|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-555 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 591.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIYTNPTVDYsdnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQE 80
Cdd:COG1132 32 LSALLELLLPLLLGRIIDALLAGGDLSA---LLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADLRRDLFEHLLRLP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 81 VAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKL 160
Cdd:COG1132 109 LSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRRLRKL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 161 TKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGL 240
Cdd:COG1132 189 FRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 241 LMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPFNEGVIlNEKSFQGALEFKNVHF 320
Cdd:COG1132 269 LVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAV-PLPPVRGEIEFENVSF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 321 AYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPIL 400
Cdd:COG1132 348 SYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFL 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 401 FSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDE 480
Cdd:COG1132 426 FSGTIRENIRYGRPD---ATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDE 502
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 481 ATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMNKQS 555
Cdd:COG1132 503 ATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRLQF 576
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1-550 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 535.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIYTNPTVD-YSDNLTRLCLGLSAVFLCGAAANAIRVYLMQtsgqRIVNRLRTSLFSSILRQ 79
Cdd:TIGR00958 172 LSSLGEMFIPFYTGRVIDTLGGDKGPPaLASAIFFMCLLSIASSVSAGLRGGSFNYTMA----RINLRIREDLFRSLLRQ 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 80 EVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRK 159
Cdd:TIGR00958 248 DLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGKRYQL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 160 LTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGG 239
Cdd:TIGR00958 328 LSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYYGG 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 240 LLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPFNegVILNEKSFQGALEFKNVH 319
Cdd:TIGR00958 408 QLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLT--GTLAPLNLEGLIEFQDVS 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 320 FAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPI 399
Cdd:TIGR00958 486 FSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPV 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 400 LFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLD 479
Cdd:TIGR00958 566 LFSGSVRENIAYGLTD---TPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILD 642
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912302 480 EATSALDAENEYLVQEalDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPnGIYRKL 550
Cdd:TIGR00958 643 EATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQ-GCYKHL 710
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
2-554 |
3.15e-169 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 491.91 E-value: 3.15e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVIYTNptvDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEV 81
Cdd:TIGR02204 30 TAAATLSLPYAVRLMIDHGFSK---DSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADIRRAVFAHLISLSP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 82 AFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLT 161
Cdd:TIGR02204 107 SFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLLPILLFGRRVRKLS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 162 KVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGffgatgLSGNLIVLS------VL 235
Cdd:TIGR02204 187 RESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRTRAL------LTAIVIVLVfgaivgVL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 236 YKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPFNEGVILNEKSFQGALEF 315
Cdd:TIGR02204 261 WVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEF 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 316 KNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVS 395
Cdd:TIGR02204 341 EQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVP 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 396 QEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKI 475
Cdd:TIGR02204 421 QDPVLFAASVMENIRYGRPD---ATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPI 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 476 LLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMNKQ 554
Cdd:TIGR02204 498 LLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAK-GGLYARLARLQ 575
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-554 |
2.08e-154 |
|
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: 458.91 E-value: 2.08e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIID-VIYTNptvdYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQ 79
Cdd:COG2274 167 LINLLALATPLFTQVVIDrVLPNQ----DLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLSSRFFRHLLRL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 80 EVAFFDKTRTGELINRLSsDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRK 159
Cdd:COG2274 243 PLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLLGLLFQPRLRR 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 160 LTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGG 239
Cdd:COG2274 322 LSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQLATVALLWLGA 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 240 LLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPFNEGVILNEKsFQGALEFKNVH 319
Cdd:COG2274 402 YLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPR-LKGDIELENVS 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 320 FAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPI 399
Cdd:COG2274 481 FRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVF 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 400 LFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLD 479
Cdd:COG2274 560 LFSGTIRENITLGDPD---ATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILD 636
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 480 EATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMNKQ 554
Cdd:COG2274 637 EATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLAR-KGLYAELVQQQ 710
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
2-286 |
1.29e-153 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 441.57 E-value: 1.29e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVIYTN--PTVDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQ 79
Cdd:cd18573 8 SSAVTMSVPFAIGKLIDVASKEsgDIEIFGLSLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 80 EVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRK 159
Cdd:cd18573 88 DAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 160 LTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGG 239
Cdd:cd18573 168 LSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767912302 240 LLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 286
Cdd:cd18573 248 SLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
314-554 |
3.15e-143 |
|
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: 412.70 E-value: 3.15e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 314 EFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 393
Cdd:cd03249 2 EFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 394 VSQEPILFSCSIAENIAYGADDPssvTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNP 473
Cdd:cd03249 82 VSQEPVLFDGTIAENIRYGKPDA---TDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 474 KILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMNK 553
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQ-KGVYAKLVKA 237
|
.
gi 767912302 554 Q 554
Cdd:cd03249 238 Q 238
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
32-554 |
1.13e-132 |
|
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: 398.32 E-value: 1.13e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 32 LTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENL 111
Cdd:TIGR02203 53 LWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 112 SDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKE 191
Cdd:TIGR02203 133 IVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 192 MTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSS 271
Cdd:TIGR02203 213 AYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTN 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 272 FYSELMKGLGAGGRLWELLEREPKLpfNEGVILNEKSfQGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSG 351
Cdd:TIGR02203 293 VNAPMQRGLAAAESLFTLLDSPPEK--DTGTRAIERA-RGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSG 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 352 SGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGAddPSSVTAEEIQRVAEVA 431
Cdd:TIGR02203 369 SGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR--TEQADRAEIERALAAA 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 432 NAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAH 511
Cdd:TIGR02203 447 YAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAH 526
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 767912302 512 RLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMNKQ 554
Cdd:TIGR02203 527 RLSTIEKADRIVVMDDGRIVERGTHNELLAR-NGLYAQLHNMQ 568
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
313-550 |
1.06e-115 |
|
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: 342.29 E-value: 1.06e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 392
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKN 472
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRPG---ATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912302 473 PKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKL 550
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKL 233
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
60-554 |
1.58e-115 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 354.71 E-value: 1.58e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 60 SGqRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFV 139
Cdd:PRK11176 93 SG-KVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSLIL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 140 LSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGF 219
Cdd:PRK11176 172 IVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSIS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 220 FGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLpfN 299
Cdd:PRK11176 252 DPIIQLIASLALAFVLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTLFAILDLEQEK--D 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 300 EGVILNEKSfQGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI 379
Cdd:PRK11176 330 EGKRVIERA-KGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 380 RQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSvtAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQ 459
Cdd:PRK11176 408 RDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYS--REQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQ 485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 460 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEEL 539
Cdd:PRK11176 486 RQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAEL 565
|
490
....*....|....*
gi 767912302 540 LSKpNGIYRKLMNKQ 554
Cdd:PRK11176 566 LAQ-NGVYAQLHKMQ 579
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
1-286 |
3.82e-112 |
|
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: 335.30 E-value: 3.82e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIYTNptvDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQE 80
Cdd:cd18557 7 ISSAAQLLLPYLIGRLIDTIIKG---GDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 81 VAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKL 160
Cdd:cd18557 84 IAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 161 TKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGL 240
Cdd:cd18557 164 SKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGY 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767912302 241 LMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 286
Cdd:cd18557 244 LVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
313-554 |
1.08e-107 |
|
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: 321.87 E-value: 1.08e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 392
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKN 472
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD---ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 473 PKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMN 552
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAK-GGLYAEMWK 234
|
..
