGLD 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492039060 503 AESEKKVQQALEHEL-PDTTTFIIA--EKIVSVINADTILVLDDGKLVAQGTHE 553
Cdd:COG0396  173 IDALRIVAEGVNKLRsPDRGILIIThyQRILDYIKPDFVHVLVDGRIVKSGGKE 226
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
333-546 1.48e-23

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: 99.02  E-value: 1.48e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAA---LRKT 409
Cdd:cd03292    1 IEFINVTKTYP-NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRAVLfsgtiasnlrqgnaqakLHELQRAANMAQASEFI--------ERYNDSFD-----HEVEERSANFSGGQK 476
Cdd:cd03292   80 IGVVFQDFRL-----------------LPDRNVYENVAFALEVTgvppreirKRVPAALElvglsHKHRALPAELSGGEQ 142
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 477 QRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADT--ILVLDDGKL 546
Cdd:cd03292  143 QRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
21-281 2.00e-23

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.


Pssm-ID: 349991 [Multi-domain]  Cd Length: 298  Bit Score: 100.56  E-value: 2.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  21 AIIAILVSAFSGLYQPKLLENI--QKALMANQKQAVLSDGIW--LVVLGIIAIISGIFNV---YFAAKIAQGVVSDLRED 93
Cdd:cd18547    4 VIILAIISTLLSVLGPYLLGKAidLIIEGLGGGGGVDFSGLLriLLLLLGLYLLSALFSYlqnRLMARVSQRTVYDLRKD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  94 TYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGA 173
Cdd:cd18547   84 LFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTK 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 174 YVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMI---AY 250
Cdd:cd18547  164 FIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFInnlGY 243
                        250       260       270
                 ....*....|....*....|....*....|...
gi 492039060 251 TVIALI--VYLIGKNITahpsdIAVVSPFVNYV 281
Cdd:cd18547  244 VLVAVVggLLVINGALT-----VGVIQAFLQYS 271
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
332-549 2.28e-23

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 102.03  E-value: 2.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAalRKTVS 411
Cdd:PRK11000   3 SVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSG-TIASNLRQGNAQAKLHELQRAANMAQASEFIEryndsFDHEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:PRK11000  79 MVFQSYALYPHlSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQ-----LAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 491 ILILDDSTSALDAesEKKVQQALE----HE-LPDTTTFIIAEKIVSVINADTILVLDDGKlVAQ 549
Cdd:PRK11000 154 VFLLDEPLSNLDA--ALRVQMRIEisrlHKrLGRTMIYVTHDQVEAMTLADKIVVLDAGR-VAQ 214
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
350-554 2.69e-23

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: 99.34  E-value: 2.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIK-----DVTEAALRKTvsFvlQRAVLFSG-T 423
Cdd:COG0411   20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglpphRIARLGIART--F--QNPRLFPElT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 424 IASNLRQGnAQAKLHE-------------LQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:COG0411   96 VLENVLVA-AHARLGRgllaallrlprarREEREARERAEELLERVG--LADRADEPAGNLSYGQQRRLEIARALATEPK 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 491 ILILDDSTSALDAEsEKKVQQALEHELPDT--TTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEE 554
Cdd:COG0411  173 LLLLDEPAAGLNPE-ETEELAELIRRLRDErgITILLIEHDMDLVMglADRIVVLDFGRVIAEGTPAE 239
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
337-550 2.91e-23

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: 98.21  E-value: 2.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 337 HVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQR 416
Cdd:cd03266    8 TKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDST 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 417 AVLFSGTIASNLRQgnaQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDD 496
Cdd:cd03266   88 GLYDRLTARENLEY---FAGLYGLKGDELTARLEELADRLG--MEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDE 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 497 STSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINA--DTILVLDDGKLVAQG 550
Cdd:cd03266  163 PTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERlcDRVVVLHRGRVVYEG 218
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
350-561 3.98e-23

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 102.79  E-value: 3.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ--NIKDVTEAaLRKTVSFVLQRAVLFSG-TIAS 426
Cdd:COG1129   20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEpvRFRSPRDA-QAAGIAIIHQELNLVPNlSVAE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 NLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDheVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDaESE 506
Cdd:COG1129   99 NIFLGREPRRGGLIDWRAMRRRARELLARLGLDID--PDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT-ERE 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 507 KKVQQALEHELpdtttfiiAEKIVSVI-----------NADTILVLDDGKLVAQGTHEELLKTSLV 561
Cdd:COG1129  176 VERLFRIIRRL--------KAQGVAIIyishrldevfeIADRVTVLRDGRLVGTGPVAELTEDELV 233
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
345-555 9.30e-23

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: 96.67  E-value: 9.30e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI-KDVTEaaLRKTVSFVLQRAVLFSG- 422
Cdd:cd03265   11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvREPRE--VRRRIGIVFQDLSVDDEl 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 TIASNLRqgnAQAKLHELQRaanmAQASEFIERYNDSFD-HEVEER-SANFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:cd03265   89 TGWENLY---IHARLYGVPG----AERRERIDELLDFVGlLEAADRlVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 501 LDAESEKKVQQALE--HELPDTTTFII------AEKIvsvinADTILVLDDGKLVAQGTHEEL 555
Cdd:cd03265  162 LDPQTRAHVWEYIEklKEEFGMTILLTthymeeAEQL-----CDRVAIIDHGRIIAEGTPEEL 219
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
352-559 1.05e-22

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: 99.80  E-value: 1.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  352 DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD----VTEAALRKTVSFVLQRAVLFSG-TIAS 426
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPHlSVRG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  427 NLRQGNAQAKLHelQRAANMAQASEFIeryndSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESE 506
Cdd:TIGR02142  95 NLRYGMKRARPS--ERRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRK 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060  507 KKVQQALE--HELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEELLKTS 559
Cdd:TIGR02142 168 YEILPYLErlHAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
335-505 1.30e-22

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 101.29  E-value: 1.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 335 FDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGqnikdvteaalRKTVSFVL 414
Cdd:COG0488    1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYLP 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 415 QRAVLFSG-TIASNLRQGNA--QAKLHELQRA-ANMAQASEFIERYND-----------SFDHEVEE------------- 466
Cdd:COG0488   68 QEPPLDDDlTVLDTVLDGDAelRALEAELEELeAKLAEPDEDLERLAElqeefealggwEAEARAEEilsglgfpeedld 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 492039060 467 -RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAES 505
Cdd:COG0488  148 rPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
333-563 1.47e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 97.50  E-value: 1.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:PRK13647   5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRA--VLFSGTIASNLRQG--NAQAKLHELQRAANMAQASEFIERYNDSFDHeveersaNFSGGQKQRLSIArGLIAK 488
Cdd:PRK13647  84 VFQDPddQVFSSTVWDDVAFGpvNMGLDKDEVERRVEEALKAVRMWDFRDKPPY-------HLSYGQKKRVAIA-GVLAM 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 489 AP-ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELLKTSLVYQ 563
Cdd:PRK13647 156 DPdVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAewADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
333-561 1.52e-22

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: 97.08  E-value: 1.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGK-VKIGGQNIKDVTEAALRKTVS 411
Cdd:COG1119    4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRIG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FV---LQR----------AVLfSGTIASNLRQGNAQAKlhELQRAANMAQASEFIERYNDSFDHeveersanFSGGQKQR 478
Cdd:COG1119   82 LVspaLQLrfprdetvldVVL-SGFFDSIGLYREPTDE--QRERARELLELLGLAHLADRPFGT--------LSQGEQRR 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIARGLIAKAPILILDDSTSALDAESEKKVQQALEH--ELPDTTTFII---AEKIVSVINadTILVLDDGKLVAQGTHE 553
Cdd:COG1119  151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVthhVEEIPPGIT--HVLLLKDGRVVAAGPKE 228

                 ....*...
gi 492039060 554 ELLKTSLV 561
Cdd:COG1119  229 EVLTSENL 236
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
332-553 1.59e-22

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 96.62  E-value: 1.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGG------QNIKDVTEAA 405
Cdd:COG4161    2 SIQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 LRKTVSFVLQRAVLFSG-TIASNLRQgnAQAKLHELQRAANMAQASEFIER-----YNDSFdheveerSANFSGGQKQRL 479
Cdd:COG4161   80 LRQKVGMVFQQYNLWPHlTVMENLIE--APCKVLGLSKEQAREKAMKLLARlrltdKADRF-------PLHLSGGQQQRV 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 480 SIARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDT--TTFII------AEKIvsvinADTILVLDDGKLVAQGT 551
Cdd:COG4161  151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEII-RELSQTgiTQVIVthevefARKV-----ASQVVYMEKGRIIEQGD 224

                 ..
gi 492039060 552 HE 553
Cdd:COG4161  225 AS 226
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
334-515 1.60e-22

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 96.32  E-value: 1.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFV 413
Cdd:PRK10247   9 QLQNVGYLA--GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRAVLFSGTIASNL------RqgnaqaklhelQRAANMAQASEFIERYNDSfDHEVEERSANFSGGQKQRLSIARGLIA 487
Cdd:PRK10247  87 AQTPTLFGDTVYDNLifpwqiR-----------NQQPDPAIFLDDLERFALP-DTILTKNIAELSGGEKQRISLIRNLQF 154
                        170       180
                 ....*....|....*....|....*...
gi 492039060 488 KAPILILDDSTSALDAESEKKVQQALEH 515
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHR 182
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
350-563 2.91e-22

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 96.38  E-value: 2.91e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTvsfvlqRAVL-------FSG 422
Cdd:PRK13548  18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR------RAVLpqhsslsFPF 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 TI-------ASNLRQGNAQAKlhELQRAAnMAQA--SEFIERYNDSFdheveersanfSGGQKQRLSIARGLI------A 487
Cdd:PRK13548  92 TVeevvamgRAPHGLSRAEDD--ALVAAA-LAQVdlAHLAGRDYPQL-----------SGGEQQRVQLARVLAqlwepdG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 488 KAPILILDDSTSALDaesekkvqqaLEHELpdtTTFIIA-----EKIVSVI------N-----ADTILVLDDGKLVAQGT 551
Cdd:PRK13548 158 PPRWLLLDEPTSALD----------LAHQH---HVLRLArqlahERGLAVIvvlhdlNlaaryADRIVLLHQGRLVADGT 224
                        250
                 ....*....|....*
gi 492039060 552 HEELLKTSL---VYQ 563
Cdd:PRK13548 225 PAEVLTPETlrrVYG 239
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
333-564 5.36e-22

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 98.10  E-value: 5.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVteAALRKTVSF 412
Cdd:PRK09452  15 VELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHV--PAENRHVNT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSG-TIASNLRQGNAQAKL--HELQR----AANMAQASEFIERyndsfdheveeRSANFSGGQKQRLSIARGL 485
Cdd:PRK09452  91 VFQSYALFPHmTVFENVAFGLRMQKTpaAEITPrvmeALRMVQLEEFAQR-----------KPHQLSGGQQQRVAIARAV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 486 IAKAPILILDDSTSALDAESEKKVQQ---ALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEEllktslVY 562
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNelkALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE------IY 233

                 ..
gi 492039060 563 QE 564
Cdd:PRK09452 234 EE 235
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
348-555 1.41e-21

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


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 94.92  E-value: 1.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikdvteaalrktVSFVLQRAVLFSGTIASN 427
Cdd:cd03291   51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKEN 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 428 LRQGNAQAKlHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEK 507
Cdd:cd03291  118 IIFGVSYDE-YRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 492039060 508 KV-QQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEEL 555
Cdd:cd03291  197 EIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
345-556 1.44e-21

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: 93.89  E-value: 1.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDV-TEAALRKTVSFVLQRAVLFSG- 422
Cdd:COG0410   14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLpPHRIARLGIGYVPEGRRIFPSl 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 TIASNLRQGnAQAKLHELQRAANMAQASEFIERyndsfdheVEERSANF----SGGQKQRLSIARGLIAKAPILILDDST 498
Cdd:COG0410   94 TVEENLLLG-AYARRDRAEVRADLERVYELFPR--------LKERRRQRagtlSGGEQQMLAIGRALMSRPKLLLLDEPS 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 499 SALdaeSEKKVQQALE--HELPDT-TTFIIAEKIVSVI--NADTILVLDDGKLVAQGTHEELL 556
Cdd:COG0410  165 LGL---APLIVEEIFEiiRRLNREgVTILLVEQNARFAleIADRAYVLERGRIVLEGTAAELL 224
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
345-569 1.84e-21

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 93.93  E-value: 1.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTI 424
Cdd:PRK11231  13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGIT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 ASNL----RQ------GNAQAKLHEL-QRAANMAQASEFIERyndsfdheveeRSANFSGGQKQRLSIARGLIAKAPILI 493
Cdd:PRK11231  93 VRELvaygRSpwlslwGRLSAEDNARvNQAMEQTRINHLADR-----------RLTDLSGGQRQRAFLAMVLAQDTPVVL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 494 LDDSTSALDAESEKKVqQALEHELPDTTTFIIAekIVSVIN-----ADTILVLDDGKLVAQGTHEELLKTSLVyQEIFKT 568
Cdd:PRK11231 162 LDEPTTYLDINHQVEL-MRLMRELNTQGKTVVT--VLHDLNqasryCDHLVVLANGHVMAQGTPEEVMTPGLL-RTVFDV 237

                 .
gi 492039060 569 Q 569
Cdd:PRK11231 238 E 238
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
333-568 2.29e-21

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 93.61  E-value: 2.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:COG4604    2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQravlfSGTIASNLR-------------QGNAQAKLHELqraanMAQASEFIE------RYNDSfdheveersanFSG 473
Cdd:COG4604   80 LRQ-----ENHINSRLTvrelvafgrfpysKGRLTAEDREI-----IDEAIAYLDledladRYLDE-----------LSG 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 474 GQKQRLSIARGLIAKAPILILDDSTSALD---AESEKKVQQALEHELPDTttfiiaekIVSV---IN-----ADTILVLD 542
Cdd:COG4604  139 GQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkhSVQMMKLLRRLADELGKT--------VVIVlhdINfascyADHIVAMK 210
                        250       260
                 ....*....|....*....|....*.
gi 492039060 543 DGKLVAQGTHEELLkTSLVYQEIFKT 568
Cdd:COG4604  211 DGRVVAQGTPEEII-TPEVLSDIYDT 235
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
332-553 2.44e-21

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 93.16  E-value: 2.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGG------QNIKDVTEAA 405
Cdd:PRK11124   2 SIQLNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 LRKTVSFVLQRAVLFSG-TIASNLRQgnAQAKLHELQRAANMAQASEFIERYndsfdhEVEERSANF----SGGQKQRLS 480
Cdd:PRK11124  80 LRRNVGMVFQQYNLWPHlTVQQNLIE--APCRVLGLSKDQALARAEKLLERL------RLKPYADRFplhlSGGQQQRVA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 481 IARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDT--TTFI------IAEKIvsvinADTILVLDDGKLVAQGTH 552
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDPEITAQIVSII-RELAETgiTQVIvtheveVARKT-----ASRVVYMENGHIVEQGDA 225

                 .
gi 492039060 553 E 553
Cdd:PRK11124 226 S 226
cbiO PRK13650
energy-coupling factor transporter ATPase;
329-555 2.52e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 94.03  E-value: 2.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 329 LSGSVEFDHVSFTY-PDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALR 407
Cdd:PRK13650   1 MSNIIEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQRA-VLFSGT-----IASNLR-QGNAQAKLHE-LQRAANMAQASEFIERyndsfdheveeRSANFSGGQKQRL 479
Cdd:PRK13650  81 HKIGMVFQNPdNQFVGAtveddVAFGLEnKGIPHEEMKErVNEALELVGMQDFKER-----------EPARLSGGQKQRV 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 480 SIArGLIAKAP-ILILDDSTSALDAESEKKVQQALE--HELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK13650 150 AIA-GAVAMRPkIIILDEATSMLDPEGRLELIKTIKgiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPREL 227
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
333-557 4.37e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 93.61  E-value: 4.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDPT----LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA-ALR 407
Cdd:PRK13633   5 IKCKNVSYKYESNEESTeklaLDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwDIR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 408 KTVSFVLQR------AVLFSGTIA---SNL--RQGNAQAKLHELQRAANMAQasefierYNDSFDHEVeersanfSGGQK 476
Cdd:PRK13633  85 NKAGMVFQNpdnqivATIVEEDVAfgpENLgiPPEEIRERVDESLKKVGMYE-------YRRHAPHLL-------SGGQK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 477 QRLSIArGLIAKAP-ILILDDSTSALDAESEKKVQQALEhELPDT---TTFIIAEKIVSVINADTILVLDDGKLVAQGTH 552
Cdd:PRK13633 151 QRVAIA-GILAMRPeCIIFDEPTAMLDPSGRREVVNTIK-ELNKKygiTIILITHYMEEAVEADRIIVMDSGKVVMEGTP 228

                 ....*
gi 492039060 553 EELLK 557
Cdd:PRK13633 229 KEIFK 233
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
18-308 6.32e-21

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: 93.34  E-value: 6.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  18 VVCAIIAILVSAFSGLYQPKLleniQKALM----ANQKQAVLSDGIWLVVLGIIAI-----ISGIFNVYFAAKIAQGVVS 88
Cdd:cd18563    1 LILGFLLMLLGTALGLVPPYL----TKILIddvlIQLGPGGNTSLLLLLVLGLAGAyvlsaLLGILRGRLLARLGERITA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  89 DLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIF---------CIVIIPrfww 159
Cdd:cd18563   77 DLRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVlfslnwklaLLVLIP---- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 160 APVVmVALIFGFGayvlRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFS 239
Cdd:cd18563  153 VPLV-VWGSYFFW----KKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWA 227
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 240 AIMPAFQMIAYTVIALIVYL-----IGKNITahpsdIAVVSPFVNYvLTLLFT-IMIAGMTLMQFSRANISLGRI 308
Cdd:cd18563  228 TFFPLLTFLTSLGTLIVWYFggrqvLSGTMT-----LGTLVAFLSY-LGMFYGpLQWLSRLNNWITRALTSAERI 296
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
333-558 7.30e-21

