|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
15-581 |
7.23e-173 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 502.39 E-value: 7.23e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 15 NAFQTLLHLYQGNYWRFAMSGLFFIIKHLPSWLMPIAIANVINAASSKdsSQLQAIYFNAFLMACLIGQNILTNYFHVKY 94
Cdd:COG1132 7 KLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAG--GDLSALLLLLLLLLGLALLRALLSYLQRYL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 95 HSTSIRQVEAGLRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVF 174
Cdd:COG1132 85 LARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 175 MFFLLTVPLAAFVTLFFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQ 254
Cdd:COG1132 165 LIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 255 SVFGSVSWASFQIFQLICLIFTGILALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGMESITSIGELL-IAGDV 333
Cdd:COG1132 245 ALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLdEPPEI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 334 ETYHGKKKIQHLDGNFRFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQP 413
Cdd:COG1132 325 PDPPGAVPLPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 414 LDELDMRSVRNYLAVVPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQ 493
Cdd:COG1132 404 IRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQ 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 494 CISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLA 573
Cdd:COG1132 484 RIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA 563
|
....*...
gi 1158646300 574 QKGYFYRL 581
Cdd:COG1132 564 RGGLYARL 571
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
43-581 |
4.64e-137 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 415.00 E-value: 4.64e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 43 LPSWLMPIAIANVIN-AASSKDSSQLQAIyfnAFLMACLIGQNILTNYFHVKYHSTSIRQVEAGLRATLIKKIQELSIPY 121
Cdd:COG2274 170 LLALATPLFTQVVIDrVLPNQDLSTLWVL---AIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRLPLSF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 122 QKELQSGRIQSKIiRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFVTLFFRKRIRQSNSD 201
Cdd:COG2274 247 FESRSVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSRE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 202 FRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIFQLICLIFTGILAL 281
Cdd:COG2274 326 ESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVI 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 282 QGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGMESITSIGELLiAGDVETYHGKKKIQ--HLDGNFRFEDVSFLYP 359
Cdd:COG2274 406 DGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDIL-DLPPEREEGRSKLSlpRLKGDIELENVSFRYP 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 360 DSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQTTLLFSAS 439
Cdd:COG2274 485 GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGT 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 440 IKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDN 519
Cdd:COG2274 565 IRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDA 644
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 520 QSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYFYRL 581
Cdd:COG2274 645 ETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
350-581 |
2.95e-105 |
|
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: 316.48 E-value: 2.95e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVV 429
Cdd:cd03251 2 EFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIIL 509
Cdd:cd03251 82 SQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 510 LDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYFYRL 581
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
29-583 |
8.72e-105 |
|
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: 327.06 E-value: 8.72e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 29 WRFAMSGLFFIIKHLPSWLMPIAIANVINAASSK-DSSQLQAIYFNAFLMACLIGqniLTNYFHVKYHSTSIRQVEAGLR 107
Cdd:TIGR02203 14 AGLVLAGVAMILVAATESTLAALLKPLLDDGFGGrDRSVLWWVPLVVIGLAVLRG---ICSFVSTYLLSWVSNKVVRDIR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 108 ATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFV 187
Cdd:TIGR02203 91 VRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSIL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 188 TLFFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIyeKGFHLDILQSvfGSVSWASFQI 267
Cdd:TIGR02203 171 MRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRN--RRLAMKMTSA--GSISSPITQL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 268 FQLICLIF----TGILALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGMESITSIGELLIAGDvETYHGKKKIQ 343
Cdd:TIGR02203 247 IASLALAVvlfiALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPP-EKDTGTRAIE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 344 HLDGNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVR 423
Cdd:TIGR02203 326 RARGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 424 NYLAVVPQTTLLFSASIKENITYG-LKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALI 502
Cdd:TIGR02203 406 RQVALVSQDVVLFNDTIANNIAYGrTEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 503 RQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYFYRLK 582
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLH 565
|
.
gi 1158646300 583 N 583
Cdd:TIGR02203 566 N 566
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
350-581 |
1.08e-99 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 302.54 E-value: 1.08e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLK-PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAV 428
Cdd:cd03249 2 EFKNVSFRYPSRPDvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 VPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPKII 508
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 509 LLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYFYRL 581
Cdd:cd03249 162 LLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
46-576 |
1.11e-98 |
|
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: 310.92 E-value: 1.11e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 46 WLMPIAIANVINAASSKdSSQLQAIyfnAFLMACLIGQnILTNYFHVKYHSTSIRQVEAGLRATLIKKIQELSIPYQKEL 125
Cdd:COG4988 38 WLLASLLAGLIIGGAPL-SALLPLL---GLLLAVLLLR-ALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 126 QSGRIQSKIIRDVEAIQT-LS---SQVFVSGLnIAVNLFVALgitLYKSPVVFMFFLLTVPLAAFVTLFFRKRIRQSNSD 201
Cdd:COG4988 113 STGELATLLTEGVEALDGyFArylPQLFLAAL-VPLLILVAV---FPLDWLSGLILLVTAPLIPLFMILVGKGAAKASRR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 202 FRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNK---HFTQIYEK--------GFHLDIlqsvFGSVSWAsfqifql 270
Cdd:COG4988 189 QWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEaseDFRKRTMKvlrvaflsSAVLEF----FASLSIA------- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 271 ICLIFTGILALQGRIqpgdvvmyqTYFTTIVnsvsgMITLIP--------------TISKGMESITSIGELLIAGDVETY 336
Cdd:COG4988 258 LVAVYIGFRLLGGSL---------TLFAALF-----VLLLAPefflplrdlgsfyhARANGIAAAEKIFALLDAPEPAAP 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 337 HGKKKIQHLDGN-FRFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLD 415
Cdd:COG4988 324 AGTAPLPAAGPPsIELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLS 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 416 ELDMRSVRNYLAVVPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCI 495
Cdd:COG4988 403 DLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 496 SIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQK 575
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
.
gi 1158646300 576 G 576
Cdd:COG4988 563 G 563
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
114-581 |
4.76e-98 |
|
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: 310.60 E-value: 4.76e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 114 IQELSIPYQKELQSGRIqSKII-RDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMF-FLLTVPLAAFVTLFF 191
Cdd:COG5265 121 LHALSLRFHLERQTGGL-SRDIeRGTKGIEFLLRFLLFNILPTLLEIALVAGILLVKYDWWFALiTLVTVVLYIAFTVVV 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 192 -RKRIRqsnsdFRQEMEE----TSAKVIE-------VielapiaRAHGLEKHETTRLNKHFTQiYEKG--------FHLD 251
Cdd:COG5265 200 tEWRTK-----FRREMNEadseANTRAVDsllnyetV-------KYFGNEAREARRYDEALAR-YERAavksqtslALLN 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 252 ILQSVfgsvswasfqIFQL---ICLIFTGILALQGRIQPGDVVMYQTYfttivnsvsgMITL-IPTISKGM------ESI 321
Cdd:COG5265 267 FGQAL----------IIALgltAMMLMAAQGVVAGTMTVGDFVLVNAY----------LIQLyIPLNFLGFvyreirQAL 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 322 TSIGELL----IAGDVETYHGKKKIQHLDGNFRFEDVSFLYpDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLI 397
Cdd:COG5265 327 ADMERMFdlldQPPEVADAPDAPPLVVGGGEVRFENVSFGY-DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLF 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 398 GFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLD 477
Cdd:COG5265 406 RFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYD 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 478 TLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVI 557
Cdd:COG5265 486 TRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVL 565
|
490 500
....*....|....*....|....
gi 1158646300 558 DEGKIVEIGTYEKLLAQKGYFYRL 581
Cdd:COG5265 566 EAGRIVERGTHAELLAQGGLYAQM 589
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
104-583 |
1.44e-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: 300.53 E-value: 1.44e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 104 AGLRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQVF---VSGLniAVNLFVALGITLYKSPVVFMFFLLT 180
Cdd:COG4987 88 ADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLlplLVAL--LVILAAVAFLAFFSPALALVLALGL 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 181 VPLAAFVTLFFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSV 260
Cdd:COG4987 166 LLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQAL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 261 SWASFQIFQLICLIFTGILALQGRIQPGDVVMyqtyFTTIVNSVSGMITLIPT----ISKGMESITSIGELLIAGDVETY 336
Cdd:COG4987 246 LQLAAGLAVVAVLWLAAPLVAAGALSGPLLAL----LVLAALALFEALAPLPAaaqhLGRVRAAARRLNELLDAPPAVTE 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 337 HGKKKIQHLDGNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDE 416
Cdd:COG4987 322 PAEPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 417 LDMRSVRNYLAVVPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCIS 496
Cdd:COG4987 402 LDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLA 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 497 IARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKG 576
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNG 561
|
....*..
gi 1158646300 577 YFYRLKN 583
Cdd:COG4987 562 RYRQLYQ 568
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
350-581 |
1.10e-93 |
|
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: 286.82 E-value: 1.10e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVV 429
Cdd:cd03253 2 EFENVTFAYDPG-RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIIL 509
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 510 LDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYFYRL 581
Cdd:cd03253 161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
347-576 |
5.97e-92 |
|
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: 282.19 E-value: 5.97e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 347 GNFRFEDVSFLYpDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYL 426
Cdd:cd03254 1 GEIEFENVNFSY-DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPK 506
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 507 IILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKG 576
Cdd:cd03254 160 ILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-582 |
2.89e-85 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 280.07 E-value: 2.89e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 24 YQGNYWRFAMSGLFFIIKhlpSWLMPIAIANVINAASS--KDSSQLQAIYFNAFLMACL-IGQNILTNYFHVKYHSTSIR 100
Cdd:TIGR00958 155 LSGRDWPWLISAFVFLTL---SSLGEMFIPFYTGRVIDtlGGDKGPPALASAIFFMCLLsIASSVSAGLRGGSFNYTMAR 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 101 qVEAGLRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAI-QTLSSQVFVsGLNIAVNLFVALGITLYKSPVVFMFFLL 179
Cdd:TIGR00958 232 -INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMsRSLSLNVNV-LLRNLVMLLGLLGFMLWLSPRLTMVTLI 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 180 TVPLAAFVTLFFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGS 259
Cdd:TIGR00958 310 NLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLW 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 260 VSWASFQIFQLICLIFTGILALQGRIQPGDVV---MYQTYFTtivNSVSGMITLIPTISKGMESITSIGELLIAGDVETY 336
Cdd:TIGR00958 390 TTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVsflLYQEQLG---EAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 337 HGKKKIQHLDGNFRFEDVSFLYPD-SLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLD 415
Cdd:TIGR00958 467 TGTLAPLNLEGLIEFQDVSFSYPNrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 416 ELDMRSVRNYLAVVPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCI 495
Cdd:TIGR00958 547 QYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRI 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 496 SIARALIRQPKIILLDEATSALDNQSEKKIQQALNYltETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQK 575
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ 704
|
....*..
gi 1158646300 576 GYFYRLK 582
Cdd:TIGR00958 705 GCYKHLV 711
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
270-581 |
2.54e-83 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 271.83 E-value: 2.54e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 270 LICLIFTGI-LALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGMESITSIGELLIA-GDVETYHGKKKIQHLDG 347
Cdd:PRK13657 254 MLAILVLGAaLVQKGQLRVGEVVAFVGFATLLIGRLDQVVAFINQVFMAAPKLEEFFEVEDAvPDVRDPPGAIDLGRVKG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 348 NFRFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLA 427
Cdd:PRK13657 334 AVEFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 VVPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPKI 507
Cdd:PRK13657 413 VVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPI 492
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 508 ILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYFYRL 581
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAAL 566
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
106-581 |
2.29e-81 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 266.50 E-value: 2.29e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 106 LRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQVFVS----GLNIaVNLFValgITLYKSPVVFMFFLLTV 181
Cdd:PRK11176 100 MRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITvvreGASI-IGLFI---MMFYYSWQLSLILIVIA 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 182 PLAAFVTLFFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVfgsvs 261
Cdd:PRK11176 176 PIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSI----- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 262 waSFQIFQLIcliftGILALQgriqpgdVVMYQTYFTTIVNSV---------SGMITLI-PTIS---------KGMESIT 322
Cdd:PRK11176 251 --SDPIIQLI-----ASLALA-------FVLYAASFPSVMDTLtagtitvvfSSMIALMrPLKSltnvnaqfqRGMAACQ 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 323 SIGELLiagDVETYH--GKKKIQHLDGNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFI 400
Cdd:PRK11176 317 TLFAIL---DLEQEKdeGKRVIERAKGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFY 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 401 QPTSGKIFLDDQPLDELDMRSVRNYLAVVPQTTLLFSASIKENITYGLKNV-SKERLDEVIEAAQLSSLIDQLPDGLDTL 479
Cdd:PRK11176 394 DIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTV 473
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 480 VGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDE 559
Cdd:PRK11176 474 IGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVED 553
|
490 500
....*....|....*....|..
gi 1158646300 560 GKIVEIGTYEKLLAQKGYFYRL 581
Cdd:PRK11176 554 GEIVERGTHAELLAQNGVYAQL 575
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
25-581 |
5.10e-81 |
|
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: 267.98 E-value: 5.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 25 QGNYWRFAMSGLFFIIKHLPSWLMPIAIANVINAA-SSKDSSQLQAIYFnaFLMACLIGQNIltnyFHVKYHSTSIR--- 100
Cdd:TIGR03797 132 RGARRDLLAILAMGLLGTLLGMLVPIATGILIGTAiPDADRSLLVQIAL--ALLAAAVGAAA----FQLAQSLAVLRlet 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 101 QVEAGLRATLIKKIQELSIPYQKELQSGRIQSKiirdVEAIQTLSSQVFVSGLNIAVNLFVA---LGITLYKSP----VV 173
Cdd:TIGR03797 206 RMDASLQAAVWDRLLRLPVSFFRQYSTGDLASR----AMGISQIRRILSGSTLTTLLSGIFAllnLGLMFYYSWklalVA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 174 FMFFLLTVPLAAFVTLFFRKRIRQSnsdfrQEME-ETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDI 252
Cdd:TIGR03797 282 VALALVAIAVTLVLGLLQVRKERRL-----LELSgKISGLTVQLINGISKLRVAGAENRAFARWAKLFSRQRKLELSAQR 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 253 LQSVFGSVSwASFQIFQLICLI-FTGILALQGRIQPGDVVMYQTYFTT-------IVNSVSGMITLIPTiskgMESITSI 324
Cdd:TIGR03797 357 IENLLTVFN-AVLPVLTSAALFaAAISLLGGAGLSLGSFLAFNTAFGSfsgavtqLSNTLISILAVIPL----WERAKPI 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 325 GELLiagdVETYHGKKKIQHLDGNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTS 404
Cdd:TIGR03797 432 LEAL----PEVDEAKTDPGKLSGAIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPES 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 405 GKIFLDDQPLDELDMRSVRNYLAVVPQTTLLFSASIKENITYGlknvSKERLDEVIEAAQLSSL---IDQLPDGLDTLVG 481
Cdd:TIGR03797 508 GSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGG----APLTLDEAWEAARMAGLaedIRAMPMGMHTVIS 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 482 EHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLteTPTTFIVAHRLSTIKEADKIVVIDEGK 561
Cdd:TIGR03797 584 EGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGR 661
|
570 580
....*....|....*....|
gi 1158646300 562 IVEIGTYEKLLAQKGYFYRL 581
Cdd:TIGR03797 662 VVQQGTYDELMAREGLFAQL 681
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
350-561 |
3.90e-79 |
|
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: 246.91 E-value: 3.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVV 429
Cdd:cd03228 2 EFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLFSASIKENItyglknvskerldevieaaqlsslidqlpdgldtlvgehgnkLSGGQKQCISIARALIRQPKIIL 509
Cdd:cd03228 82 PQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 510 LDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGK 561
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
347-563 |
1.04e-75 |
|
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: 239.80 E-value: 1.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 347 GNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYL 426
Cdd:cd03245 1 GRIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPK 506
Cdd:cd03245 81 GYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 507 IILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIV 563
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
343-562 |
1.21e-72 |
|
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: 231.98 E-value: 1.21e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 343 QHLDGNFRFEDVSFLYPD-SLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRS 421
Cdd:cd03248 6 DHLKGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 422 VRNYLAVVPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARAL 501
Cdd:cd03248 86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 502 IRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKI 562
Cdd:cd03248 166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
351-581 |
6.44e-72 |
|
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: 230.45 E-value: 6.44e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 351 FEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVP 430
Cdd:cd03252 3 FEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 431 QTTLLFSASIKENITYGLKNVSKERldeVIEAAQLS---SLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPKI 507
Cdd:cd03252 83 QENVLFNRSIRDNIALADPGMSMER---VIEAAKLAgahDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 508 ILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYFYRL 581
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
347-567 |
1.56e-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: 223.52 E-value: 1.56e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 347 GNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYL 426
Cdd:cd03244 1 GDIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQTTLLFSASIKENITyGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPK 506
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLD-PFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 507 IILLDEATSALDNQSEKKIQQAL-NYLTETpTTFIVAHRLSTIKEADKIVVIDEGKIVEIGT 567
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIrEAFKDC-TVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
109-581 |
9.37e-69 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 235.79 E-value: 9.37e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 109 TLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALgITLYKSPVVFMFFLLTVPLAAFVT 188
Cdd:TIGR01193 234 SYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGL-FLVRQNMLLFLLSLLSIPVYAVII 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 189 LFFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIF 268
Cdd:TIGR01193 313 ILFKRTFNKLNHDAMQANAVLNSSIIEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLIL 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 269 QLICLIFTGILALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGMESITSIGE-LLIAGDVETYHGKKKIQHLDG 347
Cdd:TIGR01193 393 NVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvYLVDSEFINKKKRTELNNLNG 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 348 NFRFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLA 427
Cdd:TIGR01193 473 DIVINDVSYSYGYG-SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFIN 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 VVPQTTLLFSASIKENITYGLK-NVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPK 506
Cdd:TIGR01193 552 YLPQEPYIFSGSILENLLLGAKeNVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 507 IILLDEATSALDNQSEKKIQQALNYLTETpTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYFYRL 581
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNLQDK-TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
347-581 |
3.38e-68 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 231.53 E-value: 3.38e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 347 GNFRFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYL 426
Cdd:PRK10790 339 GRIDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQTTLLFSASIKENITYGlKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPK 506
Cdd:PRK10790 418 AMVQQDPVVLADTFLANVTLG-RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 507 IILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYFYRL 581
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQM 571
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
32-557 |
4.63e-68 |
|
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: 229.87 E-value: 4.63e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 32 AMSGLFFIIKhlpSWLMPIAIANVINAASskdssQLQAIYFNAFLMACLIGQNILTNYFHVKYHSTSIRQVEAGLRATLI 111
Cdd:TIGR02857 13 VLGALLIIAQ---AWLLARVVDGLISAGE-----PLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 112 KKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQvFVSGLNIAVNLFVALGIT-LYKSPVVFMFFLLTVPL-AAFVTL 189
Cdd:TIGR02857 85 EAVAALGPRWLQGRPSGELATLALEGVEALDGYFAR-YLPQLVLAVIVPLAILAAvFPQDWISGLILLLTAPLiPIFMIL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 190 FFRKRIRQSNSDFRqEMEETSAKVIEVIELAPIARAHGLEKHETTRLnKHFTQIYEKGfHLDILQSVFGSvswaSFqIFQ 269
Cdd:TIGR02857 164 IGWAAQAAARKQWA-ALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAI-RRSSEEYRER-TMRVLRIAFLS----SA-VLE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 270 LICLIFTGILALQ-G-RIQPGDVVMYQTYFTTIvnsvsgmitLIPTI--------------SKGMESITSIGELLIAGDV 333
Cdd:TIGR02857 236 LFATLSVALVAVYiGfRLLAGDLDLATGLFVLL---------LAPEFylplrqlgaqyharADGVAAAEALFAVLDAAPR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 334 ETYHGKKKIQHLDGNFRFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQP 413
Cdd:TIGR02857 307 PLAGKAPVTAAPASSLEFSGVSVAYPGR-RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 414 LDELDMRSVRNYLAVVPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQ 493
Cdd:TIGR02857 386 LADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQ 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 494 CISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVI 557
Cdd:TIGR02857 466 RLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
323-581 |
4.04e-66 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 225.88 E-value: 4.04e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 323 SIGELLIAGDVETYHGKKKIQHLDGN-FRFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIq 401
Cdd:PRK11174 323 SLVTFLETPLAHPQQGEKELASNDPVtIEAEDLEILSPDG-KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 402 PTSGKIFLDDQPLDELDMRSVRNYLAVVPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVG 481
Cdd:PRK11174 401 PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIG 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 482 EHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGK 561
Cdd:PRK11174 481 DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQ 560
|
250 260
....*....|....*....|
gi 1158646300 562 IVEIGTYEKLLAQKGYFYRL 581
Cdd:PRK11174 561 IVQQGDYAELSQAGGLFATL 580
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
347-582 |
3.73e-64 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 220.47 E-value: 3.73e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 347 GNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYL 426
Cdd:PRK11160 337 VSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQlPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPK 506
Cdd:PRK11160 417 SVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAP 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1158646300 507 IILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYFYRLK 582
Cdd:PRK11160 496 LLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLK 571
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
267-581 |
7.11e-63 |
|
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: 217.45 E-value: 7.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 267 IFQLICLIFTGILALQGRIQPGDVVMYQTYFTTIV---NSVSGMITLIPTISKGMESITSIGELLIagDVETYHGKKKIQ 343
Cdd:TIGR01192 252 ISMMCILVIGTVLVIKGELSVGEVIAFIGFANLLIgrlDQMSGFITQIFEARAKLEDFFDLEDSVF--QREEPADAPELP 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 344 HLDGNFRFEDVSFLYPDSLKPIIDhFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVR 423
Cdd:TIGR01192 330 NVKGAVEFRHITFEFANSSQGVFD-VSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLR 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 424 NYLAVVPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIR 503
Cdd:TIGR01192 409 KSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILK 488
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 504 QPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYFYRL 581
Cdd:TIGR01192 489 NAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKL 566
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
255-574 |
1.08e-62 |
|
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: 216.15 E-value: 1.08e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 255 SVFGSVSwASFQIFQLICLIFTG-ILALQGRIQPGdvVMyqtyfttIVNS---------VSGMITLIPTISKGMESITSI 324
Cdd:COG4618 239 GGFSALS-KFLRLLLQSAVLGLGaYLVIQGEITPG--AM-------IAASilmgralapIEQAIGGWKQFVSARQAYRRL 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 325 GELLiagdvETYHGKKKIQHL---DGNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQ 401
Cdd:COG4618 309 NELL-----AAVPAEPERMPLprpKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWP 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 402 PTSGKIFLDDQPLDELDMRSVRNYLAVVPQTTLLFSASIKENITyglknvskeRLDE-----VIEAAQLSS---LIDQLP 473
Cdd:COG4618 384 PTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIA---------RFGDadpekVVAAAKLAGvheMILRLP 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 474 DGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTT-FIVAHRLSTIKEAD 552
Cdd:COG4618 455 DGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATvVVITHRPSLLAAVD 534
|
330 340
....*....|....*....|..
gi 1158646300 553 KIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:COG4618 535 KLLVLRDGRVQAFGPRDEVLAR 556
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
349-575 |
5.78e-57 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 191.01 E-value: 5.78e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAV 428
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 VPQ--TTLLFSASIKENITYGLKN--VSKE----RLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARA 500
Cdd:COG1122 80 VFQnpDDQLFAPTVEEDVAFGPENlgLPREeireRVEEALELVGLEHLADRPP-----------HELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 501 LIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVA-HRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQK 575
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVAElADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
355-580 |
3.03e-54 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 193.39 E-value: 3.03e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 355 SFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQTTL 434
Cdd:PRK10789 320 QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 435 LFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEAT 514
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDAL 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1158646300 515 SALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYfYR 580
Cdd:PRK10789 480 SAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGW-YR 544
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
346-561 |
5.84e-53 |
|
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: 179.59 E-value: 5.84e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 346 DGNFRFEDVSFLYPDSLKPIidhfSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFlddqpldeldmrsVRNY 425
Cdd:cd03250 5 DASFTWDSGEQETSFTLKDI----NLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS-------------VPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 426 LAVVPQTTLLFSASIKENITYGlKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQP 505
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFG-KPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYSDA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 506 KIILLDEATSALDNQSEKKI-QQALN-YLTETPTTFIVAHRLSTIKEADKIVVIDEGK 561
Cdd:cd03250 147 DIYLLDDPLSAVDAHVGRHIfENCILgLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
350-561 |
1.14e-52 |
|
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: 178.81 E-value: 1.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVV 429
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQ--TTLLFSASIKENITYGLKN------VSKERLDEVIEAAQLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIARAL 501
Cdd:cd03225 81 FQnpDDQFFGPTVEEEVAFGLENlglpeeEIEERVEEALELVGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 502 IRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVA-HRLSTIKE-ADKIVVIDEGK 561
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
349-562 |
2.74e-52 |
|
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: 176.64 E-value: 2.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAV 428
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 VPQTTLLFSASIKENItyglknvskerldevieaaqlsslidqlpdgldtlvgehgnkLSGGQKQCISIARALIRQPKII 508
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 509 LLDEATSALDNQSEKKIQQALNYLTETPTTFI-VAHRLSTIKEADKIVVIDEGKI 562
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAIAALKAAGATRIvIAHRPETLASADRILVLEDGRV 173
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
256-574 |
2.99e-51 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 184.86 E-value: 2.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 256 VFGSVSWASFQIFQLICLIFTGILALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGMESITSIGELLIAgdVET 335
Cdd:TIGR01842 226 MLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQAYKRLNELLAN--YPS 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 336 YHGKKKIQHLDGNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLD 415
Cdd:TIGR01842 304 RDPAMPLPEPEGHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 416 ELDMRSVRNYLAVVPQTTLLFSASIKENITYGLKNVSKErldEVIEAAQLS---SLIDQLPDGLDTLVGEHGNKLSGGQK 492
Cdd:TIGR01842 384 QWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPE---KIIEAAKLAgvhELILRLPDGYDTVIGPGGATLSGGQR 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 493 QCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYL-TETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKL 571
Cdd:TIGR01842 461 QRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEV 540
|
...
gi 1158646300 572 LAQ 574
Cdd:TIGR01842 541 LAK 543
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
95-545 |
6.27e-51 |
|
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: 183.33 E-value: 6.27e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 95 HSTSIRqVEAGLRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQVFV-SGLNIAVNLFVALGITLYkSPVV 173
Cdd:TIGR02868 78 HDAALR-SLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVpAGVALVVGAAAVAAIAVL-SVPA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 174 FMFFLLTVPLAAFVT-LFFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEK---HETTRLNKHFTQIYEKgfh 249
Cdd:TIGR02868 156 ALILAAGLLLAGFVApLVSLRAARAAEQALARLRGELAAQLTDALDGAAELVASGALPaalAQVEEADRELTRAERR--- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 250 ldilQSVFGSVSWASFQIF---QLICLIFTGILA-LQGRIQP---GDVVMYQTYFTTIVNSVSGMITLIPTISKGMESIT 322
Cdd:TIGR02868 233 ----AAAATALGAALTLLAaglAVLGALWAGGPAvADGRLAPvtlAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIV 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 323 SIGELLIAGDVETYHGKKKIQHLDGNFRFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQP 402
Cdd:TIGR02868 309 EVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGA-PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 403 TSGKIFLDDQPLDELDMRSVRNYLAVVPQTTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGE 482
Cdd:TIGR02868 388 LQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGE 467
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 483 HGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRL 545
Cdd:TIGR02868 468 GGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
349-562 |
4.32e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 171.92 E-value: 4.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAV 428
Cdd:COG4619 1 LELEGLSFRVGG--KPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 VPQTTLLFSASIKENITYGL----KNVSKERLDEVIEAAQLSslidqlPDGLDTLVGEhgnkLSGGQKQCISIARALIRQ 504
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFqlreRKFDRERALELLERLGLP------PDILDKPVER----LSGGERQRLALIRALLLQ 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 505 PKIILLDEATSALDNQSEKKIQQAL-NYLTETPTT-FIVAHRLSTIKE-ADKIVVIDEGKI 562
Cdd:COG4619 149 PDVLLLDEPTSALDPENTRRVEELLrEYLAEEGRAvLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
350-567 |
1.70e-49 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 174.90 E-value: 1.70e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDEL--DMRSVrnylA 427
Cdd:COG3842 7 ELENVSKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppEKRNV----G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 VVPQTTLLFS-ASIKENITYGLK--NVSK----ERLDEVIEAAQLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIARA 500
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGLRmrGVPKaeirARVAELLELVGLEGLADRYPH-----------QLSGGQQQRVALARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1158646300 501 LIRQPKIILLDEATSALDN------QSE-KKIQQALNyltetpTTFI-VAHRLStikEA----DKIVVIDEGKIVEIGT 567
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAklreemREElRRLQRELG------ITFIyVTHDQE---EAlalaDRIAVMNDGRIEQVGT 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
346-567 |
1.06e-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: 168.36 E-value: 1.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 346 DGNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNY 425
Cdd:cd03369 4 HGEIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 426 LAVVPQTTLLFSASIKENItyglkNVSKERLDEVIEAAqLSslidqlpdgldtlVGEHGNKLSGGQKQCISIARALIRQP 505
Cdd:cd03369 84 LTIIPQDPTLFSGTIRSNL-----DPFDEYSDEEIYGA-LR-------------VSEGGLNLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 506 KIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGT 567
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
350-574 |
1.50e-48 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 168.70 E-value: 1.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDElDMRSVRNYLAVV 429
Cdd:COG1131 2 EVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLFSA-SIKENIT-----YGL-KNVSKERLDEVIEAAQLSslidqlpDGLDTLVGehgnKLSGGQKQCISIARALI 502
Cdd:COG1131 79 PQEPALYPDlTVRENLRffarlYGLpRKEARERIDELLELFGLT-------DAADRKVG----TLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 503 RQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVA-HRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
349-571 |
3.39e-48 |
|
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: 167.74 E-value: 3.39e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLL---NLLIGFI--QPTSGKIFLDDQPLDELDMR--S 421
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLrllNRLNDLIpgAPDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 422 VRNYLAVVPQTTLLFSASIKENITYGLK---NVSKERLDEVIEAA-QLSSLIDQLPDGLdtlvgeHGNKLSGGQKQCISI 497
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgIKLKEELDERVEEAlRKAALWDEVKDRL------HALGLSGGQQQRLCL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 498 ARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKL 571
Cdd:cd03260 153 ARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
350-573 |
3.90e-48 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 167.85 E-value: 3.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELD---MRSVRNYL 426
Cdd:COG1127 7 EVRNLTKSFGD--RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQTTLLFSA-SIKENITYGLK---NVSK----ERLDEVIEAAQLSSLIDQLPdgldtlvGEhgnkLSGGQKQCISIA 498
Cdd:COG1127 85 GMLFQGGALFDSlTVFENVAFPLRehtDLSEaeirELVLEKLELVGLPGAADKMP-------SE----LSGGMRKRVALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 499 RALIRQPKIILLDEATSALDNQSEKKI-------QQALNYltetpTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEK 570
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIdelirelRDELGL-----TSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
...