gi 767912302 553 KQ 554
Cdd:cd03253 235 AQ 236
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
181-555 |
3.88e-107 |
|
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: 333.33 E-value: 3.88e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 181 NVRTVRAFGKEMTEIEKYASkvdhvmQLARKEAFARAGFfgaTGLSGNLIVLSVLYKGGL--LMGSA-------HMTVGE 251
Cdd:COG5265 227 NYETVKYFGNEAREARRYDE------ALARYERAAVKSQ---TSLALLNFGQALIIALGLtaMMLMAaqgvvagTMTVGD 297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 252 L---SSFLMYAFwvgISIGGLSSFYSELMKGLGAGGRLWELLEREPK---------LPFNegvilneksfQGALEFKNVH 319
Cdd:COG5265 298 FvlvNAYLIQLY---IPLNFLGFVYREIRQALADMERMFDLLDQPPEvadapdappLVVG----------GGEVRFENVS 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 320 FAYpaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPI 399
Cdd:COG5265 365 FGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTV 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 400 LFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLD 479
Cdd:COG5265 443 LFNDTIAYNIAYGRPD---ASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFD 519
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 480 EATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMNKQS 555
Cdd:COG5265 520 EATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQ-GGLYAQMWARQQ 594
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
30-542 |
2.37e-104 |
|
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: 324.79 E-value: 2.37e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 30 DNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELInrlssdtALLGRSVtE 109
Cdd:COG4988 55 SALLPLLGLLLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLLEKLLALGPAWLRGKSTGELA-------TLLTEGV-E 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 110 NLsDGLRAG----AQASVGISMM-----FFVSPNLATFVLSVVP--PVSIIAViyGRYLRKLTkvtQDSLAQATQLAE-- 176
Cdd:COG4988 127 AL-DGYFARylpqLFLAALVPLLilvavFPLDWLSGLILLVTAPliPLFMILV--GKGAAKAS---RRQWRALARLSGhf 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 177 -ERIGNVRTVRAFGKEmteiEKYASKVDHVMQLARKE-------AFARAG---FFGAtgLSgnlIVLSVLYkGGLLMGSA 245
Cdd:COG4988 201 lDRLRGLTTLKLFGRA----KAEAERIAEASEDFRKRtmkvlrvAFLSSAvleFFAS--LS---IALVAVY-IGFRLLGG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 246 HMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPFNEGVILNEKSfQGALEFKNVHFAYPAR 325
Cdd:COG4988 271 SLTLFAALFVLLLAPEFFLPLRDLGSFYHARANGIAAAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGG 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 326 PevPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSI 405
Cdd:COG4988 350 R--PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTI 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 406 AENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSAL 485
Cdd:COG4988 428 RENLRLGRPD---ASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHL 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 486 DAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSK 542
Cdd:COG4988 505 DAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
63-552 |
1.05e-102 |
|
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: 320.95 E-value: 1.05e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 63 RIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLA-TFVLS 141
Cdd:COG4987 85 RLLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALAlVLALG 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 142 VVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFG 221
Cdd:COG4987 165 LLLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 222 ATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPFNEG 301
Cdd:COG4987 245 LLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAE 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 302 VILNEKsfQGALEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQ 381
Cdd:COG4987 325 PAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 382 LNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQ 461
Cdd:COG4987 402 LDEDDLRRRIAVVPQRPHLFDTTLRENLRLARPD---ATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERR 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 462 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLS 541
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA 558
|
490
....*....|.
gi 767912302 542 KpNGIYRKLMN 552
Cdd:COG4987 559 Q-NGRYRQLYQ 568
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
2-285 |
2.45e-102 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 310.72 E-value: 2.45e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVIYTNPTVDYSD---NLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILR 78
Cdd:cd18780 8 SSGTNLALPYFFGQVIDAVTNHSGSGGEEalrALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 79 QEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLR 158
Cdd:cd18780 88 QEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 159 KLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKG 238
Cdd:cd18780 168 KLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767912302 239 GLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGR 285
Cdd:cd18780 248 GRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVR 294
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
311-542 |
5.48e-101 |
|
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: 304.53 E-value: 5.48e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 311 GALEFKNVHFAYpaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSK 390
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEPILFSCSIAENIAYGADDPssvTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALL 470
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNA---TDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912302 471 KNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSK 542
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
4-555 |
3.37e-100 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 318.23 E-value: 3.37e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 4 VISMSAPFFLGKIIDVIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAF 83
Cdd:TIGR01846 153 LFALVTPLLFQVVIDKVLVHRGLS---TLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGY 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 84 FDKTRTGELINRLSSdtallgrsvTENLSDGLRAGAQAS--------VGISMMFFVSPNLATFVLSVVPPVSIIAVIYGR 155
Cdd:TIGR01846 230 FESRRVGDTVARVRE---------LEQIRNFLTGSALTVvldllfvvVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGP 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 156 YLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVdhVMQLARKEAFARAGFFG--ATGLSGNLIVLS 233
Cdd:TIGR01846 301 ILRKRVEDKFERSAAATSFLVESVTGIETIKATATEPQFQNRWDRQL--AAYVAASFRVTNLGNIAgqAIELIQKLTFAI 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 234 VLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLErEPKLPFNEGVILNEKsFQGAL 313
Cdd:TIGR01846 379 LLWFGAHLVIGGALSPGQLVAFNMLAGRVTQPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPRSAGLAALPE-LRGAI 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 314 EFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 392
Cdd:TIGR01846 457 TFENIRFRY--APDSPeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFSCSIAENIAYGadDPSsVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKN 472
Cdd:TIGR01846 535 VVLQENVLFSRSIRDNIALC--NPG-APFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGN 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 473 PKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLMN 552
Cdd:TIGR01846 612 PRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLAL-QGLYARLWQ 690
|
...