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 94.40  E-value: 7.30e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikDVTEAALR-KTVS 411
Cdd:PRK11432   7 VVLKNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE---DVTHRSIQqRDIC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSG-TIASNLRQGNAQAKLHELQRAANMAQASE------FIERYNDsfdheveersaNFSGGQKQRLSIARG 484
Cdd:PRK11432  82 MVFQSYALFPHmSLGENVGYGLKMLGVPKEERKQRVKEALElvdlagFEDRYVD-----------QISGGQQQRVALARA 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 485 LIAKAPILILDDSTSALDA---ESEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDAnlrRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
cbiO PRK13642
energy-coupling factor transporter ATPase;
333-559 1.61e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 91.69  E-value: 1.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTY-PDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVS 411
Cdd:PRK13642   5 LEVENLVFKYeKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRA--VLFSGTIASNLRQGNAQaklHELQRAANMAQASEFIERYNdSFDHEVEErSANFSGGQKQRLSIArGLIAKA 489
Cdd:PRK13642  85 MVFQNPdnQFVGATVEDDVAFGMEN---QGIPREEMIKRVDEALLAVN-MLDFKTRE-PARLSGGQKQRVAVA-GIIALR 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 490 P-ILILDDSTSALDAESEKKVQQALeHELPDT---TTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTS 559
Cdd:PRK13642 159 PeIIILDESTSMLDPTGRQEIMRVI-HEIKEKyqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
333-556 2.06e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 91.45  E-value: 2.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI----KDVTEaaLRK 408
Cdd:PRK13636   6 LKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysrKGLMK--LRE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 409 TVSFVLQRA--VLFSGTIASNLRQG--NAQAKLHELQRAANMAQASEFIERYNDSFDHEVeersanfSGGQKQRLSIARG 484
Cdd:PRK13636  83 SVGMVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCL-------SFGQKKRVAIAGV 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQALEHELPDT-TTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELgLTIIIATHDIDIVPlyCDNVFVMKEGRVILQGNPKEVF 230
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
330-570 2.29e-20

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 90.53  E-value: 2.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 330 SGSVEFDHVSFTYPDGDDPT--------------------LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKG 389
Cdd:COG1134    2 SSMIEVENVSKSYRLYHEPSrslkelllrrrrtrreefwaLKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 390 KVKIGGqnikdvteaalrkTVSFVLQRAVLF----SGtiasnlRQgNA--QAKLHELQRA---ANMAQASEF--IERYnd 458
Cdd:COG1134   82 RVEVNG-------------RVSALLELGAGFhpelTG------RE-NIylNGRLLGLSRKeidEKFDEIVEFaeLGDF-- 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 459 sFDHEVEersaNFSGGQKQRL--SIArglIAKAP-ILILDDSTSALDAESEKKVQQALEHELPDTTTFIiaekIVS---- 531
Cdd:COG1134  140 -IDQPVK----TYSSGMRARLafAVA---TAVDPdILLVDEVLAVGDAAFQKKCLARIRELRESGRTVI----FVShsmg 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 492039060 532 VIN--ADTILVLDDGKLVAQGTHEELLKtslVYQEIFKTQK 570
Cdd:COG1134  208 AVRrlCDRAIWLEKGRLVMDGDPEEVIA---AYEALLAGRE 245
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
345-557 2.88e-20

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: 89.12  E-value: 2.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARL--YDPTKGKVKIGGQNIKD--VTEAALRK-TVSFvlQRAVL 419
Cdd:cd03217   11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDlpPEERARLGiFLAF--QYPPE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 420 FSGTiasnlrqgnaqaKLHELQRAANMaqasefieryndsfdheveersaNFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:cd03217   89 IPGV------------KNADFLRYVNE-----------------------GFSGGEKKRNEILQLLLLEPDLAILDEPDS 133
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 500 ALDAESEKKVQQALEHELPDTTTFIIA---EKIVSVINADTILVLDDGKLVAQGTHEELLK 557
Cdd:cd03217  134 GLDIDALRLVAEVINKLREEGKSVLIIthyQRLLDYIKPDRVHVLYDGRIVKSGDKELALE 194
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
333-524 3.11e-20

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: 87.98  E-value: 3.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIggqnikdvteaALRKTVSF 412
Cdd:cd03223    1 IELENLSLATPDGR-VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM-----------PEGEDLLF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTiasnLRQgnaqAKLHELQRAanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03223   69 LPQRPYLPLGT----LRE----QLIYPWDDV---------------------------LSGGEQQRLAFARLLLHKPKFV 113
                        170       180       190
                 ....*....|....*....|....*....|..
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELpdtTTFI 524
Cdd:cd03223  114 FLDEATSALDEESEDRLYQLLKELG---ITVI 142
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
333-549 3.92e-20

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: 87.48  E-value: 3.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGddPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ--NIKDVTEaALRKTV 410
Cdd:cd03216    1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRD-ARRAGI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQravlfsgtiasnlrqgnaqaklhelqraanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKAP 490
Cdd:cd03216   78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 491 ILILDDSTSALDAESEKKVQQALeHELPDT-TTFI-IAEKIVSVIN-ADTILVLDDGKLVAQ 549
Cdd:cd03216  103 LLILDEPTAALTPAEVERLFKVI-RRLRAQgVAVIfISHRLDEVFEiADRVTVLRDGRVVGT 163
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
18-308 3.93e-20

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


Pssm-ID: 349989 [Multi-domain]  Cd Length: 293  Bit Score: 90.99  E-value: 3.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  18 VVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTYA 96
Cdd:cd18545    2 LLLALLLMLLSTAASLAGPYLIKIaIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  97 KIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVL 176
Cdd:cd18545   82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 177 RQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIALI 256
Cdd:cd18545  162 RRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTALV 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 492039060 257 VYLIGKNITAHPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18545  242 YWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
333-547 4.40e-20

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 93.59  E-value: 4.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIgGQNIKdvteaalrktVSF 412
Cdd:COG0488  316 LELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IGY 382
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQ-RAVLFSG-TIASNLRQGNAQAKlhelqraanMAQASEFIERYNDSFDhEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:COG0488  383 FDQhQEELDPDkTVLDELRDGAPGGT---------EQEVRGYLGRFLFSGD-DAFKPVGVLSGGEKARLALAKLLLSPPN 452
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 491 ILILDDSTSALDAESekkvQQALEHELPDTT-TFIiaekIVS----VIN--ADTILVLDDGKLV 547
Cdd:COG0488  453 VLLLDEPTNHLDIET----LEALEEALDDFPgTVL----LVShdryFLDrvATRILEFEDGGVR 508
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
343-555 4.85e-20

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 94.98  E-value: 4.85e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   343 PDGDD------------PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikdvteaalrktV 410
Cdd:TIGR01271  423 PNGDDglffsnfslyvtPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------I 489
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   411 SFVLQRAVLFSGTIASNLRQGNAQAKlHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAP 490
Cdd:TIGR01271  490 SFSPQTSWIMPGTIKDNIIFGLSYDE-YRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDAD 568
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060   491 ILILDDSTSALDAESEKKV-QQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEEL 555
Cdd:TIGR01271  569 LYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSEL 634
PTZ00243 PTZ00243
ABC transporter; Provisional
350-560 5.16e-20

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 94.85  E-value: 5.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVkiggqnikdvteaALRKTVSFVLQRAVLFSGTIASNL- 428
Cdd:PTZ00243  676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNIl 742
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  429 --RQGNAqAKLHELQRA----ANMAQASEFIERyndsfdhEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:PTZ00243  743 ffDEEDA-ARLADAVRVsqleADLAQLGGGLET-------EIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060  503 AE-SEKKVQQALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKTSL 560
Cdd:PTZ00243  815 AHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTSL 873
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
350-555 5.21e-20

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 91.18  E-value: 5.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD---VTEAALRKTVSFVLQRAVlfsgtiAS 426
Cdd:PRK11308  31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKadpEAQKLLRQKIQIVFQNPY------GS 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 -NLRQGNAQ---------AKLHELQRAAN----MAQA---SEFIERYndsfDHEveersanFSGGQKQRLSIARGLIAKA 489
Cdd:PRK11308 105 lNPRKKVGQileepllinTSLSAAERREKalamMAKVglrPEHYDRY----PHM-------FSGGQRQRIAIARALMLDP 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 490 PILILDDSTSALDAESEKKVQQA---LEHELPDTTTFI-----IAEKIvsvinADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK11308 174 DVVVADEPVSALDVSVQAQVLNLmmdLQQELGLSYVFIshdlsVVEHI-----ADEVMVMYLGRCVEKGTKEQI 242
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
348-544 6.05e-20

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: 88.54  E-value: 6.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKV----KIGGQNIKDVTEAALRKTVSFVLQRAVLFSGT 423
Cdd:cd03290   15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLLNAT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 424 IASNLRQGNAQAKlhelQRAANMAQASEF---IERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:cd03290   95 VEENITFGSPFNK----QRYKAVTDACSLqpdIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSA 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 492039060 501 LDAE-SEKKVQQALEHELPDT--TTFIIAEKIVSVINADTILVLDDG 544
Cdd:cd03290  171 LDIHlSDHLMQEGILKFLQDDkrTLVLVTHKLQYLPHADWIIAMKDG 217
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
334-513 6.53e-20

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 89.54  E-value: 6.53e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikDVTEAALRKTVs 411
Cdd:COG4525    5 TVRHVSVRYPGGGQPQpaLQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGADRGV- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 fVLQRAVLFSG-TIASNLRQGnaqAKLHELQRAANMAQASEFIER-----YNDSFDHEVeersanfSGGQKQRLSIARGL 485
Cdd:COG4525   81 -VFQKDALLPWlNVLDNVAFG---LRLRGVPKAERRARAEELLALvgladFARRRIWQL-------SGGMRQRVGIARAL 149
                        170       180
                 ....*....|....*....|....*...
gi 492039060 486 IAKAPILILDDSTSALDAESEKKVQQAL 513
Cdd:COG4525  150 AADPRFLLMDEPFGALDALTREQMQELL 177
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
18-308 9.77e-20

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: 89.80  E-value: 9.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  18 VVCAIIAILVSAFSGLYQPKLLENIQKALMANQkqavlSDGIWLVVLGIIAIISGIFNV---YFAAKIAQGVVSDLREDT 94
Cdd:cd18551    1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGG-----SSGGLLALLVALFLLQAVLSAlssYLLGRTGERVVLDLRRRL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  95 YAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAY 174
Cdd:cd18551   76 WRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 175 VLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIA 254
Cdd:cd18551  156 LGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALL 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492039060 255 LIVYLIGKNITAHPSDIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18551  236 VVLGVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
323-557 1.39e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 90.28  E-value: 1.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 323 SGSVAPLSGS-----VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQN 397
Cdd:PRK13536  27 SEAKASIPGSmstvaIDLAGVSKSY--GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 398 IKDVTEAAlRKTVSFVLQRAVL-FSGTIASNLRQGNAQAKLHELQRAANMAQASEFIEryndsFDHEVEERSANFSGGQK 476
Cdd:PRK13536 105 VPARARLA-RARIGVVPQFDNLdLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFAR-----LESKADARVSDLSGGMK 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 477 QRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEE 554
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAErlCDRLCVLEAGRKIAEGRPHA 258

                 ...
gi 492039060 555 LLK 557
Cdd:PRK13536 259 LID 261
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
350-544 1.77e-19

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 87.52  E-value: 1.77e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIkdvTEAALRKTVsfVLQRAVLFSGTIAsnlR 429
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI---TEPGPDRMV--VFQNYSLLPWLTV---R 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  430 QGNAQAkLHELQRAANMAQASEFIERYND--SFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEK 507
Cdd:TIGR01184  73 ENIALA-VDRVLPDLSKSERRAIVEEHIAlvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 492039060  508 KVQQAL-----EHELpdtTTFIIAEKI-VSVINADTILVLDDG 544
Cdd:TIGR01184 152 NLQEELmqiweEHRV---TVLMVTHDVdEALLLSDRVVMLTNG 191
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
21-292 1.77e-19

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: 89.08  E-value: 1.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  21 AIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLsDGIWLVVLGIIAI--ISGIFNVYFAAKIAQGVVSDLREDTYAKI 98
Cdd:cd18576    1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGDTASL-NQIALLLLGLFLLqaVFSFFRIYLFARVGERVVADLRKDLYRHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  99 QTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPR-----FWWAPVVMVALIFgFGA 173
Cdd:cd18576   80 QRLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKltllmLATVPVVVLVAVL-FGR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 174 YvLRQMNslfTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVI 253
Cdd:cd18576  159 R-IRKLS---KKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAI 234
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 492039060 254 ALIVYLIGKNITAHPSDIAVVSPFvnyvltLLFTIMIAG 292
Cdd:cd18576  235 VAVLWYGGRLVLAGELTAGDLVAF------LLYTLFIAG 267
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
336-513 2.11e-19

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 87.56  E-value: 2.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYPDGDDPT--LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAA---LR-KT 409
Cdd:PRK11629   9 DNLCKRYQEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRnQK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRAVL---FSG--TIASNLRQGN---AQAKlhelQRAANMAQASefieryndSFDHEVEERSANFSGGQKQRLSI 481
Cdd:PRK11629  89 LGFIYQFHHLlpdFTAleNVAMPLLIGKkkpAEIN----SRALEMLAAV--------GLEHRANHRPSELSGGERQRVAI 156
                        170       180       190
                 ....*....|....*....|....*....|..
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQAL 513
Cdd:PRK11629 157 ARALVNNPRLVLADEPTGNLDARNADSIFQLL 188
cbiO PRK13649
energy-coupling factor transporter ATPase;
332-565 2.72e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 88.26  E-value: 2.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYPDG---DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI------KDVT 402
Cdd:PRK13649   2 GINLQNVSYTYQAGtpfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsknKDIK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 403 EaaLRKTVSFVLQ--RAVLFSGTIASNLRQG--NAQAKLHELQRAANMAQASEFIeryndsfDHEVEERSA-NFSGGQKQ 477
Cdd:PRK13649  82 Q--IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAREKLALVGI-------SESLFEKNPfELSGGQMR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 478 RLSIArGLIAKAP-ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIV-SVIN-ADTILVLDDGKLVAQGthee 554
Cdd:PRK13649 153 RVAIA-GILAMEPkILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMdDVANyADFVYVLEKGKLVLSG---- 227
                        250
                 ....*....|.
gi 492039060 555 llKTSLVYQEI 565
Cdd:PRK13649 228 --KPKDIFQDV 236
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
350-556 4.18e-19

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 87.11  E-value: 4.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIkDVTEA---------ALRKTVSFVLQRAVLF 420
Cdd:PRK11264  19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI-DTARSlsqqkglirQLRQHVGFVFQNFNLF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SG-TIASNLRQGNAQAKlhELQRAANMAQASEFIERYNDSFDHEVEERsaNFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:PRK11264  98 PHrTVLENIIEGPVIVK--GEPKEEATARARELLAKVGLAGKETSYPR--RLSGGQQQRVAIARALAMRPEVILFDEPTS 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 500 ALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARdvADRAIFMDQGRIVEQGPAKALF 232
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
338-558 6.43e-19

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 89.13  E-value: 6.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 338 VSFtypdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRA 417
Cdd:PRK09536  11 VEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 418 VL-FSGTIASNLRQGNA----------QAKLHELQRAANMAQASEFIERYNDSfdheveersanFSGGQKQRLSIARGLI 486
Cdd:PRK09536  87 SLsFEFDVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTGVAQFADRPVTS-----------LSGGERQRVLLARALA 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 487 AKAPILILDDSTSALDAesEKKVQQ-ALEHELPDTTTFIIAEkiVSVIN-----ADTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK09536 156 QATPVLLLDEPTASLDI--NHQVRTlELVRRLVDDGKTAVAA--IHDLDlaaryCDELVLLADGRVRAAGPPADVLTA 229
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
350-550 9.01e-19

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


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 85.28  E-value: 9.01e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikdVTeAALRKTVSFVLQ----RAVLFSGTIa 425
Cdd:cd03220   38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR----VS-SLLGLGGGFNPEltgrENIYLNGRL- 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 426 SNLRQGNAQAKLHELQraanmaqasEFIErYNDSFDHEVEersaNFSGGQKQRLSIARGLIAKAPILILDDSTSALDAES 505
Cdd:cd03220  112 LGLSRKEIDEKIDEII---------EFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 492039060 506 EKKVQQALEHELPDTTTFIIAEKIVSVI--NADTILVLDDGKLVAQG 550
Cdd:cd03220  178 QEKCQRRLRELLKQGKTVILVSHDPSSIkrLCDRALVLEKGKIRFDG 224
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
344-555 1.57e-18

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 87.58  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 344 DGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVteAALRKTVSFVLQRAVLFSG- 422
Cdd:PRK11607  30 DGQ-HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFPHm 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 TIASNLRQGNAQAKLHE---LQRAANM---AQASEFIERyndsfdheveeRSANFSGGQKQRLSIARGLIAKAPILILDD 496
Cdd:PRK11607 107 TVEQNIAFGLKQDKLPKaeiASRVNEMlglVHMQEFAKR-----------KPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 497 STSALDaeseKKVQQALEHELPD-------TTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK11607 176 PMGALD----KKLRDRMQLEVVDilervgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
333-545 2.42e-18

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 81.73  E-value: 2.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIgGQNIKdvteaalrktVSF 412
Cdd:cd03221    1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW-GSTVK----------IGY 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQravlfsgtiasnlrqgnaqaklhelqraanmaqasefieryndsfdheveersanFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03221   68 FEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 493 ILDDSTSALDAESekkvQQALEHELPDTT-TFIiaekIVS----VIN--ADTILVLDDGK 545
Cdd:cd03221   93 LLDEPTNHLDLES----IEALEEALKEYPgTVI----LVShdryFLDqvATKIIELEDGK 144
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
332-558 2.99e-18

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 85.55  E-value: 2.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVT--------- 402
Cdd:COG4152    1 MLELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDrrrigylpe 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 403 EAALRKTVSfVLQRAVLFsgtiasnlrqgnaqAKLHELQRAANMAQASEFIERYN--DSFDHEVEErsanFSGGQKQRLS 480
Cdd:COG4152   79 ERGLYPKMK-VGEQLVYL--------------ARLKGLSKAEAKRRADEWLERLGlgDRANKKVEE----LSKGNQQKVQ 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 481 IARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDTTTFII--------AEKIvsvinADTILVLDDGKLVAQGTH 552
Cdd:COG4152  140 LIAALLHDPELLILDEPFSGLDPVNVELLKDVI-RELAAKGTTVIfsshqmelVEEL-----CDRIVIINKGRKVLSGSV 213

                 ....*.
gi 492039060 553 EELLKT 558
Cdd:COG4152  214 DEIRRQ 219
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
345-507 3.24e-18