gi 1158646300 571 LLA 573
Cdd:COG1127 229 LLA 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
350-564 |
2.75e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 165.22 E-value: 2.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYP--DSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELD------MRs 421
Cdd:COG1136 6 ELRNLTKSYGtgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSerelarLR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 422 vRNYLAVVPQT-TLLFSASIKENITYGL------KNVSKERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQC 494
Cdd:COG1136 85 -RRHIGFVFQFfNLLPELTALENVALPLllagvsRKERRERARELLERVGLGDRLDHRP-----------SQLSGGQQQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 495 ISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETP-TTFIVA-HRLSTIKEADKIVVIDEGKIVE 564
Cdd:COG1136 153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELgTTIVMVtHDPELAARADRVIRLRDGRIVS 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
350-567 |
8.79e-47 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 167.56 E-value: 8.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSvRNyLAVV 429
Cdd:COG3839 5 ELENVSKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-RN-IAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLF-SASIKENITYGLKN--VSKERLDE-VIEAA---QLSSLIDQLPDGldtlvgehgnkLSGGQKQCISIARALI 502
Cdd:COG3839 81 FQSYALYpHMTVYENIAFPLKLrkVPKAEIDRrVREAAellGLEDLLDRKPKQ-----------LSGGQRQRVALGRALV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1158646300 503 RQPKIILLDEATSALDNQ------SE-KKIQQALNyltetpTTFI-VAHRLS---TIkeADKIVVIDEGKIVEIGT 567
Cdd:COG3839 150 REPKVFLLDEPLSNLDAKlrvemrAEiKRLHRRLG------TTTIyVTHDQVeamTL--ADRIAVMNDGRIQQVGT 217
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
350-574 |
2.26e-46 |
|
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: 170.47 E-value: 2.26e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLK---PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNY- 425
Cdd:COG1123 262 EVRNLSKRYPVRGKggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRELr 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 426 --LAVVPQ--TTLLFSA-SIKENITYGLKN---VSKERLDEVIEAaqlssLIDQLpdGLDTlvgEHGNK----LSGGQKQ 493
Cdd:COG1123 342 rrVQMVFQdpYSSLNPRmTVGDIIAEPLRLhglLSRAERRERVAE-----LLERV--GLPP---DLADRypheLSGGQRQ 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 494 CISIARALIRQPKIILLDEATSALD--NQSE-----KKIQQALN--YLtetpttFIvAHRLSTIKE-ADKIVVIDEGKIV 563
Cdd:COG1123 412 RVAIARALALEPKLLILDEPTSALDvsVQAQilnllRDLQRELGltYL------FI-SHDLAVVRYiADRVAVMYDGRIV 484
|
250
....*....|.
gi 1158646300 564 EIGTYEKLLAQ 574
Cdd:COG1123 485 EDGPTEEVFAN 495
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
350-565 |
2.65e-46 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 162.26 E-value: 2.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDS--LKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDEldmrsVRNYLA 427
Cdd:cd03293 2 EVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG-----PGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 VVPQTTLLFS-ASIKENITYGLKNV------SKERLDEVIEAAQLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIARA 500
Cdd:cd03293 77 YVFQQDALLPwLTVLDNVALGLELQgvpkaeARERAEELLELVGLSGFENAYPH-----------QLSGGMRQRVALARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 501 LIRQPKIILLDEATSALDNQSEKKIQQAL-NYLTET-PTTFIVAHRLStikEA----DKIVVIDE--GKIVEI 565
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELlDIWRETgKTVLLVTHDID---EAvflaDRVVVLSArpGRIVAE 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
354-566 |
4.89e-46 |
|
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: 161.90 E-value: 4.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 354 VSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELD---MRSVRNYLAVVP 430
Cdd:cd03257 9 VSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRRKEIQMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 431 Q---TTLLFSASIKENITYGLKNVSKERLDEVIEAA--QLSSLIDQLPDGLDTLVGEhgnkLSGGQKQCISIARALIRQP 505
Cdd:cd03257 89 QdpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAvlLLLVGVGLPEEVLNRYPHE----LSGGQRQRVAIARALALNP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 506 KIILLDEATSALD--NQSE-----KKIQQALNyltetpTTFI-VAHRLSTIKE-ADKIVVIDEGKIVEIG 566
Cdd:cd03257 165 KLLIADEPTSALDvsVQAQildllKKLQEELG------LTLLfITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
350-565 |
1.13e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 161.80 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLK--PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRsvrnyLA 427
Cdd:COG1116 9 ELRGVSKRFPTGGGgvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----RG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 VVPQTTLLFS-ASIKENITYGLKNV------SKERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARA 500
Cdd:COG1116 84 VVFQEPALLPwLTVLDNVALGLELRgvpkaeRRERARELLELVGLAGFEDAYP-----------HQLSGGMRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 501 LIRQPKIILLDEATSALDNQSEKKIQQ-ALNYLTETPTTFI-VAHrlsTIKEA----DKIVVIDE--GKIVEI 565
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDeLLRLWQETGKTVLfVTH---DVDEAvflaDRVVVLSArpGRIVEE 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
350-566 |
1.40e-45 |
|
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: 159.99 E-value: 1.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSvRNyLAVV 429
Cdd:cd03259 2 ELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER-RN-IGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLF-SASIKENITYGLKN------VSKERLDEVIEAAQLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIARALI 502
Cdd:cd03259 78 FQDYALFpHLTVAENIAFGLKLrgvpkaEIRARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 503 RQPKIILLDEATSALDNQSEKKIQQAL-NYLTETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIVEIG 566
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELkELQRELGITTIyVTHDQEEALAlADRIAVMNEGRIVQVG 213
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
349-566 |
2.69e-45 |
|
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: 158.25 E-value: 2.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDmRSVRNYLAV 428
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 VPQTTLLFSASIKENItyglknvskerldevieaaqlsslidqlpdgldtlvgehGNKLSGGQKQCISIARALIRQPKII 508
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 509 LLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIG 566
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
350-573 |
6.18e-45 |
|
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: 159.20 E-value: 6.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDEL---DMRSVRNYL 426
Cdd:cd03261 2 ELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQTTLLFSA-SIKENITYGLK---NVSKERLDEV----IEAAQLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIA 498
Cdd:cd03261 80 GMLFQSGALFDSlTVFENVAFPLRehtRLSEEEIREIvlekLEAVGLRGAEDLYPA-----------ELSGGMKKRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 499 RALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETP--TTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLA 573
Cdd:cd03261 149 RALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELglTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
347-576 |
9.17e-45 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 171.07 E-value: 9.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 347 GNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYL 426
Cdd:PLN03130 1236 GSIKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQTTLLFSASIKENITyGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPK 506
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLD-PFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSK 1394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 507 IILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKG 576
Cdd:PLN03130 1395 ILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
52-580 |
1.10e-44 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 170.98 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 52 IANVINAASSKDSSQLQAIYFNAFLMACLIGQNiLTNYfhvkYHSTSIRQVEAGLRATLIKKI--QELSIPYQKELQSGR 129
Cdd:PTZ00265 852 VSTLFDFANLEANSNKYSLYILVIAIAMFISET-LKNY----YNNVIGEKVEKTMKRRLFENIlyQEISFFDQDKHAPGL 926
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 130 IQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVV-----FMFFLLTVPLAAFVTL-----FFRKRIRQSN 199
Cdd:PTZ00265 927 LSAHINRDVHLLKTGLVNNIVIFTHFIVLFLVSMVMSFYFCPIVaavltGTYFIFMRVFAIRARLtankdVEKKEINQPG 1006
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 200 SDF----RQEM-EETSAKVIEVIELAPIARAHGLEKHETTRLNKHFtQIYEKGFHLDILqsvFGSVSWASFQIFQLI--- 271
Cdd:PTZ00265 1007 TVFaynsDDEIfKDPSFLIQEAFYNMNTVIIYGLEDYFCNLIEKAI-DYSNKGQKRKTL---VNSMLWGFSQSAQLFins 1082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 272 -CLIFTGILALQGRIQPGDVVmyQTYFTTI-VNSVSGMITLIPTISKGME-SITSIGELLIAG---DVETyHGKKKIQH- 344
Cdd:PTZ00265 1083 fAYWFGSFLIRRGTILVDDFM--KSLFTFLfTGSYAGKLMSLKGDSENAKlSFEKYYPLIIRKsniDVRD-NGGIRIKNk 1159
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 345 --LDGNFRFEDVSFLY---PDSlkPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGF-------------------- 399
Cdd:PTZ00265 1160 ndIKGKIEIMDVNFRYisrPNV--PIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFydlkndhhivfknehtndmt 1237
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 400 ----------------------------------IQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQTTLLFSASIKENIT 445
Cdd:PTZ00265 1238 neqdyqgdeeqnvgmknvnefsltkeggsgedstVFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIK 1317
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 446 YGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKI 525
Cdd:PTZ00265 1318 FGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 526 QQALNYLTETP--TTFIVAHRLSTIKEADKIVVIDE----GKIVEI-GTYEKLLAQKGYFYR 580
Cdd:PTZ00265 1398 EKTIVDIKDKAdkTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLSVQDGVYK 1459
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
349-572 |
1.96e-44 |
|
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: 158.28 E-value: 1.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAV 428
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 VPQ-TTLLFSASIKENITYG-------LKNVSKE---RLDEVIEAAQLSSLIDQLpdgLDTlvgehgnkLSGGQKQCISI 497
Cdd:COG1120 80 VPQePPAPFGLTVRELVALGryphlglFGRPSAEdreAVEEALERTGLEHLADRP---VDE--------LSGGERQRVLI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 498 ARALIRQPKIILLDEATSALD--NQSEkkIQQALNYLTETP--TTFIVAHRLS-TIKEADKIVVIDEGKIVEIGTYEKLL 572
Cdd:COG1120 149 ARALAQEPPLLLLDEPTSHLDlaHQLE--VLELLRRLARERgrTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
350-575 |
1.07e-43 |
|
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: 156.82 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDD-QPLDELDMRSVRNYLAV 428
Cdd:TIGR04520 2 EVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGlDTLDEENLWEIRKKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 VPQ--TTLLFSASIKENITYGLKN--VS----KERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARA 500
Cdd:TIGR04520 82 VFQnpDNQFVGATVEDDVAFGLENlgVPreemRKRVDEALKLVGMEDFRDREP-----------HLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 501 LIRQPKIILLDEATSALDNQSEKKIQQALNYL-TETPTTFI-VAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQK 575
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVIsITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
350-562 |
2.88e-43 |
|
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: 153.80 E-value: 2.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYP--DSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELD----MRSVR 423
Cdd:cd03255 2 ELKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 424 NYLAVVPQT-TLLFSASIKENITYGL------KNVSKERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCIS 496
Cdd:cd03255 82 RHIGFVFQSfNLLPDLTALENVELPLllagvpKKERRERAEELLERVGLGDRLNHYP-----------SELSGGQQQRVA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 497 IARALIRQPKIILLDEATSALDNQSEKKIQQALNYLT-ETPTTFIVA-HRLSTIKEADKIVVIDEGKI 562
Cdd:cd03255 151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
350-573 |
7.58e-43 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 153.61 E-value: 7.58e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVV 429
Cdd:cd03295 2 EFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLFS-ASIKENITY--GLKNVSKERLDEviEAAQLSSLIDqLPDGldTLVGEHGNKLSGGQKQCISIARALIRQPK 506
Cdd:cd03295 81 IQQIGLFPhMTVEENIALvpKLLKWPKEKIRE--RADELLALVG-LDPA--EFADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 507 IILLDEATSALDN------QSE-KKIQQALNyltetPTTFIVAHRL-STIKEADKIVVIDEGKIVEIGTYEKLLA 573
Cdd:cd03295 156 LLLMDEPFGALDPitrdqlQEEfKRLQQELG-----KTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
345-575 |
8.68e-43 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 153.91 E-value: 8.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 345 LDGNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRN 424
Cdd:cd03288 16 LGGEIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 425 YLAVVPQTTLLFSASIKENITYGLKnVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQ 504
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDPECK-CTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRK 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 505 PKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQK 575
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
307-557 |
9.55e-43 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 165.20 E-value: 9.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 307 MITLI-PTISKGMESITSIGEL--------LIAG--DVETYHGKKKIQhldgnfrFEDVSFLYpDSLK--PIIDHFSLEV 373
Cdd:PTZ00265 337 MLTIIlPNITEYMKSLEATNSLyeiinrkpLVENndDGKKLKDIKKIQ-------FKNVRFHY-DTRKdvEIYKDLNFTL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 374 KAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDD-QPLDELDMRSVRNYLAVVPQTTLLFSASIKENITYGL---- 448
Cdd:PTZ00265 409 TEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDsHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSLyslk 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 449 ------------KNVSKERLD-----------------------EVIEAAQLSSLIDQ------------------LPDG 475
Cdd:PTZ00265 489 dlealsnyynedGNDSQENKNkrnscrakcagdlndmsnttdsnELIEMRKNYQTIKDsevvdvskkvlihdfvsaLPDK 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 476 LDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYL--TETPTTFIVAHRLSTIKEADK 553
Cdd:PTZ00265 569 YETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTIRYANT 648
|
....
gi 1158646300 554 IVVI 557
Cdd:PTZ00265 649 IFVL 652
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
345-581 |
1.50e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 164.38 E-value: 1.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 345 LDGNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRN 424
Cdd:PLN03232 1231 SRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 425 YLAVVPQTTLLFSASIKENITyGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQ 504
Cdd:PLN03232 1311 VLSIIPQSPVLFSGTVRFNID-PFSEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 505 PKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGY-FYRL 581
Cdd:PLN03232 1390 SKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSaFFRM 1467
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
127-581 |
1.75e-42 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 164.35 E-value: 1.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 127 SGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVvfmFFLLTVPLAA---FVTLFFRKRIRQ------ 197
Cdd:TIGR00957 1061 SGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPI---AAVIIPPLGLlyfFVQRFYVASSRQlkrles 1137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 198 -SNSDFRQEMEET--SAKVIEVIElapiaRAHGLEKHETTRLNKHftqiyEKGFHLDILqsvfgSVSWASFQI-FQLICL 273
Cdd:TIGR00957 1138 vSRSPVYSHFNETllGVSVIRAFE-----EQERFIHQSDLKVDEN-----QKAYYPSIV-----ANRWLAVRLeCVGNCI 1202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 274 I-FTGILALQGR--IQPGDVVMYQTYFTTIVNSVSGMITLiptiSKGMES-ITSIGELLIAGDVETyHGKKKIQHL---- 345
Cdd:TIGR00957 1203 VlFAALFAVISRhsLSAGLVGLSVSYSLQVTFYLNWLVRM----SSEMETnIVAVERLKEYSETEK-EAPWQIQETapps 1277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 346 ----DGNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRS 421
Cdd:TIGR00957 1278 gwppRGRVEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD 1357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 422 VRNYLAVVPQTTLLFSASIKENITyGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARAL 501
Cdd:TIGR00957 1358 LRFKITIIPQDPVLFSGSLRMNLD-PFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARAL 1436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 502 IRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYFYRL 581
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
350-574 |
2.07e-42 |
|
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: 151.96 E-value: 2.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLK--PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLA 427
Cdd:cd03258 3 ELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 ----VVPQTTLLFSASIKENITYGLK--NVSK----ERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISI 497
Cdd:cd03258 83 rigmIFQHFNLLSSRTVFENVALPLEiaGVPKaeieERVLELLELVGLEDKADAYP-----------AQLSGGQKQRVGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 498 ARALIRQPKIILLDEATSALDNQSE-------KKIQQALNyltetPTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYE 569
Cdd:cd03258 152 ARALANNPKVLLCDEATSALDPETTqsilallRDINRELG-----LTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVE 226
|
....*
gi 1158646300 570 KLLAQ 574
Cdd:cd03258 227 EVFAN 231
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
350-562 |
3.29e-42 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 151.78 E-value: 3.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLdeldmRSVRNYLAVV 429
Cdd:COG1121 8 ELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP-----RRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLL---FSASIKENITYGL----------KNVSKERLDEVIEAAQLSSLIDQlpdgldtLVGEhgnkLSGGQKQCIS 496
Cdd:COG1121 81 PQRAEVdwdFPITVRDVVLMGRygrrglfrrpSRADREAVDEALERVGLEDLADR-------PIGE----LSGGQQQRVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 497 IARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFI-VAHRLSTIKE-ADKIVVIDEGKI 562
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILvVTHDLGAVREyFDRVLLLNRGLV 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
366-515 |
6.75e-42 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 147.79 E-value: 6.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQTTLLFSA-SIKENI 444
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 445 TYG--LKNVSKERLDEVIEAAqLSSLidQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATS 515
Cdd:pfam00005 81 RLGllLKGLSKREKDARAEEA-LEKL--GLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
350-570 |
8.75e-42 |
|
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: 150.46 E-value: 8.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDM--RSVRnyla 427
Cdd:cd03300 2 ELENVSKFYGG--FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPhkRPVN---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 VVPQTTLLFS-ASIKENITYGL------KNVSKERLDEVIEAAQLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIARA 500
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGLrlkklpKAEIKERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 501 LIRQPKIILLDEATSALDNQSEKKIQQALNYL-TETPTTFI-VAHRLStikEA----DKIVVIDEGKIVEIGT----YEK 570
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLqKELGITFVfVTHDQE---EAltmsDRIAVMNKGKIQQIGTpeeiYEE 221
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
363-574 |
1.20e-41 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 150.14 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLD--ELDMRSVRNYLAVVPQTTLLFS-AS 439
Cdd:COG1126 14 LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLRRKVGMVFQQFNLFPhLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 440 IKENITYGLKNVSKERLDEVIEAAQlsSLIDQLpdGLdtlvGEHGNK----LSGGQKQCISIARALIRQPKIILLDEATS 515
Cdd:COG1126 94 VLENVTLAPIKVKKMSKAEAEERAM--ELLERV--GL----ADKADAypaqLSGGQQQRVAIARALAMEPKVMLFDEPTS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 516 ALDNQSEKKIQQALNYLTETPTTFIVA-HRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:COG1126 166 ALDPELVGEVLDVMRDLAKEGMTMVVVtHEMGFAREvADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
354-573 |
1.28e-41 |
|
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: 150.34 E-value: 1.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 354 VSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRN--------- 424
Cdd:COG1124 9 VSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRrvqmvfqdp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 425 YLAVVPQTTLLfsASIKENIT-YGLKNVsKERLDEVIEAAQL-SSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALI 502
Cdd:COG1124 89 YASLHPRHTVD--RILAEPLRiHGLPDR-EERIAELLEQVGLpPSFLDRYP-----------HQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 503 RQPKIILLDEATSALD--NQSE-----KKIQQALNyltetpTTFI-VAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLA 573
Cdd:COG1124 155 LEPELLLLDEPTSALDvsVQAEilnllKDLREERG------LTYLfVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
350-562 |
1.30e-41 |
|
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: 149.22 E-value: 1.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDEldmrsVRNYLAVV 429
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLL---FSASIKENITYGL----------KNVSKERLDEVIEAAQLSSLIDQlpdgldtLVGEhgnkLSGGQKQCIS 496
Cdd:cd03235 74 PQRRSIdrdFPISVRDVVLMGLyghkglfrrlSKADKAKVDEALERVGLSELADR-------QIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 497 IARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTT-FIVAHRLSTIKE-ADKIVVIDEGKI 562
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTiLVVTHDLGLVLEyFDRVLLLNRTVV 210
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
352-576 |
2.28e-41 |
|
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: 149.62 E-value: 2.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 352 EDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDmRSVRNYLAVVPQ 431
Cdd:COG4555 5 ENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP-REARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 432 TTLLFSA-SIKENITY--GLKNVSKERLDEVIEaaQLSSLIDqLPDGLDTLVGEhgnkLSGGQKQCISIARALIRQPKII 508
Cdd:COG4555 82 ERGLYDRlTVRENIRYfaELYGLFDEELKKRIE--ELIELLG-LEEFLDRRVGE----LSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 509 LLDEATSALDNQSEKKIQQALNYLTETPTTFIVA-HRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQKG 576
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
367-574 |
3.20e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 152.22 E-value: 3.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 367 DHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLD-ELDMRSvRNyLAVVPQTTLLF-SASIKENI 444
Cdd:COG1118 19 DDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRE-RR-VGFVFQHYALFpHMTVAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 445 TYGL------KNVSKERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLDEATSALD 518
Cdd:COG1118 97 AFGLrvrppsKAEIRARVEELLELVQLEGLADRYP-----------SQLSGGQRQRVALARALAVEPEVLLLDEPFGALD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 519 NQSEKKIQQAL-NYLTETP-TTFIVAH------RLstikeADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:COG1118 166 AKVRKELRRWLrRLHDELGgTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
350-561 |
6.66e-41 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 145.47 E-value: 6.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVV 429
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQttllfsasikenityglknvskerldevieaaqlsslidqlpdgldtlvgehgnkLSGGQKQCISIARALIRQPKIIL 509
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 510 LDEATSALDNQSEKKIQQALNYLTETPTTFIVA-HRLSTIKEA-DKIVVIDEGK 561
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEEGRTVIIVtHDPELAELAaDRVIVLKDGK 157
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
350-574 |
8.16e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 155.06 E-value: 8.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPT---SGKIFLDDQPLDELDMRSVRNYL 426
Cdd:COG1123 6 EVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQ--TTLLFSASIKENITYGLKNVS---KERLDEVIEAAQLSslidqlpdGLDTLVGEHGNKLSGGQKQCISIARAL 501
Cdd:COG1123 86 GMVFQdpMTQLNPVTVGDQIAEALENLGlsrAEARARVLELLEAV--------GLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1158646300 502 IRQPKIILLDEATSALDNQSEKKIQQALNYLT-ETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQrERGTTVLlITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
350-574 |
1.69e-40 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 146.82 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLKpiidHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDEL--DMRSVrnylA 427
Cdd:COG3840 3 RLDDLTYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppAERPV----S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 VVPQTTLLFSA-SIKENITYGLK------NVSKERLDEVIEAAQLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIARA 500
Cdd:COG3840 75 MLFQENNLFPHlTVAQNIGLGLRpglkltAEQRAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 501 LIRQPKIILLDEATSALDN--QSE-----KKIQQALNyltetPTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLL 572
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPalRQEmldlvDELCRERG-----LTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALL 218
|
..
gi 1158646300 573 AQ 574
Cdd:COG3840 219 DG 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
350-564 |
3.20e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.97 E-value: 3.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSlKPIIDHFSLEVKAGEtIAF-VGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSV---RNY 425
Cdd:COG2884 3 RFENVSKRYPGG-REALSDVSLEIEKGE-FVFlTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIpylRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 426 LAVVPQTT-LLFSASIKENITYGL------KNVSKERLDEVIEAAQLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIA 498
Cdd:COG2884 81 IGVVFQDFrLLPDRTVYENVALPLrvtgksRKEIRRRVREVLDLVGLSDKAKALPH-----------ELSGGEQQRVAIA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 499 RALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVA-HRLSTIKEADK-IVVIDEGKIVE 564
Cdd:COG2884 150 RALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
352-566 |
3.55e-40 |
|
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: 144.12 E-value: 3.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 352 EDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQ 431
Cdd:cd03214 3 ENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 432 ttllfsasikenityglknvskerldeVIEAAQLSSLIDQlpdGLDTlvgehgnkLSGGQKQCISIARALIRQPKIILLD 511
Cdd:cd03214 81 ---------------------------ALELLGLAHLADR---PFNE--------LSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 512 EATSALD--NQSE-----KKIQQALNYltetpTTFIVAHRLS-TIKEADKIVVIDEGKIVEIG 566
Cdd:cd03214 123 EPTSHLDiaHQIEllellRRLARERGK-----TVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
370-572 |
4.09e-39 |
|
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: 143.24 E-value: 4.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 370 SLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDEL--DMRSVrnylAVVPQTTLLF-SASIKENITY 446
Cdd:cd03299 19 SLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLppEKRDI----SYVPQNYALFpHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 447 GLKNVSKERLD---EVIEAAQLSslidqlpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEK 523
Cdd:cd03299 95 GLKKRKVDKKEierKVLEIAEML--------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 524 KIQQALNYL-TETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLL 572
Cdd:cd03299 167 KLREELKKIrKEFGVTVLhVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
222-560 |
5.05e-39 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 150.73 E-value: 5.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 222 IARAHGlEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIFQLICLIFTGILALQGRIQPGDVVMYQTYFTTIV 301
Cdd:COG4178 234 IALYRG-EAAERRRLRRRFDAVIANWRRLIRRQRNLTFFTTGYGQLAVIFPILVAAPRYFAGEITLGGLMQAASAFGQVQ 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 302 NSVSGMITLIPTISK---GMESITSIGELLIAGDVETYHGKKKIQHLDGNFRFEDVSFLYPDSlKPIIDHFSLEVKAGET 378
Cdd:COG4178 313 GALSWFVDNYQSLAEwraTVDRLAGFEEALEAADALPEAASRIETSEDGALALEDLTLRTPDG-RPLLEDLSLSLKPGER 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 379 IAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDdqPLDELdmrsvrnylAVVPQTTLLFSASIKENITY--GLKNVSKERL 456
Cdd:COG4178 392 LLITGPSGSGKSTLLRAIAGLWPYGSGRIARP--AGARV---------LFLPQRPYLPLGTLREALLYpaTAEAFSDAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 457 DEVIEAAQLSSLIDQLPDGLDTlvgehGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALnyLTETP 536
Cdd:COG4178 461 REALEAVGLGHLAERLDEEADW-----DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLL--REELP 533
|
330 340
....*....|....*....|....*.
gi 1158646300 537 -TTFI-VAHRLSTIKEADKIVVIDEG 560
Cdd:COG4178 534 gTTVIsVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
349-561 |
5.51e-39 |
|
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: 140.79 E-value: 5.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSV--RNYL 426
Cdd:cd03229 1 LELKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPplRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQTTLLFS-ASIKENITYGlknvskerldevieaaqlsslidqlpdgldtlvgehgnkLSGGQKQCISIARALIRQP 505
Cdd:cd03229 79 GMVFQDFALFPhLTVLENIALG---------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1158646300 506 KIILLDEATSALDNQSEKKIQQALNYLTETP--TTFIVAHRLS-TIKEADKIVVIDEGK 561
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAQLgiTVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
350-574 |
8.88e-38 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 140.92 E-value: 8.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVV 429
Cdd:PRK13635 7 RVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQT--TLLFSASIKENITYGLKN--VSK----ERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARAL 501
Cdd:PRK13635 87 FQNpdNQFVGATVQDDVAFGLENigVPReemvERVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAIAGVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 502 IRQPKIILLDEATSALDNQSEKKIQQALNYLTE--TPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:PRK13635 156 ALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKS 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
370-562 |
2.51e-37 |
|
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: 137.66 E-value: 2.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 370 SLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPL--DELDMRSVRNYLAVVPQTTLLFS-ASIKENITY 446
Cdd:cd03262 20 DLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFPhLTVLENITL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 447 GLKNVSKERLDEVIEAAQlsSLIDQLpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQ 526
Cdd:cd03262 100 APIKVKGMSKAEAEERAL--ELLEKV--GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVL 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 1158646300 527 QALNYLTETPTTF-IVAHRLSTIKE-ADKIVVIDEGKI 562
Cdd:cd03262 176 DVMKDLAEEGMTMvVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
352-562 |
5.48e-37 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 135.22 E-value: 5.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 352 EDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDElDMRSVRNYLAVVPQ 431
Cdd:cd03230 4 RNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 432 TTLLFSA-SIKENItyglknvskerldevieaaqlsslidqlpdgldtlvgehgnKLSGGQKQCISIARALIRQPKIILL 510
Cdd:cd03230 81 EPSLYENlTVRENL-----------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 511 DEATSALDNQSEKKIQQALNYLTETPTTFIVA-HRLSTIKE-ADKIVVIDEGKI 562
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSsHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
350-567 |
1.06e-36 |
|
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: 136.70 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSlkPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSvRNyLAVV 429
Cdd:cd03296 4 EVRNVSKRFGDF--VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-RN-VGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLFS-ASIKENITYGL----------KNVSKERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIA 498
Cdd:cd03296 80 FQHYALFRhMTVFDNVAFGLrvkprserppEAEIRAKVHELLKLVQLDWLADRYP-----------AQLSGGQRQRVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 499 RALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETP--TTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGT 567
Cdd:cd03296 149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELhvTTVFVTHDQEEALEvADRVVVMNKGRIEQVGT 220
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
349-571 |
1.36e-36 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 137.09 E-value: 1.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLL---NLLIGFI--QPTSGKIFLDDQPL--DELDMRS 421
Cdd:COG1117 12 IEVRNLNVYYGD--KQALKDINLDIPENKVTALIGPSGCGKSTLLrclNRMNDLIpgARVEGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 422 VRNYLAVVPQTTLLFSASIKENITYGLK---NVSKERLDEVIEAA-QLSSLIDQLPDGLDtlvgEHGNKLSGGQKQCISI 497
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDNVAYGLRlhgIKSKSELDEIVEESlRKAALWDEVKDRLK----KSALGLSGGQQQRLCI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 498 ARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAH------RLStikeaDKIVVIDEGKIVEIGTYEKL 571
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYLGELVEFGPTEQI 240
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
350-566 |
3.22e-36 |
|
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: 134.69 E-value: 3.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSvRNyLAVV 429
Cdd:cd03301 2 ELENVTKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-RD-IAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLF-SASIKENITYGLK--NVSKERLDE-VIEAA---QLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIARALI 502
Cdd:cd03301 78 FQNYALYpHMTVYDNIAFGLKlrKVPKDEIDErVREVAellQIEHLLDRKPK-----------QLSGGQRQRVALGRAIV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 503 RQPKIILLDEATSALDN------QSE-KKIQQALNYltetpTTFIVAH-RLSTIKEADKIVVIDEGKIVEIG 566
Cdd:cd03301 147 REPKVFLMDEPLSNLDAklrvqmRAElKRLQQRLGT-----TTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
350-574 |
3.84e-36 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 137.90 E-value: 3.84e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLKPII--DHFSLEVKAGETIAFVGPSGSGKSTLL---NLLIgfiQPTSGKIFLDDQPLDELD---MRS 421
Cdd:COG1135 3 ELENLSKTFPTKGGPVTalDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLE---RPTSGSVLVDGVDLTALSereLRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 422 VRNYLAVVPQT-TLLFSASIKENITYGLK--NVSK----ERLDEVIEaaqlsslidqlpdgldtLVG--EHGNK----LS 488
Cdd:COG1135 80 ARRKIGMIFQHfNLLSSRTVAENVALPLEiaGVPKaeirKRVAELLE-----------------LVGlsDKADAypsqLS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 489 GGQKQCISIARALIRQPKIILLDEATSALDNQSE-------KKIQQALNyLTetpttfIV--AHRLSTIKE-ADKIVVID 558
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALDPETTrsildllKDINRELG-LT------IVliTHEMDVVRRiCDRVAVLE 215
|
250
....*....|....*.
gi 1158646300 559 EGKIVEIGTYEKLLAQ 574
Cdd:COG1135 216 NGRIVEQGPVLDVFAN 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
349-575 |
7.11e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 135.50 E-value: 7.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAV 428
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 VPQT--TLLFSASIKENITYGL--KNVSKERLDEVIE----AAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARA 500
Cdd:PRK13632 88 IFQNpdNQFIGATVEDDIAFGLenKKVPPKKMKDIIDdlakKVGMEDYLDKEP-----------QNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 501 LIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPT-TFI-VAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQK 575
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLIsITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
369-566 |
8.52e-36 |
|
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: 133.57 E-value: 8.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 369 FSLEVK---AGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDE----LDMRSVRNYLAVVPQTTLLFS-ASI 440
Cdd:cd03297 13 FTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPhLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 441 KENITYGLK----NVSKERLDEVIEAAQLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIARALIRQPKIILLDEATSA 516
Cdd:cd03297 93 RENLAFGLKrkrnREDRISVDELLDLLGLDHLLNRYPA-----------QLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1158646300 517 LDNQSEKKIQQalnYLTETPTTF-----IVAHRLSTI-KEADKIVVIDEGKIVEIG 566
Cdd:cd03297 162 LDRALRLQLLP---ELKQIKKNLnipviFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
358-571 |
8.83e-36 |
|
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: 133.40 E-value: 8.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 358 YPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDElDMRSVRNYLAVVPQTTLLFS 437
Cdd:cd03263 10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 438 A-SIKENITY--GLKNVSKERLDEVIEAaqlssLIDQ--LPDGLDTLVGEhgnkLSGGQKQCISIARALIRQPKIILLDE 512
Cdd:cd03263 89 ElTVREHLRFyaRLKGLPKSEIKEEVEL-----LLRVlgLTDKANKRART----LSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 513 ATSALDNQSEKKIQQALNYLTETPTTFIVAHrlsTIKEA----DKIVVIDEGKIVEIGTYEKL 571
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRKGRSIILTTH---SMDEAealcDRIAIMSDGKLRCIGSPQEL 219
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
354-574 |
8.90e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 136.34 E-value: 8.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 354 VSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQP---TSGKIFLDDQPLDELD---MRSVR-NYL 426
Cdd:COG0444 9 VYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekeLRKIRgREI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQ---TTL--LFSasIKENITYGLK---NVSK-ERLDEVIEAAQL------SSLIDQLPdgldtlvgeHgnKLSGGQ 491
Cdd:COG0444 89 QMIFQdpmTSLnpVMT--VGDQIAEPLRihgGLSKaEARERAIELLERvglpdpERRLDRYP---------H--ELSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 492 KQCISIARALIRQPKIILLDEATSALD--NQSE-----KKIQQALNyltetpTTFI-VAHRLSTIKE-ADKIVVIDEGKI 562
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDvtIQAQilnllKDLQRELG------LAILfITHDLGVVAEiADRVAVMYAGRI 229
|
250
....*....|..