gi 767912302 553 KQS 555
Cdd:TIGR01846 691 QQS 693
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
313-529 |
6.84e-89 |
|
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: 271.18 E-value: 6.84e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 392
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFSCSIAENIaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARALLKN 472
Cdd:cd03228 80 YVPQDPFLFSGTIRENI---------------------------------------------LSGGQRQRIAIARALLRD 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 473 PKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGK 529
Cdd:cd03228 115 PPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
304-530 |
5.78e-88 |
|
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: 270.88 E-value: 5.78e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 304 LNEKSFQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLN 383
Cdd:cd03248 3 LAPDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 384 PVWLRSKIGTVSQEPILFSCSIAENIAYGAddpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRI 463
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFARSLQDNIAYGL---QSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 464 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKI 530
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
4-557 |
1.48e-87 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 281.85 E-value: 1.48e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 4 VISMSAPFFLGKIIDVIYTNPTVdysdnltrlcLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLR----TSLFSSILRQ 79
Cdd:PRK13657 33 AATFAEPILFGRIIDAISGKGDI----------FPLLAAWAGFGLFNIIAGVLVARHADRLAHRRRlavlTEYFERIIQL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 80 EVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATfVLSVVppvSIIAVIYGRYLRK 159
Cdd:PRK13657 103 PLAWHSQRGSGRALHTLLRGTDALFGLWLEFMREHLATLVALVVLLPLALFMNWRLSL-VLVVL---GIVYTLITTLVMR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 160 LTKVTQDSL-AQATQLAE---ERIGNVRTVRAFGKEMTEIEKYASKVDHVM--QLARKEAFARAGffGATGLSGNLIVLS 233
Cdd:PRK13657 179 KTKDGQAAVeEHYHDLFAhvsDAIGNVSVVQSYNRIEAETQALRDIADNLLaaQMPVLSWWALAS--VLNRAASTITMLA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 234 VLYKGGLLMGSAHMTVGELSSFLMYAfwvGISIGGL---SSFYSELMKglgAGGRLWELLEREPKLPFNE---GVIlNEK 307
Cdd:PRK13657 257 ILVLGAALVQKGQLRVGEVVAFVGFA---TLLIGRLdqvVAFINQVFM---AAPKLEEFFEVEDAVPDVRdppGAI-DLG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 308 SFQGALEFKNVHFAYPARPevPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL 387
Cdd:PRK13657 330 RVKGAVEFDDVSFSYDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 388 RSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIAR 467
Cdd:PRK13657 408 RRNIAVVFQDAGLFNRSIEDNIRVGRPD---ATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIAR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 468 ALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIY 547
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVAR-GGRF 563
|
570
....*....|
gi 767912302 548 RKLMNKQSFI 557
Cdd:PRK13657 564 AALLRAQGML 573
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
313-554 |
1.14e-86 |
|
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: 268.20 E-value: 1.14e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKI 391
Cdd:cd03252 1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEPILFSCSIAENIAYGADDPSsvtAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLK 471
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGMS---MERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 472 NPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIYRKLM 551
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLY 234
|
...
gi 767912302 552 NKQ 554
Cdd:cd03252 235 QLQ 237
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
53-554 |
1.23e-80 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 263.50 E-value: 1.23e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 53 RVYLMQTSGQRIVnRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALL----GRSVTeNLSDGLRAGAqaSVGISMM 128
Cdd:PRK10789 57 RVLLFGASYQLAV-ELREDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVvfaaGEGVL-TLVDSLVMGC--AVLIVMS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 129 FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHV--- 205
Cdd:PRK10789 133 TQISWQLTLLALLPMPVMAIMIKRYGDQLHERFKLAQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTgkk 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 206 -MQLARKEAFARAGFFGATGLSgNLIVLSvlykGGLLM---GSahMTVGELSSFLMYafwVGISIG---GLSSFYSELMK 278
Cdd:PRK10789 213 nMRVARIDARFDPTIYIAIGMA-NLLAIG----GGSWMvvnGS--LTLGQLTSFVMY---LGLMIWpmlALAWMFNIVER 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 279 GLGAGGRLWELLEREPKLPFNEGVILNEKsfqGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVL 358
Cdd:PRK10789 283 GSAAYSRIRAMLAEAPVVKDGSEPVPEGR---GELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 359 SLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIR 438
Cdd:PRK10789 359 SLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPD---ATQQEIEHVARLASVHDDIL 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 439 NFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKN 518
Cdd:PRK10789 436 RLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTE 515
|
490 500 510
....*....|....*....|....*....|....*.
gi 767912302 519 ANMVAVLDQGKITEYGKHEELLSKPnGIYRKLMNKQ 554
Cdd:PRK10789 516 ASEILVMQHGHIAQRGNHDQLAQQS-GWYRDMYRYQ 550
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
2-283 |
2.74e-77 |
|
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: 245.53 E-value: 2.74e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVIYTNPTvdySDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEV 81
Cdd:cd18572 8 AALSELAIPHYTGAVIDAVVADGS---REAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 82 AFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLT 161
Cdd:cd18572 85 AFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 162 KVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLL 241
Cdd:cd18572 165 KEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767912302 242 MGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAG 283
Cdd:cd18572 245 VLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAA 286
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
2-286 |
6.65e-75 |
|
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: 239.31 E-value: 6.65e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEV 81
Cdd:cd18576 8 SSAIGLVFPLLAGQLIDAALGGGDTA---SLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 82 AFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLT 161
Cdd:cd18576 85 SFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 162 KVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLL 241
Cdd:cd18576 165 KKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767912302 242 MGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 286
Cdd:cd18576 245 VLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
311-530 |
1.42e-74 |
|
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: 235.95 E-value: 1.42e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 311 GALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSK 390
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEPILFSCSIAENIAYGAddpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALL 470
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGA---PLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 471 KNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKI 530
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
64-542 |
3.37e-74 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 246.94 E-value: 3.37e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 64 IVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVV 143
Cdd:PRK10790 96 VVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMALVAIMIF 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 144 PPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNV------RTVRAFGKEMTEiekyASKvDHVMqlARKEAFARA 217
Cdd:PRK10790 176 PAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMsviqqfRQQARFGERMGE----ASR-SHYM--ARMQTLRLD 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 218 GFFgatgLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFwvgISIGG--------LSSFYSELMKGLGAGGRLWEL 289
Cdd:PRK10790 249 GFL----LRPLLSLFSALILCGLLMLFGFSASGTIEVGVLYAF---ISYLGrlneplieLTTQQSMLQQAVVAGERVFEL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 290 LERePKLPFNEGVILNEksfQGALEFKNVHFAYpaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPAS 369
Cdd:PRK10790 322 MDG-PRQQYGNDDRPLQ---SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTE 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 370 GTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADdpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVG 449
Cdd:PRK10790 396 GEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD----ISEEQVWQALETVQLAELARSLPDGLYTPLG 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 450 EKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGK 529
Cdd:PRK10790 472 EQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQ 551
|
490
....*....|...