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 83.38  E-value: 3.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIkdvTEAALRKTVSFVLQR-AVLFSGT 423
Cdd:PRK13539  13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI---DDPDVAEACHYLGHRnAMKPALT 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 424 IASNLR-----QGNAQAKLHElqraanmaqASEFIERyndsfdHEVEERSANF-SGGQKQRLSIARGLIAKAPILILDDS 497
Cdd:PRK13539  90 VAENLEfwaafLGGEELDIAA---------ALEAVGL------APLAHLPFGYlSAGQKRRVALARLLVSNRPIWILDEP 154
                        170
                 ....*....|
gi 492039060 498 TSALDAESEK 507
Cdd:PRK13539 155 TAALDAAAVA 164
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
348-555 3.93e-18

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 87.38  E-value: 3.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ--NIKDVTEA-----AL----RKTVSFVLQR 416
Cdd:COG1129  266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAiragiAYvpedRKGEGLVLDL 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 417 AVLFSGTIAsNLRQgnaQAKLHELQRAANMAQASEFIERYN---DSFDHEVeersANFSGGQKQRLSIARGLIAKAPILI 493
Cdd:COG1129  346 SIRENITLA-SLDR---LSRGGLLDRRRERALAEEYIKRLRiktPSPEQPV----GNLSGGNQQKVVLAKWLATDPKVLI 417
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 494 LDDSTSALD--AESEkkVQQALeHELpdtttfiiAEKIVSVI-----------NADTILVLDDGKLVAQGTHEEL 555
Cdd:COG1129  418 LDEPTRGIDvgAKAE--IYRLI-REL--------AAEGKAVIvisselpellgLSDRILVMREGRIVGELDREEA 481
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
350-547 3.99e-18

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 84.74  E-value: 3.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---ALRKTVSFVLQRAV-------L 419
Cdd:PRK10419  28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAqrkAFRRDIQMVFQDSIsavnprkT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 420 FSGTIASNLRQgnaqakLHELQRAANMAQASEFIeRYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:PRK10419 108 VREIIREPLRH------LLSLDKAERLARASEML-RAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVS 180
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 500 ALDAESEKKVQQ---ALEHELPDTTTFI-----IAEKIvsvinADTILVLDDGKLV 547
Cdd:PRK10419 181 NLDLVLQAGVIRllkKLQQQFGTACLFIthdlrLVERF-----CQRVMVMDNGQIV 231
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
350-555 4.85e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 85.29  E-value: 4.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGG------------------QNIKDVTEaaLRKTVS 411
Cdd:PRK13631  42 LNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhelitnpysKKIKNFKE--LRRRVS 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQ--RAVLFSGTIASNLRQGN---AQAKLHELQRAA----NMAQASEFIERynDSFDheveersanFSGGQKQRLSIA 482
Cdd:PRK13631 120 MVFQfpEYQLFKDTIEKDIMFGPvalGVKKSEAKKLAKfylnKMGLDDSYLER--SPFG---------LSGGQKRRVAIA 188
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 483 rGLIAKAP-ILILDDSTSALDAESEKK-VQQALEHELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK13631 189 -GILAIQPeILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTPYEI 263
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
333-555 4.97e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 84.47  E-value: 4.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSF 412
Cdd:PRK13652   4 IETRDLCYSY-SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRA--VLFSGTIASNLRQGNAQAKLHELQRAANMAQASEF--IERYNDSFDHeveersaNFSGGQKQRLSIArGLIAK 488
Cdd:PRK13652  83 VFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMlgLEELRDRVPH-------HLSGGEKKRVAIA-GVIAM 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 489 AP-ILILDDSTSALDAESEKKVQQALeHELPDT--TTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK13652 155 EPqVLVLDEPTAGLDPQGVKELIDFL-NDLPETygMTVIFSTHQLDLVPemADYIYVMDKGRIVAYGTVEEI 225
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
21-308 5.34e-18

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: 84.53  E-value: 5.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  21 AIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLSDgiWLVVLGIIAIISGIFNV---YFAAKIAQGVVSDLREDTYAK 97
Cdd:cd18557    1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNE--LALILLAIYLLQSVFTFvryYLFNIAGERIVARLRRDLFSS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  98 IQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVLR 177
Cdd:cd18557   79 LLRQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 178 QMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIALIV 257
Cdd:cd18557  159 YIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 492039060 258 YLIGKNITA-HPSDIAVVSpFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18557  239 WYGGYLVLSgQLTVGELTS-FILYTIMVASSVGGLSSLLADIMKALGASERV 289
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
345-525 7.15e-18

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 83.68  E-value: 7.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD--PT---KGKVKIGGQNI--KDVTEAALRKTVSFVLQRA 417
Cdd:PRK14243  21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKP 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 418 VLFSGTIASNLRQG----NAQAKLHEL-QRAanMAQASEFierynDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:PRK14243 101 NPFPKSIYDNIAYGarinGYKGDMDELvERS--LRQAALW-----DEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
                        170       180       190
                 ....*....|....*....|....*....|...
gi 492039060 493 ILDDSTSALDAESEKKVQQaLEHELPDTTTFII 525
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEE-LMHELKEQYTIII 205
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
345-567 8.45e-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: 86.39  E-value: 8.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARL--YDPTKGKV-----------------KIGGQ--------- 396
Cdd:TIGR03269  11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpsKVGEPcpvcggtle 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  397 -------NIKDVTEAALRKTVSFVLQRAVLFSG--TIASNLRQGnaqakLHELQRAANMA--QASEFIERYNdsFDHEVE 465
Cdd:TIGR03269  91 peevdfwNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVLEA-----LEEIGYEGKEAvgRAVDLIEMVQ--LSHRIT 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  466 ERSANFSGGQKQRLSIARGLiAKAPILIL-DDSTSALDAESEKKVQQALEHELPDT-TTFIIAEKIVSVIN--ADTILVL 541
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQL-AKEPFLFLaDEPTGTLDPQTAKLVHNALEEAVKASgISMVLTSHWPEVIEdlSDKAIWL 242
                         250       260
                  ....*....|....*....|....*.
gi 492039060  542 DDGKLVAQGTHEELLKtslVYQEIFK 567
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVA---VFMEGVS 265
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
345-556 9.01e-18

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 83.48  E-value: 9.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA-------------ALRKTVS 411
Cdd:PRK10619  16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrLLRTRLT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQRAVLFSG-TIASNLRQGNAQAklhelqRAANMAQASEFIERYNDSFDheVEERS-----ANFSGGQKQRLSIARGL 485
Cdd:PRK10619  96 MVFQHFNLWSHmTVLENVMEAPIQV------LGLSKQEARERAVKYLAKVG--IDERAqgkypVHLSGGQQQRVSIARAL 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 486 IAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARhvSSHVIFLHQGKIEEEGAPEQLF 240
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
350-556 9.13e-18

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 85.47  E-value: 9.13e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL----RKTVSFVLQR-AVLFSGTI 424
Cdd:PRK10070  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSfALMPHMTV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 ASNLRQGNAQAKL--HELQRAANMAQASEFIERYNDSFDHEVeersanfSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:PRK10070 124 LDNTAFGMELAGInaEERREKALDALRQVGLENYAHSYPDEL-------SGGMRQRVGLARALAINPDILLMDEAFSALD 196
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 503 AESEKKVQQ---ALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK10070 197 PLIRTEMQDelvKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
21-257 1.35e-17

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


Pssm-ID: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 83.35  E-value: 1.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  21 AIIAILVSAFSGLYQPKLLENIQKALMANQKQAvlsDGIWLVVLGIIA--IISGIFN---VYFAAKIAQGVVSDLREDTY 95
Cdd:cd18778    4 TLLCALLSTLLGLVPPWLIRELVDLVTIGSKSL---GLLLGLALLLLGayLLRALLNflrIYLNHVAEQKVVADLRSDLY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  96 AKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLfmqmlrLPILIVGSFIFCIVIIPRFW--W-------APVVMVA 166
Cdd:cd18778   81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADG------IPQGITNVLTLVGVAIILFSinPklalltlIPIPFLA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 167 LI-FGFGAYVLRqmnsLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAF 245
Cdd:cd18778  155 LGaWLYSKKVRP----RYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLM 230
                        250
                 ....*....|....
gi 492039060 246 QMIAY--TVIALIV 257
Cdd:cd18778  231 EFLTSlgTVLVLGF 244
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
350-563 1.48e-17

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 82.21  E-value: 1.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD--VTEAAlRKTVSFVLQRAVLFSG-TIAS 426
Cdd:cd03218   16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlpMHKRA-RLGIGYLPQEASIFRKlTVEE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 NLRqgnAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESE 506
Cdd:cd03218   95 NIL---AVLEIRGLSKKEREEKLEELLEEFH--ITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAV 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 507 KKVQQaLEHELPDTTTFII-----AEKIVSVInaDTILVLDDGKLVAQGTHEELLKTSLVYQ 563
Cdd:cd03218  170 QDIQK-IIKILKDRGIGVLitdhnVRETLSIT--DRAYIIYEGKVLAEGTPEEIAANELVRK 228
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
348-550 1.53e-17

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: 82.00  E-value: 1.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGqNIKDVTEAALRKTVSFVL-QRAvlfsgTIAS 426
Cdd:cd03267   35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVPWKRRKKFLRRIGVVFgQKT-----QLWW 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 NLRQGNAQAKLHELQRAANmAQASEFIERYNDSFD--HEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAE 504
Cdd:cd03267  109 DLPVIDSFYLLAAIYDLPP-ARFKKRLDELSELLDleELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 492039060 505 SEKKVQQALEHELPDT-TTFIIAEKIVSVIN--ADTILVLDDGKLVAQG 550
Cdd:cd03267  188 AQENIRNFLKEYNRERgTTVLLTSHYMKDIEalARRVLVIDKGRLLYDG 236
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
345-555 1.54e-17

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: 81.80  E-value: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI-KDVTEAALRKTVSFVLQRAVLFSG- 422
Cdd:TIGR03410  11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDItKLPPHERARAGIAYVPQGREIFPRl 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  423 TIASNLRQGnaqaklhelqrAANMAQASEFI-ERYNDSFD--HEVEERSA-NFSGGQKQRLSIARGLIAKAPILILDDST 498
Cdd:TIGR03410  91 TVEENLLTG-----------LAALPRRSRKIpDEIYELFPvlKEMLGRRGgDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060  499 SALDAESEKKVQQALehelpdttTFIIAEKIVSVI-----------NADTILVLDDGKLVAQGTHEEL 555
Cdd:TIGR03410 160 EGIQPSIIKDIGRVI--------RRLRAEGGMAILlveqyldfareLADRYYVMERGRVVASGAGDEL 219
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
17-300 1.70e-17

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: 83.27  E-value: 1.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  17 DVVCAIIAilvsAFSGLYQPKLLENI-QKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTY 95
Cdd:cd18549    7 DLFCAVLI----AALDLVFPLIVRYIiDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  96 AKIQTFSFG---NIKkfsAGSLTTRLINDMNQVMNMMMqlfmqmlRLP-------ILIVGSFIFCIVIIPRFWWAPVVMV 165
Cdd:cd18549   83 EHLQKLSFSffdNNK---TGQLMSRITNDLFDISELAH-------HGPedlfisiITIIGSFIILLTINVPLTLIVFALL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 166 ALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQL----NDYNIVIGyWFSAI 241
Cdd:cd18549  153 PLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRFleskKKAYKAMA-YFFSG 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 242 MPAF-QMIAYTVIALIVYLIGKN-ITAhpSDIAVvspFVNYVLTLLFTImiagMTLMQFSR 300
Cdd:cd18549  232 MNFFtNLLNLVVLVAGGYFIIKGeITL--GDLVA---FLLYVNVFIKPI----RRLVNFTE 283
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
337-556 2.02e-17

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: 85.51  E-value: 2.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 337 HVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP----TKGKVKIGGQNIKDVTEAALRK---- 408
Cdd:COG4172   13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLGLSERELRRirgn 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 409 TVSFVLQRAV-----LFS-GT-IASNLRqgnaqakLHE-LQRAANMAQASEFIERYN--------DSFDHEveersanFS 472
Cdd:COG4172   93 RIAMIFQEPMtslnpLHTiGKqIAEVLR-------LHRgLSGAAARARALELLERVGipdperrlDAYPHQ-------LS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 473 GGQKQRLSIARGLIAKAPILILDDSTSALDAesekKVQ-QALE-----------------HELPdtttfiiaekIVSVIn 534
Cdd:COG4172  159 GGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaQILDllkdlqrelgmalllitHDLG----------VVRRF- 223
                        250       260
                 ....*....|....*....|..
gi 492039060 535 ADTILVLDDGKLVAQGTHEELL 556
Cdd:COG4172  224 ADRVAVMRQGEIVEQGPTAELF 245
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
333-550 2.57e-17

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: 80.79  E-value: 2.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGqniKDVTEAALRKTVSF 412
Cdd:cd03269    1 LEVENVTKRF--GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG---KPLDIAARNRIGYL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 413 VLQRAVLFSGTIASNLRQgnaQAKLHELQRAANMAQASEFIERYNDSfDHEvEERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:cd03269   76 PEERGLYPKMKVIDQLVY---LAQLKGLKKEEARRRIDEWLERLELS-EYA-NKRVEELSKGNQQKVQFIAAVIHDPELL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 493 ILDDSTSALDAESEKKVQQALEhELPDTTTFII--------AEKIvsvinADTILVLDDGKLVAQG 550
Cdd:cd03269  151 ILDEPFSGLDPVNVELLKDVIR-ELARAGKTVIlsthqmelVEEL-----CDRVLLLNKGRAVLYG 210
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
352-556 2.88e-17

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: 83.61  E-value: 2.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 352 DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDvTEAAL-----RKTVSFVLQRAVLFSG-TIA 425
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQD-SARGIflpphRRRIGYVFQEARLFPHlSVR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 426 SNLRQGNAQAKLHElqRAANMAQASEF--IEryndsfdHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDA 503
Cdd:COG4148   96 GNLLYGRKRAPRAE--RRISFDEVVELlgIG-------HLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 504 ES--E-----KKVQQalEHELPdtttfIIaekIVS-----VIN-ADTILVLDDGKLVAQGTHEELL 556
Cdd:COG4148  167 ARkaEilpylERLRD--ELDIP-----IL---YVShsldeVARlADHVVLLEQGRVVASGPLAEVL 222
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
11-318 3.06e-17

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: 82.88  E-value: 3.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  11 LKRYKKDVVCAIIAILVSAFSGLYQP-------KLLENIQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIA 83
Cdd:cd18578    1 LKLNKPEWPLLLLGLIGAIIAGAVFPvfailfsKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  84 QGVVSDLREDTYAKI--QTFSFGNIKKFSAGSLTTRLINDmnqvmnMMMQLFMQMLRLPILI--VGSFIFCIVIIPRFWW 159
Cdd:cd18578   81 ERLTRRLRKLAFRAIlrQDIAWFDDPENSTGALTSRLSTD------ASDVRGLVGDRLGLILqaIVTLVAGLIIAFVYGW 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 160 --APVVMVALIFGFGAYVLRQMnsLFTKFQEMMDRI----SNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIv 233
Cdd:cd18578  155 klALVGLATVPLLLLAGYLRMR--LLSGFEEKNKKAyeesSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGL- 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 234 IGYWFSAIMPAF-QMIAYTVIALIVYLIGKNITAHPSDIAVVspFVNYVLtLLFTIMIAGMTLM---QFSRANISLGRIR 309
Cdd:cd18578  232 RRALISGLGFGLsQSLTFFAYALAFWYGGRLVANGEYTFEQF--FIVFMA-LIFGAQSAGQAFSfapDIAKAKAAAARIF 308

                 ....*....
gi 492039060 310 EVLETEPDV 318
Cdd:cd18578  309 RLLDRKPEI 317
cbiO PRK13646
energy-coupling factor transporter ATPase;
332-557 3.42e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 82.13  E-value: 3.42e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYPDG---DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI----KDVTEA 404
Cdd:PRK13646   2 TIRFDNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 405 ALRKTVSFVLQ--RAVLFSGTIASNLRQGNAQAKLhELQRAANMAqaseFIERYNDSFDHEVEERSA-NFSGGQKQRLSI 481
Cdd:PRK13646  82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKM-NLDEVKNYA----HRLLMDLGFSRDVMSQSPfQMSGGQMRKIAI 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQALEH-ELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELLK 557
Cdd:PRK13646 157 VSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENKTIILVSHDMNEVAryADEVIVMKEGSIVSQTSPKELFK 235
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
349-555 3.99e-17

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 82.83  E-value: 3.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 349 TLK---DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---ALRKTVSFVLQR--AVL- 419
Cdd:PRK15079  33 TLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDplASLn 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 420 ----FSGTIASNLRQGNAQAKLHEL-QRAANMAQA----SEFIERYndsfDHEveersanFSGGQKQRLSIARGLIAKAP 490
Cdd:PRK15079 113 prmtIGEIIAEPLRTYHPKLSRQEVkDRVKAMMLKvgllPNLINRY----PHE-------FSGGQCQRIGIARALILEPK 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 491 ILILDDSTSALDAESEKKV---QQALEHELPDTTTFIIAEkiVSVIN--ADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK15079 182 LIICDEPVSALDVSIQAQVvnlLQQLQREMGLSLIFIAHD--LAVVKhiSDRVLVMYLGHAVELGTYDEV 249
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
324-560 4.62e-17

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 82.16  E-value: 4.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 324 GSVAPLsgsvEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTE 403
Cdd:PRK13537   3 MSVAPI----DFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 404 AAlRKTVSFVLQRAVL---FsgTIASNLRQGNAQAKLHELQRAANMAQASEFiERYNDSFDHEVEErsanFSGGQKQRLS 480
Cdd:PRK13537  77 HA-RQRVGVVPQFDNLdpdF--TVRENLLVFGRYFGLSAAAARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 481 IARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFII-------AEKIvsvinADTILVLDDGKLVAQGTHE 553
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGRKIAEGAPH 223

                 ....*..
gi 492039060 554 ELLKTSL 560
Cdd:PRK13537 224 ALIESEI 230
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
138-546 4.73e-17