gi 1158646300 563 VEIGTYEKLLAQ 574
Cdd:COG0444 230 VEEGPVEELFEN 241
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
363-569 |
9.03e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 137.77 E-value: 9.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDEL--DMRSVRnylaVVPQTTLLFS-AS 439
Cdd:PRK09452 27 KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVpaENRHVN----TVFQSYALFPhMT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 440 IKENITYGLK--NVSKERLDE-VIEA---AQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLDEA 513
Cdd:PRK09452 103 VFENVAFGLRmqKTPAAEITPrVMEAlrmVQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDES 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1158646300 514 TSALDNQSEKKIQQALNYLT-ETPTTFI-VAHRLstiKEA----DKIVVIDEGKIVEIGT----YE 569
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQrKLGITFVfVTHDQ---EEAltmsDRIVVMRDGRIEQDGTpreiYE 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
336-574 |
2.21e-35 |
|
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: 133.92 E-value: 2.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 336 YHGKKKIQHLDGNFRFEDVsfLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQP-- 413
Cdd:cd03294 12 KNPQKAFKLLAKGKSKEEI--LKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDia 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 414 -LDELDMRSVR-NYLAVVPQTTLLF-SASIKENITYGL------KNVSKERLDEVIEAAQLSSLIDQLPDgldtlvgehg 484
Cdd:cd03294 90 aMSRKELRELRrKKISMVFQSFALLpHRTVLENVAFGLevqgvpRAEREERAAEALELVGLEGWEHKYPD---------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 485 nKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYL-TETPTTFI-VAHRLS-TIKEADKIVVIDEGK 561
Cdd:cd03294 160 -ELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVfITHDLDeALRLGDRIAIMKDGR 238
|
250
....*....|...
gi 1158646300 562 IVEIGTYEKLLAQ 574
Cdd:cd03294 239 LVQVGTPEEILTN 251
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
30-581 |
4.16e-35 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 141.65 E-value: 4.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 30 RFAMSGLFFIIKHLPSWLMPIAIANVINAASSKDSSQLQAIYFNAFLMACLIGQNILTNYFHvkyhstSIRQVEAGLRAT 109
Cdd:PLN03232 302 RFWLGGIFKIGHDLSQFVGPVILSHLLQSMQEGDPAWVGYVYAFLIFFGVTFGVLCESQYFQ------NVGRVGFRLRST 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 110 LI----KKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQV---FVSGLNIAVN---LFVALGI-TLYKSPVVFmffl 178
Cdd:PLN03232 376 LVaaifHKSLRLTHEARKNFASGKVTNMITTDANALQQIAEQLhglWSAPFRIIVSmvlLYQQLGVaSLFGSLILF---- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 179 LTVPLAAFVTlffrKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRL----NKHFTQIYEK----GFHL 250
Cdd:PLN03232 452 LLIPLQTLIV----RKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIqgirNEELSWFRKAqllsAFNS 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 251 DILQSVFGSVSWASFQIFQLicliftgilaLQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGMESITSIGELLI- 329
Cdd:PLN03232 528 FILNSIPVVVTLVSFGVFVL----------LGGDLTPARAFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLs 597
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 330 -----AGDVETYHGKKKIQHLDGNFRFEDvsflypDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPts 404
Cdd:PLN03232 598 eerilAQNPPLQPGAPAISIKNGYFSWDS------KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH-- 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 405 gkifLDDQPLDeldmrsVRNYLAVVPQTTLLFSASIKENITYGlKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHG 484
Cdd:PLN03232 670 ----AETSSVV------IRGSVAYVPQVSWIFNATVRENILFG-SDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERG 738
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 485 NKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKI-QQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIV 563
Cdd:PLN03232 739 VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIK 818
|
570
....*....|....*...
gi 1158646300 564 EIGTYEKLLAQKGYFYRL 581
Cdd:PLN03232 819 EEGTFAELSKSGSLFKKL 836
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
367-574 |
1.11e-34 |
|
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: 137.89 E-value: 1.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 367 DHFSLEVKAGETIAFVGPSGSGKSTL----LNLLigfiqPTSGKIFLDDQPLDELD---MRSVRNYLAVV---PqttllF 436
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVfqdP-----F 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 437 SA-----SIKENITYGLK----NVSK-ERLDEVIEAaqlsslidqLPD-GLDtlvGEHGNK----LSGGQKQCISIARAL 501
Cdd:COG4172 373 GSlsprmTVGQIIAEGLRvhgpGLSAaERRARVAEA---------LEEvGLD---PAARHRypheFSGGQRQRIAIARAL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 502 IRQPKIILLDEATSALDN--QSE-----KKIQQALN--YLtetpttFIvAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKL 571
Cdd:COG4172 441 ILEPKLLVLDEPTSALDVsvQAQildllRDLQREHGlaYL------FI-SHDLAVVRAlAHRVMVMKDGKVVEQGPTEQV 513
|
...
gi 1158646300 572 LAQ 574
Cdd:COG4172 514 FDA 516
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
349-563 |
1.17e-34 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 131.33 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDEL---DMRSVRNY 425
Cdd:COG3638 3 LELRNLSKRYPGG-TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgrALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 426 LAVVPQ-------TTLLfsasikENITYG-----------LKNVSKERLDEVIEAaqlsslIDQLpdGLdtlvGEHGNK- 486
Cdd:COG3638 82 IGMIFQqfnlvprLSVL------TNVLAGrlgrtstwrslLGLFPPEDRERALEA------LERV--GL----ADKAYQr 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 487 ---LSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIqqaLNYLTETP-----TTFIVAHRLSTIKE-ADKIVVI 557
Cdd:COG3638 144 adqLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQV---MDLLRRIAredgiTVVVNLHQVDLARRyADRIIGL 220
|
....*.
gi 1158646300 558 DEGKIV 563
Cdd:COG3638 221 RDGRVV 226
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
367-574 |
1.27e-34 |
|
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: 134.07 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 367 DHFSLEVK----AGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLdeLDMRSVRNY------LAVVPQTTLLF 436
Cdd:COG4148 12 GGFTLDVDftlpGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL--QDSARGIFLpphrrrIGYVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 437 S-ASIKENITYGLKNV----SKERLDEVIEAAQLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIARALIRQPKIILLD 511
Cdd:COG4148 90 PhLSVRGNLLYGRKRApraeRRISFDEVVELLGIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 512 EATSALDNQSEKKIqqaLNYLTETPTTF-----IVAH------RLstikeADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:COG4148 159 EPLAALDLARKAEI---LPYLERLRDELdipilYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
367-571 |
2.10e-34 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 132.93 E-value: 2.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 367 DHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQP---LDELDMRSVRNYLAVV---PQTTLLFSASI 440
Cdd:COG4608 35 DGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDitgLSGRELRPLRRRMQMVfqdPYASLNPRMTV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 441 KENITYGLKN---VSK-ERLDEVIEaaqlssLIDQLpdGLDTlvgEHGNK----LSGGQKQCISIARALIRQPKIILLDE 512
Cdd:COG4608 115 GDIIAEPLRIhglASKaERRERVAE------LLELV--GLRP---EHADRypheFSGGQRQRIGIARALALNPKLIVCDE 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 513 ATSALDnqseKKIQ-QALN------------YLtetpttFIvAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKL 571
Cdd:COG4608 184 PVSALD----VSIQaQVLNlledlqdelgltYL------FI-SHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
31-318 |
3.80e-34 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 131.13 E-value: 3.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 31 FAMSGLFFIIKHLPSWLMPIAIANVIN-AASSKDSSQLqaIYFNAFLMACLIGQnILTNYFHVKYHSTSIRQVEAGLRAT 109
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIDdVIPAGDLSLL--LWIALLLLLLALLR-ALLSYLRRYLAARLGQRVVFDLRRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 110 LIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFVTL 189
Cdd:cd07346 78 LFRHLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 190 FFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIFQ 269
Cdd:cd07346 158 YFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGT 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1158646300 270 LICLIFTGILALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGM 318
Cdd:cd07346 238 ALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQAL 286
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
349-530 |
9.03e-34 |
|
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: 127.60 E-value: 9.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDmRSVRNYLAV 428
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR-EDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 VPQTTLLFSA-SIKENIT-----YGLKnVSKERLDEVIEAAQLSSLidqlpdgLDTLVGehgnKLSGGQKQCISIARALI 502
Cdd:COG4133 80 LGHADGLKPElTVRENLRfwaalYGLR-ADREAIDEALEAVGLAGL-------ADLPVR----QLSAGQKRRVALARLLL 147
|
170 180
....*....|....*....|....*...
gi 1158646300 503 RQPKIILLDEATSALDNQSEKKIQQALN 530
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIA 175
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
364-573 |
4.42e-33 |
|
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: 126.01 E-value: 4.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 364 PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDEL--DMRsVRNYLAVVPQTTLLF-SASI 440
Cdd:cd03224 14 QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLppHER-ARAGIGYVPEGRRIFpELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 441 KENITYGLKNVSKERLDEVIEaaQLSSLIDQLPDGLDTLVGEhgnkLSGGQKQCISIARALIRQPKIILLDEATSALDNQ 520
Cdd:cd03224 93 EENLLLGAYARRRAKRKARLE--RVYELFPRLKERRKQLAGT----LSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 521 SEKKIQQALNYLTETPTT-FIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLA 573
Cdd:cd03224 167 IVEEIFEAIRELRDEGVTiLLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
350-575 |
6.48e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 125.85 E-value: 6.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYpDSLkPIidHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQplDELDMRSVRNYLAVV 429
Cdd:PRK10771 3 KLTDITWLY-HHL-PM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHTTTPPSRRPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLFS-ASIKENITYG------LKNVSKERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALI 502
Cdd:PRK10771 77 FQENNLFShLTVAQNIGLGlnpglkLNAAQREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1158646300 503 RQPKIILLDEATSALDNQSEKKIQQALNYLTETP--TTFIVAHRLS-TIKEADKIVVIDEGKIVEIGTYEKLLAQK 575
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-578 |
1.17e-32 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 134.30 E-value: 1.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 2 EERIQKSYQKYHANAFQTLLHLYQGNYwrFAMSGLFFIIKHLPSWLMPIAIANVINAASSKDSSQLQAIYFNAFLMACLI 81
Cdd:TIGR00957 292 EALIVKSPHKPRKPSLFKVLYKTFGPY--FLMSFCFKAIHDLMMFIGPQILSLLIRFVNDPMAPDWQGYFYTGLLFVCAC 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 82 GQN-ILTNYFHVKYhsTSIRQVEAGLRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSS---QVFVSGLNIAV 157
Cdd:TIGR00957 370 LQTlILHQYFHICF--VSGMRIKTAVMGAVYRKALVITNSARKSSTVGEIVNLMSVDAQRFMDLATyinMIWSAPLQVIL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 158 NLF---VALGITLYkSPVVFMffLLTVPLAAFVTLFFRK-RIRQSNS-DFRQEMEETSAKVIEVI-----ELAPIARAHG 227
Cdd:TIGR00957 448 ALYflwLNLGPSVL-AGVAVM--VLMVPLNAVMAMKTKTyQVAHMKSkDNRIKLMNEILNGIKVLklyawELAFLDKVEG 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 228 LEKHETtrlnkhftQIYEKGFHLdilqSVFGSVSWASFQIFQLICliftgILALQGRIQPGDVVMYQTYFTTIV--NSVS 305
Cdd:TIGR00957 525 IRQEEL--------KVLKKSAYL----HAVGTFTWVCTPFLVALI-----TFAVYVTVDENNILDAEKAFVSLAlfNILR 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 306 GMITLIP-TISKGMESITSIGELLIAGDVETYHG----KKKIQHLDGN-FRFEDVSFLYPDSLKPIIDHFSLEVKAGETI 379
Cdd:TIGR00957 588 FPLNILPmVISSIVQASVSLKRLRIFLSHEELEPdsieRRTIKPGEGNsITVHNATFTWARDLPPTLNGITFSIPEGALV 667
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 380 AFVGPSGSGKSTLLNLLIGFIQPTSGKIflddqpldeldmrSVRNYLAVVPQTTLLFSASIKENITYGlKNVSKERLDEV 459
Cdd:TIGR00957 668 AVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSLRENILFG-KALNEKYYQQV 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 460 IEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQAL---NYLTETP 536
Cdd:TIGR00957 734 LEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNK 813
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1158646300 537 TTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYF 578
Cdd:TIGR00957 814 TRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
363-567 |
1.43e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 125.65 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQ-TTLLFSASIK 441
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQhSSLSFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITYGLK--NVSKERLDEVIEAAqlsslIDQLpdGLDTLVGEHGNKLSGGQKQCISIARALIR------QPKIILLDEA 513
Cdd:PRK13548 95 EVVAMGRAphGLSRAEDDALVAAA-----LAQV--DLAHLAGRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 514 TSALDNQSEKKIQQAL-NYLTETPTTFI-VAHRLS-TIKEADKIVVIDEGKIVEIGT 567
Cdd:PRK13548 168 TSALDLAHQHHVLRLArQLAHERGLAVIvVLHDLNlAARYADRIVLLHQGRLVADGT 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
365-574 |
1.64e-32 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 128.30 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 365 IIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDEldmRSVRNY-LAVVPQTTLLFS-ASIKE 442
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH---RSIQQRdICMVFQSYALFPhMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 443 NITYGLK--NVSKE----RLDEVIEAAQLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIARALIRQPKIILLDEATSA 516
Cdd:PRK11432 98 NVGYGLKmlGVPKEerkqRVKEALELVDLAGFEDRYVD-----------QISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1158646300 517 LD-----NQSEK--KIQQALNYltetpTTFIVAHRLStikEA----DKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:PRK11432 167 LDanlrrSMREKirELQQQFNI-----TSLYVTHDQS---EAfavsDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
350-563 |
6.19e-32 |
|
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: 122.37 E-value: 6.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLKpIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYlavV 429
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGY---V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTT--LLFSASIKENITYGLKNVSKERldEVIEAaQLSSLidqlpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKI 507
Cdd:cd03226 77 MQDVdyQLFTDSVREELLLGLKELDAGN--EQAET-VLKDL------DLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 508 ILLDEATSALDNQSEKKIQQALNYLTETPTTFIVA-HRLSTIKE-ADKIVVIDEGKIV 563
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVItHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
349-563 |
1.27e-31 |
|
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: 122.68 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAv 428
Cdd:cd03256 1 IEVENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 vpQTTLLF-SASIKENITYgLKNVSKERLDEV------------IEAAQLSSLIDQLpdGLDTLVGEHGNKLSGGQKQCI 495
Cdd:cd03256 79 --QIGMIFqQFNLIERLSV-LENVLSGRLGRRstwrslfglfpkEEKQRALAALERV--GLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 496 SIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETP--TTFIVAHRLSTIKE-ADKIVVIDEGKIV 563
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEgiTVIVSLHQVDLAREyADRIVGLKDGRIV 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
363-564 |
1.43e-31 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 123.38 E-value: 1.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELD---MRSVRNYLAVVPQTTllFSA- 438
Cdd:TIGR02769 24 APVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDS--PSAv 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 439 ----SIKENITYGLKNVskERLDEVIEAAQLSSLIDQLpdGLDTlvgEHGNK----LSGGQKQCISIARALIRQPKIILL 510
Cdd:TIGR02769 102 nprmTVRQIIGEPLRHL--TSLDESEQKARIAELLDMV--GLRS---EDADKlprqLSGGQLQRINIARALAVKPKLIVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 511 DEATSALDNQSEKKIQQALNYL-TETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIVE 564
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLqQAFGTAYLfITHDLRLVQSfCQRVAVMDKGQIVE 231
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
350-566 |
1.63e-31 |
|
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: 121.45 E-value: 1.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSlkPIidHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQplDELDMRSVRNYLAVV 429
Cdd:cd03298 2 RLDKIRFSYGEQ--PM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV--DVTAAPPADRPVSML 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLFS-ASIKENITYG------LKNVSKERLDEVIEAAQLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIARALI 502
Cdd:cd03298 76 FQENNLFAhLTVEQNVGLGlspglkLTAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLV 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 503 RQPKIILLDEATSALDNQSEKKIQQALNYL-TETP-TTFIVAHRLSTIKE-ADKIVVIDEGKIVEIG 566
Cdd:cd03298 145 RDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
351-584 |
6.02e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.83 E-value: 6.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 351 FEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTS---GKIFLDDQPLDELDMRSVRNYLA 427
Cdd:PRK13640 8 FKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIREKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 VVPQT--TLLFSASIKENITYGLKN--VSKERLDEVIEAAqLSSLidqlpDGLDTLVGEHGNkLSGGQKQCISIARALIR 503
Cdd:PRK13640 88 IVFQNpdNQFVGATVGDDVAFGLENraVPRPEMIKIVRDV-LADV-----GMLDYIDSEPAN-LSGGQKQRVAIAGILAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 504 QPKIILLDEATSALDNQSEKKIQQALNYLTETP--TTFIVAHRLSTIKEADKIVVIDEGKI------VEIGTYEKLLAQK 575
Cdd:PRK13640 161 EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLlaqgspVEIFSKVEMLKEI 240
|
250
....*....|...
gi 1158646300 576 G----YFYRLKNE 584
Cdd:PRK13640 241 GldipFVYKLKNK 253
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
360-574 |
1.14e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 120.71 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 360 DSLKPIidHFSLEvkAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVV---PQTTL-- 434
Cdd:COG4167 27 EAVKPV--SFTLE--AGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIfqdPNTSLnp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 435 ------LFSASIKENITYglknVSKERLDEVIEAAQLSSLidqLPDGLDTlvgeHGNKLSGGQKQCISIARALIRQPKII 508
Cdd:COG4167 103 rlnigqILEEPLRLNTDL----TAEEREERIFATLRLVGL---LPEHANF----YPHMLSSGQKQRVALARALILQPKII 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 509 LLDEATSALDnQSEKkiQQALNYLTETPTT----FI-VAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:COG4167 172 IADEALAALD-MSVR--SQIINLMLELQEKlgisYIyVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFAN 240
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
364-560 |
2.04e-30 |
|
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: 118.59 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 364 PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIF----LDDQPLDELDMRSVRNYLAVVPQTTLLFSAS 439
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQKPWLLNAT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 440 IKENITYGlKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDN 519
Cdd:cd03290 95 VEENITFG-SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1158646300 520 QSEKKIQQA--LNYLTETPTTFI-VAHRLSTIKEADKIVVIDEG 560
Cdd:cd03290 174 HLSDHLMQEgiLKFLQDDKRTLVlVTHKLQYLPHADWIIAMKDG 217
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
350-564 |
3.23e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 119.41 E-value: 3.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYL--- 426
Cdd:PRK10419 12 HYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRrdi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 ---------AVVPQTTLlfSASIKENITYgLKNVSK----ERLDEVIEAAQLS-SLIDQLPdgldtlvgehgNKLSGGQK 492
Cdd:PRK10419 92 qmvfqdsisAVNPRKTV--REIIREPLRH-LLSLDKaerlARASEMLRAVDLDdSVLDKRP-----------PQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 493 QCISIARALIRQPKIILLDEATSALDN--QSE-----KKIQQalnyltETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIV 563
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLvlQAGvirllKKLQQ------QFGTACLfITHDLRLVERfCQRVMVMDNGQIV 231
|
.
gi 1158646300 564 E 564
Cdd:PRK10419 232 E 232
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
349-545 |
4.29e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 119.12 E-value: 4.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDSLKpiIDHFSLEVKAGETIAFVGPSGSGKSTLL-------NLLIGFiqPTSGKIFLDDQPL--DELDM 419
Cdd:PRK14243 11 LRTENLNVYYGSFLA--VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGF--RVEGKVTFHGKNLyaPDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 420 RSVRNYLAVVPQTTLLFSASIKENITYGLK-NVSKERLDEVIEAA-QLSSLIDQLPDGLDtlvgEHGNKLSGGQKQCISI 497
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFPKSIYDNIAYGARiNGYKGDMDELVERSlRQAALWDEVKDKLK----QSGLSLSGGQQQRLCI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1158646300 498 ARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRL 545
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
318-578 |
4.31e-30 |
|
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: 119.58 E-value: 4.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 318 MESITS-----IGELLIAGDVEtyHGKKKIQHLDGNFRFEDVSFLypdsLKPIIDHFSLEVKAGETIAFVGPSGSGKSTL 392
Cdd:cd03291 6 MENVTAfwdegFGELLEKAKQE--NNDRKHSSDDNNLFFSNLCLV----GAPVLKNINLKIEKGEMLAITGSTGSGKTSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 393 LNLLIGFIQPTSGKIflddqpldeldMRSVRnyLAVVPQTTLLFSASIKENITYGLkNVSKERLDEVIEAAQLSSLIDQL 472
Cdd:cd03291 80 LMLILGELEPSEGKI-----------KHSGR--ISFSSQFSWIMPGTIKENIIFGV-SYDEYRYKSVVKACQLEEDITKF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 473 PDGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKI-QQALNYLTETPTTFIVAHRLSTIKEA 551
Cdd:cd03291 146 PEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIfESCVCKLMANKTRILVTSKMEHLKKA 225
|
250 260
....*....|....*....|....*..
gi 1158646300 552 DKIVVIDEGKIVEIGTYEKLLAQKGYF 578
Cdd:cd03291 226 DKILILHEGSSYFYGTFSELQSLRPDF 252
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
351-567 |
4.50e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 119.09 E-value: 4.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 351 FEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVP 430
Cdd:PRK13648 10 FKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 431 QTTL-LFSASI-KENITYGLKNVS------KERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALI 502
Cdd:PRK13648 90 QNPDnQFVGSIvKYDVAFGLENHAvpydemHRRVSEALKQVDMLERADYEP-----------NALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 503 RQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVA--HRLSTIKEADKIVVIDEGKIVEIGT 567
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISitHDLSEAMEADHVIVMNKGTVYKEGT 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
363-573 |
4.87e-30 |
|
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: 118.03 E-value: 4.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDM-RSVRNYLAVVPQTTLLF-SASI 440
Cdd:cd03218 13 RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGYLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 441 KENI------TYGLKNVSKERLDEVIEAAQLSSLIDQLpdgldtlvgehGNKLSGGQKQCISIARALIRQPKIILLDEAT 514
Cdd:cd03218 93 EENIlavleiRGLSKKEREEKLEELLEEFHITHLRKSK-----------ASSLSGGERRRVEIARALATNPKFLLLDEPF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 515 SALDNQSEKKIQQALNYLTETPT-TFIVAHRLS-TIKEADKIVVIDEGKIVEIGTYEKLLA 573
Cdd:cd03218 162 AGVDPIAVQDIQKIIKILKDRGIgVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
347-578 |
6.57e-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: 118.80 E-value: 6.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 347 GNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQpTSGKIFLDDQPLDELDMRSVRNYL 426
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQTTLLFSASIKENIT-YGlkNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQP 505
Cdd:cd03289 80 GVIPQKVFIFSGTFRKNLDpYG--KWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 506 KIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYF 578
Cdd:cd03289 158 KILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
350-567 |
7.64e-30 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.29 E-value: 7.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLKPII--DHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELD---MRSVRN 424
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 425 YLAVVPQT-TLLFSASIKENITYGLK--NVSKE----RLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISI 497
Cdd:PRK11153 83 QIGMIFQHfNLLSSRTVFDNVALPLElaGTPKAeikaRVTELLELVGLSDKADRYP-----------AQLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 498 ARALIRQPKIILLDEATSALDNQSE-------KKIQQALNyLTetpttfIV--AHRLSTIKE-ADKIVVIDEGKIVEIGT 567
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTrsilellKDINRELG-LT------IVliTHEMDVVKRiCDRVAVIDAGRLVEQGT 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
351-562 |
8.20e-30 |
|
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: 116.74 E-value: 8.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 351 FEDVSFLYPDSLkPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSV---RNYLA 427
Cdd:cd03292 3 FINVTKTYPNGT-AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpylRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 VVPQ-TTLLFSASIKENITYGLKNVSK------ERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARA 500
Cdd:cd03292 82 VVFQdFRLLPDRNVYENVAFALEVTGVppreirKRVPAALELVGLSHKHRALP-----------AELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 501 LIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADK--IVVIDEGKI 562
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
363-563 |
9.48e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 117.88 E-value: 9.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDEL--DMRSvrNYLAVVPQTTLLFSA-- 438
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLpeYKRA--KYIGRVFQDPMMGTAps 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 439 -SIKENI--------TYGLKN-VSKERLDEVIEaaQLSSLIDQLPDGLDTLVGehgnKLSGGQKQCISIARALIRQPKII 508
Cdd:COG1101 97 mTIEENLalayrrgkRRGLRRgLTKKRRELFRE--LLATLGLGLENRLDTKVG----LLSGGQRQALSLLMATLTKPKLL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 509 LLDEATSALDNQSEKKIQQalnyLTETP------TTFIVAHRLS-TIKEADKIVVIDEGKIV 563
Cdd:COG1101 171 LLDEHTAALDPKTAALVLE----LTEKIveennlTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
363-518 |
1.04e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 116.43 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQP---TSGKIFLDDQPLDELDMRSVRnyLAVVPQTTLLFS-A 438
Cdd:COG4136 14 RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRR--IGILFQDDLLFPhL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 439 SIKENITYGL-KNVSKERLDEVIEAAqLSSLidqlpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSAL 517
Cdd:COG4136 92 SVGENLAFALpPTIGRAQRRARVEQA-LEEA------GLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
.
gi 1158646300 518 D 518
Cdd:COG4136 165 D 165
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
365-567 |
2.18e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 119.42 E-value: 2.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 365 IIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRnyLAVVPQTTLLFS-ASIKEN 443
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFRhMTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 444 ITYGLK----------NVSKERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLDEA 513
Cdd:PRK10851 95 IAFGLTvlprrerpnaAAIKAKVTQLLEMVQLAHLADRYP-----------AQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 514 TSALDNQSEKKIQQALNYLTETP--TTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGT 567
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEvADRVVVMSQGNIEQAGT 220
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
371-573 |
3.31e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 116.00 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 371 LEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLD--------ELDMRSVRNYLAVVPQTTLLFS-ASIK 441
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarslsqqKGLIRQLRQHVGFVFQNFNLFPhRTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITYGLKNVSKERLDEVIEAAQlsSLIDQLpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQS 521
Cdd:PRK11264 104 ENIIEGPVIVKGEPKEEATARAR--ELLAKV--GLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPEL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 522 EKKIQQALNYLTETPTTF-IVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLA 573
Cdd:PRK11264 180 VGEVLNTIRQLAQEKRTMvIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
366-569 |
3.32e-29 |
|
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: 115.61 E-value: 3.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDM-RSVRNYLAVVPQTTLLFSA-SIKEN 443
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPhEIARLGIGRTFQIPRLFPElTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 444 ITYGLKNVSKERLDEVIEAAQLSSLIDQ---------LPDGLDTLVGEhgnkLSGGQKQCISIARALIRQPKIILLDEAT 514
Cdd:cd03219 96 VMVAAQARTGSGLLLARARREEREARERaeellervgLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 515 SALdNQSEkkIQQALNYLTETP----TTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYE 569
Cdd:cd03219 172 AGL-NPEE--TEELAELIRELRergiTVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPD 228
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
362-564 |
4.27e-29 |
|
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: 115.22 E-value: 4.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 362 LKPIidhfSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSV----RNYLAVVPQT-TLLF 436
Cdd:COG4181 28 LKGI----SLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQSfQLLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 437 SASIKENITY-----GLKNvSKERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLD 511
Cdd:COG4181 104 TLTALENVMLplelaGRRD-ARARARALLERVGLGHRLDHYP-----------AQLSGGEQQRVALARAFATEPAILFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 512 EATSALDNQSEKKIQQALNYLT-ETPTT-FIVAHRLSTIKEADKIVVIDEGKIVE 564
Cdd:COG4181 172 EPTGNLDAATGEQIIDLLFELNrERGTTlVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
364-566 |
4.58e-29 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 118.59 E-value: 4.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 364 PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELD--MRSVrnylAVVPQTTLLFS-ASI 440
Cdd:PRK11000 17 VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPpaERGV----GMVFQSYALYPhLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 441 KENITYGLK--NVSKE----RLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLDEAT 514
Cdd:PRK11000 93 AENMSFGLKlaGAKKEeinqRVNQVAEVLQLAHLLDRKP-----------KALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 515 SALD-----------NQSEKKIQQALNYLTetpttfivaH-RLSTIKEADKIVVIDEGKIVEIG 566
Cdd:PRK11000 162 SNLDaalrvqmrieiSRLHKRLGRTMIYVT---------HdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
346-581 |
8.27e-29 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 122.54 E-value: 8.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 346 DGNFRFEdvsflyPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLddqpldeldmrsVRNY 425
Cdd:PLN03130 619 NGYFSWD------SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRGT 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 426 LAVVPQTTLLFSASIKENITYGLKnVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQP 505
Cdd:PLN03130 681 VAYVPQVSWIFNATVRDNILFGSP-FDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 506 KIILLDEATSALDNQS-----EKKIQQALnyltETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYFYR 580
Cdd:PLN03130 760 DVYIFDDPLSALDAHVgrqvfDKCIKDEL----RGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQK 835
|
.
gi 1158646300 581 L 581
Cdd:PLN03130 836 L 836
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
350-573 |
9.16e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 115.47 E-value: 9.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLddQPLDELD---MRSVRNYL 426
Cdd:PRK13644 3 RLENVSYSYPDG-TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLV--SGIDTGDfskLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQT--TLLFSASIKENITYGLKNVS------KERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIA 498
Cdd:PRK13644 80 GIVFQNpeTQFVGRTVEEDLAFGPENLClppieiRKRVDRALAEIGLEKYRHRSP-----------KTLSGGQGQCVALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1158646300 499 RALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFI-VAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLA 573
Cdd:PRK13644 149 GILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVyITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-429 |
1.29e-28 |
|
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: 119.90 E-value: 1.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 20 LLHLYQGNYWRFAMSGLFFIIkhlpSWLMPIAIANVINAASSKDSSqLQAIYFNAFLMAC---LIGQNILTNYFhvkyhS 96
Cdd:COG4615 4 LRLLLRESRWLLLLALLLGLL----SGLANAGLIALINQALNATGA-ALARLLLLFAGLLvllLLSRLASQLLL-----T 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 97 TSIRQVEAGLRATLIKKIqeLSIPYQK--ELQSGRIQSKIIRDVEAIqtlsSQVFVSGLNIAVNLFVALGITLY---KSP 171
Cdd:COG4615 74 RLGQHAVARLRLRLSRRI--LAAPLERleRIGAARLLAALTEDVRTI----SQAFVRLPELLQSVALVLGCLAYlawLSP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 172 VVFMFFLLTVPLAAFVTLFFRKRIRQSnsdFRQEMEETSA------KVIEVI-ELA-PIARAHGLekhettrLNKHFTQI 243
Cdd:COG4615 148 PLFLLTLVLLGLGVAGYRLLVRRARRH---LRRAREAEDRlfkhfrALLEGFkELKlNRRRRRAF-------FDEDLQPT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 244 YEKGFHLDIL-QSVFGS-VSWASFQIFQLICLIFtGILALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKG---M 318
Cdd:COG4615 218 AERYRDLRIRaDTIFALaNNWGNLLFFALIGLIL-FLLPALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRAnvaL 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 319 ESITSIGELLIAGDVETYHGKKKIQHLDGN-FRFEDVSFLYPD-------SLKPIidhfSLEVKAGETIAFVGPSGSGKS 390
Cdd:COG4615 297 RKIEELELALAAAEPAAADAAAPPAPADFQtLELRGVTYRYPGedgdegfTLGPI----DLTIRRGELVFIVGGNGSGKS 372
|
410 420 430
....*....|....*....|....*....|....*....