gi 767912302 530 ITEYGKHEELLSK 542
Cdd:PRK10790 552 AVEQGTHQQLLAA 564
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
32-550 |
2.00e-73 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 247.55 E-value: 2.00e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 32 LTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSsdtalLGRSVTENL 111
Cdd:TIGR03796 193 LRPLLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLWHILRLPVRFFAQRHAGDIASRVQ-----LNDQVAEFL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 112 SDGLRAGAQASVGI----SMMFFVSPNLATFVLSVVPpVSIIAVIYGRYLRKLT--KVTQDSlAQATQLAEERIGNVRTV 185
Cdd:TIGR03796 268 SGQLATTALDAVMLvfyaLLMLLYDPVLTLIGIAFAA-INVLALQLVSRRRVDAnrRLQQDA-GKLTGVAISGLQSIETL 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 186 RAFGKEMTEIEK----YASKVDHVMQLARKEAFARAGFFGATGLSgNLIVLSVlykGGLLMGSAHMTVGELSSFLmyafw 261
Cdd:TIGR03796 346 KASGLESDFFSRwagyQAKLLNAQQELGVLTQILGVLPTLLTSLN-SALILVV---GGLRVMEGQLTIGMLVAFQ----- 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 262 vgiSIggLSSFYSELMKGLGAGGRLWEL---LER---------EPKLPFNEGVILNEKS---FQGALEFKNVHFAYpARP 326
Cdd:TIGR03796 417 ---SL--MSSFLEPVNNLVGFGGTLQELegdLNRlddvlrnpvDPLLEEPEGSAATSEPprrLSGYVELRNITFGY-SPL 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 327 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIA 406
Cdd:TIGR03796 491 EPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVR 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 407 ENIAYGadDPSsVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALD 486
Cdd:TIGR03796 571 DNLTLW--DPT-IPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALD 647
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912302 487 AENEYLVQEALDRlmDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPnGIYRKL 550
Cdd:TIGR03796 648 PETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVG-GAYARL 708
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
3-554 |
4.90e-73 |
|
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: 246.02 E-value: 4.90e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 3 SVISMSAPFFLGKIID-VIytnPTVDySDNLTRLCLGLSAVFLCGAA---ANAIRVYLMQTsgqRIVNRLRTSLFSSILR 78
Cdd:TIGR03797 149 TLLGMLVPIATGILIGtAI---PDAD-RSLLVQIALALLAAAVGAAAfqlAQSLAVLRLET---RMDASLQAAVWDRLLR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 79 QEVAFFDKTRTGELINRLSSDTA----LLGRSVTENLSdglraGAQASVGISMMFFVSPNLATF-VLSVVPPVSIIAVIY 153
Cdd:TIGR03797 222 LPVSFFRQYSTGDLASRAMGISQirriLSGSTLTTLLS-----GIFALLNLGLMFYYSWKLALVaVALALVAIAVTLVLG 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 154 GRYLRKLTKVTQDSLAQATQLAE--ERIGNVRT----VRAFGKEMteiEKYASKVDHVMqlarkeAFARAGFFGATGLSG 227
Cdd:TIGR03797 297 LLQVRKERRLLELSGKISGLTVQliNGISKLRVagaeNRAFARWA---KLFSRQRKLEL------SAQRIENLLTVFNAV 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 228 NLIVLSVL--YKGGLLMGSAHMTVGELSSFlMYAFwvGISIGGLSSFYSELMKGLGAGgRLWE----LLEREPKlpfNEG 301
Cdd:TIGR03797 368 LPVLTSAAlfAAAISLLGGAGLSLGSFLAF-NTAF--GSFSGAVTQLSNTLISILAVI-PLWErakpILEALPE---VDE 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 302 VILNEKSFQGALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR 380
Cdd:TIGR03797 441 AKTDPGKLSGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLA 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 381 QLNPVWLRSKIGTVSQEPILFSCSIAENIAYGAddpsSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQK 460
Cdd:TIGR03797 519 GLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGA----PLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQR 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 461 QRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLmdGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELL 540
Cdd:TIGR03797 595 QRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELM 672
|
570
....*....|....
gi 767912302 541 SKPnGIYRKLMNKQ 554
Cdd:TIGR03797 673 ARE-GLFAQLARRQ 685
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-552 |
1.05e-72 |
|
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: 245.80 E-value: 1.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 4 VISMSAPFFLGKIIDVIYTNptvDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAF 83
Cdd:TIGR01193 170 LISIAGSYYLQKIIDTYIPH---KMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSF 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 84 FDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGIsmmFFVSPNLATFVLSVVP-PVSIIAVIYgrYLRKLTK 162
Cdd:TIGR01193 247 FSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWILVIVGL---FLVRQNMLLFLLSLLSiPVYAVIIIL--FKRTFNK 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 163 VTQDSLAQATQLAE---ERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGG 239
Cdd:TIGR01193 322 LNHDAMQANAVLNSsiiEDLNGIETIKSLTSEAERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGA 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 240 LLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWE--LLEREpklpFNEGVILNEKS-FQGALEFK 316
Cdd:TIGR01193 402 YLVMRGKLTLGQLITFNALLSYFLTPLENIINLQPKLQAARVANNRLNEvyLVDSE----FINKKKRTELNnLNGDIVIN 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 317 NVHFAYPARPevPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQ 396
Cdd:TIGR01193 478 DVSYSYGYGS--NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQ 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 397 EPILFSCSIAENIAYGADDpsSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKIL 476
Cdd:TIGR01193 556 EPYIFSGSILENLLLGAKE--NVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVL 633
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 477 LLDEATSALDAENEYLVQEALDRLMDgRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLsKPNGIYRKLMN 552
Cdd:TIGR01193 634 ILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELL-DRNGFYASLIH 707
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
32-525 |
3.51e-72 |
|
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: 239.88 E-value: 3.51e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 32 LTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELinrlssdTALLGRSVtENL 111
Cdd:TIGR02857 43 LLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLEAVAALGPRWLQGRPSGEL-------ATLALEGV-EAL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 112 sDGLRAGAQASVGISMM---------FFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNV 182
Cdd:TIGR02857 115 -DGYFARYLPQLVLAVIvplailaavFPQDWISGLILLLTAPLIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 183 RTVRAFGKEMTEI-------EKYASKVDHVMQLARKEAFARAgFFGAtgLSGNLIVLSVlykgGLLMGSAHMTvgelssf 255
Cdd:TIGR02857 194 PTLKLFGRAKAQAaairrssEEYRERTMRVLRIAFLSSAVLE-LFAT--LSVALVAVYI----GFRLLAGDLD------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 256 LMYAFWVGI-------SIGGLSSFYSELMKGLGAGGRLWELLEREPkLPFNEGVILNEKSFQgALEFKNVHFAYPARPEV 328
Cdd:TIGR02857 260 LATGLFVLLlapefylPLRQLGAQYHARADGVAAAEALFAVLDAAP-RPLAGKAPVTAAPAS-SLEFSGVSVAYPGRRPA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 329 PifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAEN 408
Cdd:TIGR02857 338 L--RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAEN 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 409 IAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 488
Cdd:TIGR02857 416 IRLARPD---ASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
490 500 510
....*....|....*....|....*....|....*..