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 84.25  E-value: 4.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 138 RLP------ILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQG-------- 203
Cdd:PRK10522 124 RLPelvqgiILTLGSAAYLAWLSPKMLLVTAIWMAVTIWGGFVLVARVYKHMATLRETEDKLYNDYQTVLEGrkeltlnr 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 204 VRVVKSFNQGPQE-IKKFDQTSDQLNDYNIVIGYWfSAIMpafqMIAytVIALIVYLIGKNITAhpsDIAVVSpfvNYVL 282
Cdd:PRK10522 204 ERAEYVFENEYEPdAQEYRHHIIRADTFHLSAVNW-SNIM----MLG--AIGLVFYMANSLGWA---DTNVAA---TYSL 270
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 283 TLLF--TIMIAGM----TLMQfsrANISLGRIREvLETEPDVKFVESGSVAPLSGSVEFDHVSFTYPDGDDpTLKDISFK 356
Cdd:PRK10522 271 TLLFlrTPLLSAVgalpTLLS---AQVAFNKLNK-LALAPYKAEFPRPQAFPDWQTLELRNVTFAYQDNGF-SVGPINLT 345
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 357 IKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGTIASnlrQGnaqak 436
Cdd:PRK10522 346 IKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGP---EG----- 417
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 437 lhelqRAANMAQASEFIERYNDSFDHEVEE---RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQAL 513
Cdd:PRK10522 418 -----KPANPALVEKWLERLKMAHKLELEDgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVL 492
                        410       420       430
                 ....*....|....*....|....*....|....*
gi 492039060 514 EHELPDT--TTFIIAEKIVSVINADTILVLDDGKL 546
Cdd:PRK10522 493 LPLLQEMgkTIFAISHDDHYFIHADRLLEMRNGQL 527
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
350-558 4.97e-17

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 84.37  E-value: 4.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPTKGKVKIGGQNIKDVTEAAL---RKTVSFVLQR---------A 417
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDpnsslnprlN 380
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 418 VLfsGTIASNLRQgnAQAKLHELQRAANMAQASEFIeryndSFDHEVEER-SANFSGGQKQRLSIARGLIAKAPILILDD 496
Cdd:PRK15134 381 VL--QIIEEGLRV--HQPTLSAAQREQQVIAVMEEV-----GLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDE 451
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 497 STSALDAESE-------KKVQQalEHELpdttTFIIAEKIVSVINA--DTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK15134 452 PTSSLDKTVQaqilallKSLQQ--KHQL----AYLFISHDLHVVRAlcHQVIVLRQGEVVEQGDCERVFAA 516
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
350-509 5.00e-17

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 81.29  E-value: 5.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVL---FSGTIAS 426
Cdd:COG1101   22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPSMTIEE 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 NLRQGNAQAKLHELQRAANMAQASEFIERYNdSFDHEVEER----SANFSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:COG1101  102 NLALAYRRGKRRGLRRGLTKKRRELFRELLA-TLGLGLENRldtkVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180

                 ....*..
gi 492039060 503 AESEKKV 509
Cdd:COG1101  181 PKTAALV 187
cbiO PRK13643
energy-coupling factor transporter ATPase;
333-565 7.09e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 81.32  E-value: 7.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTY-PDGD--DPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTE----AA 405
Cdd:PRK13643   2 IKFEKVNYTYqPNSPfaSRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 LRKTVSFVLQ--RAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIeryndSFDHEVEERSA-NFSGGQKQRLSIA 482
Cdd:PRK13643  82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMV-----GLADEFWEKSPfELSGGQMRRVAIA 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 483 rGLIAKAP-ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEEllkts 559
Cdd:PRK13643 157 -GILAMEPeVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVAdyADYVYLLEKGHIISCGTPSD----- 230

                 ....*.
gi 492039060 560 lVYQEI 565
Cdd:PRK13643 231 -VFQEV 235
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
18-261 7.17e-17

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


Pssm-ID: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 81.37  E-value: 7.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  18 VVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVlsdgIWLVVLGI-IAIISGIFNV---YFAAKIAQGVVSDLRE 92
Cdd:cd18550    1 LALVLLLILLSALLGLLPPLLLREiIDDALPQGDLGLL----VLLALGMVaVAVASALLGVvqtYLSARIGQGVMYDLRV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  93 DTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFI-----------FCIVIIPRFWWaP 161
Cdd:cd18550   77 QLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVamlaldwrlalLSLVLLPLFVL-P 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 162 VVMVAlifgfgayvlRQMNSLFTKFQEMMDRISNQAQETL--QGVRVVKSFNQGPQEIKKFDQTSDQLNDYNI---VIGY 236
Cdd:cd18550  156 TRRVG----------RRRRKLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARRSRELRDLGVrqaLAGR 225
                        250       260
                 ....*....|....*....|....*
gi 492039060 237 WFSAIMpafqMIAYTVIALIVYLIG 261
Cdd:cd18550  226 WFFAAL----GLFTAIGPALVYWVG 246
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
346-558 7.20e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 80.48  E-value: 7.20e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 346 DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ------NIKDVTEAALRKTVSFVLQRAVL 419
Cdd:PRK14246  22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 420 FS-----GTIASNLRQGNAQAKlHELQRAanMAQASEFIERYNDSFDhEVEERSANFSGGQKQRLSIARGLIAKAPILIL 494
Cdd:PRK14246 102 FPhlsiyDNIAYPLKSHGIKEK-REIKKI--VEECLRKVGLWKEVYD-RLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 495 DDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIFTS 242
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
332-514 9.36e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 80.47  E-value: 9.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD-----PTKGKVKIGGQNI--KDVTEA 404
Cdd:PRK14258   7 AIKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 405 ALRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARG 484
Cdd:PRK14258  85 RLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARA 164
                        170       180       190
                 ....*....|....*....|....*....|
gi 492039060 485 LIAKAPILILDDSTSALDAESEKKVQQALE 514
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQ 194
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
345-525 9.47e-17

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 80.20  E-value: 9.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD-----PTKGKVKIGGQNI----KDVTEaaLRKTVSFVLQ 415
Cdd:PRK14239  16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysprTDTVD--LRKEIGMVFQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 RAVLFSGTIASNLRQG---NAQAKLHELQRAA--NMAQAS---EFIERYNDSfdheveerSANFSGGQKQRLSIARGLIA 487
Cdd:PRK14239  94 QPNPFPMSIYENVVYGlrlKGIKDKQVLDEAVekSLKGASiwdEVKDRLHDS--------ALGLSGGQQQRVCIARVLAT 165
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 492039060 488 KAPILILDDSTSALDAESEKKVQQALeHELPDTTTFII 525
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETL-LGLKDDYTMLL 202
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
18-308 1.28e-16

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: 80.60  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  18 VVCAIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTYA 96
Cdd:cd18543    1 LILALLAALLATLAGLAIPLLTRRaIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  97 KIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQlfmqmlrLPILIVGSFIFCIVIIPRFWWAP------VVMVALIFG 170
Cdd:cd18543   81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF-------GPFLLGNLLTLVVGLVVMLVLSPplalvaLASLPPLVL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 171 FGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAY 250
Cdd:cd18543  154 VARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPE 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 251 TVIALIVyLIGKNITAHPS-DIAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18543  234 LGLAAVL-ALGGWLVANGSlTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAERV 291
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
345-546 1.45e-16

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 79.72  E-value: 1.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIkdvteAALRKTVSFVLQRAVLFS-GT 423
Cdd:PRK11247  23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPL-----AEAREDTRLMFQDARLLPwKK 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 424 IASN----LRqGNAQAKLHELQRAANMAqasefiERYNdsfdheveERSANFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:PRK11247  98 VIDNvglgLK-GQWRDAALQALAAVGLA------DRAN--------EWPAALSGGQKQRVALARALIHRPGLLLLDEPLG 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492039060 500 ALDAESEKKVQQALE-----HELpdttTFIIAEKIVS--VINADTILVLDDGKL 546
Cdd:PRK11247 163 ALDALTRIEMQDLIEslwqqHGF----TVLLVTHDVSeaVAMADRVLLIEEGKI 212
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
353-555 1.71e-16

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 79.65  E-value: 1.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 353 ISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL-RKTVSFVLQRAVLF-SGTIASNL-- 428
Cdd:PRK11300  24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMGVVRTFQHVRLFrEMTVIENLlv 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 429 ---RQGNAQAkLHEL---------QRAAnMAQASEFIERYNDSfdhEVEERSA-NFSGGQKQRLSIARGLIAKAPILILD 495
Cdd:PRK11300 104 aqhQQLKTGL-FSGLlktpafrraESEA-LDRAATWLERVGLL---EHANRQAgNLAYGQQRRLEIARCMVTQPEILMLD 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 496 DSTSALDAEsEKKVQQALEHELPD---TTTFIIAE--KIVSVInADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK11300 179 EPAAGLNPK-ETKELDELIAELRNehnVTVLLIEHdmKLVMGI-SDRIYVVNQGTPLANGTPEEI 241
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
322-558 1.72e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 79.75  E-value: 1.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 322 ESGSVAPLSGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKG-----KVKIGGQ 396
Cdd:PRK14271   9 QSGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 397 NI---KDVTEaaLRKTVSFVLQRAVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSG 473
Cdd:PRK14271  89 SIfnyRDVLE--FRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 474 GQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTH 552
Cdd:PRK14271 167 GQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPT 246

                 ....*.
gi 492039060 553 EELLKT 558
Cdd:PRK14271 247 EQLFSS 252
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
341-514 1.72e-16

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


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 78.17  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  341 TYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEaalrktvsfVLQRAVLF 420
Cdd:TIGR01189   7 ACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD---------EPHENILY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  421 SG---------TIASNLR-----QGNAQAKLHELQRAANMAQAsefieryndsfdhevEERSANF-SGGQKQRLSIARGL 485
Cdd:TIGR01189  78 LGhlpglkpelSALENLHfwaaiHGGAQRTIEDALAAVGLTGF---------------EDLPAAQlSAGQQRRLALARLW 142
                         170       180
                  ....*....|....*....|....*....
gi 492039060  486 IAKAPILILDDSTSALDAESEKKVQQALE 514
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLR 171
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
330-559 2.41e-16

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 81.88  E-value: 2.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 330 SGSVEFDHVSFTYPDGDdpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIK-DVTEAALRK 408
Cdd:PRK11288   2 SPYLSFDGIGKTFPGVK--ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 409 TVSFVLQRAVLFSG-TIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSanFSGGQKQRLSIARGLIA 487
Cdd:PRK11288  80 GVAIIYQELHLVPEmTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKY--LSIGQRQMVEIAKALAR 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 488 KAPILILDDSTSALDAEsEKKVQQALEHELPDTTTFII-----AEKIVSVinADTILVLDDGKLVAqgTHEELLKTS 559
Cdd:PRK11288 158 NARVIAFDEPTSSLSAR-EIEQLFRVIRELRAEGRVILyvshrMEEIFAL--CDAITVFKDGRYVA--TFDDMAQVD 229
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
350-546 3.15e-16

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 76.70  E-value: 3.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIK-DVTEAALRKTVSFV----LQRAVLFSGTI 424
Cdd:cd03215   16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrRSPRDAIRAGIAYVpedrKREGLVLDLSV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 ASNLrqgnaqaklhelqraanmaqaseFIERYndsfdheveersanFSGGQKQRLSIARGLIAKAPILILDDSTSALDAE 504
Cdd:cd03215   96 AENI-----------------------ALSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 492039060 505 SEKKVQQALeHELPDTTTFIIaekIVS------VINADTILVLDDGKL 546
Cdd:cd03215  139 AKAEIYRLI-RELADAGKAVL---LISseldelLGLCDRILVMYEGRI 182
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
350-565 4.27e-16

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 81.13  E-value: 4.27e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPT---KGKVKIGGQ-----NIKDvTEaalRKTVSFVLQRAVLFS 421
Cdd:PRK13549  21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEelqasNIRD-TE---RAGIAIIHQELALVK 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 G-TIASNLRQGNAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:PRK13549  96 ElSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLK--LDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 501 LdAESEKKVQQALEHELP--DTTTFIIAEKI--VSVInADTILVLDDGKLV----AQGTHEELLKTSLVYQEI 565
Cdd:PRK13549 174 L-TESETAVLLDIIRDLKahGIACIYISHKLneVKAI-SDTICVIRDGRHIgtrpAAGMTEDDIITMMVGREL 244
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
345-557 4.57e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 78.35  E-value: 4.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD-----PTKGKVKIGGQNI--KDVTEAALRKTVSFVLQRA 417
Cdd:PRK14267  15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 418 VLFSG-TIASNLRQG-------NAQAKLHELQRAA--NMAQASEFIERYNDsfdheveeRSANFSGGQKQRLSIARGLIA 487
Cdd:PRK14267  95 NPFPHlTIYDNVAIGvklnglvKSKKELDERVEWAlkKAALWDEVKDRLND--------YPSNLSGGQRQRLVIARALAM 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 488 KAPILILDDSTSALDAESEKKVQQALeHELPDTTTFII-------AEKIvsvinADTILVLDDGKLVAQGTHEELLK 557
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELL-FELKKEYTIVLvthspaqAARV-----SDYVAFLYLGKLIEVGPTRKVFE 237
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
350-555 7.38e-16

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 80.46  E-value: 7.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ--NIKDvTEAALRKTVSFVLQRAVLFSG-TIAS 426
Cdd:COG3845   21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRS-PRDAIALGIGMVHQHFMLVPNlTVAE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 NLRQGNAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSAL-DAES 505
Cdd:COG3845  100 NIVLGLEPTKGGRLDRKAARARIRELSERYG--LDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtPQEA 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 506 EkkvqqalehELpdtttFIIAEKIV----SVI-----------NADTILVLDDGKLVAQG-----THEEL 555
Cdd:COG3845  178 D---------EL-----FEILRRLAaegkSIIfithklrevmaIADRVTVLRRGKVVGTVdtaetSEEEL 233
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
350-503 7.62e-16

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: 76.93  E-value: 7.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP---TKGKVKIGGQNIKdvtEAALRKTVSFVLQRAVLFSG-TIA 425
Cdd:cd03234   23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK---PDQFQKCVAYVRQDDILLPGlTVR 99
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 426 SNLRQgNAQAKLHELQRAANMAQASEfIERYNDSFDHEV-EERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDA 503
Cdd:cd03234  100 ETLTY-TAILRLPRKSSDAIRKKRVE-DVLLRDLALTRIgGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
309-548 3.56e-15

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 78.14  E-value: 3.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 309 REVLETEPDVKfVESGSVAplsgsVEFDHVSFTYPDGDdPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTK 388
Cdd:COG3845  240 REVLLRVEKAP-AEPGEVV-----LEVENLSVRDDRGV-PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPAS 312
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 389 GKVKIGGQNIKDVTEAALRKT-VSFV----LQRAVLFSGTIASNL---RQGNAQ-AKLHELQRAANMAQASEFIERYN-- 457
Cdd:COG3845  313 GSIRLDGEDITGLSPRERRRLgVAYIpedrLGRGLVPDMSVAENLilgRYRRPPfSRGGFLDRKAIRAFAEELIEEFDvr 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 458 -DSFDHEVeersANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALehelpdtttfiIAEK-------I 529
Cdd:COG3845  393 tPGPDTPA----RSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL-----------LELRdagaavlL 457
                        250       260
                 ....*....|....*....|....*
gi 492039060 530 VS-----VIN-ADTILVLDDGKLVA 548
Cdd:COG3845  458 ISedldeILAlSDRIAVMYEGRIVG 482
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
333-547 4.39e-15

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 74.53  E-value: 4.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI---KDVTEAALRKT 409
Cdd:PRK10908   2 IRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQ-RAVLFSGTIASNLRQG--NAQAKLHELQRaanmaqasefieRYNDSFDH-EVEERSANF----SGGQKQRLSI 481
Cdd:PRK10908  81 IGMIFQdHHLLMDRTVYDNVAIPliIAGASGDDIRR------------RVSAALDKvGLLDKAKNFpiqlSGGEQQRVGI 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 482 ARGLIAKAPILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADT--ILVLDDGKLV 547
Cdd:PRK10908 149 ARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSyrMLTLSDGHLH 216
cbiO PRK13645
energy-coupling factor transporter ATPase;
329-556 5.39e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 75.81  E-value: 5.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 329 LSGSVEFDHVSFTYPDG---DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGG----QNIKDV 401
Cdd:PRK13645   3 FSKDIILDNVSYTYAKKtpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 402 TEAA-LRKTVSFVLQ--RAVLFSGTIASNLRQGnaqaklhELQRAANMAQASEFIERYND--SFDHEVEERSA-NFSGGQ 475
Cdd:PRK13645  83 KEVKrLRKEIGLVFQfpEYQLFQETIEKDIAFG-------PVNLGENKQEAYKKVPELLKlvQLPEDYVKRSPfELSGGQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 476 KQRLSIArGLIA-KAPILILDDSTSALDAESEKKVQQALEHELPDTTTFII-----AEKIVSVinADTILVLDDGKLVAQ 549
Cdd:PRK13645 156 KRRVALA-GIIAmDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIImvthnMDQVLRI--ADEVIVMHEGKVISI 232

                 ....*..
gi 492039060 550 GTHEELL 556
Cdd:PRK13645 233 GSPFEIF 239
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
348-550 7.33e-15

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: 73.45  E-value: 7.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPT---KGKVKIGGQNIKDVTEAAlRKTVSFVLQRAVLFsgti 424
Cdd:cd03233   21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKY-PGEIIYVSEEDVHF---- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 asnlrqgnAQAKLHELQRAANMAQASEFIEryndsfdheveersaNFSGGQKQRLSIARGLIAKAPILILDDSTSALDAE 504
Cdd:cd03233   96 --------PTLTVRETLDFALRCKGNEFVR---------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 492039060 505 SE---KKVQQALEHELPDTTTFII---AEKIVSVInaDTILVLDDGKLVAQG 550
Cdd:cd03233  153 TAleiLKCIRTMADVLKTTTFVSLyqaSDEIYDLF--DKVLVLYEGRQIYYG 202
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
348-555 8.15e-15

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 77.01  E-value: 8.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA-ALRKTVSFVLQRAVLFSG-TIA 425
Cdd:PRK15439  25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAkAHQLGIYLVPQEPLLFPNlSVK 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 426 SNLRQGNAqaklhelQRAANMAQASEFIERYNDSFDHEVEERSANFSggQKQRLSIARGLIAKAPILILDDSTSALD-AE 504
Cdd:PRK15439 105 ENILFGLP-------KRQASMQKMKQLLAALGCQLDLDSSAGSLEVA--DRQIVEILRGLMRDSRILILDEPTASLTpAE 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 492039060 505 SEKKVQQALEHELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEEL 555
Cdd:PRK15439 176 TERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
334-513 1.04e-14

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 74.35  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 334 EFDHVSFTYPDgdDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDvtEAALRKTVsfV 413
Cdd:PRK11248   3 QISHLYADYGG--KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG--PGAERGVV--F 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRAVLFSGTIASNLRQGnaqAKLHELQRAANMAQASEFIERYN-DSFDHeveERSANFSGGQKQRLSIARGLIAKAPIL 492
Cdd:PRK11248  77 QNEGLLPWRNVQDNVAFG---LQLAGVEKMQRLEIAHQMLKKVGlEGAEK---RYIWQLSGGQRQRVGIARALAANPQLL 150
                        170       180
                 ....*....|....*....|.
gi 492039060 493 ILDDSTSALDAESEKKVQQAL 513
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLL 171
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
333-561 1.44e-14