gi 1158646300 391 TLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVV 429
Cdd:COG4615 373 TLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAV 411
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
349-572 |
1.98e-28 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 114.03 E-value: 1.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSG---KIFldDQPLDELDMRSVRNY 425
Cdd:COG1119 4 LELRNVTVRRGG--KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLF--GERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 426 LAVV-PQTTLLFSASIK-ENI-------TYGL-KNVS---KERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQK 492
Cdd:COG1119 80 IGLVsPALQLRFPRDETvLDVvlsgffdSIGLyREPTdeqRERARELLELLGLAHLADRPF-----------GTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 493 QCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETP-TTFI-VAHRLSTIKEA-DKIVVIDEGKIVEIGTYE 569
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVlVTHHVEEIPPGiTHVLLLKDGRVVAAGPKE 228
|
...
gi 1158646300 570 KLL 572
Cdd:COG1119 229 EVL 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
366-569 |
4.44e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 113.21 E-value: 4.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSV------RNYlavvpQTTLLFSA- 438
Cdd:COG0411 20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarlgiaRTF-----QNPRLFPEl 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 439 SIKENITYGLKNVSKERL--------------DEVIEAAQlsSLIDQLpdGL----DTLVGEhgnkLSGGQKQCISIARA 500
Cdd:COG0411 95 TVLENVLVAAHARLGRGLlaallrlprarreeREARERAE--ELLERV--GLadraDEPAGN----LSYGQQRRLEIARA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 501 LIRQPKIILLDEATSALdNQSEKK-IQQALNYLTETP--TTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYE 569
Cdd:COG0411 167 LATEPKLLLLDEPAAGL-NPEETEeLAELIRRLRDERgiTILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPA 238
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
364-570 |
4.51e-28 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 115.71 E-value: 4.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 364 PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSvRNyLAVVPQTTLLFS-ASIKE 442
Cdd:PRK11650 18 QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-RD-IAMVFQNYALYPhMSVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 443 NITYGLKN--VSKERLDE-VIEAAQ---LSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLDEATSA 516
Cdd:PRK11650 96 NMAYGLKIrgMPKAEIEErVAEAARileLEPLLDRKP-----------RELSGGQRQRVAMGRAIVREPAVFLFDEPLSN 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 517 LDNQ------SE-KKIQQALNyltetpTTFI-VAH-RLSTIKEADKIVVIDEGKIVEIGT----YEK 570
Cdd:PRK11650 165 LDAKlrvqmrLEiQRLHRRLK------TTSLyVTHdQVEAMTLADRVVVMNGGVAEQIGTpvevYEK 225
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
352-574 |
5.30e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 113.64 E-value: 5.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 352 EDVSFLYPDS----LKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDD-QPLDELDMRSVRNYL 426
Cdd:PRK13633 8 KNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGlDTSDEENLWDIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQT--TLLFSASIKENITYGLKNVS------KERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIA 498
Cdd:PRK13633 88 GMVFQNpdNQIVATIVEEDVAFGPENLGippeeiRERVDESLKKVGMYEYRRHAP-----------HLLSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 499 RALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETP--TTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
350-529 |
5.43e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 113.03 E-value: 5.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSL--KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRsvRnylA 427
Cdd:COG4525 5 TVRHVSVRYPGGGqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD--R---G 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 VVPQT-TLLFSASIKENITYGLK--NVSK-ERLDEvieAAQLSSLIdqlpdGLDtlvgEHGNK----LSGGQKQCISIAR 499
Cdd:COG4525 80 VVFQKdALLPWLNVLDNVAFGLRlrGVPKaERRAR---AEELLALV-----GLA----DFARRriwqLSGGMRQRVGIAR 147
|
170 180 190
....*....|....*....|....*....|
gi 1158646300 500 ALIRQPKIILLDEATSALDNQSEKKIQQAL 529
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELL 177
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
353-575 |
7.00e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.25 E-value: 7.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 353 DVSFLYPD---SLKPIidhfSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPL--DELDMRSVRNYLA 427
Cdd:PRK13639 6 DLKYSYPDgteALKGI----NFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 VVPQTT--LLFSASIKENITYGLKNVS------KERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIAR 499
Cdd:PRK13639 82 IVFQNPddQLFAPTVEEDVAFGPLNLGlskeevEKRVKEALKAVGMEGFENKPP-----------HHLSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 500 ALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVA-HRLSTI-KEADKIVVIDEGKIVEIGTYEKLLAQK 575
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
367-569 |
9.51e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.04 E-value: 9.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 367 DHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNY-LAVVPQTTLLFSA-SIKENI 444
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQELNLVPNlSVAENI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 445 TYGLKNVSKERLD--EVIEAAQlsSLIDQLpdGLD----TLVGEhgnkLSGGQKQCISIARALIRQPKIILLDEATSALD 518
Cdd:COG1129 101 FLGREPRRGGLIDwrAMRRRAR--ELLARL--GLDidpdTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 519 NQSEKKIQQALNYLTETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIVeiGTYE 569
Cdd:COG1129 173 EREVERLFRIIRRLKAQGVAIIyISHRLDEVFEiADRVTVLRDGRLV--GTGP 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
366-571 |
1.38e-27 |
|
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: 110.54 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDqpLDEL-DMRSVRNYLAVVPQttllfSASIKENI 444
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVrEPREVRRRIGIVFQ-----DLSVDDEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 445 T-----------YGLKN-VSKERLDEVIEAAQLSslidqlpDGLDTLVGehgnKLSGGQKQCISIARALIRQPKIILLDE 512
Cdd:cd03265 89 TgwenlyiharlYGVPGaERRERIDELLDFVGLL-------EAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 513 ATSALDNQSEKKIQQALNYLTETP--TTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKL 571
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLKEEFgmTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
352-566 |
2.08e-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: 109.98 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 352 EDVSFLYPDslKPIIDHFSLEVKAGeTIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDElDMRSVRNYLAVVPQ 431
Cdd:cd03264 4 ENLTKRYGK--KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 432 TTLLFSA-SIKENITY--GLKNVS----KERLDEVIEAAQLSslidqlpDGLDTLVGehgnKLSGGQKQCISIARALIRQ 504
Cdd:cd03264 80 EFGVYPNfTVREFLDYiaWLKGIPskevKARVDEVLELVNLG-------DRAKKKIG----SLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 505 PKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIG 566
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
318-578 |
2.74e-27 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 117.70 E-value: 2.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 318 MESITS-----IGELLiaGDVETYHGKKKIQHLDGNFRFEDVSFLypdsLKPIIDHFSLEVKAGETIAFVGPSGSGKSTL 392
Cdd:TIGR01271 395 MVNVTAswdegIGELF--EKIKQNNKARKQPNGDDGLFFSNFSLY----VTPVLKNISFKLEKGQLLAVAGSTGSGKSSL 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 393 LNLLIGFIQPTSGKIflddqpldeldMRSVRnyLAVVPQTTLLFSASIKENITYGLkNVSKERLDEVIEAAQLSSLIDQL 472
Cdd:TIGR01271 469 LMMIMGELEPSEGKI-----------KHSGR--ISFSPQTSWIMPGTIKDNIIFGL-SYDEYRYTSVIKACQLEEDIALF 534
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 473 PDGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKI-QQALNYLTETPTTFIVAHRLSTIKEA 551
Cdd:TIGR01271 535 PEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIfESCLCKLMSNKTRILVTSKLEHLKKA 614
|
250 260
....*....|....*....|....*..
gi 1158646300 552 DKIVVIDEGKIVEIGTYEKLLAQKGYF 578
Cdd:TIGR01271 615 DKILLLHEGVCYFYGTFSELQAKRPDF 641
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
347-571 |
3.34e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 117.57 E-value: 3.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 347 GNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYL 426
Cdd:PTZ00243 1307 GSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQF 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQTTLLFSASIKENITYGLKNVSKerldEVIEAAQLSSLIDQL---PDGLDTLVGEHGNKLSGGQKQCISIARALI- 502
Cdd:PTZ00243 1387 SMIPQDPVLFDGTVRQNVDPFLEASSA----EVWAALELVGLRERVaseSEGIDSRVLEGGSNYSVGQRQLMCMARALLk 1462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1158646300 503 RQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKL 571
Cdd:PTZ00243 1463 KGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
363-571 |
3.63e-27 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.39 E-value: 3.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQpldelDMRSVRNY---LAVVPQTTLLFS-A 438
Cdd:PRK11607 32 QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV-----DLSHVPPYqrpINMMFQSYALFPhM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 439 SIKENITYGLKNVS------KERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLDE 512
Cdd:PRK11607 107 TVEQNIAFGLKQDKlpkaeiASRVNEMLGLVHMQEFAKRKP-----------HQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 513 ATSALDNQSEKKIQQALNYLTET--PTTFIVAH-RLSTIKEADKIVVIDEGKIVEIGTYEKL 571
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERvgVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
365-567 |
6.60e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 109.15 E-value: 6.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 365 IIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDEL--DMRsVRNYLAVVPQTTLLFSA-SIK 441
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLppHER-ARAGIAYVPQGREIFPRlTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITYGL---KNVSKERLDEVIEaaqlsslidqLPDGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALD 518
Cdd:TIGR03410 94 ENLLTGLaalPRRSRKIPDEIYE----------LFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 519 NQSEKKIQQALNYLTETP--TTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGT 567
Cdd:TIGR03410 164 PSIIKDIGRVIRRLRAEGgmAILLVEQYLDFARElADRYYVMERGRVVASGA 215
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
353-574 |
8.09e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.21 E-value: 8.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 353 DVSFLY-PDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQ 431
Cdd:PRK13650 9 NLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 432 T--TLLFSASIKENITYGLKNVS------KERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIR 503
Cdd:PRK13650 89 NpdNQFVGATVEDDVAFGLENKGipheemKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAGAVAM 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 504 QPKIILLDEATSALDN-------QSEKKIQQALNYltetpTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:PRK13650 158 RPKIIILDEATSMLDPegrleliKTIKGIRDDYQM-----TVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
363-566 |
9.17e-27 |
|
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: 108.14 E-value: 9.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDmrsvRNYLAVVPQTTLLF-SASIK 441
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITY--GLKNVSKE----RLDEVIEAAQLSslidqlpdgldtlvgEHGNK----LSGGQKQCISIARALIRQPKIILLD 511
Cdd:cd03269 89 DQLVYlaQLKGLKKEearrRIDEWLERLELS---------------EYANKrveeLSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 512 EATSALDNQSEKKIQQALNYLTETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIVEIG 566
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAGKTVIlSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
366-567 |
1.24e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.75 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDE--LDMRSVRNYLAVVPQ--TTLLFSASIK 441
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIRKKVGLVFQypEYQLFEETIE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITYGLKNVS------KERLDEVIEAAQLS--SLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLDEA 513
Cdd:PRK13637 103 KDIAFGPINLGlseeeiENRVKRAMNIVGLDyeDYKDKSP-----------FELSGGQKRRVAIAGVVAMEPKILILDEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 514 TSALDNQSEKKIQQALNYLTE--TPTTFIVAHRLSTI-KEADKIVVIDEGKIVEIGT 567
Cdd:PRK13637 172 TAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
366-566 |
1.28e-26 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 107.84 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDqpLDEL-DMRSVRNYLAVVPQTTLLFS-ASIKEN 443
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDG--FDVVkEPAEARRRLGFVSDSTGLYDrLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 444 ITY-----GLK-NVSKERLDEVIEAAQLSSLIDQlpdgldtlvgeHGNKLSGGQKQCISIARALIRQPKIILLDEATSAL 517
Cdd:cd03266 99 LEYfaglyGLKgDELTARLEELADRLGMEELLDR-----------RVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 518 DNQSEKKIQQALNYLTETPTTFIVA-HRLSTIKE-ADKIVVIDEGKIVEIG 566
Cdd:cd03266 168 DVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
351-572 |
1.77e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 108.26 E-value: 1.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 351 FEDVSFLYPDSlkPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPL--DELDMRSVRNYLAV 428
Cdd:PRK09493 4 FKNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 V-------PQTTLLfsasikENITYGLKNV---SKErldeviEAAQLSS-LIDQLpdGLDTLVGEHGNKLSGGQKQCISI 497
Cdd:PRK09493 82 VfqqfylfPHLTAL------ENVMFGPLRVrgaSKE------EAEKQAReLLAKV--GLAERAHHYPSELSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 498 ARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTF-IVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLL 572
Cdd:PRK09493 148 ARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMvIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
352-566 |
1.96e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 108.32 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 352 EDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLL--IGFIQP---TSGKIFLDDQPL--DELDMRSVRN 424
Cdd:PRK14239 9 SDLSVYYNK--KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIysPRTDTVDLRK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 425 YLAVVPQTTLLFSASIKENITYGL--KNV-SKERLDEVIEAA-QLSSLIDQLPDGL-DTLVGehgnkLSGGQKQCISIAR 499
Cdd:PRK14239 87 EIGMVFQQPNPFPMSIYENVVYGLrlKGIkDKQVLDEAVEKSlKGASIWDEVKDRLhDSALG-----LSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 500 ALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRL---STIkeADKIVVIDEGKIVEIG 566
Cdd:PRK14239 162 VLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYN 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
352-573 |
2.05e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 107.76 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 352 EDVSFLYPDSlkPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDM-RSVRNYLAVVP 430
Cdd:COG0410 7 ENLHAGYGGI--HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhRIARLGIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 431 QTTLLFSA-SIKENITYGL-----KNVSKERLDEVIEA-AQLSSLIDQLpdgldtlvgehGNKLSGGQKQCISIARALIR 503
Cdd:COG0410 85 EGRRIFPSlTVEENLLLGAyarrdRAEVRADLERVYELfPRLKERRRQR-----------AGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 504 QPKIILLDEAtsaldnqSE-------KKIQQALNYLTETPTTFIV----AHRLSTIkeADKIVVIDEGKIVEIGTYEKLL 572
Cdd:COG0410 154 RPKLLLLDEP-------SLglaplivEEIFEIIRRLNREGVTILLveqnARFALEI--ADRAYVLERGRIVLEGTAAELL 224
|
.
gi 1158646300 573 A 573
Cdd:COG0410 225 A 225
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
366-566 |
2.14e-26 |
|
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: 107.55 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELD---MRSVRNYlavvpqtTLLFSASIKE 442
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGpdrMVVFQNY-------SLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 443 NITYGLKNVSKER--------LDEVIEAAQLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIARALIRQPKIILLDEAT 514
Cdd:TIGR01184 74 NIALAVDRVLPDLskserraiVEEHIALVGLTEAADKRPG-----------QLSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 515 SALDNQSEKKIQQALNYLTET--PTTFIVAHrlsTIKEA----DKIVVIDEGKIVEIG 566
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEhrVTVLMVTH---DVDEAlllsDRVVMLTNGPAANIG 197
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
363-564 |
2.72e-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: 106.53 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQplDELDMRSVRNYLAVVPQTTLLFSA-SIK 441
Cdd:cd03268 13 KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK--SYQKNIEALRRIGALIEAPGFYPNlTAR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITYG--LKNVSKERLDEVIEAAqlsslidqlpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDN 519
Cdd:cd03268 91 ENLRLLarLLGIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1158646300 520 QSEKKIQQALNYLTETPTTFIVA-HRLSTI-KEADKIVVIDEGKIVE 564
Cdd:cd03268 160 DGIKELRELILSLRDQGITVLISsHLLSEIqKVADRIGIINKGKLIE 206
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
359-571 |
2.81e-26 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 109.80 E-value: 2.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 359 PDSLKPIiDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKI-FL--DDQPLDELDMRSVRNYLAVVPQTTLl 435
Cdd:PRK15079 31 PKTLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLgkDLLGMKDDEWRAVRSDIQMIFQDPL- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 436 fsASIKENITYG------LK----NVSKERLDEVIEAAQLSslIDQLPDgldtLVGEHGNKLSGGQKQCISIARALIRQP 505
Cdd:PRK15079 109 --ASLNPRMTIGeiiaepLRtyhpKLSRQEVKDRVKAMMLK--VGLLPN----LINRYPHEFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 506 KIILLDEATSALDnqseKKIQ-QALNYLTET------PTTFIvAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKL 571
Cdd:PRK15079 181 KLIICDEPVSALD----VSIQaQVVNLLQQLqremglSLIFI-AHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
340-578 |
4.40e-26 |
|
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: 113.85 E-value: 4.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 340 KKIQHLDGNFRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQpTSGKIFLDDQPLDELDM 419
Cdd:TIGR01271 1209 QKCWPSGGQMDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTL 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 420 RSVRNYLAVVPQTTLLFSASIKENITyGLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIAR 499
Cdd:TIGR01271 1288 QTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLAR 1366
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1158646300 500 ALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQKGYF 578
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
363-555 |
4.56e-26 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 106.34 E-value: 4.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQTTLLFSASIKE 442
Cdd:PRK10247 20 AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 443 NITYGLKnVSKERLDEVIEAAQLSSLidQLPdglDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSE 522
Cdd:PRK10247 100 NLIFPWQ-IRNQQPDPAIFLDDLERF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK 173
|
170 180 190
....*....|....*....|....*....|....*
gi 1158646300 523 KKIQQALN-YLTETPTTFI-VAHRLSTIKEADKIV 555
Cdd:PRK10247 174 HNVNEIIHrYVREQNIAVLwVTHDKDEINHADKVI 208
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
370-567 |
1.08e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 105.87 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 370 SLEVKAGETIAFVGPSGSGKSTL---LNLLIGfiqPTSGKI------FLDDQPLDELDMRSVRNYLAVVPQTTLLFS-AS 439
Cdd:PRK11124 22 TLDCPQGETLVLLGPSGAGKSSLlrvLNLLEM---PRSGTLniagnhFDFSKTPSDKAIRELRRNVGMVFQQYNLWPhLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 440 IKENIT------YGL-KNVSKERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLDE 512
Cdd:PRK11124 99 VQQNLIeapcrvLGLsKDQALARAEKLLERLRLKPYADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFDE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 513 ATSALDNQSEKKIQQALNYLTETP-TTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGT 567
Cdd:PRK11124 168 PTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEVARKtASRVVYMENGHIVEQGD 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
365-562 |
1.43e-25 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.92 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 365 IIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDEldmrsVRNylavvpQTTLLFS------- 437
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE-----ARE------DTRLMFQdarllpw 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 438 ASIKENITYGLKNVSKERLDEVIEAAqlsslidqlpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSAL 517
Cdd:PRK11247 96 KKVIDNVGLGLKGQWRDAALQALAAV-----------GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1158646300 518 DNQSEKKIQQALNYLTETP--TTFIVAHRLS-TIKEADKIVVIDEGKI 562
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
349-563 |
1.51e-25 |
|
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: 102.89 E-value: 1.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDSlkPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELD-MRSVRNYLA 427
Cdd:cd03216 1 LELRGITKRFGGV--KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 VVPQttllfsasikenityglknvskerldevieaaqlsslidqlpdgldtlvgehgnkLSGGQKQCISIARALIRQPKI 507
Cdd:cd03216 79 MVYQ-------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 508 ILLDEATSALDNQSEKKIQQALNYLTETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIV 563
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQGVAVIfISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
352-574 |
3.58e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 105.27 E-value: 3.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 352 EDVSFLYPDSLKpIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQ 431
Cdd:PRK13652 7 RDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 432 TT--LLFSASIKENITYGLKNVS------KERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIR 503
Cdd:PRK13652 86 NPddQIFSPTVEQDIAFGPINLGldeetvAHRVSSALHMLGLEELRDRVP-----------HHLSGGEKKRVAIAGVIAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 504 QPKIILLDEATSALDNQSEKKIQQALNYLTET--PTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:PRK13652 155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
352-575 |
5.17e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.93 E-value: 5.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 352 EDVSFLYPDSLKPIIDhFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLD--ELDMRSVRNYLAVV 429
Cdd:PRK13636 9 EELNYNYSDGTHALKG-ININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysRKGLMKLRESVGMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQT--TLLFSASIKENITYGLKNVS------KERLDEVIEAAQLSSLIDQlPDgldtlvgehgNKLSGGQKQCISIARAL 501
Cdd:PRK13636 88 FQDpdNQLFSASVYQDVSFGAVNLKlpedevRKRVDNALKRTGIEHLKDK-PT----------HCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 502 IRQPKIILLDEATSALDNQSEKKIQQALNYLTETP--TTFIVAHRLSTIK-EADKIVVIDEGKIVEIGTYEKLLAQK 575
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
363-575 |
9.00e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.56 E-value: 9.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQTTLLFSA-SIK 441
Cdd:PRK11231 15 KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGiTVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITYG----------LKNVSKERLDEVIEAAQLSSLIDQLPDgldtlvgehgnKLSGGQKQCISIARALIRQPKIILLD 511
Cdd:PRK11231 95 ELVAYGrspwlslwgrLSAEDNARVNQAMEQTRINHLADRRLT-----------DLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 512 EATSALD--NQSE-KKIQQALNylTETPTTFIVAHRLS-TIKEADKIVVIDEGKIVEIGTYEKLLAQK 575
Cdd:PRK11231 164 EPTTYLDinHQVElMRLMRELN--TQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
363-577 |
9.18e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 104.81 E-value: 9.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVrNYLavvPQTTLLFSA-SIK 441
Cdd:COG4152 14 KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRI-GYL---PEERGLYPKmKVG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITY-----GL-KNVSKERLDEVIEAAQLsslidqlpdgldtlvGEHGNK----LSGGQKQCISIARALIRQPKIILLD 511
Cdd:COG4152 90 EQLVYlarlkGLsKAEAKRRADEWLERLGL---------------GDRANKkveeLSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 512 EATSALD--NQSekKIQQALNYLTETPTTFIVA-HRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQKGY 577
Cdd:COG4152 155 EPFSGLDpvNVE--LLKDVIRELAAKGTTVIFSsHQMELVEElCDRIVIINKGRKVLSGSVDEIRRQFGR 222
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-566 |
1.18e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.07 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 365 IIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQ-----PTSGKIFLDDQPLDELDMRSVRNYLAVVPQT-TLLFSA 438
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIpNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 439 SIKENITYGLK-----NVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGehgnKLSGGQKQCISIARALIRQPKIILLDEA 513
Cdd:PRK14247 98 SIFENVALGLKlnrlvKSKKELQERVRWALEKAQLWDEVKDRLDAPAG----KLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 514 TSALDNQSEKKIQQALNYLTETPTTFIVAH-RLSTIKEADKIVVIDEGKIVEIG 566
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
370-567 |
1.42e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.78 E-value: 1.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 370 SLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDD------QPLDELDMRSVRNYLAVVPQTTLLFS-ASIKE 442
Cdd:COG4161 22 NLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQKVGMVFQQYNLWPhLTVME 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 443 NIT------YGL-KNVSKERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLDEATS 515
Cdd:COG4161 102 NLIeapckvLGLsKEQAREKAMKLLARLRLTDKADRFP-----------LHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 516 ALDNQSEKKIQQALNYLTETP-TTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGT 567
Cdd:COG4161 171 ALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKvASQVVYMEKGRIIEQGD 224
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
363-573 |
2.05e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.03 E-value: 2.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDM--RSVR--NYLavvPQTtllfsA 438
Cdd:COG1137 16 RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMhkRARLgiGYL---PQE-----A 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 439 SI------KENI-----TYGL-KNVSKERLDEVIEAAQLSSLIDQLpdgldtlvgehGNKLSGGQKQCISIARALIRQPK 506
Cdd:COG1137 88 SIfrkltvEDNIlavleLRKLsKKEREERLEELLEEFGITHLRKSK-----------AYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 507 IILLDEATSALDNQSEKKIQQALNYLT--------------ETpttfivahrLSTIkeaDKIVVIDEGKIVEIGTYEKLL 572
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKergigvlitdhnvrET---------LGIC---DRAYIISEGKVLAEGTPEEIL 224
|
.
gi 1158646300 573 A 573
Cdd:COG1137 225 N 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
367-563 |
2.20e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 106.65 E-value: 2.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 367 DHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPldeLDMRS----VRNYLAVVPQTTLLFSA-SIK 441
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP---VRIRSprdaIALGIGMVHQHFMLVPNlTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITYGLKNVSKERLDEVIEAAQLSSLIDQLpdGL----DTLVGEhgnkLSGGQKQCISIARALIRQPKIILLDEATSAL 517
Cdd:COG3845 99 ENIVLGLEPTKGGRLDRKAARARIRELSERY--GLdvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1158646300 518 DNQSEKKIQQALNYLTETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIV 563
Cdd:COG3845 173 TPQEADELFEILRRLAAEGKSIIfITHKLREVMAiADRVTVLRRGKVV 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
349-558 |
2.52e-24 |
|
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: 99.54 E-value: 2.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIfldDQPLDEldmrsvrnYLAV 428
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---GMPEGE--------DLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 VPQTTLLFSASIKENITYGLKNVskerldevieaaqlsslidqlpdgldtlvgehgnkLSGGQKQCISIARALIRQPKII 508
Cdd:cd03223 69 LPQRPYLPLGTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 509 LLDEATSALDNQSEKKIQQALNyltETPTTFI-VAHRLSTIKEADKIVVID 558
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLLK---ELGITVIsVGHRPSLWKFHDRVLDLD 161
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
351-564 |
2.92e-24 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 103.35 E-value: 2.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 351 FEDVSFLYPDSLkpIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDElDMRSVRNYLAVVP 430
Cdd:PRK13537 10 FRNVEKRYGDKL--VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 431 Q-TTLLFSASIKENIT-----YGLKNVS-KERLDEVIEAAQLSSlidqlpdGLDTLVGEhgnkLSGGQKQCISIARALIR 503
Cdd:PRK13537 87 QfDNLDPDFTVRENLLvfgryFGLSAAAaRALVPPLLEFAKLEN-------KADAKVGE----LSGGMKRRLTLARALVN 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1158646300 504 QPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIV-------AHRLstikeADKIVVIDEG-KIVE 564
Cdd:PRK13537 156 DPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLtthfmeeAERL-----CDRLCVIEEGrKIAE 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
350-577 |
3.93e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.55 E-value: 3.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSL---KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDD----QPLDELDMRSV 422
Cdd:PRK13646 4 RFDNVSYTYQKGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRPV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 423 RNYLAVVPQ--TTLLFSASIKENITYGLKNVsKERLDEVIEAAQlsSLIDQLPDGLDTLvGEHGNKLSGGQKQCISIARA 500
Cdd:PRK13646 84 RKRIGMVFQfpESQLFEDTVEREIIFGPKNF-KMNLDEVKNYAH--RLLMDLGFSRDVM-SQSPFQMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 501 LIRQPKIILLDEATSALDNQSEKKIQQALNYLT--ETPTTFIVAHRLSTI-KEADKIVVIDEGKIVEIGTYEKLLAQKGY 577
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKDKKK 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
349-563 |
4.63e-24 |
|
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: 99.93 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDSL----KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQP--TSGKIFLDDQPLDeldMRSV 422
Cdd:cd03213 4 LSFRNLTVTVKSSPsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLD---KRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 423 RNYLAVVPQTTLLFSA-SIKENITYglknvskerldevieAAQLSSLidqlpdgldtlvgehgnklSGGQKQCISIARAL 501
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMF---------------AAKLRGL-------------------SGGERKRVSIALEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 502 IRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVA-HRLST--IKEADKIVVIDEGKIV 563
Cdd:cd03213 127 VSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSiHQPSSeiFELFDKLLLLSQGRVI 191
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
364-572 |
4.73e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.54 E-value: 4.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 364 PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQ-TTLLFSASIKE 442
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQdTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 443 NITYGlKNVSKERLDEVIEA--AQLSSLIDQLpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQ 520
Cdd:PRK09536 97 VVEMG-RTPHRSRFDTWTETdrAAVERAMERT--GVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 521 SEKKIQQALNYLTETPTTFIVA-HRLS-TIKEADKIVVIDEGKIVEIGTYEKLL 572
Cdd:PRK09536 174 HQVRTLELVRRLVDDGKTAVAAiHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
362-563 |
6.00e-24 |
|
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: 100.87 E-value: 6.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 362 LKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKI-FLDDQPLDELDmRSVRNYLAVVPQ-TTLLFSAS 439
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrVAGLVPWKRRK-KFLRRIGVVFGQkTQLWWDLP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 440 IKENIT-----YGLKNVS-KERLDEVIEAAQLSSLidqlpdgLDTLVgehgNKLSGGQKQCISIARALIRQPKIILLDEA 513
Cdd:cd03267 112 VIDSFYllaaiYDLPPARfKKRLDELSELLDLEEL-------LDTPV----RQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 514 TSALDNQSEKKIQQALNYLT-ETPTTFIV-AHRLSTI-KEADKIVVIDEGKIV 563
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNrERGTTVLLtSHYMKDIeALARRVLVIDKGRLL 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
351-575 |
7.66e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 105.15 E-value: 7.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 351 FEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDdqpldeldmRSVRnyLAVVP 430
Cdd:COG0488 1 LENLSKSFGG--RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLR--IGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 431 QTTLLFS-ASIKENITYGLKNVSK-------------------ERLDEVIEA----------AQLSSLIDQL---PDGLD 477
Cdd:COG0488 68 QEPPLDDdLTVLDTVLDGDAELRAleaeleeleaklaepdedlERLAELQEEfealggweaeARAEEILSGLgfpEEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 478 TLVGEhgnkLSGGQKQCISIARALIRQPKIILLDEATSALDNQS----EkkiqqalNYLTETPTTFI-VAH-R--LSTIk 549
Cdd:COG0488 148 RPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlE-------EFLKNYPGTVLvVSHdRyfLDRV- 215
|
250 260
....*....|....*....|....*..
gi 1158646300 550 eADKIVVIDEGKIVEI-GTYEKLLAQK 575
Cdd:COG0488 216 -ATRILELDRGKLTLYpGNYSAYLEQR 241
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
31-304 |
1.09e-23 |
|
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: 100.80 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 31 FAMSGLFFIIKHLPSWLMPIAIANVINAASSKDSSQLQAIYFNAFLMACLIGQNILTNYFHVKYHSTSIRQVEAGLRATL 110
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 111 IKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFVTLF 190
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 191 FRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIFQL 270
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260 270
....*....|....*....|....*....|....
gi 1158646300 271 ICLIFTGILALQGRIQPGDVVMYQTYFTTIVNSV 304
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
352-576 |
1.24e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 100.97 E-value: 1.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 352 EDVSFLYPDSLKPIiDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQ 431
Cdd:PRK13647 8 EDLHFRYKDGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 432 T--TLLFSASIKENITYGLKNVS------KERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIR 503
Cdd:PRK13647 87 DpdDQVFSSTVWDDVAFGPVNMGldkdevERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 504 QPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVA-HRLSTIKE-ADKIVVIDEGKIV-----EIGTYEKLLAQKG 576
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDLAAEwADQVIVLKEGRVLaegdkSLLTDEDIVEQAG 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
351-564 |
1.25e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 102.22 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 351 FEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDElDMRSVRNYLAVVP 430
Cdd:PRK13536 44 LAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 431 Q-TTLLFSASIKEN-ITYGLKNVSKERldeVIEAAqLSSLID--QLPDGLDTLVGEhgnkLSGGQKQCISIARALIRQPK 506
Cdd:PRK13536 121 QfDNLDLEFTVRENlLVFGRYFGMSTR---EIEAV-IPSLLEfaRLESKADARVSD----LSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 507 IILLDEATSALDNQSEKKIQQAL-NYLTETPTTFIVAHrlsTIKEA----DKIVVIDEG-KIVE 564
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLrSLLARGKTILLTTH---FMEEAerlcDRLCVLEAGrKIAE 253
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
350-573 |
1.34e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 101.25 E-value: 1.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLY----PDSLKPIIDhFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPL----DELDMRS 421
Cdd:PRK13634 4 TFQKVEHRYqyktPFERRALYD-VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 422 VRNYLAVVPQ--TTLLFSASIKENITYGLKN--VSKE----RLDEVIEAAQLS-SLIDQLPdgldtlvgehgNKLSGGQK 492
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEdakqKAREMIELVGLPeELLARSP-----------FELSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 493 QCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETP--TTFIVAHRLSTI-KEADKIVVIDEGKIVEIGTYE 569
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPR 231
|
....