gi 767912302 489 NEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVL 525
Cdd:TIGR02857 493 TEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
311-534 |
2.89e-67 |
|
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: 216.98 E-value: 2.89e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 311 GALEFKNVHFAYpaRPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS 389
Cdd:cd03244 1 GDIEFKNVSLRY--RPNlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 KIGTVSQEPILFSCSIAENIaygadDP-SSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARA 468
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL-----DPfGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 469 LLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYG 534
Cdd:cd03244 154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
128-542 |
1.58e-66 |
|
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: 225.78 E-value: 1.58e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 128 MFFVSPNLATFVL--SVVppVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGkeMTE--IEKYASKVD 203
Cdd:COG4618 150 LFLFHPLLGLLALvgALV--LVALALLNERLTRKPLKEANEAAIRANAFAEAALRNAEVIEAMG--MLPalRRRWQRANA 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 204 HVMQLARKeAFARAGFFGATGLSGNLIVLS-VLYKGGLLMGSAHMTVGEL--SSFLMyafwvG-------ISIGGLSSFy 273
Cdd:COG4618 226 RALALQAR-ASDRAGGFSALSKFLRLLLQSaVLGLGAYLVIQGEITPGAMiaASILM-----GralapieQAIGGWKQF- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 274 selMKGLGAGGRLWELLEREPKLPfnEGVILNEksFQGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSG 353
Cdd:COG4618 299 ---VSARQAYRRLNELLAAVPAEP--ERMPLPR--PKGRLSVENLTVVPPGS-KRPILRGVSFSLEPGEVLGVIGPSGSG 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 354 KSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIA-YGADDPssvtaEEIQRVAEVAN 432
Cdd:COG4618 371 KSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIArFGDADP-----EKVVAAAKLAG 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 433 AVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAH 511
Cdd:COG4618 446 VHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITH 525
|
410 420 430
....*....|....*....|....*....|.
gi 767912302 512 RLSTIKNANMVAVLDQGKITEYGKHEELLSK 542
Cdd:COG4618 526 RPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
3-551 |
1.04e-65 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 224.38 E-value: 1.04e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 3 SVISMSAPFFLGKIIDVIytnptVDYSDNLTRLclglsAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSL----FSSILR 78
Cdd:TIGR01192 32 AAITIAEPILFGRIIDAI-----SSKSDVLPTL-----ALWAGFGVFNTIAYVLVAREADRLAHGRRATLlteaFGRIIS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 79 QEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLaTFVLSVVppvSIIAVIYGRYLR 158
Cdd:TIGR01192 102 MPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRL-SIVLMVL---GILYILIAKLVM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 159 KLTKVTQDSLAQATQL----AEERIGNVRTVRAFGK---EMTEIEKYASKVDHVmQLARKEAFARAGffGATGLSGNLIV 231
Cdd:TIGR01192 178 QRTKNGQAAVEHHYHNvfkhVSDSISNVSVVHSYNRieaETSALKQFTNNLLSA-QYPVLDWWALAS--GLNRMASTISM 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 232 LSVLYKGGLLMGSAHMTVGELSSFLMYAfwvGISIGGLSSFYSELMKGLGAGGRLWELLEREPKL-----PFNEGVILNE 306
Cdd:TIGR01192 255 MCILVIGTVLVIKGELSVGEVIAFIGFA---NLLIGRLDQMSGFITQIFEARAKLEDFFDLEDSVfqreePADAPELPNV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 307 KsfqGALEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVW 386
Cdd:TIGR01192 332 K---GAVEFRHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRES 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 387 LRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIA 466
Cdd:TIGR01192 407 LRKSIATVFQDAGLFNRSIRENIRLGREG---ATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIA 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 467 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGI 546
Cdd:TIGR01192 484 RAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQK-DGR 562
|
....*
gi 767912302 547 YRKLM 551
Cdd:TIGR01192 563 FYKLL 567
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
49-549 |
1.43e-64 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 229.15 E-value: 1.43e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 49 ANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRT--GELINRLSSDTALLGRSVTENLSdglragaqASVGIS 126
Cdd:PTZ00265 882 SETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHapGLLSAHINRDVHLLKTGLVNNIV--------IFTHFI 953
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 127 MMFFVSPNLATFVLSVVppVSIIAVIYGRYLR------KLTK--------VTQDSLAQA-----------TQLAEERIGN 181
Cdd:PTZ00265 954 VLFLVSMVMSFYFCPIV--AAVLTGTYFIFMRvfairaRLTAnkdvekkeINQPGTVFAynsddeifkdpSFLIQEAFYN 1031
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 182 VRTVRAFGKE---MTEIEKyasKVDHVMQLARKEAFARAGFFGATGlSGNLIVLSVLYK-GGLLMGSAHMTVGELSSFLM 257
Cdd:PTZ00265 1032 MNTVIIYGLEdyfCNLIEK---AIDYSNKGQKRKTLVNSMLWGFSQ-SAQLFINSFAYWfGSFLIRRGTILVDDFMKSLF 1107
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 258 YAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPF--NEGV-ILNEKSFQGALEFKNVHFAYPARPEVPIFQDF 334
Cdd:PTZ00265 1108 TFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVrdNGGIrIKNKNDIKGKIEIMDVNFRYISRPNVPIYKDL 1187
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 335 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD------------------------------------------------ 366
Cdd:PTZ00265 1188 TFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsg 1267
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 367 ------PASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNF 440
Cdd:PTZ00265 1268 edstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKED---ATREDVKRACKFAAIDEFIESL 1344
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 441 PQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN 518
Cdd:PTZ00265 1345 PNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKR 1424
|
570 580 590
....*....|....*....|....*....|....*.