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 73.37  E-value: 1.44e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD-VTEAALRKTVS 411
Cdd:PRK11614   6 LSFDKVSAHY--GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKIMREAVA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 412 FVLQ-RAVLFSGTIASNLRQGNAQAKLHELQraanmaqasEFIERYNDSFDHEVE---ERSANFSGGQKQRLSIARGLIA 487
Cdd:PRK11614  84 IVPEgRRVFSRMTVEENLAMGGFFAERDQFQ---------ERIKWVYELFPRLHErriQRAGTMSGGEQQMLAIGRALMS 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 488 KAPILILDDSTSALDA----ESEKKVQQALEHELpdtTTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEELLKTSLV 561
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPiiiqQIFDTIEQLREQGM---TIFLVEQNANQALKlADRGYVLENGHVVLEDTGDALLANEAV 230
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
353-556 1.53e-14

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: 76.38  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  353 ISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIG-GQNIKDVTEAAL------RKTVSFVLQRAVLFS-GTI 424
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPdgrgraKRYIGILHQEYDLYPhRTV 382
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  425 ASNLRQGNAQAKLHEL--QRAANMAQASEFIERYNDSFdheVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:TIGR03269 383 LDNLTEAIGLELPDELarMKAVITLKMVGFDEEKAEEI---LDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMD 459
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060  503 AESEKKVQQALEH---ELPDttTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELL 556
Cdd:TIGR03269 460 PITKVDVTHSILKareEMEQ--TFIIVSHDMDFVLdvCDRAALMRDGKIVKIGDPEEIV 516
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
22-308 1.84e-14

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: 74.43  E-value: 1.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  22 IIAILVSAFSGLYQP-------KLLENIQKALMANQKQAVLSDGI-----WLVVLGIIAIISGIFNVYFAAKIAQGVVSD 89
Cdd:cd18577    2 IIGLLAAIAAGAALPlmtivfgDLFDAFTDFGSGESSPDEFLDDVnkyalYFVYLGIGSFVLSYIQTACWTITGERQARR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  90 LREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQlfmqmlRLPILI--VGSFIFCIVIIprFWWAP---VVM 164
Cdd:cd18577   82 IRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGE------KLGLLIqsLSTFIAGFIIA--FIYSWkltLVL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 165 VA---LIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAI 241
Cdd:cd18577  154 LAtlpLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLG 233
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 242 MPAFQMIAYTVIALIVYLIGKNITAHPSDIAVvspfvnyVLTLLFTIMIAGMTLMQ-------FSRANISLGRI 308
Cdd:cd18577  234 LGLLFFIIFAMYALAFWYGSRLVRDGEISPGD-------VLTVFFAVLIGAFSLGQiapnlqaFAKARAAAAKI 300
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
346-505 1.94e-14

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 72.29  E-value: 1.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 346 DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDvTEAALRKTVSFVLQRavlfSGtIA 425
Cdd:PRK13540  13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHR----SG-IN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 426 SNLRQgnAQAKLHELQRAANMAQASEFIERYndSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAES 505
Cdd:PRK13540  87 PYLTL--RENCLYDIHFSPGAVGITELCRLF--SLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
350-557 2.16e-14

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 76.24  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIArLYDPTKgkVKIGGQ---NIKDVTEAALRKTVSFVLQRAvLFSGT--- 423
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKG--VKGSGSvllNGMPIDAKEMRAISAYVQQDD-LFIPTltv 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  424 -----IASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDheVEERSANFSGGQKQRLSIARGLIAKAPILILDDST 498
Cdd:TIGR00955 117 rehlmFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRIG--VPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPT 194
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060  499 SALDAESEKKVQQALEHelpdtttfiIAEKIVSVI------------NADTILVLDDGKLVAQGTHEELLK 557
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKG---------LAQKGKTIIctihqpsselfeLFDKIILMAEGRVAYLGSPDQAVP 256
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
345-556 2.46e-14

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 73.02  E-value: 2.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD-----PTKGKVKIGGQNIKDVTEAALRKTVSFVLQ-RAV 418
Cdd:PRK14247  14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQiPNP 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 419 LFSGTIASNLRQGnaqAKLHELQRAAnmaqaSEFIERYNDSFD-----HEVEER----SANFSGGQKQRLSIARGLIAKA 489
Cdd:PRK14247  94 IPNLSIFENVALG---LKLNRLVKSK-----KELQERVRWALEkaqlwDEVKDRldapAGKLSGGQQQRLCIARALAFQP 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 490 PILILDDSTSALDAESEKKVqQALEHELPDTTTFII-------AEKIvsvinADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK14247 166 EVLLADEPTANLDPENTAKI-ESLFLELKKDMTIVLvthfpqqAARI-----SDYVAFLYKGQIVEWGPTREVF 233
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
352-515 2.61e-14

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 71.76  E-value: 2.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 352 DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAalrktvsfvLQRAVLFSG--------- 422
Cdd:PRK13538  19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE---------YHQDLLYLGhqpgiktel 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 TIASNLRqgnAQAKLHELQRAANMAQASEFI--ERYNDSFDHeveersaNFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:PRK13538  90 TALENLR---FYQRLHGPGDDEALWEALAQVglAGFEDVPVR-------QLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
                        170
                 ....*....|....*
gi 492039060 501 LDAESEKKVQQALEH 515
Cdd:PRK13538 160 IDKQGVARLEALLAQ 174
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
346-556 3.31e-14

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 73.12  E-value: 3.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 346 DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA--ALRKTVSFVLQ---RAVLF 420
Cdd:PRK13638  13 DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVFQdpeQQIFY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 S---GTIASNLRQ-GNAQAKL-HELQRAANMAQASEFIERYNDSFDHeveersanfsgGQKQRLSIARGLIAKAPILILD 495
Cdd:PRK13638  93 TdidSDIAFSLRNlGVPEAEItRRVDEALTLVDAQHFRHQPIQCLSH-----------GQKKRVAIAGALVLQARYLLLD 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 496 DSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYeiSDAVYVLRQGQILTHGAPGEVF 224
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
337-555 3.72e-14

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 73.61  E-value: 3.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 337 HVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP---TKGKVKIGGQNIKDVTEAALRKTVSfv 413
Cdd:PRK09473  19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKLRA-- 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQRAVLFSGTIAS-N--LRQGNAQAKLHELQRAANMAQASEFIERYNDS------------FDHEveersanFSGGQKQR 478
Cdd:PRK09473  97 EQISMIFQDPMTSlNpyMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAvkmpearkrmkmYPHE-------FSGGMRQR 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 479 LSIARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPD--TTTFIIAEKIVSVINA--DTILVLDDGKLVAQGTHEE 554
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLL-NELKRefNTAIIMITHDLGVVAGicDKVLVMYAGRTMEYGNARD 248

                 .
gi 492039060 555 L 555
Cdd:PRK09473 249 V 249
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
350-546 5.46e-14

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 71.73  E-value: 5.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTE---AALR-KTVSFVLQRAVLFSGTIA 425
Cdd:PRK10584  26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRaKHVGFVFQSFMLIPTLNA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 426 snlrQGNAQakLHELQRAAN----MAQASEFIERYN--DSFDHeveeRSANFSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:PRK10584 106 ----LENVE--LPALLRGESsrqsRNGAKALLEQLGlgKRLDH----LPAQLSGGEQQRVALARAFNGRPDVLFADEPTG 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 492039060 500 ALDAESEKKVQQ---ALEHELpDTTTFIIAEKIVSVINADTILVLDDGKL 546
Cdd:PRK10584 176 NLDRQTGDKIADllfSLNREH-GTTLILVTHDLQLAARCDRRLRLVNGQL 224
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
353-513 8.03e-14

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


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 70.60  E-value: 8.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 353 ISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAalrktvsfvLQRAVLFSGTIASNLRQGN 432
Cdd:cd03231   19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS---------IARGLLYLGHAPGIKTTLS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 433 AQAKLHELQRAANMAQASEFIERYN-DSFDHEVeerSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQ 511
Cdd:cd03231   90 VLENLRFWHADHSDEQVEEALARVGlNGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAE 166

                 ..
gi 492039060 512 AL 513
Cdd:cd03231  167 AM 168
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
333-514 1.16e-13

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 73.82  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGgqnikdvteaalrKTV-- 410
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG-------------ETVkl 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  411 SFVLQ-RAVLFSG-TIASNLRQGNAQAKL--HELQ-RAanmaqaseFIERYNdsF---DHevEERSANFSGGQKQRLSIA 482
Cdd:TIGR03719 388 AYVDQsRDALDPNkTVWEEISGGLDIIKLgkREIPsRA--------YVGRFN--FkgsDQ--QKKVGQLSGGERNRVHLA 455
                         170       180       190
                  ....*....|....*....|....*....|..
gi 492039060  483 RGLIAKAPILILDDSTSALDAESEKKVQQALE 514
Cdd:TIGR03719 456 KTLKSGGNVLLLDEPTNDLDVETLRALEEALL 487
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
325-563 2.00e-13

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 70.79  E-value: 2.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 325 SVAPLSGsvefDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA 404
Cdd:PRK10253   4 SVARLRG----EQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 405 ALRKTVSFVLQRAVLFSGTIASNL--RQGNAQAKL-----HELQRAANMA-QASEFIERYNDSFDheveersaNFSGGQK 476
Cdd:PRK10253  78 EVARRIGLLAQNATTPGDITVQELvaRGRYPHQPLftrwrKEDEEAVTKAmQATGITHLADQSVD--------TLSGGQR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 477 QRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEhELPDTTTFIIAeKIVSVIN-----ADTILVLDDGKLVAQGT 551
Cdd:PRK10253 150 QRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLS-ELNREKGYTLA-AVLHDLNqacryASHLIALREGKIVAQGA 227
                        250
                 ....*....|..
gi 492039060 552 HEELLKTSLVYQ 563
Cdd:PRK10253 228 PKEIVTAELIER 239
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
350-557 2.51e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 70.89  E-value: 2.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA------------------------A 405
Cdd:PRK13651  23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkekekvleklviqktrfkkikkikE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 406 LRKTVSFVLQRA--VLFSGTIASNLRQGNAQ---AKLHELQRAAnmaqasEFIERYNdsFDHEVEERSA-NFSGGQKQRL 479
Cdd:PRK13651 103 IRRRVGVVFQFAeyQLFEQTIEKDIIFGPVSmgvSKEEAKKRAA------KYIELVG--LDESYLQRSPfELSGGQKRRV 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 480 SIArGLIAKAP-ILILDDSTSALDAESEKKVQQALEHELPDTTTFIIAEKIVSVINADT--ILVLDDGKLVAQGTHEELL 556
Cdd:PRK13651 175 ALA-GILAMEPdFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTkrTIFFKDGKIIKDGDTYDIL 253

                 .
gi 492039060 557 K 557
Cdd:PRK13651 254 S 254
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
332-557 4.36e-13

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 72.20  E-value: 4.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 332 SVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ----------NIKDV 401
Cdd:PRK10261  14 AVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqviELSEQ 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 402 TEAALRKT----VSFVLQRAVLFSGTIASNLRQGNAQAKLHE-LQRAANMAQASEFIERYNDSFDHEVEERSAN-FSGGQ 475
Cdd:PRK10261  94 SAAQMRHVrgadMAMIFQEPMTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEAQTILSRYPHqLSGGM 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 476 KQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQ---ALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTH 552
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQlikVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSV 253

                 ....*
gi 492039060 553 EELLK 557
Cdd:PRK10261 254 EQIFH 258
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
336-566 5.31e-13

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 69.43  E-value: 5.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYPDgdDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQ 415
Cdd:PRK10575  15 RNVSFRVPG--RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 RAVLFSGTIASNL-------------RQGnaQAKLHELQRAANMAQASEFIERYNDSfdheveersanFSGGQKQRLSIA 482
Cdd:PRK10575  93 QLPAAEGMTVRELvaigrypwhgalgRFG--AADREKVEEAISLVGLKPLAHRLVDS-----------LSGGERQRAWIA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 483 RGLIAKAPILILDDSTSALDAESEKKVQ---QALEHELPDTTTFIIAEKIVSVINADTILVLDDGKLVAQGTHEELLKtS 559
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLalvHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR-G 238

                 ....*..
gi 492039060 560 LVYQEIF 566
Cdd:PRK10575 239 ETLEQIY 245
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
21-226 7.31e-13

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: 69.44  E-value: 7.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  21 AIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLSDGIW--LVVLGIIAIISGiFNVYFAAKIAQGVVSDLREDTYAKI 98
Cdd:cd18575    1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLllLAVALVLALASA-LRFYLVSWLGERVVADLRKAVFAHL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  99 QTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVLRQ 178
Cdd:cd18575   80 LRLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRR 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 492039060 179 MNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQ 226
Cdd:cd18575  160 VRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEA 207
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
350-556 7.92e-13

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 68.38  E-value: 7.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVT-EAALRKTVSFVLQRAVLFSGTIASNL 428
Cdd:PRK10895  19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQEASIFRRLSVYDN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 429 RQGNAQAKlHELQRAANMAQASEFIERYNDSfdHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKK 508
Cdd:PRK10895  99 LMAVLQIR-DDLSAEQREDRANELMEEFHIE--HLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 492039060 509 VQQALEHELPDTTTFIIAEKIV--SVINADTILVLDDGKLVAQGTHEELL 556
Cdd:PRK10895 176 IKRIIEHLRDSGLGVLITDHNVreTLAVCERAYIVSQGHLIAHGTPTEIL 225
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
349-554 9.77e-13

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 69.52  E-value: 9.77e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 349 TLKDISFKIK---PGQMV-GIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTE----AALRKTVSFVLQRAVLF 420
Cdd:PRK11144   9 QLGDLCLTVNltlPAQGItAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgiclPPEKRRIGYVFQDARLF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SG-TIASNLRQGnaqaklhelqraanMAQASefieryNDSFDHEVE--------ER-SANFSGGQKQRLSIARGLIAKAP 490
Cdd:PRK11144  89 PHyKVRGNLRYG--------------MAKSM------VAQFDKIVAllgiepllDRyPGSLSGGEKQRVAIGRALLTAPE 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 491 ILILDDSTSALDAESEKKVQQALEHELPDTTTFII-----AEKIVSVinADTILVLDDGKLVAQGTHEE 554
Cdd:PRK11144 149 LLLMDEPLASLDLPRKRELLPYLERLAREINIPILyvshsLDEILRL--ADRVVVLEQGKVKAFGPLEE 215
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
350-502 9.79e-13

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 71.04  E-value: 9.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA---ALRKTVSFVLQ---------RA 417
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGklqALRRDIQFIFQdpyasldprQT 419
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 418 VLFSgtIASNLR-----QGNAQAKlhelqRAANMAQASEFIERYNDSFDHEveersanFSGGQKQRLSIARGLIAKAPIL 492
Cdd:PRK10261 420 VGDS--IMEPLRvhgllPGKAAAA-----RVAWLLERVGLLPEHAWRYPHE-------FSGGQRQRICIARALALNPKVI 485
                        170
                 ....*....|
gi 492039060 493 ILDDSTSALD 502
Cdd:PRK10261 486 IADEAVSALD 495
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
336-520 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 492039060  336 DHVSFTYPdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGK------VKIG----------GQNIK 399
Cdd:TIGR03719   8 NRVSKVVP-PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEarpqpgIKVGylpqepqldpTKTVR 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  400 DVTEAALRKTVSfVLQR----AVLFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSF-----DHEVEersaN 470
Cdd:TIGR03719  87 ENVEEGVAEIKD-ALDRfneiSAKYAEPDADFDKLAAEQAELQEIIDAADAWDLDSQLEIAMDALrcppwDADVT----K 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 492039060  471 FSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALeHELPDT 520
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL-QEYPGT 210
ycf16 CHL00131
sulfate ABC transporter protein; Validated
345-553 1.90e-12

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 67.36  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIA--RLYDPTKGKVKIGGQNIKDVT-EAALRKTVSFVLQRAVLFS 421
Cdd:CHL00131  18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEpEERAHLGIFLAFQYPIEIP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 GTiaSN---LRQG-NAQAKLHELqraaNMAQASEFIERYND-----SFDHEVEERSAN--FSGGQKQRLSIARGLIAKAP 490
Cdd:CHL00131  98 GV--SNadfLRLAyNSKRKFQGL----PELDPLEFLEIINEklklvGMDPSFLSRNVNegFSGGEKKRNEILQMALLDSE 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 491 ILILDDSTSALDAESEKKVQQALeHELPDTTTFIIA----EKIVSVINADTILVLDDGKLVAQGTHE 553
Cdd:CHL00131 172 LAILDETDSGLDIDALKIIAEGI-NKLMTSENSIILithyQRLLDYIKPDYVHVMQNGKIIKTGDAE 237
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
346-558 2.18e-12

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 67.42  E-value: 2.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 346 DDPTLKDISFKIKPGQMVGIVGATGAGKS-TLAQLIARLydP-----TKGKVKIGGQnikDVTEAALR-KTVSFVLQ--R 416
Cdd:PRK10418  15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGIL--PagvrqTAGRVLLDGK---PVAPCALRgRKIATIMQnpR 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 417 AvlfsgtiASN-LRQGNAQAK--LHELQRAANMAQASEFIERYNDSFDHEVEERSA-NFSGGQKQRLSIARGLIAKAPIL 492
Cdd:PRK10418  90 S-------AFNpLHTMHTHARetCLALGKPADDATLTAALEAVGLENAARVLKLYPfEMSGGMLQRMMIALALLCEAPFI 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHelpdtttfIIAEK-----IVS----VIN--ADTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLES--------IVQKRalgmlLVThdmgVVArlADDVAVMSHGRIVEQGDVETLFNA 231
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
352-502 2.37e-12

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 67.26  E-value: 2.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 352 DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ-----NIKDVTEAALRKTV----SFVLQRAvlfsg 422
Cdd:PRK11701  24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRRLLrtewGFVHQHP----- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 423 tiASNLRQG-NAQAKLHELQRAANM-------AQASEFIERyndsfdheVE-------ERSANFSGGQKQRLSIARGLIA 487
Cdd:PRK11701  99 --RDGLRMQvSAGGNIGERLMAVGArhygdirATAGDWLER--------VEidaaridDLPTTFSGGMQQRLQIARNLVT 168
                        170
                 ....*....|....*
gi 492039060 488 KAPILILDDSTSALD 502
Cdd:PRK11701 169 HPRLVFMDEPTGGLD 183
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
348-551 4.18e-12