gi 1158646300 570 KLLA 573
Cdd:PRK13634 232 EIFA 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
364-557 |
1.93e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.07 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 364 PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIflddqpldeldMRSVRNYLAVVPQTTLL---FSASI 440
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVpdsLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 441 KENITYGL--KNVSKERL---DEVIEAAQLSSLidqlpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATS 515
Cdd:NF040873 75 RDLVAMGRwaRRGLWRRLtrdDRAAVDDALERV------GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1158646300 516 ALDNQSEKKIQQALNYLTETPTTFIVA-HRLSTIKEADKIVVI 557
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVtHDLELVRRADPCVLL 191
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
363-577 |
2.40e-23 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 98.99 E-value: 2.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFI--QPTSGKIFLDDQPLDEL--DMRSVRN-YLAV--------V 429
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELspDERARAGiFLAFqypveipgV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLFSAsikenitygLKNVSKERLDEVIEAAQLSSLIDQL---PDGLDTLVGEhgnKLSGGQKQCISIARALIRQPK 506
Cdd:COG0396 93 SVSNFLRTA---------LNARRGEELSAREFLKLLKEKMKELgldEDFLDRYVNE---GFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1158646300 507 IILLDEATSALDNQSEKKIQQALNYLTETPTTFIV-AH--RLSTIKEADKIVVIDEGKIVEIGTYE--KLLAQKGY 577
Cdd:COG0396 161 LAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIiTHyqRILDYIKPDFVHVLVDGRIVKSGGKElaLELEEEGY 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
354-574 |
5.23e-23 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 102.84 E-value: 5.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 354 VSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKS----TLLNLLIGFIQPTSGKIFLDDQPL---DELDMRSVR-NY 425
Cdd:COG4172 14 VAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLlglSERELRRIRgNR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 426 LAVV---PQTTL--LFsaSIKENITYGL---KNVSK--------ERLDEV-IEAAQlsSLIDQLPdgldtlvgeHgnKLS 488
Cdd:COG4172 94 IAMIfqePMTSLnpLH--TIGKQIAEVLrlhRGLSGaaararalELLERVgIPDPE--RRLDAYP---------H--QLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 489 GGQKQCISIARALIRQPKIILLDEATSALD--NQSE-----KKIQQALNY--LtetpttFIvAHRLSTIKE-ADKIVVID 558
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDvtVQAQildllKDLQRELGMalL------LI-THDLGVVRRfADRVAVMR 231
|
250
....*....|....*.
gi 1158646300 559 EGKIVEIGTYEKLLAQ 574
Cdd:COG4172 232 QGEIVEQGPTAELFAA 247
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
362-573 |
7.81e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 102.09 E-value: 7.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 362 LKPIIDH------FSLEVKAGETIAFVGPSGSGKST----LLNLLigfiqPTSGKIFLDDQPLDELDMRS---VRNYLAV 428
Cdd:PRK15134 292 LKRTVDHnvvvknISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQllpVRHRIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 V---PQTTLLFSASIKENITYGL----KNVS-KERLDEVIEAAQlsslidqlPDGLD-TLVGEHGNKLSGGQKQCISIAR 499
Cdd:PRK15134 367 VfqdPNSSLNPRLNVLQIIEEGLrvhqPTLSaAQREQQVIAVME--------EVGLDpETRHRYPAEFSGGQRQRIAIAR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 500 ALIRQPKIILLDEATSALDNQSEKKIQQALNYLTET---PTTFIvAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLA 573
Cdd:PRK15134 439 ALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhqlAYLFI-SHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
363-529 |
1.03e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.85 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDM-RSVrnylaVVPQTTLLFSASIK 441
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAeRGV-----VFQNEGLLPWRNVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITYGLKNVSKERLDEVIEAAQLSSLIDqlpdgldtLVGEHGN---KLSGGQKQCISIARALIRQPKIILLDEATSALD 518
Cdd:PRK11248 89 DNVAFGLQLAGVEKMQRLEIAHQMLKKVG--------LEGAEKRyiwQLSGGQRQRVGIARALAANPQLLLLDEPFGALD 160
|
170
....*....|.
gi 1158646300 519 NQSEKKIQQAL 529
Cdd:PRK11248 161 AFTREQMQTLL 171
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
349-569 |
1.53e-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: 1.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKI----------FldDQPLDELD 418
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVklgetvkigyF--DQHQEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 419 M-----------------RSVRNYLAvvpqtTLLFSasikenityglknvskerldevieaaqlsslidqlPDGLDTLVG 481
Cdd:COG0488 392 PdktvldelrdgapggteQEVRGYLG-----RFLFS-----------------------------------GDDAFKPVG 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 482 ehgnKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSekkiQQALN-YLTETP-TTFIVAH-R--LSTIkeADKIVV 556
Cdd:COG0488 432 ----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET----LEALEeALDDFPgTVLLVSHdRyfLDRV--ATRILE 501
|
250
....*....|....
gi 1158646300 557 IDEGKIVE-IGTYE 569
Cdd:COG0488 502 FEDGGVREyPGGYD 515
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
352-563 |
1.79e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.72 E-value: 1.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 352 EDVSFLYP--DSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSV----RNY 425
Cdd:PRK10535 8 KDIRRSYPsgEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 426 LAVVPQTT-LLFSASIKEN-----ITYGLKnvSKERLDEVIEaaqlssLIDQLpdGLDTLVGEHGNKLSGGQKQCISIAR 499
Cdd:PRK10535 88 FGFIFQRYhLLSHLTAAQNvevpaVYAGLE--RKQRLLRAQE------LLQRL--GLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 500 ALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETP-TTFIVAHRLSTIKEADKIVVIDEGKIV 563
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGhTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
366-574 |
2.48e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 98.24 E-value: 2.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKI-FLDDQPLDElDMRSVRNYLAVVPQ-TTLLFSASIKEN 443
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVrVLGYVPFKR-RKEFARRIGVVFGQrSQLWWDLPAIDS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 444 IT-----YGL-KNVSKERLDEVIEAAQLSSLIDQlPdgldtlVgehgNKLSGGQKQCISIARALIRQPKIILLDEATSAL 517
Cdd:COG4586 117 FRllkaiYRIpDAEYKKRLDELVELLDLGELLDT-P------V----RQLSLGQRMRCELAAALLHRPKILFLDEPTIGL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 518 DNQSEKKIQQALNYL-TETPTTFIVA-HRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:COG4586 186 DVVSKEAIREFLKEYnRERGTTILLTsHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
350-566 |
4.61e-22 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 95.03 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVS--FLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQP---TSGKIFLDDQPLDELDMRSVRN 424
Cdd:cd03234 5 PWWDVGlkAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQKCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 425 YlavVPQT-TLLFSASIKENITYG----LKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGehgnkLSGGQKQCISIAR 499
Cdd:cd03234 85 Y---VRQDdILLPGLTVRETLTYTailrLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKG-----ISGGERRRVSIAV 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 500 ALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVA-H--RLSTIKEADKIVVIDEGKIVEIG 566
Cdd:cd03234 157 QLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTiHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
333-573 |
4.95e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 96.01 E-value: 4.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 333 VETYHGKKKIQHLDGNFRFEDVsflypDSLKPIidhfSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQ 412
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWFRRQTV-----EAVKPL----SFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 413 PLDELD--MRSVRNYLAVV-PQTTLLFSASIKENITYGLK-NV---SKERLDEVIEAAQLSSLidqLPDGldtlVGEHGN 485
Cdd:PRK15112 76 PLHFGDysYRSQRIRMIFQdPSTSLNPRQRISQILDFPLRlNTdlePEQREKQIIETLRQVGL---LPDH----ASYYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 486 KLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETP-TTFI-VAHRLSTIKE-ADKIVVIDEGKI 562
Cdd:PRK15112 149 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgISYIyVTQHLGMMKHiSDQVLVMHQGEV 228
|
250
....*....|.
gi 1158646300 563 VEIGTYEKLLA 573
Cdd:PRK15112 229 VERGSTADVLA 239
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
47-324 |
7.55e-22 |
|
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: 95.96 E-value: 7.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 47 LMPIAIANVINAASSKDSSQLQAIyfnaFLMACLIGQNILT--NYFHVKYhsTSIRQVeAGLRATLIKKIQELSIPYQKE 124
Cdd:cd18551 17 AQPLLVKNLIDALSAGGSSGGLLA----LLVALFLLQAVLSalSSYLLGR--TGERVV-LDLRRRLWRRLLRLPVSFFDR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 125 LQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFVTLFFRKRIRQSNSDFRQ 204
Cdd:cd18551 90 RRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 205 EMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIFQLICLIFTGILALQGR 284
Cdd:cd18551 170 ALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGARVASGA 249
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1158646300 285 IQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGMESITSI 324
Cdd:cd18551 250 LTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
365-572 |
1.36e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.52 E-value: 1.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 365 IIDHFSLEVKAGETIAFVGPSGSGKSTLL---NLLIGFIQPT----SGKIFLDDQPLDELDMRSVRNYLAVVPQTTLLFS 437
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEArvegEVRLFGRNIYSPDVDPIEVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 438 -ASIKENITYGLK----NVSKERLDEVIE-AAQLSSLIDQLPDGLDtlvgEHGNKLSGGQKQCISIARALIRQPKIILLD 511
Cdd:PRK14267 99 hLTIYDNVAIGVKlnglVKSKKELDERVEwALKKAALWDEVKDRLN----DYPSNLSGGQRQRLVIARALAMKPKILLMD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 512 EATSALDNQSEKKIQQALNYLTETPTTFIVAHR-LSTIKEADKIVVIDEGKIVEIGTYEKLL 572
Cdd:PRK14267 175 EPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
351-567 |
1.53e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.81 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 351 FEDVSFLY----PDSLKPIIDhFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPL----DELDMRSV 422
Cdd:PRK13649 5 LQNVSYTYqagtPFEGRALFD-VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 423 RNYLAVVPQ--TTLLFSASIKENITYGLKN--VSKErldeviEAAQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIA 498
Cdd:PRK13649 84 RKKVGLVFQfpESQLFEETVLKDVAFGPQNfgVSQE------EAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 499 RALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIVEIGT 567
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVlVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
330-569 |
1.55e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 99.47 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 330 AGDVETyhGKKKIQHLDGNFRFEdvsfLYPdslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFL 409
Cdd:PTZ00243 649 ATPTSE--RSAKTPKMKTDDFFE----LEP---KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA 719
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 410 DdqpldeldmRSVrnylAVVPQTTLLFSASIKENITYgLKNVSKERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNKLSG 489
Cdd:PTZ00243 720 E---------RSI----AYVPQQAWIMNATVRGNILF-FDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSG 785
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 490 GQKQCISIARALIRQPKIILLDEATSALDNQ-SEKKIQQALNYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTY 568
Cdd:PTZ00243 786 GQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSS 865
|
.
gi 1158646300 569 E 569
Cdd:PTZ00243 866 A 866
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
365-575 |
1.97e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.42 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 365 IIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRS-VRNYLAVVPQTTLLFSA-SIKE 442
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 443 NITYGL---KNVSKE----RLDEVIEAAQLSSLIDQLpdgldtlvgehGNKLSGGQKQCISIARALIRQPKIILLDEATS 515
Cdd:PRK10895 98 NLMAVLqirDDLSAEqredRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 516 ALDNQSEKKIQQALNYLTETPT-TFIVAHRL-STIKEADKIVVIDEGKIVEIGTYEKLLAQK 575
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLgVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDE 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
350-567 |
2.45e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.42 E-value: 2.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLY----PDSLKPIIDhFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDD----QPLDELDMRS 421
Cdd:PRK13643 3 KFEKVNYTYqpnsPFASRALFD-IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 422 VRNYLAVVPQ--TTLLFSASIKENITYGLKN--VSKERLDEVieAAQLSSLIdqlpdGLDTLVGEHGN-KLSGGQKQCIS 496
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEETVLKDVAFGPQNfgIPKEKAEKI--AAEKLEMV-----GLADEFWEKSPfELSGGQMRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 497 IARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTET-PTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGT 567
Cdd:PRK13643 155 IAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
361-565 |
2.54e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.40 E-value: 2.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 361 SLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPldeLDMRS----VRNYLAVVP----QT 432
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKP---VRIRSprdaIRAGIAYVPedrkGE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 433 TLLFSASIKENITYG-LKNVSKE-RLDEVIEAAQLSSLIDQL---PDGLDTLVGEhgnkLSGGQKQCISIARALIRQPKI 507
Cdd:COG1129 340 GLVLDLSIRENITLAsLDRLSRGgLLDRRRERALAEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKV 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 508 ILLDEATSALD--NQSEkkIQQALNYLTETPTTFIVAhrLSTIKE----ADKIVVIDEGKIVEI 565
Cdd:COG1129 416 LILDEPTRGIDvgAKAE--IYRLIRELAAEGKAVIVI--SSELPEllglSDRILVMREGRIVGE 475
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
363-523 |
3.70e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 91.86 E-value: 3.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAvvPQTTLLFSASIKE 442
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVAE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 443 NITY--GLKNVSKERLDEVIEAAQLSSLIDqLPdgldtlvgehGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQ 520
Cdd:PRK13539 93 NLEFwaAFLGGEELDIAAALEAVGLAPLAH-LP----------FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161
|
...
gi 1158646300 521 SEK 523
Cdd:PRK13539 162 AVA 164
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
363-566 |
5.93e-21 |
|
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: 91.83 E-value: 5.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDdqpldeldmRSVRNYLAVvpQTTLLFSASIKE 442
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVR---------GRVSSLLGL--GGGFNPELTGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 443 NIT-----YGLKNVS-KERLDEVIEAAqlsslidQLPDGLDTLVGEhgnkLSGGQKQCISIARALIRQPKIILLDEATSA 516
Cdd:cd03220 104 NIYlngrlLGLSRKEiDEKIDEIIEFS-------ELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 517 LDNQSEKKIQQALNYLTETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIVEIG 566
Cdd:cd03220 173 GDAAFQEKCQRRLRELLKQGKTVIlVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
350-572 |
6.15e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.79 E-value: 6.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYpDSLKpIIDHFSLEVKAGETIAFVGPSGSGKSTLL------NLLIGFIQpTSGKIFLDDQPLDE--LDMRS 421
Cdd:PRK14258 9 KVNNLSFYY-DTQK-ILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnrmNELESEVR-VEGRVEFFNQNIYErrVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 422 VRNYLAVVPQTTLLFSASIKENITYGLKNVS---KERLDEVIEAA-QLSSLIDQLPDGLDTLVGEhgnkLSGGQKQCISI 497
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGwrpKLEIDDIVESAlKDADLWDEIKHKIHKSALD----LSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 498 ARALIRQPKIILLDEATSALDNQSEKKIQQALN--YLTETPTTFIVAHRLSTIKEADKIVVIDEG------KIVEIGTYE 569
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenrigQLVEFGLTK 241
|
...
gi 1158646300 570 KLL 572
Cdd:PRK14258 242 KIF 244
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
350-575 |
6.44e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 92.07 E-value: 6.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYP------DSLKPII--------------DHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIfl 409
Cdd:COG1134 6 EVENVSKSYRlyhepsRSLKELLlrrrrtrreefwalKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 410 ddqpldELDMRsVRNYLAV----VPQTT----LLFSASIkenitYGLKNVS-KERLDEVIEAAQLSSLIDQlPdgldtlV 480
Cdd:COG1134 84 ------EVNGR-VSALLELgagfHPELTgrenIYLNGRL-----LGLSRKEiDEKFDEIVEFAELGDFIDQ-P------V 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 481 GehgnKLSGGQKqcisiAR-----ALIRQPKIILLDEATSALD----NQSEKKIQQalnYLTETPTTFIVAHRLSTIKE- 550
Cdd:COG1134 145 K----TYSSGMR-----ARlafavATAVDPDILLVDEVLAVGDaafqKKCLARIRE---LRESGRTVIFVSHSMGAVRRl 212
|
250 260 270
....*....|....*....|....*....|..
gi 1158646300 551 ADKIVVIDEGKIVEIGT-------YEKLLAQK 575
Cdd:COG1134 213 CDRAIWLEKGRLVMDGDpeeviaaYEALLAGR 244
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
47-318 |
7.57e-21 |
|
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: 93.01 E-value: 7.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 47 LMPIAIANVINAASSKDSsqLQAIYFNAFLMACLIGQNILTNYFHVKYHSTSIRQVEAGLRATLIKKIQELSIPYQKELQ 126
Cdd:cd18557 14 LLPYLIGRLIDTIIKGGD--LDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 127 SGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFVTLFFRKRIRQSNSDFRQEM 206
Cdd:cd18557 92 TGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 207 EETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIFQLICLIFTGILALQGRIQ 286
Cdd:cd18557 172 AKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLT 251
|
250 260 270
....*....|....*....|....*....|..
gi 1158646300 287 PGDVVMYQTYFTTIVNSVSGMITLIPTISKGM 318
Cdd:cd18557 252 VGELTSFILYTIMVASSVGGLSSLLADIMKAL 283
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
363-577 |
9.98e-21 |
|
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: 90.28 E-value: 9.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGF--IQPTSGKIFLDDQPLDELDMrSVRNYLAVvpqtTLLFSASI 440
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPP-EERARLGI----FLAFQYPP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 441 KenityglknvskerldevIEAAQLSSLIDQLPDGldtlvgehgnkLSGGQKQCISIARALIRQPKIILLDEATSALDNQ 520
Cdd:cd03217 88 E------------------IPGVKNADFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 521 SEKKIQQALNYLTETPTTF-IVAH--RLSTIKEADKIVVIDEGKIVEIGTYE--KLLAQKGY 577
Cdd:cd03217 139 ALRLVAEVINKLREEGKSVlIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKElaLEIEKKGY 200
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
361-562 |
1.34e-20 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 89.41 E-value: 1.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 361 SLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNY-LAVVP---QTTLLF 436
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPedrKREGLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 437 -SASIKENITyglknvskerldevieaaqLSSLidqlpdgldtlvgehgnkLSGGQKQCISIARALIRQPKIILLDEATS 515
Cdd:cd03215 91 lDLSVAENIA-------------------LSSL------------------LSGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 516 ALDNQSEKKIQQALNYLTETPTTFIVahrLST-----IKEADKIVVIDEGKI 562
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADAGKAVLL---ISSeldelLGLCDRILVMYEGRI 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
380-570 |
1.48e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 93.40 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 380 AFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSvrnYLAV-------VPQTTLLFSA-SIKENITYGLKNV 451
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGI---CLPPekrrigyVFQDARLFPHyKVRGNLRYGMAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 452 SKERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNY 531
Cdd:PRK11144 105 MVAQFDKIVALLGIEPLLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1158646300 532 LTETPTTFI--VAHRLSTI-KEADKIVVIDEGKIVEIGTYEK 570
Cdd:PRK11144 174 LAREINIPIlyVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
366-574 |
1.89e-20 |
|
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: 94.87 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIF--LDDQPLDELDMR-----SVRNYLAVVPQTTLLFS- 437
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEWVDMTKPGpdgrgRAKRYIGILHQEYDLYPh 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 438 ASIKENITyglKNVSKERLDE--------VIEAAQLS-----SLIDQLPDgldtlvgehgnKLSGGQKQCISIARALIRQ 504
Cdd:TIGR03269 380 RTVLDNLT---EAIGLELPDElarmkaviTLKMVGFDeekaeEILDKYPD-----------ELSEGERHRVALAQVLIKE 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 505 PKIILLDEATSALDNQSEKKIQQA-LNYLTETPTTF-IVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:TIGR03269 446 PRIVILDEPTGTMDPITKVDVTHSiLKAREEMEQTFiIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
357-562 |
3.22e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.87 E-value: 3.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 357 LYPDSLKPIidhfSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRS---VRNY-LAVVPQ- 431
Cdd:PRK11629 20 VQTDVLHNV----SFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 432 TTLLFSASIKENITYGLKnVSKERLDEVIEAAQ--LSSLidqlpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIIL 509
Cdd:PRK11629 96 HHLLPDFTALENVAMPLL-IGKKKPAEINSRALemLAAV------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 510 LDEATSALDNQSEKKIQQALNYLTETPTT--FIVAHRLSTIKEADKIVVIDEGKI 562
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGELNRLQGTafLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
369-563 |
4.49e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 89.90 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 369 FSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIqPTSGKIFLDDQPLDELDMRSVRNYLAVVPQ-TTLLFSASIKENITYG 447
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQqQSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 448 LKnvSKERLDEVIEAaqLSSLIDQLpdGLDTLVGEHGNKLSGGQKQCISIARALIR-------QPKIILLDEATSALDnq 520
Cdd:COG4138 94 QP--AGASSEAVEQL--LAQLAEAL--GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD-- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1158646300 521 sekKIQQA-----LNYLTETPTTFIV-AHRLS-TIKEADKIVVIDEGKIV 563
Cdd:COG4138 166 ---VAQQAaldrlLRELCQQGITVVMsSHDLNhTLRHADRVWLLKQGKLV 212
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
366-569 |
4.63e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.05 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDEL---------------------DMRSVRN 424
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLpghqiarmgvvrtfqhvrlfrEMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 425 YLavVPQ----TTLLFSASIKeniTYGLKNVSKERLDeviEAAQlssLIDQLpdGLDTLVGEHGNKLSGGQKQCISIARA 500
Cdd:PRK11300 101 LL--VAQhqqlKTGLFSGLLK---TPAFRRAESEALD---RAAT---WLERV--GLLEHANRQAGNLAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 501 LIRQPKIILLDEATSALDNQSEKKIQQALNYLTET--PTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYE 569
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhnVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPE 239
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
350-575 |
5.60e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 90.27 E-value: 5.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLY-PDSL--KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLD----ELDMRSV 422
Cdd:PRK13641 4 KFENVDYIYsPGTPmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKNLKKL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 423 RNYLAVVPQ--TTLLFSASIKENITYGLKNVSKERlDEVIEAAQlsSLIDQLpdGLDTLVGEHGN-KLSGGQKQCISIAR 499
Cdd:PRK13641 84 RKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSE-DEAKEKAL--KWLKKV--GLSEDLISKSPfELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 500 ALIRQPKIILLDEATSALDNQSEKKIQQA-LNYLTETPTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQK 575
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
370-572 |
1.19e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 91.25 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 370 SLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDD---QPLDELDMRSVR-NYLAVVPQT-TLLFSASIKENI 444
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRrKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 445 TYGLKnvskerLDEVIEAAQLSSLIDQLPD-GLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEK 523
Cdd:PRK10070 128 AFGME------LAGINAEERREKALDALRQvGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 524 KIQQALNYL--TETPTTFIVAHRL-STIKEADKIVVIDEGKIVEIGTYEKLL 572
Cdd:PRK10070 202 EMQDELVKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
364-521 |
1.79e-19 |
|
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: 87.49 E-value: 1.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 364 PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQ----------PLDELDMRS-----VRNYLAV 428
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvdlaqasPREILALRRrtigyVSQFLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 VPQTTLLfsasikenityglkNVSKERL-------DEVIEAAQ--LSSLidQLPDGLDTLvgeHGNKLSGGQKQCISIAR 499
Cdd:COG4778 105 IPRVSAL--------------DVVAEPLlergvdrEEARARARelLARL--NLPERLWDL---PPATFSGGEQQRVNIAR 165
|
170 180
....*....|....*....|..
gi 1158646300 500 ALIRQPKIILLDEATSALDNQS 521
Cdd:COG4778 166 GFIADPPLLLLDEPTASLDAAN 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
363-573 |
2.32e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.61 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQTTLLFS----- 437
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQrpnpf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 438 -ASIKENITYGLK-----------NVSKERLDEVieaaqlsSLIDQLPDGLDtlvgEHGNKLSGGQKQCISIARALIRQP 505
Cdd:PRK14271 114 pMSIMDNVLAGVRahklvprkefrGVAQARLTEV-------GLWDAVKDRLS----DSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1158646300 506 KIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLS-TIKEADKIVVIDEGKIVEIGTYEKLLA 573
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
370-574 |
3.01e-19 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 87.72 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 370 SLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPL-------------DELDMRSVRNYLAVVPQTTLLF 436
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvaDKNQLRLLRTRLTMVFQHFNLW 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 437 S-ASIKENI------TYGL-KNVSKER----LDEV--IEAAQlsslidqlpdgldtlvGEHGNKLSGGQKQCISIARALI 502
Cdd:PRK10619 105 ShMTVLENVmeapiqVLGLsKQEARERavkyLAKVgiDERAQ----------------GKYPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 503 RQPKIILLDEATSALDNQSEKKIQQALNYLTET-PTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
69-324 |
3.72e-19 |
|
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: 88.25 E-value: 3.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 69 AIYFNAFLMAcLIGQNILTNyfhvkyhstsirqveagLRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQV 148
Cdd:cd18552 55 ASYLQTYLMA-YVGQRVVRD-----------------LRNDLFDKLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 149 FVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFVTLFFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGL 228
Cdd:cd18552 117 LTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 229 EKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSwasfQIFQLIC----LIFTGILALQGRIQPGDVVMYQTYFTTIVNSV 304
Cdd:cd18552 197 EDYEIKRFRKANERLRRLSMKIARARALSSPLM----ELLGAIAialvLWYGGYQVISGELTPGEFISFITALLLLYQPI 272
|
250 260
....*....|....*....|
gi 1158646300 305 SGMITLIPTISKGMESITSI 324
Cdd:cd18552 273 KRLSNVNANLQRGLAAAERI 292
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
350-561 |
4.22e-19 |
|
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: 84.04 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDqpldeldmrsvRNYLAVV 429
Cdd:cd03221 2 ELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQttllfsasikenityglknvskerldevieaaqlsslidqlpdgldtlvgehgnkLSGGQKQCISIARALIRQPKIIL 509
Cdd:cd03221 69 EQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 510 LDEATSALDNQSekkiQQAL-NYLTETPTTFI-VAH-R--LSTIkeADKIVVIDEGK 561
Cdd:cd03221 94 LDEPTNHLDLES----IEALeEALKEYPGTVIlVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
350-575 |
4.80e-19 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 90.80 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPD---SLKPIidhfSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYL 426
Cdd:PRK10522 324 ELRNVTFAYQDngfSVGPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQTTLLFSASIKEnityGLKNVSKERLDEVIEAAQLSSLIdQLPDG--LDTlvgehgnKLSGGQKQCISIARALIRQ 504
Cdd:PRK10522 400 SAVFTDFHLFDQLLGP----EGKPANPALVEKWLERLKMAHKL-ELEDGriSNL-------KLSKGQKKRLALLLALAEE 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 505 PKIILLDEATSALDNQSEKKI-QQALNYLTET-PTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLAQK 575
Cdd:PRK10522 468 RDILLLDEWAADQDPHFRREFyQVLLPLLQEMgKTIFAISHDDHYFIHADRLLEMRNGQLSELTGEERDAASR 540
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
370-560 |
5.18e-19 |
|
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: 85.62 E-value: 5.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 370 SLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQTTLLFSASIKENITYGLK 449
Cdd:cd03231 20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWHA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 450 NVSKERLDEVIEAAQLSSLIDqLPdgldtlvgehGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQAL 529
Cdd:cd03231 100 DHSDEQVEEALARVGLNGFED-RP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170 180 190
....*....|....*....|....*....|.
gi 1158646300 530 NYLTETPTTFIVAHRLSTIKEADKIVVIDEG 560
Cdd:cd03231 169 AGHCARGGMVVLTTHQDLGLSEAGARELDLG 199
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
362-563 |
5.69e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 5.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 362 LKPIidHFSLevKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNY-LAVVPQTTLLF-SAS 439
Cdd:PRK15439 27 LKGI--DFTL--HAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 440 IKENITYGL--KNVSKERLDEVIeaAQLSSLIDqlpdgLDTLVGehgnKLSGGQKQCISIARALIRQPKIILLDEATSAL 517
Cdd:PRK15439 103 VKENILFGLpkRQASMQKMKQLL--AALGCQLD-----LDSSAG----SLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1158646300 518 D-NQSEKKIQQALNYLTETPTTFIVAHRLSTIKE-ADKIVVIDEGKIV 563
Cdd:PRK15439 172 TpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIA 219
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
370-574 |
5.95e-19 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 88.10 E-value: 5.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 370 SLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPL---DELDMRSVRNYLAVVPQTTLlfsASIKENITY 446
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkaDPEAQKLLRQKIQIVFQNPY---GSLNPRKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 447 G-------LKNVSKERLDEVIEAAQLSSLIdqlpdGLDTlvgEHGNK----LSGGQKQCISIARALIRQPKIILLDEATS 515
Cdd:PRK11308 112 GqileeplLINTSLSAAERREKALAMMAKV-----GLRP---EHYDRyphmFSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 516 ALDnqseKKIQ-QALNYLTE------TPTTFIvAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:PRK11308 184 ALD----VSVQaQVLNLMMDlqqelgLSYVFI-SHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNN 245
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
366-567 |
6.24e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.99 E-value: 6.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGfIQPT---SGKIFLDDQPLDeldMRSVRNY-----------LAVVPQ 431
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQ---ASNIRDTeragiaiihqeLALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 432 TTLLfsasikENITYGLKNVSKERLD--EVIEAAQlsSLIDQLPDGLD--TLVGEHGnklsGGQKQCISIARALIRQPKI 507
Cdd:PRK13549 97 LSVL------ENIFLGNEITPGGIMDydAMYLRAQ--KLLAQLKLDINpaTPVGNLG----LGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 508 ILLDEATSALdnqSEKKIQQALNYLTETPTTFI----VAHRLSTIKE-ADKIVVIDEGKivEIGT 567
Cdd:PRK13549 165 LILDEPTASL---TESETAVLLDIIRDLKAHGIaciyISHKLNEVKAiSDTICVIRDGR--HIGT 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
370-573 |
1.00e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 85.70 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 370 SLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDM-RSVRNYLAVVPQTTLLFS-ASIKENITYG 447
Cdd:PRK11614 25 SLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTaKIMREAVAIVPEGRRVFSrMTVEENLAMG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 448 LKNVSKERLDEVIEaaqlsSLIDQLPDGLDTLVGEHGNkLSGGQKQCISIARALIRQPKIILLDEATSALdnqSEKKIQQ 527
Cdd:PRK11614 105 GFFAERDQFQERIK-----WVYELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLDEPSLGL---APIIIQQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 528 ALNYL----TETPTTFIVAHRLS-TIKEADKIVVIDEGKIVEIGTYEKLLA 573
Cdd:PRK11614 176 IFDTIeqlrEQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
352-567 |
1.38e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 85.52 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 352 EDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQ 431
Cdd:COG4604 5 KNVSKRYGG--KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 432 TTLLFSA-SIKENITYGLKNVSKERL----DEVIEAAqlsslIDQLpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPK 506
Cdd:COG4604 83 ENHINSRlTVRELVAFGRFPYSKGRLtaedREIIDEA-----IAYL--DLEDLADRYLDELSGGQRQRAFIAMVLAQDTD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 507 IILLDEATSALDNQSEKKIQQALNYLTET--PTTFIVAHRLS-TIKEADKIVVIDEGKIVEIGT 567
Cdd:COG4604 156 YVLLDEPLNNLDMKHSVQMMKLLRRLADElgKTVVIVLHDINfASCYADHIVAMKDGRVVAQGT 219
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
356-572 |
1.79e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.48 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 356 FLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLD------ELDMRSVRNYLAVV 429
Cdd:PRK14246 17 YLYIND-KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYfgkdifQIDAIKLRKEVGMV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLFS-ASIKENITYGLKN---VSKERLDEVIEAA-QLSSLIDQLPDGLDTlvgeHGNKLSGGQKQCISIARALIRQ 504
Cdd:PRK14246 96 FQQPNPFPhLSIYDNIAYPLKShgiKEKREIKKIVEEClRKVGLWKEVYDRLNS----PASQLSGGQQQRLTIARALALK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1158646300 505 PKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTI-KEADKIVVIDEGKIVEIGTYEKLL 572
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
341-518 |
1.99e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.22 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 341 KIQHLDGNFRFEDVSFLYPDS--LKPIidhfSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELD 418
Cdd:PRK10575 4 YTNHSDTTFALRNVSFRVPGRtlLHPL----SLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 419 MRSVRNYLAVVPQTtlLFSA---SIKENITYG----------LKNVSKERLDEVIEAAQLSSLIDQLPDgldtlvgehgn 485
Cdd:PRK10575 80 SKAFARKVAYLPQQ--LPAAegmTVRELVAIGrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVD----------- 146
|
170 180 190
....*....|....*....|....*....|...