gi 767912302 519 ANMVAVLDQGK-----ITEYGKHEELLSKPNGIYRK 549
Cdd:PTZ00265 1425 SDKIVVFNNPDrtgsfVQAHGTHEELLSVQDGVYKK 1460
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
2-285 |
2.85e-64 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 212.02 E-value: 2.85e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVI--YTNPTV-DYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILR 78
Cdd:cd18574 8 AALVNIQIPLLLGDLVNVIsrSLKETNgDFIEDLKKPALKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 79 QEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLR 158
Cdd:cd18574 88 QDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 159 KLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKG 238
Cdd:cd18574 168 KLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLNEKLGLGIGIFQGLSNLALNGIVLGVLYYG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767912302 239 GLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGR 285
Cdd:cd18574 248 GSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGAR 294
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-558 |
2.93e-63 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 225.29 E-value: 2.93e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 8 SAPFFLgKIIDVIYTNptVDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKT 87
Cdd:PTZ00265 75 TLPFFV-SVFGVIMKN--MNLGENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFYQDGQFHDNN 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 88 RTgeliNRLSSDTALLGRSVTENLSDG---LRAGAQASVGISMM-FFVSPNLATFVLSVVPPVSIIAVIYGRYLrKLTKV 163
Cdd:PTZ00265 152 PG----SKLTSDLDFYLEQVNAGIGTKfitIFTYASAFLGLYIWsLFKNARLTLCITCVFPLIYICGVICNKKV-KINKK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 164 TQDSLAQAT-QLAEERIGNVRTVRAFGKEMTEIEKYaskvdHVMQLARKEAFARAGFFGA--TGLSGNLIVLSvlYKGGL 240
Cdd:PTZ00265 227 TSLLYNNNTmSIIEEALVGIRTVVSYCGEKTILKKF-----NLSEKLYSKYILKANFMESlhIGMINGFILAS--YAFGF 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 241 LMGSaHMTVGELSSF-----LMYAFWVGISIGGLSSFY---------SELMKGLGAGGRLWELLEREPKLPFN-EGVILN 305
Cdd:PTZ00265 300 WYGT-RIIISDLSNQqpnndFHGGSVISILLGVLISMFmltiilpniTEYMKSLEATNSLYEIINRKPLVENNdDGKKLK 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 306 EKSfqgALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISL-DGHDIRQLNP 384
Cdd:PTZ00265 379 DIK---KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINL 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 385 VWLRSKIGTVSQEPILFSCSIAENIAY------------------------GADDPSSVTAE------------------ 422
Cdd:PTZ00265 456 KWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRNSCRAKcagdlndmsnttdsneli 535
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 423 ---------EIQRVAEVANAVA---FIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENE 490
Cdd:PTZ00265 536 emrknyqtiKDSEVVDVSKKVLihdFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSE 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 491 YLVQEALDRLM--DGRTVLVIAHRLSTIKNANMVAVL------------------------------DQGK--------- 529
Cdd:PTZ00265 616 YLVQKTINNLKgnENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnKDDNnnnnnnnnn 695
|
650 660 670
....*....|....*....|....*....|....*..
gi 767912302 530 --------ITEYGKHEELLSKPNGIYRKLMNKQSFIS 558
Cdd:PTZ00265 696 kinnagsyIIEQGTHDALMKNKNGIYYTMINNQKVSS 732
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
4-542 |
5.71e-62 |
|
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: 213.36 E-value: 5.71e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 4 VISMSAPFFLGKIIDVIYTNPTVDYSDNLTRLCLGLSAVFlcgAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAF 83
Cdd:TIGR01842 20 ILMLAPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFL---GLLDALRSFVLVRIGEKLDGALNQPIFAASFSATLRR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 84 FDKtRTGELINrlssDTALLGRSVTenlSDGLRAGAQAS-----VGISMMFFVSPNLATFVLSVVPPVsiIAVIYGRYLR 158
Cdd:TIGR01842 97 GSG-DGLQALR----DLDQLRQFLT---GPGLFAFFDAPwmpiyLLVCFLLHPWIGILALGGAVVLVG--LALLNNRATK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 159 KLTKVTQDSLAQATQLAEERIGNVRTVRAFG-------KEMTEIEKYASkvdhvmqlARKEAFARAGFFGATGLSGNLIV 231
Cdd:TIGR01842 167 KPLKEATEASIRANNLADSALRNAEVIEAMGmmgnltkRWGRFHSKYLS--------AQSAASDRAGMLSNLSKYFRIVL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 232 LS-VLYKGGLLMGSAHMTVGEL--SSFLMYAFWVGI--SIGGLSSFyselMKGLGAGGRLWELLEREP------KLPFNE 300
Cdd:TIGR01842 239 QSlVLGLGAYLAIDGEITPGMMiaGSILVGRALAPIdgAIGGWKQF----SGARQAYKRLNELLANYPsrdpamPLPEPE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 301 GVILNEksfqgalefkNVHFAyPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR 380
Cdd:TIGR01842 315 GHLSVE----------NVTIV-PPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 381 QLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQK 460
Cdd:TIGR01842 384 QWDRETFGKHIGYLPQDVELFPGTVAENIARFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 461 QRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEEL 539
Cdd:TIGR01842 461 QRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEV 540
|
...
gi 767912302 540 LSK 542
Cdd:TIGR01842 541 LAK 543
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
285-554 |
5.10e-61 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 211.22 E-value: 5.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 285 RLWELLEREPKLPFNEGVilNEKSFQGALEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRL 364
Cdd:PRK11160 313 RINEITEQKPEVTFPTTS--TAAADQVSLTLNNVSFTYPDQPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 365 YDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSvtaeeiQRVAEVANAV--AFIRNFPQ 442
Cdd:PRK11160 390 WDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASD------EALIEVLQQVglEKLLEDDK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 443 GFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMV 522
Cdd:PRK11160 464 GLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRI 543
|
250 260 270
....*....|....*....|....*....|..
gi 767912302 523 AVLDQGKITEYGKHEELLSKpNGIYRKLMNKQ 554
Cdd:PRK11160 544 CVMDNGQIIEQGTHQELLAQ-QGRYYQLKQRL 574
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
1-286 |
1.73e-60 |
|
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: 201.94 E-value: 1.73e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIYTNPTvdySDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQE 80
Cdd:cd18575 7 IAAAATLALGQGLRLLIDQGFAAGN---TALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 81 VAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKL 160
Cdd:cd18575 84 PSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 161 TKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGL 240
Cdd:cd18575 164 SRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGAH 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767912302 241 LMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 286
Cdd:cd18575 244 DVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAERL 289
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
63-513 |
2.69e-57 |
|
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: 200.28 E-value: 2.69e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 63 RIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPN-----LAT 137
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAAAVAAIAVLSVPaalilAAG 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 138 FVLS--VVPPVSIIAV-IYGRYLRKL-TKVTQDSLAQATQLAEERI-----GNVRTVRAFGKEMTEIEKYASKVDHVMQl 208
Cdd:TIGR02868 163 LLLAgfVAPLVSLRAArAAEQALARLrGELAAQLTDALDGAAELVAsgalpAALAQVEEADRELTRAERRAAAATALGA- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 209 arkeafaragffGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWE 288
Cdd:TIGR02868 242 ------------ALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 289 LLE-----REPKLPFNEGVILNEKSfqgaLEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLR 363
Cdd:TIGR02868 310 VLDaagpvAEGSAPAAGAVGLGKPT----LELRDLSAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 364 LYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGADDpssVTAEEIQRVAEVANAVAFIRNFPQG 443
Cdd:TIGR02868 384 LLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPD---ATDEELWAALERVGLADWLRALPDG 460
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 444 FNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRL 513
Cdd:TIGR02868 461 LDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
10-286 |
2.23e-56 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 190.99 E-value: 2.23e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 10 PFFLGKIIDVIytnpTVDYS-DNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTR 88
Cdd:cd18784 16 PYYTGQVIDGI----VIEKSqDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFDTVK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 89 TGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSL 168
Cdd:cd18784 92 TGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 169 AQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMT 248
Cdd:cd18784 172 AKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYYGGHLVITGQIS 251
|
250 260 270
....*....|....*....|....*....|....*...