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: 69.66  E-value: 4.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAaLRKTVSFVLQRAVLFSGTIASN 427
Cdd:TIGR01257  944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDA-VRQSLGMCPQHNILFHHLTVAE 1022
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   428 LRQGNAQAKlhelQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEK 507
Cdd:TIGR01257 1023 HILFYAQLK----GRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 492039060   508 KVQQALEHELPDTTTFIIAEKIVSV-INADTILVLDDGKLVAQGT 551
Cdd:TIGR01257 1099 SIWDLLLKYRSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSGT 1143
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
348-556 5.64e-12

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 68.11  E-value: 5.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVT-EAAL----------RKTVSFVLQR 416
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSpQDGLangivyisedRKRDGLVLGM 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 417 AVLFSGTIASnLRQGNAQAKlhELQRAANMAQASEFIERYN---DSFDHEVeersANFSGGQKQRLSIARGLIAKAPILI 493
Cdd:PRK10762 346 SVKENMSLTA-LRYFSRAGG--SLKHADEQQAVSDFIRLFNiktPSMEQAI----GLLSGGNQQKVAIARGLMTRPKVLI 418
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 494 LDDSTSALDAESEKKVQQaLEHELPDTTTFIIaekIVS-----VIN-ADTILVLDDGKL-----VAQGTHEELL 556
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQ-LINQFKAEGLSII---LVSsempeVLGmSDRILVMHEGRIsgeftREQATQEKLM 488
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
350-547 5.99e-12

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 65.36  E-value: 5.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLY--DPTKGKVKIGGQNIKDvtEAALrktvsfvlqravlfsgtIASN 427
Cdd:COG2401   46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--EASL-----------------IDAI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 428 LRQGNAQAKLhELQRAANMAQASEFIERYndsfdheveersANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEK 507
Cdd:COG2401  107 GRKGDFKDAV-ELLNAVGLSDAVLWLRRF------------KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 492039060 508 KVQQALeHELPDT--TTFIIA---EKIVSVINADTILVLDDGKLV 547
Cdd:COG2401  174 RVARNL-QKLARRagITLVVAthhYDVIDDLQPDLLIFVGYGGVP 217
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
350-560 6.15e-12

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 66.35  E-value: 6.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAvlfsgTIASNLR 429
Cdd:PRK15112  29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP-----STSLNPR 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 430 QgnaqaklhelqraaNMAQASEFIERYNDSFDHEVEERSAN-------------------FSGGQKQRLSIARGLIAKAP 490
Cdd:PRK15112 104 Q--------------RISQILDFPLRLNTDLEPEQREKQIIetlrqvgllpdhasyyphmLAPGQKQRLGLARALILRPK 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 491 ILILDDSTSALDAESEKK-VQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEELLKTSL 560
Cdd:PRK15112 170 VIIADEALASLDMSMRSQlINLMLELQEKQGISYIYVTQHLGMMKhiSDQVLVMHQGEVVERGSTADVLASPL 242
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
350-550 7.10e-12

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 67.89  E-value: 7.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEA-ALRKTVSFVLQR-AVLFSGTIASN 427
Cdd:PRK09700  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQElSVIDELTVLEN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 428 LRQGNAQAK----LHELQRAANMAQASEFIERYNDSFDheVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSAL-D 502
Cdd:PRK09700 101 LYIGRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVD--LDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLtN 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492039060 503 AESEK--KVQQALEHElpDTTTFIIAEKIVSVIN-ADTILVLDDGKLVAQG 550
Cdd:PRK09700 179 KEVDYlfLIMNQLRKE--GTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
350-495 9.09e-12

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 65.05  E-value: 9.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikDVTEAAL----RKTVSFVLQRAVLFSG-TI 424
Cdd:COG1137   19 VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE---DITHLPMhkraRLGIGYLPQEASIFRKlTV 95
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 425 ASNLRqgnAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILD 495
Cdd:COG1137   96 EDNIL---AVLELRKLSKKEREERLEELLEEFG--ITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
350-558 9.46e-12

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 66.26  E-value: 9.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI-KDvtEAALRKTVSFVL-QRAVLF------- 420
Cdd:COG4586   38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPfKR--RKEFARRIGVVFgQRSQLWwdlpaid 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SGTIasnlrqgnaQAKLHELQRAANMAQASEFIERYndsfdhEVEE------RsaNFSGGQKQRLSIARGLIAKAPILIL 494
Cdd:COG4586  116 SFRL---------LKAIYRIPDAEYKKRLDELVELL------DLGElldtpvR--QLSLGQRMRCELAAALLHRPKILFL 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 495 DDSTSALDAESEKKVQQAL-----EHElpdtTTFIIA-------EKIvsvinADTILVLDDGKLVAQGTHEELLKT 558
Cdd:COG4586  179 DEPTIGLDVVSKEAIREFLkeynrERG----TTILLTshdmddiEAL-----CDRVIVIDHGRIIYDGSLEELKER 245
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
343-513 1.06e-11

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: 64.19  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 343 PDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDP--TKGKVKIGGQNIKDvteaALRKTVSFVLQRAVLF 420
Cdd:cd03232   16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDK----NFQRSTGYVEQQDVHS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SG-TIASNLRqgnAQAKLHELqraanmaqasefieryndsfdheveersanfSGGQKQRLSIARGLIAKAPILILDDSTS 499
Cdd:cd03232   92 PNlTVREALR---FSALLRGL-------------------------------SVEQRKRLTIGVELAAKPSILFLDEPTS 137
                        170
                 ....*....|....
gi 492039060 500 ALDAESEKKVQQAL 513
Cdd:cd03232  138 GLDSQAAYNIVRFL 151
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
333-514 1.98e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 66.68  E-value: 1.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGgqnikdvteaalrKTV-- 410
Cdd:PRK11819 325 IEAENLSKSF--GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG-------------ETVkl 389
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 411 SFVLQ-RAVLFSG-TIASNLRQGNAQAKLHELQ---RAanmaqaseFIERYNdsF---DHevEERSANFSGGQKQRLSIA 482
Cdd:PRK11819 390 AYVDQsRDALDPNkTVWEEISGGLDIIKVGNREipsRA--------YVGRFN--FkggDQ--QKKVGVLSGGERNRLHLA 457
                        170       180       190
                 ....*....|....*....|....*....|..
gi 492039060 483 RGLIAKAPILILDDSTSALDAESEKKVQQALE 514
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
346-552 2.00e-11

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 64.43  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 346 DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIA--RLYDPTKGKVKIGGQNIKDVT-EAALRKTVSFVLQRAV---- 418
Cdd:PRK09580  13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVeipg 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 419 ----LFSGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDsfdheVEERSAN--FSGGQKQRLSIARGLIAKAPIL 492
Cdd:PRK09580  93 vsnqFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPED-----LLTRSVNvgFSGGEKKRNDILQMAVLEPELC 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 493 ILDDSTSALDAESEKKVQQALEHELPDTTTFIIA---EKIVSVINADTILVLDDGKLVAQGTH 552
Cdd:PRK09580 168 ILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVthyQRILDYIKPDYVHVLYQGRIVKSGDF 230
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
351-546 3.41e-11

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 65.84  E-value: 3.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 351 KDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI-KDVTEAALRKTVSFV---LQRAVLFsgtIAS 426
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInALSTAQRLARGLVYLpedRQSSGLY---LDA 356
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 427 NLRQGNAQAKLHELQRAANMAQASEFIERY----NDSFDHEvEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:PRK15439 357 PLAWNVCALTHNRRGFWIKPARENAVLERYrralNIKFNHA-EQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 503 AESEKKVQQALEHelpdtttfiIAEKIVSVI-----------NADTILVLDDGKL 546
Cdd:PRK15439 436 VSARNDIYQLIRS---------IAAQNVAVLfissdleeieqMADRVLVMHQGEI 481
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
341-503 5.12e-11

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 64.48  E-value: 5.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 341 TYpDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVtEAALRKtVSFVLQRAVLF 420
Cdd:PRK11650  12 SY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL-EPADRD-IAMVFQNYALY 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SG-TIASNLRQG--NAQAKLHELQR----AANMAQASEFIERyndsfdheveeRSANFSGGQKQRLSIARGLIAKAPILI 493
Cdd:PRK11650  89 PHmSVRENMAYGlkIRGMPKAEIEErvaeAARILELEPLLDR-----------KPRELSGGQRQRVAMGRAIVREPAVFL 157
                        170
                 ....*....|
gi 492039060 494 LDDSTSALDA 503
Cdd:PRK11650 158 FDEPLSNLDA 167
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
329-502 7.22e-11

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 62.82  E-value: 7.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 329 LSGSVEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVK------IGGQNIKDVT 402
Cdd:PRK09544   1 MTSLVSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKrngklrIGYVPQKLYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 403 EAALRKTVS-FVLQRAVLFSGTIASNLRQGNAQaklhelqraanmaqasefieryndsfdHEVEERSANFSGGQKQRLSI 481
Cdd:PRK09544  79 DTTLPLTVNrFLRLRPGTKKEDILPALKRVQAG---------------------------HLIDAPMQKLSGGETQRVLL 131
                        170       180
                 ....*....|....*....|.
gi 492039060 482 ARGLIAKAPILILDDSTSALD 502
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGVD 152
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
350-556 1.22e-10

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 62.17  E-value: 1.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPTKGKVKIGGQNIKDVTEAALRKTVSFVLQRAVLFSGT------ 423
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMpvfqyl 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 424 ---IASNLRQGNAQAKLHELQRAANMAqasefiERYNDSFDHeveersanFSGGQKQRLSIARGLI-------AKAPILI 493
Cdd:COG4138   91 alhQPAGASSEAVEQLLAQLAEALGLE------DKLSRPLTQ--------LSGGEWQRVRLAAVLLqvwptinPEGQLLL 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 494 LDDSTSALDAesekkVQQALehelpdTTTFI--IAEKIVSVI------N-----ADTILVLDDGKLVAQGTHEELL 556
Cdd:COG4138  157 LDEPMNSLDV-----AQQAA------LDRLLreLCQQGITVVmsshdlNhtlrhADRVWLLKQGKLVASGETAEVM 221
hmuV PRK13547
heme ABC transporter ATP-binding protein;
350-563 1.24e-10

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 62.54  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIA-RLYDPT-------KGKVKIGGQNIKDVTE---AALRKTVSFVLQRAV 418
Cdd:PRK13547  17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAprlARLRAVLPQAAQPAF 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 419 LFSGTiasnlrqgnaqaKLHELQRAANMAQASEFIERYNDSFDHEVEERSAN---------FSGGQKQRLSIARGL---- 485
Cdd:PRK13547  97 AFSAR------------EIVLLGRYPHARRAGALTHRDGEIAWQALALAGATalvgrdvttLSGGELARVQFARVLaqlw 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 486 -----IAKAPILILDDSTSALDAesekkvqqALEHELPDTTTFIIAE------KIVSVIN-----ADTILVLDDGKLVAQ 549
Cdd:PRK13547 165 pphdaAQPPRYLLLDEPTAALDL--------AHQHRLLDTVRRLARDwnlgvlAIVHDPNlaarhADRIAMLADGAIVAH 236
                        250
                 ....*....|....
gi 492039060 550 GTHEELLKTSLVYQ 563
Cdd:PRK13547 237 GAPADVLTPAHIAR 250
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
21-308 1.51e-10

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: 62.51  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  21 AIIAILVSAFSGLYQPKLLEN-IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTYAKIQ 99
Cdd:cd18546    4 ALLLVVVDTAASLAGPLLVRYgIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 100 TFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLfmqmlrLPILIVGSFIFCIVIIPRFWWAP----VVMVALIFGFGAYV 175
Cdd:cd18546   84 RLSLDFHERETSGRIMTRMTSDIDALSELLQTG------LVQLVVSLLTLVGIAVVLLVLDPrlalVALAALPPLALATR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 176 LRQMNSLFTkFQEMMDRISN---QAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTV 252
Cdd:cd18546  158 WFRRRSSRA-YRRARERIAAvnaDLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLA 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 253 IALIVYLIGKNITAHPSDIAVVSPFVNYvLTLLFT-IMIAGMTLMQFSRANISLGRI 308
Cdd:cd18546  237 TAAVLLVGAWRVAAGTLTVGVLVAFLLY-LRRFFApIQQLSQVFDSYQQARAALEKI 292
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
59-226 2.31e-10

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: 62.14  E-value: 2.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  59 IWLVVLGI--IAIISGIF---NVYFAAKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLF 133
Cdd:cd18564   53 LLLAAAALvgIALLRGLAsyaGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGV 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 134 mqmlrLPIL-----IVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVK 208
Cdd:cd18564  133 -----LPLLtnlltLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQ 207
                        170
                 ....*....|....*...
gi 492039060 209 SFNQGPQEIKKFDQTSDQ 226
Cdd:cd18564  208 AFGREEHEERRFARENRK 225
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
350-513 2.45e-10

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 61.18  E-value: 2.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLY--DPTKGK--------VKIGGQNIKDVTEAalRKTVSFVLQRAVL 419
Cdd:PRK09984  20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShiellgrtVQREGRLARDIRKS--RANTGYIFQQFNL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 420 FS----------GTIASN------LRQGNAQAKLHELQRAANMAQAsefieryndsfdHEVEERSANFSGGQKQRLSIAR 483
Cdd:PRK09984  98 VNrlsvlenvliGALGSTpfwrtcFSWFTREQKQRALQALTRVGMV------------HFAHQRVSTLSGGQQQRVAIAR 165
                        170       180       190
                 ....*....|....*....|....*....|
gi 492039060 484 GLIAKAPILILDDSTSALDAESEKKVQQAL 513
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTL 195
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
347-569 2.45e-10

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 61.10  E-value: 2.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 347 DPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPTKGKVKIGGQNIKDVTEAAL-RKTVSFVLQRAVLFSGTI- 424
Cdd:PRK03695   9 STRLGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVf 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 425 -------ASNLRQGNAQAKLHELQRAANMAqasefierynDSFdheveERSAN-FSGGQKQR-------LSIARGLIAKA 489
Cdd:PRK03695  88 qyltlhqPDKTRTEAVASALNEVAEALGLD----------DKL-----GRSVNqLSGGEWQRvrlaavvLQVWPDINPAG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 490 PILILDDSTSALDAESEKKVQQALEHelpdtttfiIAEKIVSVI-----------NADTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK03695 153 QLLLLDEPMNSLDVAQQAALDRLLSE---------LCQQGIAVVmsshdlnhtlrHADRVWLLKQGKLLASGRRDEVLTP 223
                        250
                 ....*....|.
gi 492039060 559 SlVYQEIFKTQ 569
Cdd:PRK03695 224 E-NLAQVFGVN 233
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
336-558 4.48e-10

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 61.30  E-value: 4.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYPDGDDP--TLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYD-PTK---GKVKIGGQNIKDVTEAALRK- 408
Cdd:PRK11022   7 DKLSVHFGDESAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRvmaEKLEFNGQDLQRISEKERRNl 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 409 ---TVSFVLQRA---------VLFSGTIASNLRQGNAQAKLHelQRAANM-------AQASEFierynDSFDHEVeersa 469
Cdd:PRK11022  87 vgaEVAMIFQDPmtslnpcytVGFQIMEAIKVHQGGNKKTRR--QRAIDLlnqvgipDPASRL-----DVYPHQL----- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 470 nfSGGQKQRLSIARGLIAKAPILILDDSTSALDA-----------ESEKKVQQAL---EHELPdtttfIIAEKivsvinA 535
Cdd:PRK11022 155 --SGGMSQRVMIAMAIACRPKLLIADEPTTALDVtiqaqiielllELQQKENMALvliTHDLA-----LVAEA------A 221
                        250       260
                 ....*....|....*....|...
gi 492039060 536 DTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK11022 222 HKIIVMYAGQVVETGKAHDIFRA 244
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
333-565 5.31e-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: 61.76  E-value: 5.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLY--DPTKGKVKIGGQ-----NIKDvTEaa 405
Cdd:TIGR02633   2 LEMKGIVKTF--GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSplkasNIRD-TE-- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  406 lRKTVSFVLQRAVLFSG-TIASNLRQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEERSANFSGGQKQRLSIARG 484
Cdd:TIGR02633  77 -RAGIVIIHQELTLVPElSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  485 LIAKAPILILDDSTSALdAESEKKVQQALEHELP--DTTTFIIAEKIVSVIN-ADTILVLDDGKLVA----QGTHEELLK 557
Cdd:TIGR02633 156 LNKQARLLILDEPSSSL-TEKETEILLDIIRDLKahGVACVYISHKLNEVKAvCDTICVIRDGQHVAtkdmSTMSEDDII 234

                  ....*...
gi 492039060  558 TSLVYQEI 565
Cdd:TIGR02633 235 TMMVGREI 242
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
259-507 7.52e-10

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 62.34  E-value: 7.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   259 LIGKNITAhpsdiAVVSPFVNYVLTLLFTimiagmtlMQFSRANISLGRIREVLETEPDVKFVESGSVapLSGS-----V 333
Cdd:TIGR01257 1874 LIGKNLVA-----MAVEGVVYFLLTLLIQ--------HHFFLSRWIAEPAKEPIFDEDDDVAEERQRI--ISGGnktdiL 1938
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   334 EFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ----NIKDVTEA----- 404
Cdd:TIGR01257 1939 RLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKsiltNISDVHQNmgycp 2018
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   405 ALRKTVSFVLQRAVLFsgtIASNLRQGNAQaklhELQRAANMAQASEFIERYNDSFdheveerSANFSGGQKQRLSIARG 484
Cdd:TIGR01257 2019 QFDAIDDLLTGREHLY---LYARLRGVPAE----EIEKVANWSIQSLGLSLYADRL-------AGTYSGGNKRKLSTAIA 2084
                          250       260
                   ....*....|....*....|...
gi 492039060   485 LIAKAPILILDDSTSALDAESEK 507
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARR 2107
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
338-505 8.97e-10

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 61.29  E-value: 8.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 338 VSFTYPdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKV------KIG----------GQNIKDV 401
Cdd:PRK11819  12 VSKVVP-PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEArpapgiKVGylpqepqldpEKTVREN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 402 TEAALRKTVSfVLQRavlFSGtIASNLrqGNAQAKLHELqrAANMAQASEFIERYN-DSFDHEVE------------ERS 468
Cdd:PRK11819  91 VEEGVAEVKA-ALDR---FNE-IYAAY--AEPDADFDAL--AAEQGELQEIIDAADaWDLDSQLEiamdalrcppwdAKV 161
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 492039060 469 ANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAES 505
Cdd:PRK11819 162 TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
333-555 1.23e-09