gi 1158646300 486 KLSGGQKQCISIARALIRQPKIILLDEATSALD 518
Cdd:PRK10575 147 SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
353-571 |
2.06e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 86.29 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 353 DVSFLY----PDSLKpIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKI---FLDDQPLDELD------- 418
Cdd:PRK13651 7 NIVKIFnkklPTELK-ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKekekvle 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 419 --------------MRSVRNYLAVVPQTT--LLFSASIKENITYGL------KNVSKERLDEVIEAAQLS-SLIDQLPDG 475
Cdd:PRK13651 86 klviqktrfkkikkIKEIRRRVGVVFQFAeyQLFEQTIEKDIIFGPvsmgvsKEEAKKRAAKYIELVGLDeSYLQRSPFE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 476 LdtlvgehgnklSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFI-VAHRLSTIKE-ADK 553
Cdd:PRK13651 166 L-----------SGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIIlVTHDLDNVLEwTKR 234
|
250
....*....|....*....
gi 1158646300 554 IVVIDEGKIVEIG-TYEKL 571
Cdd:PRK13651 235 TIFFKDGKIIKDGdTYDIL 253
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
363-567 |
2.38e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.57 E-value: 2.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLiGFIQPT----SGKIFLDDQPLDELDMRSVRNYLA----VVPQTT- 433
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNAL-AFRSPKgvkgSGSVLLNGMPIDAKEMRAISAYVQqddlFIPTLTv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 434 ---LLFSASIK--ENITyglKNVSKERLDEVIEaaQLSslidqLPDGLDTLVGEHGNK--LSGGQKQCISIARALIRQPK 506
Cdd:TIGR00955 117 rehLMFQAHLRmpRRVT---KKEKRERVDEVLQ--ALG-----LRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 507 IILLDEATSALDNQSEKKIQQALNYLTETPTTFIVA-HR-LSTIKEA-DKIVVIDEGKIVEIGT 567
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTiHQpSSELFELfDKIILMAEGRVAYLGS 250
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
370-573 |
4.06e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 84.76 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 370 SLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQT--TLLFSASIKENITYG 447
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNpdNQFVGATVEDDVAFG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 448 LKN--VSKE----RLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQS 521
Cdd:PRK13642 107 MENqgIPREemikRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 522 EKKIQQALNYLTET--PTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLLA 573
Cdd:PRK13642 176 RQEIMRVIHEIKEKyqLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
354-583 |
5.49e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 87.07 E-value: 5.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 354 VSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKS-TLLNLLIGFIQP----TSGKIFLDDQPL---DELDMRSVR-N 424
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlhaSEQTLRGVRgN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 425 YLAVVPQTTLLfsaSIKEnitygLKNVSKErLDEVI--------EAAQ---LSSL----IDQLPDGLdtlvGEHGNKLSG 489
Cdd:PRK15134 93 KIAMIFQEPMV---SLNP-----LHTLEKQ-LYEVLslhrgmrrEAARgeiLNCLdrvgIRQAAKRL----TDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 490 GQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTE---TPTTFIvAHRLSTIKE-ADKIVVIDEGKIVEI 565
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelnMGLLFI-THNLSIVRKlADRVAVMQNGRCVEQ 238
|
250 260
....*....|....*....|
gi 1158646300 566 GTYEKLLA--QKGYFYRLKN 583
Cdd:PRK15134 239 NRAATLFSapTHPYTQKLLN 258
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
46-324 |
6.78e-18 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 84.41 E-value: 6.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 46 WLMPIAIANVINAAsskdssQLQAIYFNAFLMACLIGQNILTNYFHVKYHSTSIRQVEAGLRATLIKKIQELSIPYQKEL 125
Cdd:cd18542 20 LLIRRIIDSVIGGG------LRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLSFSFHDKA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 126 QSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFVTLFFRKRIRQSNSDFRQE 205
Cdd:cd18542 94 RTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 206 MEETSAKV------IEVIelapiaRAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIFQLICLIFTGIL 279
Cdd:cd18542 174 EGELNTVLqenltgVRVV------KAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYL 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1158646300 280 ALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGMESITSI 324
Cdd:cd18542 248 VINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAERI 292
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
365-564 |
7.67e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 82.90 E-value: 7.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 365 IIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELD------MRS-----VRNYLAVVPQTT 433
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearakLRAkhvgfVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 434 LLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLDEA 513
Cdd:PRK10584 105 ALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 514 TSALDNQSEKKIQQALNYLT-ETPTTFI-VAHRLSTIKEADKIVVIDEGKIVE 564
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNrEHGTTLIlVTHDLQLAARCDRRLRLVNGQLQE 226
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
363-567 |
9.81e-18 |
|
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: 87.76 E-value: 9.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLdELDMRSVRNYLAVVPQTTLLF-SASIK 441
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFhHLTVA 1021
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITY--GLKNVSKERLDEVIEAaqlsslidQLPD-GLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALD 518
Cdd:TIGR01257 1022 EHILFyaQLKGRSWEEAQLEMEA--------MLEDtGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 519 NQSEKKIQQALNYLTETPTTFIVAHRLStikEA----DKIVVIDEGKIVEIGT 567
Cdd:TIGR01257 1094 PYSRRSIWDLLLKYRSGRTIIMSTHHMD---EAdllgDRIAIISQGRLYCSGT 1143
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
365-569 |
9.84e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.52 E-value: 9.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 365 IIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDD----------QPLDELDMRSVRNY------LAV 428
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhELITNPYSKKIKNFkelrrrVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 VPQ--TTLLFSASIKENITYG------LKNVSKERLDEVIEAAQL-SSLIDQLPDGLdtlvgehgnklSGGQKQCISIAR 499
Cdd:PRK13631 121 VFQfpEYQLFKDTIEKDIMFGpvalgvKKSEAKKLAKFYLNKMGLdDSYLERSPFGL-----------SGGQKRRVAIAG 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 500 ALIRQPKIILLDEATSALDNQSEKKIQQ-ALNYLTETPTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGT-YE 569
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQlILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGTpYE 262
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
369-572 |
1.07e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 82.67 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 369 FSLEVKAGETIAFVGPSGSGKSTLLNLLIGfIQPTSGKIFLDDQPLDELDMRS---VRNYLAvvPQTTLLFSASIKENIT 445
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAElarHRAYLS--QQQTPPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 446 ygLKNVSKERLDEVieAAQLSSLIDQLpdGLDTLVGEHGNKLSGGQKQ-------CISIARALIRQPKIILLDEATSALD 518
Cdd:PRK03695 92 --LHQPDKTRTEAV--ASALNEVAEAL--GLDDKLGRSVNQLSGGEWQrvrlaavVLQVWPDINPAGQLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1158646300 519 NQSEKKIQQALNYLTETPTTFIVA-HRLS-TIKEADKIVVIDEGKIVEIGTYEKLL 572
Cdd:PRK03695 166 VAQQAALDRLLSELCQQGIAVVMSsHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
49-318 |
3.43e-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: 82.50 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 49 PIAIANVIN-AASSKDssqLQAIYFNAFLMACLIGQNILTNYFHVKY-HSTSIRqVEAGLRATLIKKIQELSIPYQKELQ 126
Cdd:cd18549 22 PLIVRYIIDdLLPSKN---LRLILIIGAILLALYILRTLLNYFVTYWgHVMGAR-IETDMRRDLFEHLQKLSFSFFDNNK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 127 SGRIQSKIIRDVEAIQTLSSQ----VFVSGLNIAVNLFVALGITLYKSPVVFMFflltVPLAAFVTLFFRKRIRQSNSDF 202
Cdd:cd18549 98 TGQLMSRITNDLFDISELAHHgpedLFISIITIIGSFIILLTINVPLTLIVFAL----LPLMIIFTIYFNKKMKKAFRRV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 203 RQEMEETSAKVIEVIELAPIARAHGLEKHETTR---LNKHFTQIYEKGFHLdilQSVFGSVSWASFQIFQLICLIFTGIL 279
Cdd:cd18549 174 REKIGEINAQLEDSLSGIRVVKAFANEEYEIEKfdeGNDRFLESKKKAYKA---MAYFFSGMNFFTNLLNLVVLVAGGYF 250
|
250 260 270
....*....|....*....|....*....|....*....
gi 1158646300 280 ALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGM 318
Cdd:cd18549 251 IIKGEITLGDLVAFLLYVNVFIKPIRRLVNFTEQYQKGM 289
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
102-309 |
9.79e-17 |
|
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: 80.99 E-value: 9.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 102 VEAGLRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQvfvsGLNIAVNLF---VALGITLYKSPVVFMFFL 178
Cdd:cd18543 70 VEHDLRTDLFAHLQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAF----GPFLLGNLLtlvVGLVVMLVLSPPLALVAL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 179 LTVPLAAFVTLFFRKRIR-------QSNSDFRQEMEEtSAKVIEVIelapiaRAHGLEKHETTRLNKHFTQIYEKGFHLD 251
Cdd:cd18543 146 ASLPPLVLVARRFRRRYFpasrraqDQAGDLATVVEE-SVTGIRVV------KAFGRERRELDRFEAAARRLRATRLRAA 218
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 252 ILQSVFgsvsWASFQIF----QLICLIFTGILALQGRIQPGDVV---MYQTYFTTIVNSVSGMIT 309
Cdd:cd18543 219 RLRARF----WPLLEALpelgLAAVLALGGWLVANGSLTLGTLVafsAYLTMLVWPVRMLGWLLA 279
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
366-563 |
1.01e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.30 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMR-SVRNYLAVVPQT-TLLFSASIKEN 443
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 444 ITYGLKNVSK----ERLD--EVIEAAQLSSLIDQLPDGLDTLVGEhgnkLSGGQKQCISIARALIRQPKIILLDEATSAL 517
Cdd:PRK09700 101 LYIGRHLTKKvcgvNIIDwrEMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1158646300 518 DNQSEKKIQQALNYLTETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIV 563
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVyISHKLAEIRRiCDRYTVMKDGSSV 224
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
351-566 |
1.11e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.97 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 351 FEDVSF-LYPdslkpiidhfslevkaGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKI--------FLDDQPLDELDMRS 421
Cdd:PRK11701 22 CRDVSFdLYP----------------GEVLGIVGESGSGKTTLLNALSARLAPDAGEVhyrmrdgqLRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 422 V-RNYLAVV---PQTTLLFSASIKENIT----------YG-LKNVSKERLDEV-IEAAQlsslIDQLPdgldtlvgehgN 485
Cdd:PRK11701 86 LlRTEWGFVhqhPRDGLRMQVSAGGNIGerlmavgarhYGdIRATAGDWLERVeIDAAR----IDDLP-----------T 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 486 KLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETP--TTFIVAHRLSTIK-EADKIVVIDEGKI 562
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELglAVVIVTHDLAVARlLAHRLLVMKQGRV 230
|
....
gi 1158646300 563 VEIG 566
Cdd:PRK11701 231 VESG 234
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
370-569 |
1.36e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 80.31 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 370 SLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDeldmRSVR-NYLAVVPQTTLL---FSASIKENIT 445
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQkNLVAYVPQSEEVdwsFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 446 YG------LKNVSKERLDEVIEAAQlsSLIDQLpDGLDTLVGEhgnkLSGGQKQCISIARALIRQPKIILLDEATSALDN 519
Cdd:PRK15056 103 MGryghmgWLRRAKKRDRQIVTAAL--ARVDMV-EFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 520 QSEKKIQQALNYLTETPTTFIVA-HRLSTIKEADKIVVIDEGKIVEIGTYE 569
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVStHNLGSVTEFCDYTVMVKGTVLASGPTE 226
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
366-567 |
1.42e-16 |
|
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: 82.57 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGfIQPT---SGKIFLDDQPLDELDMRSV-RNYLAVVPQT-TLLFSASI 440
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQElTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 441 KENITYGLK----------NVSKERLDEVIEAAQLSSLIDQLPdgldtlVGEHGnklsGGQKQCISIARALIRQPKIILL 510
Cdd:TIGR02633 96 AENIFLGNEitlpggrmayNAMYLRAKNLLRELQLDADNVTRP------VGDYG----GGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 511 DEATSALdnqSEKKIQQALNYLTETPTTFI----VAHRLSTIKE-ADKIVVIDEGKivEIGT 567
Cdd:TIGR02633 166 DEPSSSL---TEKETEILLDIIRDLKAHGVacvyISHKLNEVKAvCDTICVIRDGQ--HVAT 222
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
47-301 |
1.63e-16 |
|
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: 80.15 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 47 LMPIAIANVINAASSKDSSQLQAIYFNAFLMACLIGQNILTNYFHVKYHSTSiRQVEAGLRATLIKKIQELSIPYQKELQ 126
Cdd:cd18541 17 LIPRIIGRAIDALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGAS-RRIEYDLRNDLFAHLLTLSPSFYQKNR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 127 SGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFVTLFFRKRIRQSNSDFRQEM 206
Cdd:cd18541 96 TGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 207 EETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIFQLICLIFTGILALQGRIQ 286
Cdd:cd18541 176 SDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTIT 255
|
250
....*....|....*
gi 1158646300 287 PGDVVMYQTYFTTIV 301
Cdd:cd18541 256 LGDLVAFNSYLGMLI 270
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
364-529 |
1.77e-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: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 364 PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRN--YLAVVP--QTTLlfsaS 439
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENilYLGHLPglKPEL----S 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 440 IKENITYGLKNVSKERLD--EVIEAAQLSSLiDQLPdgldtlvgehGNKLSGGQKQCISIARALIRQPKIILLDEATSAL 517
Cdd:TIGR01189 90 ALENLHFWAAIHGGAQRTieDALAAVGLTGF-EDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
170
....*....|..
gi 1158646300 518 DNQSEKKIQQAL 529
Cdd:TIGR01189 159 DKAGVALLAGLL 170
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
367-564 |
5.64e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.73 E-value: 5.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 367 DHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPldeLDMRSVRNYLA-----------VVPQTTll 435
Cdd:PRK11288 21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE---MRFASTTAALAagvaiiyqelhLVPEMT-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 436 fsasIKENITYG-LKN----VSKERLDEVIeAAQLSSL-IDQLPdglDTLVGEhgnkLSGGQKQCISIARALIRQPKIIL 509
Cdd:PRK11288 96 ----VAENLYLGqLPHkggiVNRRLLNYEA-REQLEHLgVDIDP---DTPLKY----LSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 510 LDEATSALdnqSEKKIQQ---ALNYLTETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIVE 564
Cdd:PRK11288 164 FDEPTSSL---SAREIEQlfrVIRELRAEGRVILyVSHRMEEIFAlCDAITVFKDGRYVA 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
349-565 |
8.12e-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: 8.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLyPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNY-LA 427
Cdd:COG3845 258 LEVENLSVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 VVPQ----TTLLFSASIKENI---TYGLKNVSK---ERLDEVIEAAQlsSLIDQL---PDGLDTLVGehgnKLSGG--QK 492
Cdd:COG3845 337 YIPEdrlgRGLVPDMSVAENLilgRYRRPPFSRggfLDRKAIRAFAE--ELIEEFdvrTPGPDTPAR----SLSGGnqQK 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 493 qcISIARALIRQPKIILLDEATSALDNQSEKKIQQALnyltetpttfiVAHR------------LSTIKE-ADKIVVIDE 559
Cdd:COG3845 411 --VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL-----------LELRdagaavllisedLDEILAlSDRIAVMYE 477
|
....*.
gi 1158646300 560 GKIVEI 565
Cdd:COG3845 478 GRIVGE 483
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
363-565 |
8.47e-16 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.54 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFI--QPTSGKIFLDDQPLDEldmrsvrnylavvpQTTLLFSASI 440
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR--------------EASLIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 441 KENITYGLknvskerldEVIEAAQLSS--LIDQLPDgldtlvgehgnKLSGGQKQCISIARALIRQPKIILLDEATSALD 518
Cdd:COG2401 109 KGDFKDAV---------ELLNAVGLSDavLWLRRFK-----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 519 NQSEKKIQQALNYLT-ETPTTFIVA-HRLSTIK--EADKIVVIDEGKIVEI 565
Cdd:COG2401 169 RQTAKRVARNLQKLArRAGITLVVAtHHYDVIDdlQPDLLIFVGYGGVPEE 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
338-518 |
9.87e-16 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 80.38 E-value: 9.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 338 GKKKIQHLDGN------FRFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIF--- 408
Cdd:PRK11147 303 GTAKMQVEEASrsgkivFEMENVNYQIDG--KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHcgt 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 409 -LD----DQPLDELDmrsvrnylavvPQTTLLfsasikENITYGLKNVSKERLDEVIeaaqLSSLIDQL--PDGLDTLVg 481
Cdd:PRK11147 381 kLEvayfDQHRAELD-----------PEKTVM------DNLAEGKQEVMVNGRPRHV----LGYLQDFLfhPKRAMTPV- 438
|
170 180 190
....*....|....*....|....*....|....*..
gi 1158646300 482 ehgNKLSGGQKQCISIARALIRQPKIILLDEATSALD 518
Cdd:PRK11147 439 ---KALSGGERNRLLLARLFLKPSNLLILDEPTNDLD 472
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
71-317 |
1.08e-15 |
|
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: 77.94 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 71 YFNAFLMAcLIGQNILTnyfhvkyhstsirqveaGLRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLssqvFV 150
Cdd:cd18564 72 YAGTYLTA-LVGQRVVL-----------------DLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDL----LV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 151 SG-LNIAVNLFVALGItlykspVVFMFF---------LLTVPLAAFVTLFFRKRIRQSNSDFRQEMEETSAKVIEVIELA 220
Cdd:cd18564 130 SGvLPLLTNLLTLVGM------LGVMFWldwqlaliaLAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAI 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 221 PIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSwasfQIFQLIC----LIFTGILALQGRIQPGDVVMYQTY 296
Cdd:cd18564 204 RVVQAFGREEHEERRFARENRKSLRAGLRAARLQALLSPVV----DVLVAVGtalvLWFGAWLVLAGRLTPGDLLVFLAY 279
|
250 260
....*....|....*....|.
gi 1158646300 297 FTTIVNSVSGMITLIPTISKG 317
Cdd:cd18564 280 LKNLYKPVRDLAKLTGRIAKA 300
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
347-567 |
1.29e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 77.74 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 347 GNFRFEDVSFLY----PDSLKPIiDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDE-----L 417
Cdd:PRK13645 5 KDIILDNVSYTYakktPFEFKAL-NNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkiK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 418 DMRSVRNYLAVVPQ--TTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIdQLPDgldTLVGEHGNKLSGGQKQCI 495
Cdd:PRK13645 84 EVKRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPE---DYVKRSPFELSGGQKRRV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 496 SIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTET--PTTFIVAHRLSTI-KEADKIVVIDEGKIVEIGT 567
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGS 234
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
363-573 |
1.76e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 79.46 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGF--IQPTSGKIF-------------------------------- 408
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 409 -LDDQPLDELDMRSVRNYLAVVPQTT--LLFSASIKENITYGLKNVSKE------RLDEVIEAAQLSSLIDQLpdgldtl 479
Cdd:TIGR03269 93 eVDFWNLSDKLRRRIRKRIAIMLQRTfaLYGDDTVLDNVLEALEEIGYEgkeavgRAVDLIEMVQLSHRITHI------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 480 vgehGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLT--ETPTTFIVAHRLSTIKE-ADKIVV 556
Cdd:TIGR03269 166 ----ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIEDlSDKAIW 241
|
250
....*....|....*..
gi 1158646300 557 IDEGKIVEIGTYEKLLA 573
Cdd:TIGR03269 242 LENGEIKEEGTPDEVVA 258
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
364-571 |
3.02e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 78.74 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 364 PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPL-------------DELDMRSVRNY-LAVV 429
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLrrrsrqvielseqSAAQMRHVRGAdMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 ---PQTTLLFSASIKENITYGLK---NVSKErlDEVIEAAQLSSLIdQLPDGlDTLVGEHGNKLSGGQKQCISIARALIR 503
Cdd:PRK10261 110 fqePMTSLNPVFTVGEQIAESIRlhqGASRE--EAMVEAKRMLDQV-RIPEA-QTILSRYPHQLSGGMRQRVMIAMALSC 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 504 QPKIILLDEATSALDNQSEKKIQQALNYLTETPT--TFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKL 571
Cdd:PRK10261 186 RPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETGSVEQI 256
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
353-566 |
3.36e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 76.20 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 353 DVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLD--ELDMRSVRNYLAVVP 430
Cdd:PRK13638 6 DLWFRYQD--EPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDysKRGLLALRQQVATVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 431 Q--TTLLFSASIKENITYGLKNVSkerldevIEAAQLSSLIDqlpDGLdTLVGEHGNK------LSGGQKQCISIARALI 502
Cdd:PRK13638 84 QdpEQQIFYTDIDSDIAFSLRNLG-------VPEAEITRRVD---EAL-TLVDAQHFRhqpiqcLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 503 RQPKIILLDEATSALDNQSE-------KKIQQALNYLTetpttfIVAHRLSTIKE-ADKIVVIDEGKIVEIG 566
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRtqmiaiiRRIVAQGNHVI------ISSHDIDLIYEiSDAVYVLRQGQILTHG 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
363-573 |
4.67e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 75.12 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKS----TLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRnyLAVVPQTTLlfSA 438
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGRK--IATIMQNPR--SA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 439 SikeNITYGLKNVSKERLDEVIEAAQLSSLIDQLPD-GLD---TLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEAT 514
Cdd:PRK10418 92 F---NPLHTMHTHARETCLALGKPADDATLTAALEAvGLEnaaRVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 515 SALDNQSEKKIQQALNYLTET--PTTFIVAHRLSTI-KEADKIVVIDEGKIVEIGTYEKLLA 573
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKraLGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
47-296 |
4.82e-15 |
|
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: 75.89 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 47 LMPIAIANVINAASSKDSSQLQAIYFNAFLMACLIGQNILTNYFHVKYHSTSIRQVEAGLRATLIKKIQELSIPYQKELQ 126
Cdd:cd18544 17 LGPLLIKRAIDDYIVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFDRTP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 127 SGRIQSKIIRDVEAIQTLSSQVFVsglNIAVNLFVALGItlykspVVFMFF---------LLTVPLAAFVTLFFRKRIRQ 197
Cdd:cd18544 97 VGRLVTRVTNDTEALNELFTSGLV---TLIGDLLLLIGI------LIAMFLlnwrlalisLLVLPLLLLATYLFRKKSRK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 198 SNSDFRQEMEETSAKVIEVIELAPIARAHGLEKhettRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIFQLICLI--- 274
Cdd:cd18544 168 AYREVREKLSRLNAFLQESISGMSVIQLFNREK----REFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALAlvl 243
|
250 260
....*....|....*....|...
gi 1158646300 275 -FTGILALQGRIQPGDVVMYQTY 296
Cdd:cd18544 244 wYGGGQVLSGAVTLGVLYAFIQY 266
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
371-562 |
5.14e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.43 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 371 LEVKAGETIAFVGPSGSGKSTLLNLLIGFIQ----PTSGKIFLDD--QPLDEL--DMRSVRNYLA-VVPQTTLLFSASIK 441
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGRtvQREGRLarDIRKSRANTGyIFQQFNLVNRLSVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITYG-----------LKNVSKERLDEVIEAaqLSSLidqlpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILL 510
Cdd:PRK09984 105 ENVLIGalgstpfwrtcFSWFTREQKQRALQA--LTRV------GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 511 DEATSALDNQSEKKIQQALNYLTETP--TTFIVAHRLS-TIKEADKIVVIDEGKI 562
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
43-311 |
6.04e-15 |
|
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: 75.52 E-value: 6.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 43 LPSWLMPIAIANVINAASSKDSSQLQAIYFNAFLMACLIGQNILTNYFHVKYHSTSIRQVEAGLRATLIKKIQELSIPYQ 122
Cdd:cd18547 17 LGPYLLGKAIDLIIEGLGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 123 KELQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFVTLFFRKRIRQSNSDF 202
Cdd:cd18547 97 DTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQ 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 203 RQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIFQLICLIFTGILALQ 282
Cdd:cd18547 177 QKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLLVIN 256
|
250 260 270
....*....|....*....|....*....|..
gi 1158646300 283 GRIQPGDVVMYQTY---FTTIVNSVSGMITLI 311
Cdd:cd18547 257 GALTVGVIQAFLQYsrqFSQPINQISQQINSL 288
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
363-566 |
6.60e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.02 E-value: 6.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPQ-TTLLFSASIK 441
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQnATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITYG-------LKNVSKERLDEVIEAAQLSslidqlpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEAT 514
Cdd:PRK10253 100 ELVARGryphqplFTRWRKEDEEAVTKAMQAT--------GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 515 SALDNQSEKKIQQALNYLTETP--TTFIVAHRLS-TIKEADKIVVIDEGKIVEIG 566
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREKgyTLAAVLHDLNqACRYASHLIALREGKIVAQG 226
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
106-306 |
8.45e-15 |
|
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: 75.27 E-value: 8.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 106 LRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAA 185
Cdd:cd18778 75 LRSDLYDKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 186 FVTLFFRKRIRQSNSDFRQEMEETSAKV------IEVIelapiaRAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFG- 258
Cdd:cd18778 155 LGAWLYSKKVRPRYRKVREALGELNALLqdnlsgIREI------QAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHp 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 259 SVSWASfQIFQLICLIFTGILALQGRIQPGDVV---MYQTYFTTIVNSVSG 306
Cdd:cd18778 229 LMEFLT-SLGTVLVLGFGGRLVLAGELTIGDLVaflLYLGLFYEPITSLHG 278
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
366-566 |
1.53e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.82 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELD---MRSVRNYLAVVPQTTLlfsASIKE 442
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQDPY---ASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 443 NITYGLKNVSKERLDEVIE----AAQLSSLIDQLpdgldTLVGEHG----NKLSGGQKQCISIARALIRQPKIILLDEAT 514
Cdd:PRK10261 417 RQTVGDSIMEPLRVHGLLPgkaaAARVAWLLERV-----GLLPEHAwrypHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 515 SALDNQSEKKIqqaLNYLTETPTTFIVA-----HRLSTIKE-ADKIVVIDEGKIVEIG 566
Cdd:PRK10261 492 SALDVSIRGQI---INLLLDLQRDFGIAylfisHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
367-564 |
1.56e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 76.37 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 367 DHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGfIQPT---SGKIFLDDQPLDELDMRS--------VRNYLAVVPQTtll 435
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVCRFKDIRDsealgiviIHQELALIPYL--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 436 fsaSIKENITYGLKNVSKERLD--EVIEAAQlsSLIDQ--LPDGLDTLVGEHGNklsgGQKQCISIARALIRQPKIILLD 511
Cdd:NF040905 94 ---SIAENIFLGNERAKRGVIDwnETNRRAR--ELLAKvgLDESPDTLVTDIGV----GKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 512 EATSAL-DNQSEKKIQQALNYLTETPTTFIVAHRLSTIKE-ADKIVVIDEGKIVE 564
Cdd:NF040905 165 EPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
350-563 |
2.15e-14 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 72.60 E-value: 2.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSV---RNYL 426
Cdd:PRK10908 3 RFEHVSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpflRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 427 AVVPQTT-LLFSASIKENITYGL--KNVSKERLDEVIEAAqlsslIDQLpdGLDTLVGEHGNKLSGGQKQCISIARALIR 503
Cdd:PRK10908 82 GMIFQDHhLLMDRTVYDNVAIPLiiAGASGDDIRRRVSAA-----LDKV--GLLDKAKNFPIQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 504 QPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVA-HRLSTIKEAD-KIVVIDEGKIV 563
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMAtHDIGLISRRSyRMLTLSDGHLH 216
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
47-307 |
2.61e-14 |
|
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: 73.67 E-value: 2.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 47 LMPIAIANVINAA-SSKDSSQLQAIYfnAFLMACLIGQNILTnYFHVKYHSTSIRQVEAGLRATLIKKIQELSIPYQKEL 125
Cdd:cd18576 14 VFPLLAGQLIDAAlGGGDTASLNQIA--LLLLGLFLLQAVFS-FFRIYLFARVGERVVADLRKDLYRHLQRLPLSFFHER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 126 QSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFVTLFFRKRIRQSNSDFRQE 205
Cdd:cd18576 91 RVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 206 MEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVswASFQIFQLICLI--FTGILALQG 283
Cdd:cd18576 171 LAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSF--IIFLLFGAIVAVlwYGGRLVLAG 248
|
250 260
....*....|....*....|....
gi 1158646300 284 RIQPGDVVMYQTYFTTIVNSVSGM 307
Cdd:cd18576 249 ELTAGDLVAFLLYTLFIAGSIGSL 272
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
367-527 |
3.84e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.37 E-value: 3.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 367 DHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNylavvpqttLLF---SASIK-- 441
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD---------LLYlghQPGIKte 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ----ENITYglknvskerldevieAAQLSSLID--QLPDGLDTlVGEHG------NKLSGGQKQCISIARALIRQPKIIL 509
Cdd:PRK13538 89 ltalENLRF---------------YQRLHGPGDdeALWEALAQ-VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLWI 152
|
170
....*....|....*...
gi 1158646300 510 LDEATSALDNQSEKKIQQ 527
Cdd:PRK13538 153 LDEPFTAIDKQGVARLEA 170
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
106-320 |
4.40e-14 |
|
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: 72.93 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 106 LRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQtlssQVFVSGL-NIAVNLFVALGIT---LYKSPVVFMFFLLTV 181
Cdd:cd18563 78 LRRDLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQ----DFLSDGLpDFLTNILMIIGIGvvlFSLNWKLALLVLIPV 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 182 PLAAFVTLFFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVS 261
Cdd:cd18563 154 PLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLL 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1158646300 262 WASFQIFQLICLIFTGILALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGMES 320
Cdd:cd18563 234 TFLTSLGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTS 292
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
111-314 |
5.35e-14 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 72.86 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 111 IKKIQELSIPYQKELQSGRIQSKIiRDVEAIQTLSSQVFVSglnIAVNLFVAL--GITLYK-SPVVFMFFLLTVPLAAFV 187
Cdd:cd18570 82 FKHLLKLPLSFFETRKTGEIISRF-NDANKIREAISSTTIS---LFLDLLMVIisGIILFFyNWKLFLITLLIIPLYILI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 188 TLFFRKRIRQSNsdfRQEME---ETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWAS 264
Cdd:cd18570 158 ILLFNKPFKKKN---REVMEsnaELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLI 234
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1158646300 265 FQIFQLICLIFTGILALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTI 314
Cdd:cd18570 235 SLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKI 284
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
358-558 |
6.96e-14 |
|
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: 71.67 E-value: 6.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 358 YPdSLKPIIDHFSLEVKAG-----ETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIflddqpldELDMRSVrnylAVVPQT 432
Cdd:cd03237 3 YP-TMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--------EIELDTV----SYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 433 -TLLFSASIKE---NITYGLKNVSKERlDEVIEAAQLSSLID-QLPDgldtlvgehgnkLSGGQKQCISIARALIRQPKI 507
Cdd:cd03237 70 iKADYEGTVRDllsSITKDFYTHPYFK-TEIAKPLQIEQILDrEVPE------------LSGGELQRVAIAACLSKDADI 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 508 ILLDEATSALDNQSEKKIQQALNYLTET--PTTFIVAHRLSTIKE-ADKIVVID 558
Cdd:cd03237 137 YLLDEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEHDIIMIDYlADRLIVFE 190
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
353-512 |
8.34e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.72 E-value: 8.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 353 DVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELD---MRSVRNYLAVV 429
Cdd:PRK11831 12 GVSFTRGN--RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRKRMSML 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLFS-ASIKENITYGLKNVSkeRLDEVI---------EAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIAR 499
Cdd:PRK11831 90 FQSGALFTdMNVFDNVAYPLREHT--QLPAPLlhstvmmklEAVGLRGAAKLMP-----------SELSGGMARRAALAR 156
|
170
....*....|...