gi 767912302 249 VGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 286
Cdd:cd18784 252 GGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
313-530 |
4.16e-55 |
|
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: 183.57 E-value: 4.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 392
Cdd:cd03246 1 LEVENVSFRYPGAEP-PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFSCSIAENIaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARALLKN 472
Cdd:cd03246 80 YLPQDDELFSGSIAENI---------------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 473 PKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKNANMVAVLDQGKI 530
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
313-549 |
1.63e-54 |
|
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: 192.43 E-value: 1.63e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARP--EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV---WL 387
Cdd:COG1123 261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslrEL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 388 RSKIGTVSQEPilFSC-----SIAENIAYGADDPSSVTAEEI-QRVAEVANAV----AFIRNFPQGFntvvgekgvllSG 457
Cdd:COG1123 341 RRRVQMVFQDP--YSSlnprmTVGDIIAEPLRLHGLLSRAERrERVAELLERVglppDLADRYPHEL-----------SG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 458 GQKQRIAIARALLKNPKILLLDEATSALDaeneYLVQEA-LDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 530
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALD----VSVQAQiLNLLRDlqrelGLTYLFISHDLAVVRYiADRVAVMYDGRI 483
|
250
....*....|....*....
gi 767912302 531 TEYGKHEELLSKPNGIYRK 549
Cdd:COG1123 484 VEDGPTEEVFANPQHPYTR 502
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
1-259 |
5.64e-54 |
|
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: 184.00 E-value: 5.64e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDvIYTNPTVDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQE 80
Cdd:pfam00664 10 LSGAISPAFPLVLGRILD-VLLPDGDPETQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKILRQP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 81 VAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKL 160
Cdd:pfam00664 89 MSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 161 TKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGL 240
Cdd:pfam00664 169 SRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAY 248
|
250
....*....|....*....
gi 767912302 241 LMGSAHMTVGELSSFLMYA 259
Cdd:pfam00664 249 LVISGELSVGDLVAFLSLF 267
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
2-286 |
1.44e-53 |
|
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: 183.40 E-value: 1.44e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVIYTNptvdysDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEV 81
Cdd:cd18551 11 GTAASLAQPLLVKNLIDALSAG------GSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLLRLPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 82 AFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLT 161
Cdd:cd18551 85 SFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGRRIRKAS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 162 KVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLL 241
Cdd:cd18551 165 KRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVLGVGGAR 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767912302 242 MGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 286
Cdd:cd18551 245 VASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALERI 289
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
313-543 |
2.82e-53 |
|
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: 180.61 E-value: 2.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 392
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPI--LFSCSIAENIAYGaddP--SSVTAEEI-QRVAEVANAV---AFIRNFPQgfntvvgekgvLLSGGQKQRIA 464
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFG---PenLGLPREEIrERVEEALELVgleHLADRPPH-----------ELSGGQKQRVA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 465 IARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSK 542
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSD 224
|
.
gi 767912302 543 P 543
Cdd:COG1122 225 Y 225
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
313-511 |
5.18e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 179.24 E-value: 5.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 392
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFSCSIAENIAYgaddPSSVTAEEIQRvaevANAVAFIRNFpqGFNTVVGEKGV-LLSGGQKQRIAIARALLK 471
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPF----PFQLRERKFDR----ERALELLERL--GLPPDILDKPVeRLSGGERQRLALIRALLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767912302 472 NPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAH 511
Cdd:COG4619 148 QPDVLLLDEPTSALDPENTRRVEELLREYLaeEGRAVLWVSH 189
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
2-286 |
6.37e-53 |
|
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: 181.98 E-value: 6.37e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVIYTNPTVDYsdnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEV 81
Cdd:cd07346 11 ATALGLALPLLTKLLIDDVIPAGDLSL---LLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRHLQRLSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 82 AFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLT 161
Cdd:cd07346 88 SFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRRRIRKAS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 162 KVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLL 241
Cdd:cd07346 168 REVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVLLYGGYL 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 767912302 242 MGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 286
Cdd:cd07346 248 VLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
335-554 |
6.29e-52 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 186.97 E-value: 6.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 335 SLSIPSGSVTALVGPSGSGKSTVLSLLLRlYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGAd 414
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 415 dpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQ 494
Cdd:PRK11174 448 --PDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 495 EALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYRKLMNKQ 554
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQ 585
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
23-547 |
1.31e-51 |
|
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: 190.93 E-value: 1.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 23 NPTVDYSDNLTRLCLGLSAVF--LCGAAanaIRVYLMQTS--GQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSS 98
Cdd:TIGR00957 994 DPMVNGTQNNTSLRLSVYGALgiLQGFA---VFGYSMAVSigGIQASRVLHQDLLHNKLRSPMSFFERTPSGNLVNRFSK 1070
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 99 DTALLGRSVTENLSDGLRAGAQAsVGISMMFFVSPNLATFVlsvVPPVSIIAVIYGRYL----RKLTKVTQDSLAQATQL 174
Cdd:TIGR00957 1071 ELDTVDSMIPPVIKMFMGSLFNV-IGALIVILLATPIAAVI---IPPLGLLYFFVQRFYvassRQLKRLESVSRSPVYSH 1146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 175 AEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVL-SVLYKgglLMGSAHMTVGELS 253
Cdd:TIGR00957 1147 FNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGNCIVLfAALFA---VISRHSLSAGLVG 1223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 254 SFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPF--NEGVILNEKSFQGALEFKNVHFAYpaRPEVP-I 330
Cdd:TIGR00957 1224 LSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEKEAPWqiQETAPPSGWPPRGRVEFRNYCLRY--REDLDlV 1301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 331 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIa 410
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL- 1380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 411 ygadDP-SSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN 489
Cdd:TIGR00957 1381 ----DPfSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 767912302 490 EYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKpNGIY 547
Cdd:TIGR00957 1457 DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ-RGIF 1513
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
313-539 |
9.06e-50 |
|
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: 171.21 E-value: 9.06e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD-----PASGTISLDGHDIRQL--NPV 385
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvDVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 386 WLRSKIGTVSQEPILFSCSIAENIAYGADDPSSVTAEEI-QRVAEVANAVAFIRNfpqgfntvVGEK--GVLLSGGQKQR 462
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWDE--------VKDRlhALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912302 463 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEEL 539
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