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 59.39  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTypDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAAL---RKT 409
Cdd:PRK11831   8 VDMRGVSFT--RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 VSFVLQRAVLFSG-----TIASNLRQGNA--QAKLHE----------LQRAANMaqasefieryndsfdheveeRSANFS 472
Cdd:PRK11831  86 MSMLFQSGALFTDmnvfdNVAYPLREHTQlpAPLLHStvmmkleavgLRGAAKL--------------------MPSELS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 473 GGQKQRLSIARGlIAKAPILIL-DDSTSALDAESEK---KVQQALEHELpDTTTFIIAEKIVSVIN-ADTILVLDDGKLV 547
Cdd:PRK11831 146 GGMARRAALARA-IALEPDLIMfDEPFVGQDPITMGvlvKLISELNSAL-GVTCVVVSHDVPEVLSiADHAYIVADKKIV 223

                 ....*...
gi 492039060 548 AQGTHEEL 555
Cdd:PRK11831 224 AHGSAQAL 231
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
357-542 1.41e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 60.59  E-value: 1.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 357 IKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKV----KIG--GQNIKDVTEAalrkTVSFVLQRAvlfSGTIASNLRQ 430
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelKISykPQYIKPDYDG----TVEDLLRSI---TDDLGSSYYK 434
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 431 gnaqaklhelqraanmaqaSEFIERYN--DSFDHEVEErsanFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKK 508
Cdd:PRK13409 435 -------------------SEIIKPLQleRLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 492039060 509 VQQALEH--ELPDTTTFIIAEKIVsVIN--ADTILVLD 542
Cdd:PRK13409 492 VAKAIRRiaEEREATALVVDHDIY-MIDyiSDRLMVFE 528
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
341-504 1.48e-09

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 58.32  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 341 TYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAalrktvsfvlqRAVLF 420
Cdd:PRK13543  18 AFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS-----------RFMAY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SGTIASNLRQGNAQAKLHEL-----QRAANMAQASEFIERYNDSFDHEVEERSAnfsgGQKQRLSIARGLIAKAPILILD 495
Cdd:PRK13543  87 LGHLPGLKADLSTLENLHFLcglhgRRAKQMPGSALAIVGLAGYEDTLVRQLSA----GQKKRLALARLWLSPAPLWLLD 162

                 ....*....
gi 492039060 496 DSTSALDAE 504
Cdd:PRK13543 163 EPYANLDLE 171
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
345-555 1.55e-09

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 59.75  E-value: 1.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAqLIARLYDPTKGKvKIGGQNIKDVTEAALRKTVSF----VLQRAVLF 420
Cdd:NF000106  24 GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR-RPWRF*TWCANRRALRRTIG*hrpvR*GRRESF 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SGTiaSNLRQgnaQAKLHELQRAANMAQASEFIERYndSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:NF000106 102 SGR--ENLYM---IGR*LDLSRKDARARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTG 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 501 LDAESEKKVQQALEHELPDTTTFIIAEKIVSVIN--ADTILVLDDGKLVAQGTHEEL 555
Cdd:NF000106 175 LDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEqlAHELTVIDRGRVIADGKVDEL 231
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
338-558 3.01e-09

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 59.72  E-value: 3.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 338 VSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPT------KGKVKIGGQNIKDVTEAALRKT-- 409
Cdd:PRK15134  13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSppvvypSGDIRFHGESLLHASEQTLRGVrg 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 --VSFVLQRAVLFSGTIASNLRQGNAQAKLHE-LQRAANMAQASEFIERYNDsfdHEVEERSANF----SGGQKQRLSIA 482
Cdd:PRK15134  92 nkIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRgMRREAARGEILNCLDRVGI---RQAAKRLTDYphqlSGGERQRVMIA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 483 RGLIAKAPILILDDSTSALDAESEKKVQQ---ALEHELPDTTTFIIAE-KIVSVInADTILVLDDGKLVAQGTHEELLKT 558
Cdd:PRK15134 169 MALLTRPELLIADEPTTALDVSVQAQILQllrELQQELNMGLLFITHNlSIVRKL-ADRVAVMQNGRCVEQNRAATLFSA 247
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
57-303 7.65e-09

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


Pssm-ID: 349984 [Multi-domain]  Cd Length: 295  Bit Score: 57.10  E-value: 7.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  57 DGIWLVVL--GIIAIISGIFN---VYFAAKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDmnqvmnmmmq 131
Cdd:cd18540   39 DGLTGFILlyLGLILIQALSVflfIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSD---------- 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 132 lfmqMLRLP--------------ILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQA 197
Cdd:cd18540  109 ----TQRLGeiiswglvdlvwgiTYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKILKAYRKVRKINSRITGAF 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 198 QETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIvIGYWFSAI-MPAFQMIAYTVIALIVYLIGKNITAHPSDIAVVSP 276
Cdd:cd18540  185 NEGITGAKTTKTLVREEKNLREFKELTEEMRRASV-RAARLSALfLPIVLFLGSIATALVLWYGGILVLAGAITIGTLVA 263
                        250       260
                 ....*....|....*....|....*....
gi 492039060 277 FVNYVLTLLFTIMIAGMTL--MQFSRANI 303
Cdd:cd18540  264 FISYATQFFEPIQQLARVLaeLQSAQASA 292
PLN03073 PLN03073
ABC transporter F family; Provisional
305-513 8.34e-09

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 58.33  E-value: 8.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 305 LGRIREVLeTEPDVKF-VESGSVAPLSGSVEFDHVSFTYPDGddPTL-KDISFKIKPGQMVGIVGATGAGKSTLAQLIAR 382
Cdd:PLN03073 481 LGHVDAVV-NDPDYKFeFPTPDDRPGPPIISFSDASFGYPGG--PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISG 557
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 383 LYDPTKG------KVKIGGQNIKDVTeaALRKTVSFVLQRAVLFSGTIASNLRqgnaqAKLHELQRAANMAQASEFiery 456
Cdd:PLN03073 558 ELQPSSGtvfrsaKVRMAVFSQHHVD--GLDLSSNPLLYMMRCFPGVPEQKLR-----AHLGSFGVTGNLALQPMY---- 626
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 457 ndsfdheveersaNFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQAL 513
Cdd:PLN03073 627 -------------TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL 670
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
356-542 1.11e-08

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: 57.87  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 356 KIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVkiggqnikdvtEAALRktVSFVLQR-AVLFSGTIASNLRQGNAQ 434
Cdd:COG1245  362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLK--ISYKPQYiSPDYDGTVEEFLRSANTD 428
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 435 AklhelqRAANMAQaSEFIERYN--DSFDHEVEErsanFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQA 512
Cdd:COG1245  429 D------FGSSYYK-TEIIKPLGleKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKA 497
                        170       180       190
                 ....*....|....*....|....*....|....
gi 492039060 513 LEH--ELPDTTTFIIAEKIVsVIN--ADTILVLD 542
Cdd:COG1245  498 IRRfaENRGKTAMVVDHDIY-LIDyiSDRLMVFE 530
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
352-502 2.12e-08

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 57.06  E-value: 2.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 352 DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIkDVTEAALRKTVSFVLQRAVLFSG-TIASNLrq 430
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV-DAGDIATRRRVGYMSQAFSLYGElTVRQNL-- 360
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492039060 431 gNAQAKLHELQRAANMAQASEFIERyndsFD--HEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALD 502
Cdd:NF033858 361 -ELHARLFHLPAAEIAARVAEMLER----FDlaDVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
336-553 2.71e-08

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 55.27  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYPDGDDpTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNikdvTEAALRKT-VSFVL 414
Cdd:PRK15056  10 NDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP----TRQALQKNlVAYVP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 415 QR-------AVLFSGTIASNlRQGNA----QAKLHELQRaanmaqASEFIERYnDSFDHEvEERSANFSGGQKQRLSIAR 483
Cdd:PRK15056  85 QSeevdwsfPVLVEDVVMMG-RYGHMgwlrRAKKRDRQI------VTAALARV-DMVEFR-HRQIGELSGGQKKRVFLAR 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 484 GLIAKAPILILDDSTSALDAESEKKVqQALEHELPD--TTTFIIAEKIVSVINADTILVLDDGKLVAQGTHE 553
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARI-ISLLRELRDegKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTE 226
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
340-550 3.05e-08

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: 54.72  E-value: 3.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 340 FTYP----DGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIggqnikdvteaaLRKTVSFVLQ 415
Cdd:cd03237    1 YTYPtmkkTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEI------------ELDTVSYKPQ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 ravlfsgTIASNlRQGNAQAKLHE-LQRAANMAQ-ASEFIE--RYNDSFDHEVEErsanFSGGQKQRLSIARGLIAKAPI 491
Cdd:cd03237   69 -------YIKAD-YEGTVRDLLSSiTKDFYTHPYfKTEIAKplQIEQILDREVPE----LSGGELQRVAIAACLSKDADI 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492039060 492 LILDDSTSALDAESEKKVQQALEHelpdtttFII-AEKIVSVINADTILV--LDDGKLVAQG 550
Cdd:cd03237  137 YLLDEPSAYLDVEQRLMASKVIRR-------FAEnNEKTAFVVEHDIIMIdyLADRLIVFEG 191
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
21-259 3.56e-08

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: 55.21  E-value: 3.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  21 AIIAILVSAFSGLYQP----KLLENIQKALMANQKQAVLSDGIWLVVLGIIAIiSGIFN---VYFAAKIAQGVVSDLRED 93
Cdd:cd18573    1 ALALLLVSSAVTMSVPfaigKLIDVASKESGDIEIFGLSLKTFALALLGVFVV-GAAANfgrVYLLRIAGERIVARLRKR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  94 TYAKI--QTFSFGNIKKfsAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFI--FCI---------VIIPrfwwa 160
Cdd:cd18573   80 LFKSIlrQDAAFFDKNK--TGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGmmLYIspkltlvmlLVVP----- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 161 PVVMVALIFGfgayvlRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSA 240
Cdd:cd18573  153 PIAVGAVFYG------RYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGL 226
                        250
                 ....*....|....*....
gi 492039060 241 IMPAFQMIAYTVIALIVYL 259
Cdd:cd18573  227 FFGSTGFSGNLSLLSVLYY 245
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
336-513 1.01e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 54.79  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 336 DHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIgGQNIKdvteaalrktVSFVLQ 415
Cdd:PRK10636 316 EKVSAGY--GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK----------LGYFAQ 382
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 416 RAVLFsgtiasnLRQGnaQAKLHELQRAAnmAQASEFIER-YNDSFDHE---VEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:PRK10636 383 HQLEF-------LRAD--ESPLQHLARLA--PQELEQKLRdYLGGFGFQgdkVTEETRRFSGGEKARLVLALIVWQRPNL 451
                        170       180
                 ....*....|....*....|..
gi 492039060 492 LILDDSTSALDAESEKKVQQAL 513
Cdd:PRK10636 452 LLLDEPTNHLDLDMRQALTEAL 473
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
333-556 1.08e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 55.13  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYpdGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIA---RLYDptkGKVKI-GGqnikDVTEAALRK 408
Cdd:NF033858   2 ARLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAgarKIQQ---GRVEVlGG----DMADARHRR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 409 TVS----FVLQravlfsG---------TIASNLR-------QGNAQ--AKLHELQRAANMAqasEFIERyndsfdhevee 466
Cdd:NF033858  73 AVCpriaYMPQ------GlgknlyptlSVFENLDffgrlfgQDAAErrRRIDELLRATGLA---PFADR----------- 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 467 RSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESekKVQ-----QALEHELPDtttfiiaekiVSVINA------ 535
Cdd:NF033858 133 PAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS--RRQfweliDRIRAERPG----------MSVLVAtaymee 200
                        250       260
                 ....*....|....*....|....*
gi 492039060 536 ----DTILVLDDGKLVAQGTHEELL 556
Cdd:NF033858 201 aerfDWLVAMDAGRVLATGTPAELL 225
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
359-514 1.26e-07

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: 51.22  E-value: 1.26e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   359 PGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVK-IGGQNIKDVTEAALRKTVsfvlqravlfsgtiasnlrqgnaqakl 437
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIyIDGEDILEEVLDQLLLII--------------------------- 53
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060   438 helqraanmaqasefieryndsfdheVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALE 514
Cdd:smart00382  54 --------------------------VGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104
ABC_6TM_ABCC_D1 cd18579
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ...
20-308 1.67e-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: 52.87  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  20 CAIIAILVSAFSGLYQPKLLENIQKALMANqKQAVLSDGIWLVV-LGIIAIISGIFN---VYFAAKIAQGVVSDLREDTY 95
Cdd:cd18579    1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSY-PDEPLSEGYLLALaLFLVSLLQSLLLhqyFFLSFRLGMRVRSALSSLIY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  96 AKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLrLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYV 175
Cdd:cd18579   80 RKALRLSSSARQETSTGEIVNLMSVDVQRIEDFFLFLHYLWS-APLQIIVALYLLYRLLGWAALAGLGVLLLLIPLQAFL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 176 LRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFN-QGP----------QEIKkfdqtsdQLNDYNIVIGyWFSAIMPA 244
Cdd:cd18579  159 AKLISKLRKKLMKATDERVKLTNEILSGIKVIKLYAwEKPflkrieelrkKELK-------ALRKFGYLRA-LNSFLFFS 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492039060 245 FQMIAyTVIALIVY-LIGKNITAhpsdiAVVSPFVNYVLTLLFTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18579  231 TPVLV-SLATFATYvLLGNPLTA-----AKVFTALSLFNLLRFPLLMLPQAISSLIEALVSLKRI 289
GguA NF040905
sugar ABC transporter ATP-binding protein;
350-547 2.23e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 53.64  E-value: 2.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPT---KGKVKIGGQ-----NIKDvTEAalrKTVSFVLQRAVLFS 421
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEvcrfkDIRD-SEA---LGIVIIHQELALIP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 G-TIASNLRQGNAQAKLHELQRAANMAQASEFIERYNdsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSA 500
Cdd:NF040905  92 YlSIAENIFLGNERAKRGVIDWNETNRRARELLAKVG--LDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492039060 501 L-DAESEKKVQQALEHELPDTTTFIIAEK---IVSVinADTILVLDDGKLV 547
Cdd:NF040905 170 LnEEDSAALLDLLLELKAQGITSIIISHKlneIRRV--ADSITVLRDGRTI 218
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
345-547 4.09e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 53.03  E-value: 4.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIAR--LYDptKGKVKIGgqniKDVteaalrkTVSFVLQ---RAVl 419
Cdd:PRK11147  14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevLLD--DGRIIYE----QDL-------IVARLQQdppRNV- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 420 fSGTIASNLRQG-NAQAKL----HELQRA----------ANMAQASEFIERYN----DSFDHEV--------EERSANFS 472
Cdd:PRK11147  80 -EGTVYDFVAEGiEEQAEYlkryHDISHLvetdpseknlNELAKLQEQLDHHNlwqlENRINEVlaqlgldpDAALSSLS 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492039060 473 GGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEhELPDTTTFIIAEKivSVIN--ADTILVLDDGKLV 547
Cdd:PRK11147 159 GGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK-TFQGSIIFISHDR--SFIRnmATRIVDLDRGKLV 232
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
350-395 5.84e-07

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 52.20  E-value: 5.84e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGG 395
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG 85
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
52-308 6.25e-07

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


Pssm-ID: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 51.41  E-value: 6.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  52 QAVLSDGIWLVVLGIIAIISGIFNVYFAAkIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLINDMNQVMNMMMQ 131
Cdd:cd18565   52 QLWLLGGLTVAAFLLESLFQYLSGVLWRR-FAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDD 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 132 LFMQMLRLPILIVGSFIFCIVIIPRFWWAPVVMVALIFGFGAYVLRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFN 211
Cdd:cd18565  131 GANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFT 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 212 QGPQEIKKFDQTSDQLNDYN---IVIGYWFSAIMPAFQMIAYTVIALI---VYLIGKNITAHPSDIAVVSPFVNYVLTLL 285
Cdd:cd18565  211 AEDFERERVADASEEYRDANwraIRLRAAFFPVIRLVAGAGFVATFVVggyWVLDGPPLFTGTLTVGTLVTFLFYTQRLL 290
                        250       260
                 ....*....|....*....|...
gi 492039060 286 FTIMIAGMTLMQFSRANISLGRI 308
Cdd:cd18565  291 WPLTRLGDLIDQYQRAMASAKRV 313
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
350-548 7.77e-07

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 51.65  E-value: 7.77e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQ--NIKDVTEaALRKTVSF-------VLQRAVLf 420
Cdd:PRK10982  14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSKE-ALENGISMvhqelnlVLQRSVM- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 sgtiaSNLRQGNAQAKlhelqraanmaqaSEFIER---YNDS--------FDHEVEERSANFSGGQKQRLSIARGLIAKA 489
Cdd:PRK10982  92 -----DNMWLGRYPTK-------------GMFVDQdkmYRDTkaifdeldIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 490 PILILDDSTSALdaeSEKKVQQALE--HELPDTTTFII-----AEKIVSVinADTILVLDDGKLVA 548
Cdd:PRK10982 154 KIVIMDEPTSSL---TEKEVNHLFTiiRKLKERGCGIVyishkMEEIFQL--CDEITILRDGQWIA 214
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
331-555 7.84e-07

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 51.85  E-value: 7.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 331 GSVEFDHVSFTYPDGDDPTLK---DISFKIKPGQMVGIVGATGAGKSTLAQLIARLYdPTK--GKVKIGGQNIK-----D 400
Cdd:PRK13549 256 GEVILEVRNLTAWDPVNPHIKrvdDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PGRweGEIFIDGKPVKirnpqQ 334
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 401 VTEAAL------RKTVSFVLQRAVLFSGTIASnLRQgnaQAKLHELQRAANMAQASEFIERYNDSFDHeVEERSANFSGG 474
Cdd:PRK13549 335 AIAQGIamvpedRKRDGIVPVMGVGKNITLAA-LDR---FTGGSRIDDAAELKTILESIQRLKVKTAS-PELAIARLSGG 409
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 475 QKQRLSIARGLIAKAPILILDDSTSALD--AESE------KKVQQAL-----EHELPDtttfiiaekIVSVinADTILVL 541
Cdd:PRK13549 410 NQQKAVLAKCLLLNPKILILDEPTRGIDvgAKYEiyklinQLVQQGVaiiviSSELPE---------VLGL--SDRVLVM 478
                        250
                 ....*....|....
gi 492039060 542 DDGKLVAQGTHEEL 555
Cdd:PRK13549 479 HEGKLKGDLINHNL 492
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
350-550 1.27e-06