gi 1158646300 500 ALIRQPKIILLDE 512
Cdd:PRK11831 157 AIALEPDLIMFDE 169
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
353-544 |
8.98e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 70.36 E-value: 8.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 353 DVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDElDMRSVRNYLAVVPQT 432
Cdd:PRK13540 6 ELDFDYHD--QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 433 TLLF-SASIKENITYGLKNVSKE-RLDEVIEAAQLSSLIDqLPDGLdtlvgehgnkLSGGQKQCISIARALIRQPKIILL 510
Cdd:PRK13540 83 SGINpYLTLRENCLYDIHFSPGAvGITELCRLFSLEHLID-YPCGL----------LSSGQKRQVALLRLWMSKAKLWLL 151
|
170 180 190
....*....|....*....|....*....|....
gi 1158646300 511 DEATSALDNQSekkiqqalnylTETPTTFIVAHR 544
Cdd:PRK13540 152 DEPLVALDELS-----------LLTIITKIQEHR 174
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
365-574 |
2.12e-13 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.48 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 365 IIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQP----TSGKIFLDDQPLDELDMRS----VRNYLAVV---PQTT 433
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRErrkiIGREIAMIfqePSSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 434 LLFSASI----KENI---TYGLK--NVSKERLDEVIE----------AAQLSSLIDQLPDGLdtlvgehgnklsgGQKqc 494
Cdd:COG4170 102 LDPSAKIgdqlIEAIpswTFKGKwwQRFKWRKKRAIEllhrvgikdhKDIMNSYPHELTEGE-------------CQK-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 495 ISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFI--VAHRLSTI-KEADKIVVIDEGKIVEIGTYEKL 571
Cdd:COG4170 167 VMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSIllISHDLESIsQWADTITVLYCGQTVESGPTEQI 246
|
...
gi 1158646300 572 LAQ 574
Cdd:COG4170 247 LKS 249
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
376-566 |
2.72e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.60 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 376 GETIAFVGPSGSGKSTLLNLLIGFIQPTS--GKIFLDDQPLDELDMRSVrnylAVVPQTTLLFS-ASIKENITYglknVS 452
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRT----GFVTQDDILYPhLTVRETLVF----CS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 453 KERL------DEVIEAAQlsSLIDQLpdGL----DTLVGEHGNK-LSGGQKQCISIARALIRQPKIILLDEATSALDNQS 521
Cdd:PLN03211 166 LLRLpksltkQEKILVAE--SVISEL--GLtkceNTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1158646300 522 EKKIQQALNYLTETPTTFIVA-HRLST--IKEADKIVVIDEGKIVEIG 566
Cdd:PLN03211 242 AYRLVLTLGSLAQKGKTIVTSmHQPSSrvYQMFDSVLVLSEGRCLFFG 289
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
354-584 |
3.20e-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: 72.28 E-value: 3.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 354 VSFLYPDSlKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLddQPldelDMRsvRNYLAVVPQtt 433
Cdd:TIGR03719 10 VSKVVPPK-KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP--QP----GIK--VGYLPQEPQ-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 434 LLFSASIKENITYGLKNVSK--ERLDEVI---------------EAAQLSSLIDQ------------------LPDGlDT 478
Cdd:TIGR03719 79 LDPTKTVRENVEEGVAEIKDalDRFNEISakyaepdadfdklaaEQAELQEIIDAadawdldsqleiamdalrCPPW-DA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 479 LVgehgNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQalnYLTETPTTFI-VAH-RLSTIKEADKIVV 556
Cdd:TIGR03719 158 DV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLER---HLQEYPGTVVaVTHdRYFLDNVAGWILE 230
|
250 260
....*....|....*....|....*....
gi 1158646300 557 IDEGK-IVEIGTYEKLLAQKGyfYRLKNE 584
Cdd:TIGR03719 231 LDRGRgIPWEGNYSSWLEQKQ--KRLEQE 257
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
369-563 |
3.25e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.25 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 369 FSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMR-SVRNYLAVVP----QTTLLFSASIKEN 443
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdAIRAGIMLCPedrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 444 ItyglkNVSKER--------LDEVIEAAQLSSLIDQL----PDGlDTLVGehgnKLSGGQKQCISIARALIRQPKIILLD 511
Cdd:PRK11288 352 I-----NISARRhhlragclINNRWEAENADRFIRSLniktPSR-EQLIM----NLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1158646300 512 EATSALDNQSEKKIQQALNYLTETPTTFIVAHrlSTIKE----ADKIVVIDEGKIV 563
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQGVAVLFVS--SDLPEvlgvADRIVVMREGRIA 475
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
364-573 |
3.67e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.96 E-value: 3.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 364 PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDeldMRSVRNYLA--VV------PQTTLL 435
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVV---TRSPQDGLAngIVyisedrKRDGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 436 FSASIKENITY-GLKNVSKE--RLDEVIEAAQLSSLID----QLPdGLDTLVGehgnKLSGGQKQCISIARALIRQPKII 508
Cdd:PRK10762 343 LGMSVKENMSLtALRYFSRAggSLKHADEQQAVSDFIRlfniKTP-SMEQAIG----LLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 509 LLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHrlSTIKE----ADKIVVIDEGKI-----VEIGTYEKLLA 573
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVS--SEMPEvlgmSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
363-577 |
4.18e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.29 E-value: 4.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGF--IQPTSGKIFLDDQPLDELD--MRSVRN-YLAV--------V 429
Cdd:CHL00131 20 NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEpeERAHLGiFLAFqypieipgV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQTTLLFSASIKENITYGLKNVSKERLDEVIeaAQLSSLIDQLPDGLDTLVGEhgnKLSGGQKQCISIARALIRQPKIIL 509
Cdd:CHL00131 100 SNADFLRLAYNSKRKFQGLPELDPLEFLEII--NEKLKLVGMDPSFLSRNVNE---GFSGGEKKRNEILQMALLDSELAI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 510 LDEATSALDNQSEKKIQQALNYL-TETPTTFIVAH--RLSTIKEADKIVVIDEGKIVEIGTYE--KLLAQKGY 577
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGINKLmTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKELEKKGY 247
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
28-324 |
5.91e-13 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 69.76 E-value: 5.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 28 YWRFAMSGLFFIIKHLPSWLMPIAIANVINAASSKDSSQLQAIYFnAFLMACLIgqnILTNYFHVKYHSTSIRQVEAG-- 105
Cdd:cd18554 2 IITIVIGLVRFGIPLLLPLILKYIVDDVIQGSSLTLDEKVYKLFT-IIGIMFFI---FLILRPPVEYYRQYFAQWIANki 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 106 ---LRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVP 182
Cdd:cd18554 78 lydIRKDLFDHLQKLSLRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 183 LAAFVTLFFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGF-HLDILQSVFGSVS 261
Cdd:cd18554 158 FYILAVKYFFGRLRKLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALkHTRWNAKTFSAVN 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 262 WASfQIFQLICLIFTGILALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGMESITSI 324
Cdd:cd18554 238 TIT-DLAPLLVIGFAAYLVIEGNLTVGTLVAFVGYMERMYSPLRRLVNSFTTLTQSFASMDRV 299
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
365-518 |
5.96e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.99 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 365 IIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIflddqpldeldMRSVRNYLAVVPQ-----TTLLFSAS 439
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVPQklyldTTLPLTVN 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1158646300 440 IKENITYGLKnvsKERLDEVIEAAQLSSLIDQlpdgldtlvgeHGNKLSGGQKQCISIARALIRQPKIILLDEATSALD 518
Cdd:PRK09544 88 RFLRLRPGTK---KEDILPALKRVQAGHLIDA-----------PMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
365-535 |
6.02e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.06 E-value: 6.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 365 IIDHFSLEVKAGETIAFVGPSGSGKSTLLNLL-----IGFIqpTSGKIFLDDQPLDELDMRS---VRNYLAVVPQTT--- 433
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSSFQRSigyVQQQDLHLPTSTvre 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 434 -LLFSASIKENityglKNVSKER----LDEVIEAAQLSSLIdqlpdglDTLVGEHGNKLSGGQKQCISIARALIRQPKII 508
Cdd:TIGR00956 856 sLRFSAYLRQP-----KSVSKSEkmeyVEEVIKLLEMESYA-------DAVVGVPGEGLNVEQRKRLTIGVELVAKPKLL 923
|
170 180
....*....|....*....|....*...
gi 1158646300 509 L-LDEATSALDNQSEKKIQQALNYLTET 535
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKLADH 951
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
364-575 |
7.58e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 71.13 E-value: 7.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 364 PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLD----------DQPLDELDmrSVRNYLA--VVPQ 431
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlqqDPPRNVEG--TVYDFVAegIEEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 432 TTLL---FSASIKENITYGLKNVSK-ERLDEVIEAAQLSSLIDQLPDGLDTLvGEHGNK----LSGGQKQCISIARALIR 503
Cdd:PRK11147 95 AEYLkryHDISHLVETDPSEKNLNElAKLQEQLDHHNLWQLENRINEVLAQL-GLDPDAalssLSGGWLRKAALGRALVS 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 504 QPKIILLDEATSALDNQSekkIQQALNYLTETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIVEI-GTYEKLLAQK 575
Cdd:PRK11147 174 NPDVLLLDEPTNHLDIET---IEWLEGFLKTFQGSIIfISHDRSFIRNmATRIVDLDRGKLVSYpGNYDQYLLEK 245
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
367-576 |
8.18e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 71.31 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 367 DHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRN--YLAvvpQTtllFS----ASI 440
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRvgYMS---QA---FSlygeLTV 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 441 KENIT-----YGL-KNVSKERLDEVIEAAQLSSLIDQLPDGldtlvgehgnkLSGGQKQCISIARALIRQPKIILLDEAT 514
Cdd:NF033858 357 RQNLElharlFHLpAAEIAARVAEMLERFDLADVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLILDEPT 425
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 515 S-----ALDNQSEKKIQQALNyltETPTTFIVAHRLStikEA---DKIVVIDEGKIVEIGTYEKLLAQKG 576
Cdd:NF033858 426 SgvdpvARDMFWRLLIELSRE---DGVTIFISTHFMN---EAercDRISLMHAGRVLASDTPAALVAARG 489
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
319-549 |
1.57e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 70.16 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 319 ESITSIGELLIAGdvETYHGKKKIQHLDGNFRFEDVSFLYPDSLKpIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLiG 398
Cdd:TIGR00954 424 EEIESGREGGRNS--NLVPGRGIVEYQDNGIKFENIPLVTPNGDV-LIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-G 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 399 FIQPTSGKIFLDDQPldeldmrsvrNYLAVVPQTTLLFSASIKENITYGL-------KNVSKERLDEVIEAAQLSSLIdQ 471
Cdd:TIGR00954 500 ELWPVYGGRLTKPAK----------GKLFYVPQRPYMTLGTLRDQIIYPDssedmkrRGLSDKDLEQILDNVQLTHIL-E 568
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1158646300 472 LPDGLDTlVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNyltETPTTFI-VAHRLSTIK 549
Cdd:TIGR00954 569 REGGWSA-VQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCR---EFGITLFsVSHRKSLWK 643
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
352-577 |
1.97e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 69.92 E-value: 1.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 352 EDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKI------------------FLDD-- 411
Cdd:PRK15064 323 ENLTKGFDN--GPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyyaqdhaydFENDlt 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 412 ---------QPLDelDMRSVRNYLAvvpqtTLLFSAsikenityglknvskerlDEVIEAAQLsslidqlpdgldtlvge 482
Cdd:PRK15064 401 lfdwmsqwrQEGD--DEQAVRGTLG-----RLLFSQ------------------DDIKKSVKV----------------- 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 483 hgnkLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQAL-NYlteTPTTFIVAH-R--LSTIkeADKIVVID 558
Cdd:PRK15064 439 ----LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALeKY---EGTLIFVSHdRefVSSL--ATRIIEIT 509
|
250 260
....*....|....*....|
gi 1158646300 559 EGKIVEI-GTYEKLLAQKGY 577
Cdd:PRK15064 510 PDGVVDFsGTYEEYLRSQGI 529
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
350-576 |
2.58e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 350 RFEDVSFLYPDSLKpiIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGF--IQptSGKIflddQPLDElDMRSVRNYLA 427
Cdd:NF033858 3 RLEGVSHRYGKTVA--LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGArkIQ--QGRV----EVLGG-DMADARHRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 VVPQT-------------TLlfsaSIKENIT-----YGL-KNVSKERLDEVIEAAQLSSLIDQlPDGldtlvgehgnKLS 488
Cdd:NF033858 74 VCPRIaympqglgknlypTL----SVFENLDffgrlFGQdAAERRRRIDELLRATGLAPFADR-PAG----------KLS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 489 GGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYL-TETPT-TFIVAhrlsT--IKEA---DKIVVIDEGK 561
Cdd:NF033858 139 GGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIrAERPGmSVLVA----TayMEEAerfDWLVAMDAGR 214
|
250
....*....|....*
gi 1158646300 562 IVEIGTYEKLLAQKG 576
Cdd:NF033858 215 VLATGTPAELLARTG 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
349-560 |
2.93e-12 |
|
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: 65.73 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSF--LYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLL-----IGFIqptSGKIFLDDQPLDEldmrS 421
Cdd:cd03232 4 LTWKNLNYtvPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVI---TGEILINGRPLDK----N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 422 VRNYLAVVPQTTLLFSasikeNITyglknvskerldeVIEAAQLSSLIdqlpdgldtlvgehgNKLSGGQKQCISIARAL 501
Cdd:cd03232 77 FQRSTGYVEQQDVHSP-----NLT-------------VREALRFSALL---------------RGLSVEQRKRLTIGVEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 502 IRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVA-HRLS--TIKEADKIVVIDEG 560
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTiHQPSasIFEKFDRLLLLKRG 185
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
365-567 |
3.97e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.77 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 365 IIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIG-FIQP-------TSGKIFLDDQPLDELDMRSVRNYLAVVPQTTL-L 435
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQpA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 436 FSASIKENITYGlknvskeRLDEVIEAAQLSSLIDQLPD------GLDTLVGEHGNKLSGGQKQCISIARAL-------- 501
Cdd:PRK13547 96 FAFSAREIVLLG-------RYPHARRAGALTHRDGEIAWqalalaGATALVGRDVTTLSGGELARVQFARVLaqlwpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 502 -IRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVA--HRLS-TIKEADKIVVIDEGKIVEIGT 567
Cdd:PRK13547 169 aAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAivHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
373-546 |
5.98e-12 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 66.24 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 373 VKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKifLDDQP-----LDELDMRSVRNYLAVVPQTTLlfSASIK----EN 443
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPdwdeiLDEFRGSELQNYFTKLLEGDV--KVIVKpqyvDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 444 ITYGLKNVSKERLDEVIEAAQLSSLIDQLpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDnqsek 523
Cdd:cd03236 99 IPKAVKGKVGELLKKKDERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD----- 171
|
170 180 190
....*....|....*....|....*....|
gi 1158646300 524 kIQQALN-------YLTETPTTFIVAHRLS 546
Cdd:cd03236 172 -IKQRLNaarlireLAEDDNYVLVVEHDLA 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
367-558 |
2.23e-11 |
|
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: 66.35 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 367 DHFSLEVKAG-----ETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDdqpldeldmrsVRnyLAVVPQttlLFSASIK 441
Cdd:COG1245 352 GGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-----------LK--ISYKPQ---YISPDYD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITYGLKNVSKERLD------EVIEAAQLSSLIDQ-LPDgldtlvgehgnkLSGGQKQCISIARALIRQPKIILLDEAT 514
Cdd:COG1245 416 GTVEEFLRSANTDDFGssyyktEIIKPLGLEKLLDKnVKD------------LSGGELQRVAIAACLSRDADLYLLDEPS 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1158646300 515 SALDnqSEKKIQ--QALNYLTET--PTTFIVAHRLSTIKE-ADKIVVID 558
Cdd:COG1245 484 AHLD--VEQRLAvaKAIRRFAENrgKTAMVVDHDIYLIDYiSDRLMVFE 530
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
351-572 |
2.59e-11 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 66.42 E-value: 2.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 351 FEDVSFLYPDSlkPII-DHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFlddqpldeldmRSVRNYLAVV 429
Cdd:PLN03073 511 FSDASFGYPGG--PLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVF 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 430 PQ----------TTLLFSASIkenitygLKNVSKERLdevieAAQLSSLidqlpdgldtlvGEHGN-------KLSGGQK 492
Cdd:PLN03073 578 SQhhvdgldlssNPLLYMMRC-------FPGVPEQKL-----RAHLGSF------------GVTGNlalqpmyTLSGGQK 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 493 QCISIARALIRQPKIILLDEATSALDNQSEKKIQQALnyLTETPTTFIVAHRLSTIK-EADKIVVIDEGKIVEI-GT--- 567
Cdd:PLN03073 634 SRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGL--VLFQGGVLMVSHDEHLISgSVDELWVVSEGKVTPFhGTfhd 711
|
....*
gi 1158646300 568 YEKLL 572
Cdd:PLN03073 712 YKKTL 716
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
363-577 |
3.12e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.66 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGF--IQPTSGKIFLDDQPLDELD--MRSVRNYLAVVPQTTLLFSA 438
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSpeDRAGEGIFMAFQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 439 SIKENITYGLKNVSKERLDEVIEAAQLSSLID------QLPDGLDTLVGEHGnkLSGGQKQCISIARALIRQPKIILLDE 512
Cdd:PRK09580 94 SNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEekiallKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 513 ATSALDNQSEKKIQQALNYLTETPTTFI-VAH--RLSTIKEADKIVVIDEGKIVEIGTYE--KLLAQKGY 577
Cdd:PRK09580 172 SDSGLDIDALKIVADGVNSLRDGKRSFIiVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTlvKQLEEQGY 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
369-558 |
3.20e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 65.99 E-value: 3.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 369 FSLEVKAG-----ETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLD------------DQPLdeldmrSVRNYLAVVPQ 431
Cdd:PRK13409 353 FSLEVEGGeiyegEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqyikpDYDG------TVEDLLRSITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 432 TtllFSAS-IKENITYGLknvskerldevieaaqlsslidQLPDGLDTLVGEhgnkLSGGQKQCISIARALIRQPKIILL 510
Cdd:PRK13409 427 D---LGSSyYKSEIIKPL----------------------QLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLL 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 511 DEATSALDnqSEKKIQ--QALNYLTET--PTTFIVAHRLSTIKE-ADKIVVID 558
Cdd:PRK13409 478 DEPSAHLD--VEQRLAvaKAIRRIAEEreATALVVDHDIYMIDYiSDRLMVFE 528
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
361-563 |
3.95e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 62.67 E-value: 3.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 361 SLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPT---SGKIFLDDQPLDELDMRSVRNYLAV------VP- 430
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVseedvhFPt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 431 ---QTTLLFSASIKENityglknvskerldEVIEaaqlsslidqlpdgldtlvgehgnKLSGGQKQCISIARALIRQPKI 507
Cdd:cd03233 98 ltvRETLDFALRCKGN--------------EFVR------------------------GISGGERKRVSIAEALVSRASV 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 508 ILLDEATSALDNQSEKKIQQALNYLTET--PTTFIVAHRLS--TIKEADKIVVIDEGKIV 563
Cdd:cd03233 140 LCWDNSTRGLDSSTALEILKCIRTMADVlkTTTFVSLYQASdeIYDLFDKVLVLYEGRQI 199
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
365-578 |
5.08e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.90 E-value: 5.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 365 IIDHFSLEVKAGETIAFVGPSGSGKSTLLNLL----IGFIQPTSGKIFLDDQPLDELdMRSVRNYLAVVPQT-------- 432
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETdvhfphlt 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 433 ---TLLFSASIKENITYGlKNVSKERLDEVIEAAQLSSLidqlpdGL----DTLVG-EHGNKLSGGQKQCISIARALIRQ 504
Cdd:TIGR00956 155 vgeTLDFAARCKTPQNRP-DGVSREEYAKHIADVYMATY------GLshtrNTKVGnDFVRGVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 505 PKIILLDEATSALDNQSEKKIQQAL----NYLTETPTTFIVAHRLSTIKEADKIVVIDEGKIVEIGTYEKLlaqKGYF 578
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALktsaNILDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKA---KQYF 302
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
353-580 |
6.82e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.98 E-value: 6.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 353 DVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKS----TLLNLL-----IGFIQPTSGKIFLDdqpLDELDMRSVR 423
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLaangrIGGSATFNGREILN---LPEKELNKLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 424 -NYLAVV---PQTTLLFSASIKENITYGL---KNVSK-ERLDEVIEaaqlssLID--QLPDGLDTLvGEHGNKLSGGQKQ 493
Cdd:PRK09473 96 aEQISMIfqdPMTSLNPYMRVGEQLMEVLmlhKGMSKaEAFEESVR------MLDavKMPEARKRM-KMYPHEFSGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 494 CISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLT-ETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIVEIGTYEK 570
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNARD 248
|
250
....*....|
gi 1158646300 571 LlaqkgyFYR 580
Cdd:PRK09473 249 V------FYQ 252
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
349-562 |
6.89e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 64.85 E-value: 6.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDSLK-PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIG-FIQPTSGKIFLDDQPLDELD-MRSVRNY 425
Cdd:TIGR02633 258 LEARNLTCWDVINPHrKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKPVDIRNpAQAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 426 LAVVPQTT----LLFSASIKENITYGLKN--VSKERLDEVIEAAQLSSLIDQL---PDGLDTLVGehgnKLSGGQKQCIS 496
Cdd:TIGR02633 338 IAMVPEDRkrhgIVPILGVGKNITLSVLKsfCFKMRIDAAAELQIIGSAIQRLkvkTASPFLPIG----RLSGGNQQKAV 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 497 IARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHrlSTIKE----ADKIVVIDEGKI 562
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVS--SELAEvlglSDRVLVIGEGKL 481
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
341-574 |
9.28e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.27 E-value: 9.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 341 KIQHLDGNFRFEDVSFLYPDSLkpiidhfslEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGkiflddqpldELDMR 420
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSL---------TLNAGDSWAFVGANGSGKSALARALAGELPLLSG----------ERQSQ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 421 SVRNYLAVVPQTTLLFSASIKENITYGL--------KNVSKERLDEVIEAAQLSSLIDQLpdGLDTLVGEHGNKLSGGQK 492
Cdd:PRK10938 64 FSHITRLSFEQLQKLVSDEWQRNNTDMLspgeddtgRTTAEIIQDEVKDPARCEQLAQQF--GITALLDRRFKYLSTGET 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 493 QCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIVEIGTYEK 570
Cdd:PRK10938 142 RKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREE 221
|
....
gi 1158646300 571 LLAQ 574
Cdd:PRK10938 222 ILQQ 225
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
35-314 |
1.07e-10 |
|
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: 62.95 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 35 GLFFIIKHLPSWL-MPIAIANVINAASSKDSSQlqAIYFNAFLMACL-IGQNILTNY----FHVKYhSTSIRQVEAGLRA 108
Cdd:cd18572 1 AFVFLVVAALSELaIPHYTGAVIDAVVADGSRE--AFYRAVLLLLLLsVLSGLFSGLrggcFSYAG-TRLVRRLRRDLFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 109 TLIKkiQELSipYQKELQSGRIQSKIIRDVeaiQTLSSQVfvsGLNIAV---NLFVALGItlykspVVFMFFL------- 178
Cdd:cd18572 78 SLLR--QDIA--FFDATKTGELTSRLTSDC---QKVSDPL---STNLNVflrNLVQLVGG------LAFMFSLswrltll 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 179 --LTVPLAAFVTLFFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRlnkhFTQIYEKGFHLDILQSV 256
Cdd:cd18572 142 afITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARR----YERALDKALKLSVRQAL 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158646300 257 FGSVSWASFQIFQLIC----LIFTGILALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTI 314
Cdd:cd18572 218 AYAGYVAVNTLLQNGTqvlvLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSL 279
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
76-310 |
1.12e-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: 349994 [Multi-domain] Cd Length: 294 Bit Score: 62.89 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 76 LMACLIGQNILTNYFHV--KYHSTSIRQ-VEAGLRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQVFVSG 152
Cdd:cd18550 41 LALGMVAVAVASALLGVvqTYLSARIGQgVMYDLRVQLYAHLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 153 LNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFVTLFFRKRIR-------QSNSDFRQEMEET-SAKVIEVIelapiaR 224
Cdd:cd18550 121 VSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRkltreqqEKLAELNSIMQETlSVSGALLV------K 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 225 AHGLEKHETTRlnkhFTQIYEKGFHLDILQSVFGSVSWASFQIFQ----LICLIFTGILALQGRIQPGDVVMYQTYFTTI 300
Cdd:cd18550 195 LFGREDDEAAR----FARRSRELRDLGVRQALAGRWFFAALGLFTaigpALVYWVGGLLVIGGGLTIGTLVAFTALLGRL 270
|
250
....*....|
gi 1158646300 301 VNSVSGMITL 310
Cdd:cd18550 271 YGPLTQLLNI 280
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
46-217 |
1.16e-10 |
|
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: 62.87 E-value: 1.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 46 WLMPIAIANVInaaSSKDSSQLQAIyfnAFLMACLIGQNILTNYFHVkYHSTSIRQ-VEAGLRATLIKKIQELSIPYQKE 124
Cdd:cd18545 21 YLIKIAIDEYI---PNGDLSGLLII---ALLFLALNLVNWVASRLRI-YLMAKVGQrILYDLRQDLFSHLQKLSFSFFDS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 125 LQSGRIQSKIIRDVEAIQTLssqvFVSGL-NIAVNLFVALGItlykspVVFMFF---------LLTVPLAAFVTLFFRKR 194
Cdd:cd18545 94 RPVGKILSRVINDVNSLSDL----LSNGLiNLIPDLLTLVGI------VIIMFSlnvrlalvtLAVLPLLVLVVFLLRRR 163
|
170 180
....*....|....*....|...
gi 1158646300 195 IRQSNSDFRQEMEETSAKVIEVI 217
Cdd:cd18545 164 ARKAWQRVRKKISNLNAYLHESI 186
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
376-549 |
1.53e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 59.69 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 376 GETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDqpldeldmrsvrnylavvpqttllfsasikenityglknvsker 455
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------------------------------------------- 37
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 456 lDEVIEAAQLSSLidqlpdgLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQA------L 529
Cdd:smart00382 38 -GEDILEEVLDQL-------LLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrllL 109
|
170 180
....*....|....*....|
gi 1158646300 530 NYLTETPTTFIVAHRLSTIK 549
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDL 129
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
370-561 |
1.56e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.48 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 370 SLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLD--------ELDMRSVRNYLAVVPQTTllfsasIK 441
Cdd:PRK10762 24 ALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqEAGIGIIHQELNLIPQLT------IA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENITYGLKNVSK-ERLDEVIEAAQLSSLIDQL--PDGLDTLVGEhgnkLSGGQKQCISIARALIRQPKIILLDEATSALD 518
Cdd:PRK10762 98 ENIFLGREFVNRfGRIDWKKMYAEADKLLARLnlRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDEPTDALT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 519 NqsekkiqqalnylTETPTTFIV--------------AHRLSTIKE-ADKIVVIDEGK 561
Cdd:PRK10762 174 D-------------TETESLFRVirelksqgrgivyiSHRLKEIFEiCDDVTVFRDGQ 218
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
47-324 |
1.90e-10 |
|
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: 62.11 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 47 LMPIAIANVINAASSKDSSQ------LQAIYFNAFLMACL-IGQNILTNYFHVKYHSTSIRQVeAGLRATLIKKIQELSI 119
Cdd:cd18577 17 LMTIVFGDLFDAFTDFGSGEsspdefLDDVNKYALYFVYLgIGSFVLSYIQTACWTITGERQA-RRIRKRYLKALLRQDI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 120 PYQKELQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFVTLFFRKRIRQSN 199
Cdd:cd18577 96 AWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 200 SDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIFQLICLIFTGIL 279
Cdd:cd18577 176 KKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRL 255
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1158646300 280 ALQGRIQPGDVVmyqTYFTTIVNSVSGMITLIP---TISKGMESITSI 324
Cdd:cd18577 256 VRDGEISPGDVL---TVFFAVLIGAFSLGQIAPnlqAFAKARAAAAKI 300
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
363-521 |
2.20e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQpldeldmRSVrNYLAVVPQttLLFSASIKE 442
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAPG-------IKV-GYLPQEPQ--LDPEKTVRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 443 NITYGLKNV--SKERLDEVIEA---------------AQLSSLID------------------QLPDGlDTLVGehgnKL 487
Cdd:PRK11819 90 NVEEGVAEVkaALDRFNEIYAAyaepdadfdalaaeqGELQEIIDaadawdldsqleiamdalRCPPW-DAKVT----KL 164
|
170 180 190
....*....|....*....|....*....|....
gi 1158646300 488 SGGQKQCISIARALIRQPKIILLDEATSALDNQS 521
Cdd:PRK11819 165 SGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
47-321 |
2.52e-10 |
|
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: 61.65 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 47 LMPIAIANVINAASSKdsSQLQAIYFNAFLMACL----IGQNILTNYFHVKyhsTSIRqVEAGLRATLIKKIQELSIPYQ 122
Cdd:cd18548 17 LLPTLMADIIDEGIAN--GDLSYILRTGLLMLLLallgLIAGILAGYFAAK---ASQG-FGRDLRKDLFEKIQSFSFAEI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 123 KELQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVP-LAAFVTLFFRK------RI 195
Cdd:cd18548 91 DKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPiLALVVFLIMKKaiplfkKV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 196 RQSNSDFRQEMEE--TSAKVIevielapiaRAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIFQLICL 273
Cdd:cd18548 171 QKKLDRLNRVVREnlTGIRVI---------RAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAIL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1158646300 274 IFTGILALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGMESI 321
Cdd:cd18548 242 WFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMVFVMLPRASASA 289
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
349-562 |
2.62e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDSL-KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQ-PTSGKIFLDDQPLDELDMR-SVRNY 425
Cdd:PRK13549 260 LEVRNLTAWDPVNPhIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQqAIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 426 LAVVPQTT----LLFSASIKENITYG-LKNVSK-ERLDEVIEAAQLSSLIDQLPDGLDTLVGEHGNkLSGGQKQCISIAR 499
Cdd:PRK13549 340 IAMVPEDRkrdgIVPVMGVGKNITLAaLDRFTGgSRIDDAAELKTILESIQRLKVKTASPELAIAR-LSGGNQQKAVLAK 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1158646300 500 ALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHrlSTIKE----ADKIVVIDEGKI 562
Cdd:PRK13549 419 CLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVIS--SELPEvlglSDRVLVMHEGKL 483
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
366-571 |
3.33e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 61.68 E-value: 3.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFI----QPTSGKIFLDDQPLDELDMRSVRNY----LAVV---PQTTL 434
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERRNLvgaeVAMIfqdPMTSL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 435 LFSASIKENITYGLK----NVSKERLDEVIEaaqLSSLIDqLPDGLDTL-VGEHgnKLSGGQKQCISIARALIRQPKIIL 509
Cdd:PRK11022 103 NPCYTVGFQIMEAIKvhqgGNKKTRRQRAID---LLNQVG-IPDPASRLdVYPH--QLSGGMSQRVMIAMAIACRPKLLI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 510 LDEATSALDNQSEKKIQQALNYLT--ETPTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKL 571
Cdd:PRK11022 177 ADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVAEaAHKIIVMYAGQVVETGKAHDI 241
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
349-582 |
3.84e-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: 63.11 E-value: 3.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLdELDMRSVRNYLAV 428
Cdd:TIGR01257 1938 LRLNELTKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGY 2016
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 VPQttllFSAsIKENIT-------YG-LKNVSKERLDEV----IEAAQLSSLIDQLpdgldtlvgehGNKLSGGQKQCIS 496
Cdd:TIGR01257 2017 CPQ----FDA-IDDLLTgrehlylYArLRGVPAEEIEKVanwsIQSLGLSLYADRL-----------AGTYSGGNKRKLS 2080
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 497 IARALIRQPKIILLDEATSALDNQSEKKIQQAL-NYLTETPTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:TIGR01257 2081 TAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
250
....*....|
gi 1158646300 575 --KGYFYRLK 582
Cdd:TIGR01257 2161 fgDGYIVTMK 2170
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
50-328 |
4.10e-10 |
|
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: 61.31 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 50 IAIANVINAASSKDSSQLQA-IYFNAFLMACLIGQNILTNYFhvKYHSTSIrqveAG------LRATLIKKI--QElsIP 120
Cdd:cd18578 30 ILFSKLISVFSLPDDDELRSeANFWALMFLVLAIVAGIAYFL--QGYLFGI----AGerltrrLRKLAFRAIlrQD--IA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 121 Y--QKELQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSP----VVfmffLLTVPLAAFVTLFFRKR 194
Cdd:cd18578 102 WfdDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWklalVG----LATVPLLLLAGYLRMRL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 195 IRQSNSDFRQEMEETSAKVIEVIElapiA----RAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIFQL 270
Cdd:cd18578 178 LSGFEEKNKKAYEESSKIASEAVS----NirtvASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYA 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 271 ICLIFTGILALQGRIQPGDvvMYQTYFTTI--VNSVSGMITLIPTISKGMESITSIGELL 328
Cdd:cd18578 254 LAFWYGGRLVANGEYTFEQ--FFIVFMALIfgAQSAGQAFSFAPDIAKAKAAAARIFRLL 311
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
364-518 |
5.45e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.48 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 364 PIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDMRSVRNYLAVVPqtTLLFSASIKEN 443
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLP--GLKADLSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 444 ITY--GLKNVSKERLDEvieaaqlSSL-IDQLPDGLDTLVgehgNKLSGGQKQCISIARALIRQPKIILLDEATSALD 518
Cdd:PRK13543 103 LHFlcGLHGRRAKQMPG-------SALaIVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
370-565 |
7.90e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 7.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 370 SLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFL---DDQPLDELDmrSVRNYLAVVPQT---TLLFSA-SIKE 442
Cdd:PRK09700 283 SFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLngkDISPRSPLD--AVKKGMAYITESrrdNGFFPNfSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 443 NI-------------TYGLKNVSKERLDEVIEAAQLS---SLIDQlpdgldtlvgeHGNKLSGGQKQCISIARALIRQPK 506
Cdd:PRK09700 361 NMaisrslkdggykgAMGLFHEVDEQRTAENQRELLAlkcHSVNQ-----------NITELSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1158646300 507 IILLDEATSALDNQSEKKIQQALNYLTET-PTTFIVAHRLSTIKEA-DKIVVIDEGKIVEI 565
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVcDRIAVFCEGRLTQI 490
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
366-574 |
1.30e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.06 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIflddqpldelDMRSVRNYLAVvpqttllfSASIKENIT 445
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----------DRNGEVSVIAI--------SAGLSGQLT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 446 yGLKNVS-------------KERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLDE 512
Cdd:PRK13546 102 -GIENIEfkmlcmgfkrkeiKAMTPKIIEFSELGEFIYQPV-----------KKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 513 ATSALDNQ-SEKKIQQALNYLTETPTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQ 574
Cdd:PRK13546 170 ALSVGDQTfAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
354-573 |
1.42e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.82 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 354 VSFLYPDSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQP----TSGKIFLDDQPLDELDMRSVRNYLA-- 427
Cdd:PRK15093 11 IEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRERRKLVGhn 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 428 -----VVPQTTLLFSASIKENI-------TYGLK--NVSKERLDEVIEAAQLSSLIDQlpdglDTLVGEHGNKLSGGQKQ 493
Cdd:PRK15093 91 vsmifQEPQSCLDPSERVGRQLmqnipgwTYKGRwwQRFGWRKRRAIELLHRVGIKDH-----KDAMRSFPYELTEGECQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 494 CISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFI--VAHRLSTI-KEADKIVVIDEGKIVEIGTYEK 570
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTIllISHDLQMLsQWADKINVLYCGQTVETAPSKE 245
|
...
gi 1158646300 571 LLA 573
Cdd:PRK15093 246 LVT 248
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
366-571 |
1.83e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 60.13 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLD-ELDMRSVRNYLAVVPQT-TLLFSASIKEN 443
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 444 ITYGLKNVSKERLDEVIEAAQLSSLIDQLpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALdnqSEK 523
Cdd:PRK10982 94 MWLGRYPTKGMFVDQDKMYRDTKAIFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEK 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 524 KIQ---QALNYLTETPTTFI-VAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKL 571
Cdd:PRK10982 169 EVNhlfTIIRKLKERGCGIVyISHKMEEIFQlCDEITILRDGQWIATQPLAGL 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
374-559 |
4.33e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 59.03 E-value: 4.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 374 KAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIflDDQP-----LDELDMRSVRNYLAVVPQTTLlfSASIK----ENI 444
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY--DEEPswdevLKRFRGTELQDYFKKLANGEI--KVAHKpqyvDLI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 445 TYGLKNVSKERLDEVIEAAQLSSLIDQLpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDnqsekk 524
Cdd:COG1245 173 PKVFKGTVRELLEKVDERGKLDELAEKL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD------ 244
|
170 180 190
....*....|....*....|....*....|....*
gi 1158646300 525 IQQALNyltetpttfiVAHRLSTIKEADKIVVIDE 559
Cdd:COG1245 245 IYQRLN----------VARLIRELAEEGKYVLVVE 269
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
366-584 |
4.63e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.13 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIflddqpldelDMRSVRNYLAVVP----QTTLLFSASIK 441
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV----------DIKGSAALIAISSglngQLTGIENIELK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 eNITYGL-KNVSKERLDEVIEAAQLSSLIDQLPdgldtlvgehgNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQ 520
Cdd:PRK13545 110 -GLMMGLtKEKIKEIIPEIIEFADIGKFIYQPV-----------KTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1158646300 521 SEKKIQQALNYLTET-PTTFIVAHRLSTIKE-ADKIVVIDEGKIVEIGTYEKLLAQKGYFYRLKNE 584
Cdd:PRK13545 178 FTKKCLDKMNEFKEQgKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQ 243
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
357-576 |
6.75e-09 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 55.66 E-value: 6.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 357 LYPDSLKPIIDHFSL----EVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKiflddqplDELDMRSVrnylAVVPQT 432
Cdd:cd03222 2 LYPDCVKRYGVFFLLvelgVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDN--------DEWDGITP----VYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 433 TllfsasikenityglknvskerldevieaaqlsslidqlpdgldtlvgehgnKLSGGQKQCISIARALIRQPKIILLDE 512
Cdd:cd03222 70 I----------------------------------------------------DLSGGELQRVAIAAALLRNATFYLFDE 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1158646300 513 ATSALDNQSEKKIQQALNYLTE--TPTTFIVAHRLSTIKEADKIVVIDEGkivEIGTYEKLLAQKG 576
Cdd:cd03222 98 PSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEG---EPGVYGIASQPKG 160
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
349-552 |
7.84e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.10 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGfiqptsgkifldDQPldeldmRSVRNYLAv 428
Cdd:PRK10938 261 IVLNNGVVSYND--RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG------------DHP------QGYSNDLT- 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 429 vpqttlLFSA---------SIKENITYglknVSKE-RLD--------EVIeaaqLSSLID------QLPD---------- 474
Cdd:PRK10938 320 ------LFGRrrgsgetiwDIKKHIGY----VSSSlHLDyrvstsvrNVI----LSGFFDsigiyqAVSDrqqklaqqwl 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 475 ---GLDTLVGEHG-NKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYL---TETPTTFI------- 540
Cdd:PRK10938 386 dilGIDKRTADAPfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLiseGETQLLFVshhaeda 465
|
250
....*....|....*
gi 1158646300 541 ---VAHRLSTIKEAD 552
Cdd:PRK10938 466 pacITHRLEFVPDGD 480
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
351-529 |
1.53e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 57.25 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 351 FEDVSFLYPDslKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDqpldeldmrSVRnyLAVVP 430
Cdd:TIGR03719 325 AENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE---------TVK--LAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 431 QT--TLLFSASIKENITYGLK--NVSKErldEVIEAAQLSSL----IDQlpdglDTLVGEhgnkLSGGQKQCISIARALI 502
Cdd:TIGR03719 392 QSrdALDPNKTVWEEISGGLDiiKLGKR---EIPSRAYVGRFnfkgSDQ-----QKKVGQ----LSGGERNRVHLAKTLK 459
|
170 180
....*....|....*....|....*..
gi 1158646300 503 RQPKIILLDEATSALDNQSEKKIQQAL 529
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEAL 486
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
47-293 |
1.92e-08 |
|
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: 55.95 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 47 LMPIAIANVINAA-SSKDSSQLQAIYFNAFLMACLIGqniLTNYFHVkYHSTSI-RQVEAGLRATLIKKIQELSIPYQKE 124
Cdd:cd18575 14 ALGQGLRLLIDQGfAAGNTALLNRAFLLLLAVALVLA---LASALRF-YLVSWLgERVVADLRKAVFAHLLRLSPSFFET 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 125 LQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFVTLFFRKRIRQSNSDFRQ 204
Cdd:cd18575 90 TRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 205 EMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSwasfqifqlICLIFTGILA---- 280
Cdd:cd18575 170 RLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALV---------IFLVFGAIVFvlwl 240
|
250 260
....*....|....*....|.
gi 1158646300 281 -----LQGRIQPGDV---VMY 293
Cdd:cd18575 241 gahdvLAGRMSAGELsqfVFY 261
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
368-562 |
2.97e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 368 HFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQpldELDMRSVRN-------YLAVVPQTTLLF-SAS 439
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGK---EINALSTAQrlarglvYLPEDRQSSGLYlDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 440 IKENITYGLKNVSKERLDEVIEAAQLSSLIDQLP---DGLDTLVGehgnKLSGGQKQCISIARALIRQPKIILLDEATSA 516
Cdd:PRK15439 358 LAWNVCALTHNRRGFWIKPARENAVLERYRRALNikfNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1158646300 517 LDNQSEKKIQQALNYLTE--TPTTFIVAHRLSTIKEADKIVVIDEGKI 562
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAqnVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
373-557 |
3.87e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 373 VKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKifLDDQP-----LDELDMRSVRNYLAVVPQTTLlfSASIK----EN 443
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEPswdevLKRFRGTELQNYFKKLYNGEI--KVVHKpqyvDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 444 ITYGLKNVSKERLDEVIEAAQLSSLIDQLpdGLDTLVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDnqsek 523
Cdd:PRK13409 172 IPKVFKGKVRELLKKVDERGKLDEVVERL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD----- 244
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1158646300 524 kIQQALNY------LTETPTTFIVAHRLSTI-KEADKIVVI 557
Cdd:PRK13409 245 -IRQRLNVarlireLAEGKYVLVVEHDLAVLdYLADNVHIA 284
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
374-540 |
2.47e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.08 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 374 KAGETIAFVGPSGSGKSTLLNLLIG-----FIQptsGKIFLDDQPLDELDMRSVRNYLAV----VPQTT----LLFSASI 440
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGrktggYIE---GDIRISGFPKKQETFARISGYCEQndihSPQVTvresLIYSAFL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 441 KENityglKNVSKER----LDEVIEAAQLSSLIDQLPdGLDTLVGehgnkLSGGQKQCISIARALIRQPKIILLDEATSA 516
Cdd:PLN03140 981 RLP-----KEVSKEEkmmfVDEVMELVELDNLKDAIV-GLPGVTG-----LSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180
....*....|....*....|....
gi 1158646300 517 LDNQSEKKIQQALNYLTETPTTFI 540
Cdd:PLN03140 1050 LDARAAAIVMRTVRNTVDTGRTVV 1073
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
129-315 |
4.62e-07 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 51.74 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 129 RIQS-KIIRdveaiQTLSSQVFVSGLNIAVnLFVALGITLYKSPVVFMFFLLTVPLAAFVTLFFRKRIRQSNSDFRQEME 207
Cdd:cd18555 104 RANSnVYIR-----QILSNQVISLIIDLLL-LVIYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKLNQEEIVAQT 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 208 ETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSwASFQIF-QLICLIFTGILALQGRIQ 286
Cdd:cd18555 178 KVQSYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSIS-SSIQFIaPLLILWIGAYLVINGELT 256
|
170 180 190
....*....|....*....|....*....|..
gi 1158646300 287 PGDVVMYQ---TYFTTIVNSVSGMITLIPTIS 315
Cdd:cd18555 257 LGELIAFSslaGSFLTPIVSLINSYNQFILLK 288
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
105-291 |
5.50e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 51.34 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 105 GLRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLA 184
Cdd:cd18546 73 DLRLRVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPL 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 185 AFVTLFFRkriRQSNSDFRQeMEETSAKVI----EVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSV-FGS 259
Cdd:cd18546 153 ALATRWFR---RRSSRAYRR-ARERIAAVNadlqETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIyFPG 228
|
170 180 190
....*....|....*....|....*....|..
gi 1158646300 260 VSWASfQIFQLICLIFTGILALQGRIQPGDVV 291
Cdd:cd18546 229 VELLG-NLATAAVLLVGAWRVAAGTLTVGVLV 259
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
432-566 |
1.22e-06 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 48.86 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 432 TTLLFSASIKENITYGLKNVSKERLDEVIEAAQLSSLIDQlpdGLDTL-VGEHGNKLSGGQKQCISIARALIRQPK--II 508
Cdd:cd03238 35 STLVNEGLYASGKARLISFLPKFSRNKLIFIDQLQFLIDV---GLGYLtLGQKLSTLSGGELQRVKLASELFSEPPgtLF 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 509 LLDEATSALDNQSEKKIQQALNYLTETPTTFIV-AHRLSTIKEADKIVVI------DEGKIVEIG 566
Cdd:cd03238 112 ILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILiEHNLDVLSSADWIIDFgpgsgkSGGKVVFSG 176
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
349-563 |
1.76e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.56 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 349 FRFEDVSFLYP-DSLKPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIG--FIQPTSGKIFLDDQpldELDMRSVR-- 423
Cdd:NF040905 258 FEVKNWTVYHPlHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGK---EVDVSTVSda 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 424 --NYLAVV----PQTTLLFSASIKENITY-GLKNVSKER-LDEVIEAAQLSSLIDQL----PdGLDTLVGehgnKLSGGQ 491
Cdd:NF040905 335 idAGLAYVtedrKGYGLNLIDDIKRNITLaNLGKVSRRGvIDENEEIKVAEEYRKKMniktP-SVFQKVG----NLSGGN 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1158646300 492 KQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHrlSTIKE----ADKIVVIDEGKIV 563
Cdd:NF040905 410 QQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVIS--SELPEllgmCDRIYVMNEGRIT 483
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
344-529 |
2.70e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 344 HLDGNFRFedvSFLYPDSL----------------KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKI 407
Cdd:PRK10636 293 HVDNPFHF---SFRAPESLpnpllkmekvsagygdRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 408 FLddqpldeldMRSVRnyLAVVPQTTLLFSASIKENITYGLKNVSKErldevieaaqlssLIDQLPDGLDTL------VG 481
Cdd:PRK10636 370 GL---------AKGIK--LGYFAQHQLEFLRADESPLQHLARLAPQE-------------LEQKLRDYLGGFgfqgdkVT 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1158646300 482 EHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQAL 529
Cdd:PRK10636 426 EETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
354-398 |
4.52e-06 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 47.78 E-value: 4.52e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1158646300 354 VSFLYPDSLKPIIDHFslevkAGETIAFVGPSGSGKSTLLNLLIG 398
Cdd:cd01854 68 VSAKTGEGLDELRELL-----KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
47-310 |
5.28e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 48.33 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 47 LMPIAIANVI-NAASSKDSSQLQAIyfnAFLMACLIGQNILTNYFHVKYHSTSIRQVEAGLRATLIKKIQELSIPYQKEL 125
Cdd:cd18568 20 ALPLFTQIILdRVLVHKNISLLNLI---LIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPLSFFASR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 126 QSGRIQSKIiRDVEAIQTLSSQvfvSGLNIAVNL---FVALGITLYKSPVVFMFFLLTVPLAAFVTLFFRKRIRQSNSDF 202
Cdd:cd18568 97 KVGDIITRF-QENQKIRRFLTR---SALTTILDLlmvFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 203 RQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSWASFQIFQLICLIFTGILALQ 282
Cdd:cd18568 173 FQANAEQQSFLVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLGTIAVLWYGAYLVIS 252
|
250 260
....*....|....*....|....*...
gi 1158646300 283 GRIQPGDVVMYQTYFTTIVNSVSGMITL 310
Cdd:cd18568 253 GQLTIGQLVAFNMLFGSVINPLLALVGL 280
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
363-565 |
7.49e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 363 KPIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELD-MRSVRNYLAVVPQ---TTLLFS- 437
Cdd:PRK10982 261 QPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaNEAINHGFALVTEerrSTGIYAy 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 438 ---------ASIKENIT-YGLKNVSKERLDE--VIEAAQLSSlidqlpDGLDTLVGEhgnkLSGGQKQCISIARALIRQP 505
Cdd:PRK10982 341 ldigfnsliSNIRNYKNkVGLLDNSRMKSDTqwVIDSMRVKT------PGHRTQIGS----LSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 506 KIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHrlSTIKE----ADKIVVIDEGKIVEI 565
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS--SEMPEllgiTDRILVMSNGLVAGI 472
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
373-573 |
8.72e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 8.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 373 VKAGETIAFVGPSGSGKSTLLNLLIGFIQPT---SGKIFLDDQPLDELDMRSVRNYLA--------VVPQTTLLFSASIK 441
Cdd:PLN03140 188 IKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTSAYISqndvhvgvMTVKETLDFSARCQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 442 ENIT-YGLKN--VSKER---------LDEVIEAAQL----SSLIDQLPD---GLD----TLVG-EHGNKLSGGQKQCISI 497
Cdd:PLN03140 268 GVGTrYDLLSelARREKdagifpeaeVDLFMKATAMegvkSSLITDYTLkilGLDickdTIVGdEMIRGISGGQKKRVTT 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 498 ARALIRQPKIILLDEATSALDNQSEKKIQQALNYLTETPTTFIVAHRLSTIKEA----DKIVVIDEGKIVEIGTYEKLLA 573
Cdd:PLN03140 348 GEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETfdlfDDIILLSEGQIVYQGPRDHILE 427
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
452-576 |
1.95e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.04 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 452 SKERLDEVIEAAQLSSLidqlpdgldtlVGEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQQALNY 531
Cdd:NF000106 121 ARARADELLERFSLTEA-----------AGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRS 189
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1158646300 532 LTETPTTFIVAHRLSTIKE--ADKIVVIDEGKIVEIGTYEKLLAQKG 576
Cdd:NF000106 190 MVRDGATVLLTTQYMEEAEqlAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
106-284 |
2.61e-05 |
|
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: 46.41 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 106 LRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAA 185
Cdd:cd18565 89 LRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLII 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 186 FVTLFFRKRIRQSNSDFRQEMEETSAKV------IEVIelapiaRAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGS 259
Cdd:cd18565 169 AGTYWFQRRIEPRYRAVREAVGDLNARLennlsgIAVI------KAFTAEDFERERVADASEEYRDANWRAIRLRAAFFP 242
|
170 180
....*....|....*....|....*
gi 1158646300 260 VSWASFQIFQLICLIFTGILALQGR 284
Cdd:cd18565 243 VIRLVAGAGFVATFVVGGYWVLDGP 267
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
106-308 |
2.70e-05 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 46.43 E-value: 2.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 106 LRATLIKKIQELSIPYQKELQSGRIQSKIiRDVEAI-QTLSSQVFVSGLNIAVnLFVALGITLYKSPVVFMFFLLTVPLA 184
Cdd:cd18782 77 LGGTIIDHLLRLPLGFFDKRPVGELSTRI-SELDTIrGFLTGTALTTLLDVLF-SVIYIAVLFSYSPLLTLVVLATVPLQ 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 185 AFVTLFFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFHLDILQSVFGSVSwAS 264
Cdd:cd18782 155 LLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLS-QF 233
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1158646300 265 FQIFQLICLIFTG-ILALQGRIQPGDVVMyqtyFTTIVNSVSGMI 308
Cdd:cd18782 234 LNKLSSLLVLWVGaYLVLRGELTLGQLIA----FRILSGYVTGPI 274
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
373-405 |
3.23e-05 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 46.47 E-value: 3.23e-05
10 20 30
....*....|....*....|....*....|....
gi 1158646300 373 VKAGETIAFVGPSGSGKSTLLNLLIGF-IQPTSG 405
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVNALLGEeVQKTGA 225
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
49-297 |
3.76e-05 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 45.95 E-value: 3.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 49 PIAIANVINAASSKDSSQLQAIYfnAFLMA---CLIGQNILTN-----YFHVKYHStsIRQVeaGLRAtlIKKIQELSIP 120
Cdd:cd18582 16 PFLLKYAVDALSAPASALLAVPL--LLLLAyglARILSSLFNElrdalFARVSQRA--VRRL--ALRV--FRHLHSLSLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 121 YQKELQSGRIQSKIIRDVEAIQTLSSQVFVSGLNIAVNLFVALGITLYK-SPVVFMFFLLTVPLAAFVTLFF-RKRIRqs 198
Cdd:cd18582 88 FHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILWYLyGWSYALITLVTVALYVAFTIKVtEWRTK-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 199 nsdFRQEM----EETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQiYEKGFhldilQSVFGSVSWASF-Q--IFQL- 270
Cdd:cd18582 166 ---FRREMneadNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALAK-YEKAA-----VKSQTSLALLNIgQalIISLg 236
|
250 260
....*....|....*....|....*....
gi 1158646300 271 --ICLIFTGILALQGRIQPGDVVMYQTYF 297
Cdd:cd18582 237 ltAIMLLAAQGVVAGTLTVGDFVLVNTYL 265
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
383-523 |
4.80e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.48 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 383 GPSGSGKSTLLNLLIGFIQPTSGKIFLDDQPLDELDmrsvRNYLAVV-PQTTLLFSASIKENITYGLKNV-SKERLDEVI 460
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA----KPYCTYIgHNLGLKLEMTVFENLKFWSEIYnSAETLYAAI 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1158646300 461 EAAQLSSLIDqlpdgldtlvgEHGNKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEK 523
Cdd:PRK13541 109 HYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
351-518 |
1.22e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.72 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 351 FEDVSFLYPDSLkpIIDHFSLEVKAGETIAFVGPSGSGKSTLLNLLIGFIQPTSGKIFLDDqpldeldmrSVRnyLAVVP 430
Cdd:PRK11819 327 AENLSKSFGDRL--LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE---------TVK--LAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 431 QttllfsasikenityglknvSKERLD------EVIEaaqlsslidqlpDGLDTL------------VGEHGNK------ 486
Cdd:PRK11819 394 Q--------------------SRDALDpnktvwEEIS------------GGLDIIkvgnreipsrayVGRFNFKggdqqk 441
|
170 180 190
....*....|....*....|....*....|....*.
gi 1158646300 487 ----LSGGQKQCISIARALIRQPKIILLDEATSALD 518
Cdd:PRK11819 442 kvgvLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
485-558 |
1.34e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 1.34e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158646300 485 NKLSGGQKQCISIARALIRQPKIILLDEATSALDNQSEKKIQqalNYLTETPTTFIVahrLSTIKEADKIVVID 558
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLE---TYLLKWPKTFIV---VSHAREFLNTVVTD 410
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
375-398 |
1.43e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 42.91 E-value: 1.43e-04
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
444-571 |
3.63e-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: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 444 ITYGLKNVSkERLD-EVIEAAQLSSLIDQLPDGLDTLV---------GEHGNKLSGGQKQCISIARALIRQ---PKIILL 510
Cdd:TIGR00630 778 VKYKGKNIA-DVLDmTVEEAYEFFEAVPSISRKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKELSKRstgRTLYIL 856
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 511 DEATSALDNQSEKKIQQALNYLTETPTTFIV-AHRLSTIKEADKIvvID--------EGKIVEIGTYEKL 571
Cdd:TIGR00630 857 DEPTTGLHFDDIKKLLEVLQRLVDKGNTVVViEHNLDVIKTADYI--IDlgpeggdgGGTVVASGTPEEV 924
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
463-560 |
4.20e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 463 AQLSSLIDqlpDGLDTL-VGEHGNKLSGGQKQCISIARALIRQPK---IILLDEATSALDNQSEKKIQQALNYL-TETPT 537
Cdd:PRK00635 1678 KPLQALID---NGLGYLpLGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLvSLGHS 1754
|
90 100
....*....|....*....|...
gi 1158646300 538 TFIVAHRLSTIKEADKIVVIDEG 560
Cdd:PRK00635 1755 VIYIDHDPALLKQADYLIEMGPG 1777
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
67-218 |
5.34e-04 |
|
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: 42.08 E-value: 5.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 67 LQAIYFNAFLMACLIGQNILTNYFhvkyhstSIRQ---VEAG----LRATLIKKIQELSIPYQKELQSGRIQSKIIRDVE 139
Cdd:cd18540 38 LDGLTGFILLYLGLILIQALSVFL-------FIRLagkIEMGvsydLRKKAFEHLQTLSFSYFDKTPVGWIMARVTSDTQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 140 AIQTLSSQVFVSGLNIAVNLFVALGITLYKSPVVFMFFLLTVPLAAFVTLFFRKRI-------RQSNSDFRQEMEE--TS 210
Cdd:cd18540 111 RLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKKIlkayrkvRKINSRITGAFNEgiTG 190
|
170
....*....|
gi 1158646300 211 AKVIE--VIE 218
Cdd:cd18540 191 AKTTKtlVRE 200
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
467-534 |
5.53e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 39.14 E-value: 5.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 467 SLIDQLPDGLDTLVGEHGNKLSGGQKQ---CISIARALIRQ----------PKIILLDEATSALDnqsEKKIQQALNYLT 533
Cdd:pfam13558 13 EVEVRDEDGSEVETYRRSGGLSGGEKQllaYLPLAAALAAQygsaegrppaPRLVFLDEAFAKLD---EENIRTALELLR 89
|
.
gi 1158646300 534 E 534
Cdd:pfam13558 90 A 90
|
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
373-403 |
7.17e-04 |
|
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.
Pssm-ID: 410874 [Multi-domain] Cd Length: 177 Bit Score: 40.60 E-value: 7.17e-04
10 20 30
....*....|....*....|....*....|.
gi 1158646300 373 VKAGETIAFVGPSGSGKSTLLNLLIGFIQPT 403
Cdd:cd01130 9 VRARKNILISGGTGSGKTTLLNALLSFIPPD 39
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
95-320 |
8.86e-04 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 41.69 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 95 HSTSIRQV-EAGLRatlikkiQELSIPYQKelQSGRIQSKIIRDVEAI-QTLSSQVFVSGLNIAVNLFVaLGITLYKSPV 172
Cdd:cd18589 68 HSRLQGLVfAAVLR-------QEIAFFDSN--QTGDIVSRVTTDTEDMsESLSENLSLLMWYLARGLFL-FIFMLWLSPK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 173 VFMFFLLTVPLAAFVTLFFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYekgfHLDI 252
Cdd:cd18589 138 LALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTY----RLNK 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 253 LQSVFGSVS-WA---SFQIFQLICLIFTGILALQGRIQPGDVV---MYQTYFTTIVNSVsgmITLIPTISKGMES 320
Cdd:cd18589 214 KEAAAYAVSmWTssfSGLALKVGILYYGGQLVTAGTVSSGDLVtfvLYELQFTSAVEVL---LSYYPSVMKAVGS 285
|
|
| CpaF |
COG4962 |
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and ... |
373-403 |
9.68e-04 |
|
Pilus assembly protein, ATPase of CpaF family [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 443988 [Multi-domain] Cd Length: 386 Bit Score: 41.69 E-value: 9.68e-04
10 20 30
....*....|....*....|....*....|.
gi 1158646300 373 VKAGETIAFVGPSGSGKSTLLNLLIGFIQPT 403
Cdd:COG4962 179 VRARLNILVSGGTGSGKTTLLNALSGFIPPD 209
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
360-398 |
1.12e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 41.34 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1158646300 360 DSLKPIIdhfslevkAGETIAFVGPSGSGKSTLLNLLIG 398
Cdd:PRK00098 156 DELKPLL--------AGKVTVLAGQSGVGKSTLLNALAP 186
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
47-318 |
1.79e-03 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 40.67 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 47 LMPIAIANVINAASSKDSSQLQAIYFNAFLMA--CLIGQNI--LTNYFHVKYHSTSIRQveagLRATLIKKIQELSIPYQ 122
Cdd:cd18560 14 LAPLFLGRAVNALTLAKVKDLESAVTLILLYAllRFSSKLLkeLRSLLYRRVQQNAYRE----LSLKTFAHLHSLSLDWH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 123 KELQSGRIQSKIIRDVEAIQTLSSQVFvsgLNIAVNLFVALGITLykspVVFMFFLLTVPLAAFVTLF----FRKRIRQS 198
Cdd:cd18560 90 LSKKTGEVVRIMDRGTESANTLLSYLV---FYLVPTLLELIVVSV----VFAFHFGAWLALIVFLSVLlygvFTIKVTEW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 199 NSDFRQEM----EETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYEKGFhldILQSVFGSVSWASFQIFQL---I 271
Cdd:cd18560 163 RTKFRRAAnkkdNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSV---KVQASLSLLNVGQQLIIQLgltL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1158646300 272 CLIFTGILALQGRIQPGDVVMYQTYFTTIVNSVSGMITLIPTISKGM 318
Cdd:cd18560 240 GLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| MMR_HSR1 |
pfam01926 |
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ... |
378-404 |
2.90e-03 |
|
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.
Pssm-ID: 460387 [Multi-domain] Cd Length: 113 Bit Score: 37.60 E-value: 2.90e-03
10 20
....*....|....*....|....*..
gi 1158646300 378 TIAFVGPSGSGKSTLLNLLIGFIQPTS 404
Cdd:pfam01926 1 RVALVGRPNVGKSTLINALTGAKAIVS 27
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
366-559 |
3.61e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 39.99 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 366 IDHFSLEVKAGETIaFVGPSGSGKSTLLNLLIGFIQPTSGKiflddqPLDELDMRSVRNYLAVVPQTTLLFSASIKENIT 445
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSR------KFDEEDFYLGDDPDLPEIEIELTFGSLLSRLLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 446 YGLKNVSKERLDEVIEaaQLSSLIDQLPDGLDTLVGEHGNKLSGGQKQCISIA----RALIRQPKIILLDEATSALDNQS 521
Cdd:COG3593 87 LLLKEEDKEELEEALE--ELNEELKEALKALNELLSEYLKELLDGLDLELELSldelEDLLKSLSLRIEDGKELPLDRLG 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1158646300 522 eKKIQQALnyltetptTFIVAHRLSTIK--EADKIVVIDE 559
Cdd:COG3593 165 -SGFQRLI--------LLALLSALAELKraPANPILLIEE 195
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
95-245 |
4.69e-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: 39.19 E-value: 4.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158646300 95 HSTSIRqVEAGLRATLIKKIQELSIPYQKELQSGRIQSKIIRDVEAIQTLSS----QVFVSGLniavnlfVALGITLYKS 170
Cdd:cd18561 61 HRAAQR-VKQHLRRRLFAKLLKLGPGYLEGERTGELQTTVVDGVEALEAYYGrylpQLLVALL-------GPLLILIYLF 132
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158646300 171 ---PVVFMFFLLTVPLAAFVTLFFRKRIRQSNSDFRQEMEETSAKVIEVIELAPIARAHGLEKHETTRLNKHFTQIYE 245
Cdd:cd18561 133 fldPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGRLSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQ 210
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
486-555 |
7.79e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 37.34 E-value: 7.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1158646300 486 KLSGGQKQCISIARALIRQPK----IILLDEATSALDNQSEKKIQQALN-YLTETPTTFIVAHRLSTIKEADKIV 555
Cdd:cd03227 77 QLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILeHLVKGAQVIVITHLPELAELADKLI 151
|
|
| |