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 51.65  E-value: 1.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIA-RLYDPTKGK---VKIGGQNIKDVtEAALRKTVSFVLQRAVLF-SGTI 424
Cdd:TIGR00956   77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsNTDGFHIGVegvITYDGITPEEI-KKHYRGDVVYNAETDVHFpHLTV 155
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060   425 ASNLrqgNAQAKLHELQRAANMAQASEFIERYND------SFDHEVEERSAN-----FSGGQKQRLSIARGLIAKAPILI 493
Cdd:TIGR00956  156 GETL---DFAARCKTPQNRPDGVSREEYAKHIADvymatyGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQC 232
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060   494 LDDSTSALDAESEKKVQQALE---HELPDTTTFII---AEKIVSVInaDTILVLDDGKLVAQG 550
Cdd:TIGR00956  233 WDNATRGLDSATALEFIRALKtsaNILDTTPLVAIyqcSQDAYELF--DKVIVLYEGYQIYFG 293
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
353-554 1.39e-06

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 51.07  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 353 ISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI-----KDVTEAAL------RKTVSFVLQRAVlfS 421
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIdirspRDAIRAGImlcpedRKAEGIIPVHSV--A 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 GTIASNLRQGNAQAK--LHELQRAANmaqASEFIERYNdsfdheVEERSA-----NFSGGQKQRLSIARGLIAKAPILIL 494
Cdd:PRK11288 350 DNINISARRHHLRAGclINNRWEAEN---ADRFIRSLN------IKTPSReqlimNLSGGNQQKAILGRWLSEDMKVILL 420
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492039060 495 DDSTSALDAESEKKVQQALeHELPDT--TTFIIAEKIVSVIN-ADTILVLDDGKLVAQGTHEE 554
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVI-YELAAQgvAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
21-261 1.49e-06

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: 50.23  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  21 AIIAILVSAFSGLYQPKLLENIQKALMANQKQAVLSDGIwlVVLGIIAIISGIFN---VYFAAKIAQGVVSDLREDTYAK 97
Cdd:cd18572    1 AFVFLVVAALSELAIPHYTGAVIDAVVADGSREAFYRAV--LLLLLLSVLSGLFSglrGGCFSYAGTRLVRRLRRDLFRS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  98 I--QTFSFgnIKKFSAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIVIIPR-----FwwAPVVMVALIFG 170
Cdd:cd18572   79 LlrQDIAF--FDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRltllaF--ITVPVIALITK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 171 -FGAYVlRQMNslfTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIA 249
Cdd:cd18572  155 vYGRYY-RKLS---KEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQ 230
                        250
                 ....*....|..
gi 492039060 250 YTVIALIVYLIG 261
Cdd:cd18572  231 NGTQVLVLFYGG 242
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
348-562 1.97e-06

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 50.50  E-value: 1.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 348 PTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKD-------------VTEAalRKTVSFVL 414
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneainhgfalVTEE--RRSTGIYA 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 415 QRAVLFSGTIaSNLRQGNAQAKLHELQRaanMAQASEFIErynDSFDHEVEERSAN---FSGGQKQRLSIARGLIAKAPI 491
Cdd:PRK10982 340 YLDIGFNSLI-SNIRNYKNKVGLLDNSR---MKSDTQWVI---DSMRVKTPGHRTQigsLSGGNQQKVIIGRWLLTQPEI 412
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492039060 492 LILDDSTSALDAESEKKVQQ-ALEHELPDTTTFIIAEKIVSVIN-ADTILVLDDGKLV-----AQGTHEELLKTSLVY 562
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQlIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLVAgivdtKTTTQNEILRLASLH 490
PLN03211 PLN03211
ABC transporter G-25; Provisional
350-550 2.45e-06

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 50.26  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIA-RLYDPT-KGKVKIGGQNIkdvTEAALRKTvSFVLQRAVLF------- 420
Cdd:PLN03211  84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKP---TKQILKRT-GFVTQDDILYphltvre 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 421 SGTIASNLRQGNAQAKLHELQRAANMAQASEFIERYN----DSFDHEVeersanfSGGQKQRLSIARGLIAKAPILILDD 496
Cdd:PLN03211 160 TLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENtiigNSFIRGI-------SGGERKRVSIAHEMLINPSLLILDE 232
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 497 STSALDAESEKKVQQALEHelpdtttfiIAEKIVSVINA------------DTILVLDDGKLVAQG 550
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGS---------LAQKGKTIVTSmhqpssrvyqmfDSVLVLSEGRCLFFG 289
GguA NF040905
sugar ABC transporter ATP-binding protein;
350-502 3.47e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.79  E-value: 3.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLA-QLIARLYDP-TKGKVKIGGQ-----NIKDVTEAAL------RKTVSFVLQR 416
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKevdvsTVSDAIDAGLayvtedRKGYGLNLID 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 417 AVLFSGTIASnlrqgnaqakLHELQRAANMAQASEFI--ERYNDSFD---HEVEERSANFSGGQKQRLSIARGLIAKAPI 491
Cdd:NF040905 356 DIKRNITLAN----------LGKVSRRGVIDENEEIKvaEEYRKKMNiktPSVFQKVGNLSGGNQQKVVLSKWLFTDPDV 425
                        170
                 ....*....|.
gi 492039060 492 LILDDSTSALD 502
Cdd:NF040905 426 LILDEPTRGID 436
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
330-504 3.51e-06

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 49.95  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 330 SGSVEFDHVSFTYPDGDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQnikdvTEAALrkt 409
Cdd:PRK11147 315 SGKIVFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK-----LEVAY--- 386
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 410 vsFVLQRAVL-FSGTIASNLRQG------NAQAK--LHELQ-------RAANMAQAsefieryndsfdheveersanFSG 473
Cdd:PRK11147 387 --FDQHRAELdPEKTVMDNLAEGkqevmvNGRPRhvLGYLQdflfhpkRAMTPVKA---------------------LSG 443
                        170       180       190
                 ....*....|....*....|....*....|.
gi 492039060 474 GQKQRLSIARGLIAKAPILILDDSTSALDAE 504
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
40-297 3.60e-06

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: 49.20  E-value: 3.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  40 ENIQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNVYFAAKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAGSLTTRLI 119
Cdd:cd18558   44 LNSSAGPFEKLEEEMTLYAYYYLIIGAIVLITAYIQGSFWGLAAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLA 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 120 NDMNQVMNMMMQLFMQMLRLPILIVGSFIFCIViipRFWWAPVVMVAL--IFGFGAYVLRQMNSLFT-KFQEMMDRISNQ 196
Cdd:cd18558  124 DDVSKINEGIGDKIGVIFQNIATFGTGFIIGFI---RGWKLTLVILAIspVLGLSAVVWAKILSGFTdKEKKAYAKAGAV 200
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 197 AQETLQGVRVVKSFNQGPQEIKKFDQTSDQLNDYNIVIGYWFSAIMPAFQMIAYTVIALIVYLIGKNITAHPSDIAvvsp 276
Cdd:cd18558  201 AEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIG---- 276
                        250       260
                 ....*....|....*....|.
gi 492039060 277 fvnYVLTLLFTIMIAGMTLMQ 297
Cdd:cd18558  277 ---EVLTVFFSVLIGAFSAGQ 294
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
346-563 6.40e-06

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 48.86  E-value: 6.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 346 DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVLQR--AVLFS-- 421
Cdd:PRK10938  15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRnnTDMLSpg 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 ----GTIASNLrqgnAQAKLHELQRAANMAQasEFieryndSFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDS 497
Cdd:PRK10938  95 eddtGRTTAEI----IQDEVKDPARCEQLAQ--QF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 498 TSALDAESEKKVQQALEHelpdtttfIIAEKI--VSVIN--------ADTILVLDDGKLVAQGTHEELLKTSLVYQ 563
Cdd:PRK10938 163 FDGLDVASRQQLAELLAS--------LHQSGItlVLVLNrfdeipdfVQFAGVLADCTLAETGEREEILQQALVAQ 230
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
333-557 6.62e-06

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 48.73  E-value: 6.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 333 VEFDHVSFTYPDGddPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVK------IG--GQNI-----K 399
Cdd:PRK15064 320 LEVENLTKGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKwsenanIGyyAQDHaydfeN 397
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 400 DVT--------------EAALRKTvsfvLQRaVLFSGtiasnlrqgnaqaklhelqraanmaqasefieryndsfdHEVE 465
Cdd:PRK15064 398 DLTlfdwmsqwrqegddEQAVRGT----LGR-LLFSQ---------------------------------------DDIK 433
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 466 ERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAESEKKVQQALEhELPDTTTFIIAEK-IVSVInADTILVLDDG 544
Cdd:PRK15064 434 KSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE-KYEGTLIFVSHDReFVSSL-ATRIIEITPD 511
                        250
                 ....*....|....
gi 492039060 545 KLVA-QGTHEELLK 557
Cdd:PRK15064 512 GVVDfSGTYEEYLR 525
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
21-297 7.55e-06

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: 48.01  E-value: 7.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  21 AIIAILVSAFSGLYQPKLLENI-----------QKALMANQKQAVLsdgIWLVVLGIIAIISGIFNVYFAAkIAQGVVSD 89
Cdd:cd18780    1 GTIALLVSSGTNLALPYFFGQVidavtnhsgsgGEEALRALNQAVL---ILLGVVLIGSIATFLRSWLFTL-AGERVVAR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  90 LREDTYAKI--QTFSFGNIKKfsAGSLTTRLINDMNQVMNMMMQLFMQMLRLPILIVGSFIF-----------CIVIIPr 156
Cdd:cd18780   77 LRKRLFSAIiaQEIAFFDVTR--TGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFmfttswkltlvMLSVVP- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 157 fwwaPVVMVALIFGfgayvlRQMNSLFTKFQEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFdqTSDQLNDYNIVIGY 236
Cdd:cd18780  154 ----PLSIGAVIYG------KYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRY--SEKINESYLLGKKL 221
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492039060 237 -----WFSAIMPAFQMIAytvIALIVYLIGKNITAHPSDIAVVSPFVNYVLTLLFTI-MIAGM--TLMQ 297
Cdd:cd18780  222 arasgGFNGFMGAAAQLA---IVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFaFLSSLygDFMQ 287
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
365-514 1.75e-05

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


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 45.77  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 365 IVGATGAGKSTLAQLIAR-LYDPTKGKVKIGGQNIKDVTEAAlrkTVSFVLQ------RAVLFSGTIASNLRQ------- 430
Cdd:COG0419   28 IVGPNGAGKSTILEAIRYaLYGKARSRSKLRSDLINVGSEEA---SVELEFEhggkryRIERRQGEFAEFLEAkpserke 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 431 -----------GNAQAKLHELQRAAN--MAQASEFIERYNDSFDHEVEERSAN-FSGGQKQRLSIARGLiakapILILDd 496
Cdd:COG0419  105 alkrllgleiyEELKERLKELEEALEsaLEELAELQKLKQEILAQLSGLDPIEtLSGGERLRLALADLL-----SLILD- 178
                        170
                 ....*....|....*...
gi 492039060 497 sTSALDAESEKKVQQALE 514
Cdd:COG0419  179 -FGSLDEERLERLLDALE 195
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
345-514 2.82e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 46.93  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 345 GDDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIA-----------RLYdptkGKVKIGGQNIKDVteaalRKTVSFV 413
Cdd:PRK10938 271 NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITgdhpqgysndlTLF----GRRRGSGETIWDI-----KKHIGYV 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 414 LQ------------RAVLFSGTIAS-NLRQG--NAQAKLhelqraanmaqASEFIERYNdsfdheVEERSAN-----FSG 473
Cdd:PRK10938 342 SSslhldyrvstsvRNVILSGFFDSiGIYQAvsDRQQKL-----------AQQWLDILG------IDKRTADapfhsLSW 404
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 492039060 474 GQkQRLS-IARGLIAKAPILILDDSTSALDAESEKKVQQALE 514
Cdd:PRK10938 405 GQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVD 445
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
350-539 3.86e-05

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 46.54  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNI-----KDVTEAAlrktVSFVLQRAVLFSG-T 423
Cdd:PRK10762  20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpKSSQEAG----IGIIHQELNLIPQlT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 424 IASNLRQGNA-QAKLHELQRAANMAQASEFIERYNDSfdHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSAL- 501
Cdd:PRK10762  96 IAENIFLGREfVNRFGRIDWKKMYAEADKLLARLNLR--FSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALt 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492039060 502 DAESEK--KVQQALE----------HELP-------DTTTF----IIAEKIVSVINADTIL 539
Cdd:PRK10762 174 DTETESlfRVIRELKsqgrgivyisHRLKeifeicdDVTVFrdgqFIAEREVADLTEDSLI 234
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
346-561 5.00e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 45.93  E-value: 5.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 346 DDPTLKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLyDPTK-GKVKIGGQNIKDVTE-AALRKTVSFVLQ--RAVLFS 421
Cdd:PRK09700 275 DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV-DKRAgGEIRLNGKDISPRSPlDAVKKGMAYITEsrRDNGFF 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 422 G--TIASNL---------RQGNAQAKLHELQRAANMAQASEFIERYNDSFDHEVEErsanFSGGQKQRLSIARGLIAKAP 490
Cdd:PRK09700 354 PnfSIAQNMaisrslkdgGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITE----LSGGNQQKVLISKWLCCCPE 429
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 491 ILILDDSTSALDAESEKKVQQaLEHELPDTTTFIIA-----EKIVSVinADTILVLDDGKLVA------QGTHEELLKTS 559
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYK-VMRQLADDGKVILMvsselPEIITV--CDRIAVFCEGRLTQiltnrdDMSEEEIMAWA 506

                 ..
gi 492039060 560 LV 561
Cdd:PRK09700 507 LP 508
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
350-577 8.71e-05

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 44.42  E-value: 8.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 350 LKDISFKIKPGQMVGIVGATGAGKSTLAQLIARLYDPTKGKVKIGGQNIKDVTEAALRKTVSFVlqRAVLFsgtiaSNLR 429
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGI--ENIEF-----KMLC 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 430 QGNAQAKLHELqraanMAQASEFIEryndsFDHEVEERSANFSGGQKQRLSIARGLIAKAPILILDDSTSALDAE-SEKK 508
Cdd:PRK13546 113 MGFKRKEIKAM-----TPKIIEFSE-----LGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTfAQKC 182
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 509 VQQALEHELPDTTTFIIAEKIVSVINADT-ILVLDDGKLVAQGTHEELLKTslvYQEIFKTQKGKKGGNE 577
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLGQVRQFCTkIAWIEGGKLKDYGELDDVLPK---YEAFLNDFKKKSKAEQ 249
ABC_6TM_ABCC_D2 cd18580
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...
141-310 1.92e-04

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: 43.65  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 141 ILIVGSFIFCIVIIPRFWWA-PVVMVALIFGFGAYV-----LRQMNS-----LFTKFqemmdrisnqaQETLQGVRVVKS 209
Cdd:cd18580  125 FSVLGSLIVIAIVSPYFLIVlPPLLVVYYLLQRYYLrtsrqLRRLESesrspLYSHF-----------SETLSGLSTIRA 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 210 FNQGpqeiKKFDQTSDQLNDYNIVIGYWFSAIMPAFQM--------IAYTVIALIVYLIGkniTAHPSDIAVVspfVNYV 281
Cdd:cd18580  194 FGWQ----ERFIEENLRLLDASQRAFYLLLAVQRWLGLrldllgalLALVVALLAVLLRS---SISAGLVGLA---LTYA 263
                        170       180       190
                 ....*....|....*....|....*....|..
gi 492039060 282 LTLLFTIMiagMTLMQFSRANISLG---RIRE 310
Cdd:cd18580  264 LSLTGSLQ---WLVRQWTELETSMVsveRILE 292
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
472-555 3.82e-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: 43.46  E-value: 3.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  472 SGGQKQRLSIARGLIAKA---PILILDDSTSALDAESEKKVQQALeHELPDT-TTFIIAEKIVSVI-NADTILVL----- 541
Cdd:TIGR00630 831 SGGEAQRIKLAKELSKRStgrTLYILDEPTTGLHFDDIKKLLEVL-QRLVDKgNTVVVIEHNLDVIkTADYIIDLgpegg 909
                          90
                  ....*....|....*
gi 492039060  542 -DDGKLVAQGTHEEL 555
Cdd:TIGR00630 910 dGGGTVVASGTPEEV 924
ABC_6TM_LapB_like cd18587
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ...
147-263 5.33e-03

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: 38.96  E-value: 5.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 147 FIFCIVIiprFW------WAPVVMVALIFGFGAYVLRQMNSLFtkfQEMMdRISNQAQ----ETLQGVRVVKSFNQGPQE 216
Cdd:cd18587  129 LLFLAVI---ALiggplaLVPLVAIPLVLLYGLLLQKPLRRLV---EESM-RESAQKNallvESLSGLETIKALGAEGRM 201
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492039060 217 IKKFDQTSDQLNDYNIVIGYWFSAIM---PAFQMIAYTVIALI-VYLIGKN 263
Cdd:cd18587  202 QRRWEEAVAALARSSLKSRLLSSSATnfaQFVQQLVTVAIVIVgVYLISDG 252
ABC_6TM_AarD_CydDC_like cd18561
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...
42-227 6.52e-03

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: 38.80  E-value: 6.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060  42 IQKALMANQKQAVLSDGIWLVVLGIIAIISGIFNV---------YFAAKIAQGVVSDLREDTYAKIQTFSFGNIKKFSAG 112
Cdd:cd18561   14 AQAWLLARALARIFAGGPWEDIMPPLAGIAGVIVLraallwlreRVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492039060 113 SLTTRLINDMNQVMNMMMQLfmqmlrLP---ILIVGSFIFCIVIIPRFWWAPV---VMVALIFGFGAYVLRQMNSLFTKF 186
Cdd:cd18561   94 ELQTTVVDGVEALEAYYGRY------LPqllVALLGPLLILIYLFFLDPLVALillVFALLIPLSPALWDRLAKDTGRRH 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 492039060 187 QEMMDRISNQAQETLQGVRVVKSFNQGPQEIKKFDQTSDQL 227
Cdd:cd18561  168 WAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDL 208
PRK09270 PRK09270
nucleoside triphosphate hydrolase domain-containing protein; Reviewed
336-383 7.10e-03

nucleoside triphosphate hydrolase domain-containing protein; Reviewed


Pssm-ID: 236442  Cd Length: 229  Bit Score: 38.38  E-value: 7.10e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492039060 336 DHVSFTYPDGD-----DPTLKDISFKIKPGQ---MVGIVGATGAGKSTLAQLIARL 383
Cdd:PRK09270   1 LKVQAQYRDEEieavhKPLLRRLAALQAEPQrrtIVGIAGPPGAGKSTLAEFLEAL 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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