313-543 |
1.80e-49 |
|
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: 170.84 E-value: 1.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---R 388
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 SKIGTVSQEPILFSC-SIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIA 464
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELLELVgleDKADAYPAQ-----------LSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 465 IARALLKNPKILLLDEATSALDAENeylVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEE 538
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPET---TQSILALLRDinrelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227
|
....*
gi 767912302 539 LLSKP 543
Cdd:cd03258 228 VFANP 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
313-534 |
1.11e-48 |
|
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: 168.45 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---R 388
Cdd:cd03257 2 LEVKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 SKIGTVSQEPilFSC-----SIAENIA--YGADDPSSVTAEEIQRVAEVANAV----AFIRNFPQGfntvvgekgvlLSG 457
Cdd:cd03257 82 KEIQMVFQDP--MSSlnprmTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVglpeEVLNRYPHE-----------LSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 458 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 534
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
313-543 |
1.11e-48 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 171.80 E-value: 1.11e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---R 388
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 SKIGTVSQEPILF-SCSIAENIAYgaddP---SSVTAEEI-QRVAEVANAV---AFIRNFP-QgfntvvgekgvlLSGGQ 459
Cdd:COG1135 82 RKIGMIFQHFNLLsSRTVAENVAL----PleiAGVPKAEIrKRVAELLELVglsDKADAYPsQ------------LSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 460 KQRIAIARALLKNPKILLLDEATSALDAENeylVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEY 533
Cdd:COG1135 146 KQRVGIARALANNPKVLLCDEATSALDPET---TRSILDLLKDinrelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQ 222
|
250
....*....|
gi 767912302 534 GKHEELLSKP 543
Cdd:COG1135 223 GPVLDVFANP 232
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
10-286 |
2.65e-48 |
|
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: 169.53 E-value: 2.65e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 10 PFFLGKIIDVIYTNPTVDYsdnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRT 89
Cdd:cd18552 19 AWLLKPLLDDIFVEKDLEA---LLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFDKLLRLPLSFFDRNSS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 90 GELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLA 169
Cdd:cd18552 96 GDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 170 QATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAG------FFGATGLSGnlivlsVLYKGGLLMG 243
Cdd:cd18552 176 DLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALssplmeLLGAIAIAL------VLWYGGYQVI 249
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 767912302 244 SAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 286
Cdd:cd18552 250 SGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
312-544 |
3.90e-48 |
|
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: 167.91 E-value: 3.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKI 391
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEPIL-FSCSIAENIAYG----ADDPSSVTAEEIQRVAEV---ANAVAFI-RNFPQgfntvvgekgvlLSGGQKQR 462
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGryphLGLFGRPSAEDREAVEEAlerTGLEHLAdRPVDE------------LSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 463 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEEL 539
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
....*
gi 767912302 540 LSKPN 544
Cdd:COG1120 226 LTPEL 230
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
11-286 |
4.45e-48 |
|
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: 169.19 E-value: 4.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 11 FFLGKIIDVI--YTNPTVDYS---DNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFD 85
Cdd:cd18577 20 IVFGDLFDAFtdFGSGESSPDeflDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQARRIRKRYLKALLRQDIAWFD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 86 KTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQ 165
Cdd:cd18577 100 KNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 166 DSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSA 245
Cdd:cd18577 180 EAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDG 259
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 767912302 246 HMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRL 286
Cdd:cd18577 260 EISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
313-529 |
4.47e-48 |
|
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: 166.11 E-value: 4.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPEV--PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlnpvwlrsK 390
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEPILFSCSIAENIAYGADdpssvtaEEIQRVAEVANAVAF---IRNFPQGFNTVVGEKGVLLSGGQKQRIAIAR 467
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKP-------FDEERYEKVIKACALepdLEILPDGDLTEIGEKGINLSGGQKQRISLAR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912302 468 ALLKNPKILLLDEATSALDAE-NEYLVQEAL-DRLMDGRTVLVIAHRLSTIKNANMVAVLDQGK 529
Cdd:cd03250 141 AVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
7-285 |
1.18e-46 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 165.20 E-value: 1.18e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 7 MSAPFFLGKIIDVIYTnptvDYSDNLTRLCLGLSAVFLCGAAANA-IRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFD 85
Cdd:cd18590 13 TFIPYYTGRVIDILGG----EYQHNAFTSAIGLMCLFSLGSSLSAgLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 86 KTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQ 165
Cdd:cd18590 89 KTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 166 DSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSA 245
Cdd:cd18590 169 DSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSG 248
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767912302 246 HMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGR 285
Cdd:cd18590 249 HLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAK 288
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
313-542 |
7.84e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 161.00 E-value: 7.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 392
Cdd:COG1131 1 IEVRGLTKRYGDKTAL---DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILF-SCSIAENIAYGAD---DPSSVTAEEIQRVAEVANAVAFIrnfpqgfNTVVGEkgvlLSGGQKQRIAIARA 468
Cdd:COG1131 77 YVPQEPALYpDLTVRENLRFFARlygLPRKEARERIDELLELFGLTDAA-------DRKVGT----LSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 469 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSK 542
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
1-262 |
1.05e-45 |
|
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: 162.60 E-value: 1.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIYTNptvDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQE 80
Cdd:cd18542 10 LATALNLLIPLLIRRIIDSVIGG---GLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 81 VAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKL 160
Cdd:cd18542 87 FSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKVRPA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 161 TKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGL 240
Cdd:cd18542 167 FEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWVGGY 246
|
250 260
....*....|....*....|..
gi 767912302 241 LMGSAHMTVGELSSFLMYAFWV 262
Cdd:cd18542 247 LVINGEITLGELVAFISYLWML 268
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
314-529 |
1.16e-45 |
|
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: 157.79 E-value: 1.16e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 314 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 393
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 394 VSQepilfscsiaeniaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARALLKNP 473
Cdd:cd00267 78 VPQ----------------------------------------------------------LSGGQRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767912302 474 KILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNA-NMVAVLDQGK 529
Cdd:cd00267 100 DLLLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
312-552 |
1.56e-45 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 160.74 E-value: 1.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSK 390
Cdd:COG1124 1 MLEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEPilfscsiaeniaYGADDPSSvTAEEI--------------QRVAEVANAV----AFIRNFP-Qgfntvvgek 451
Cdd:COG1124 81 VQMVFQDP------------YASLHPRH-TVDRIlaeplrihglpdreERIAELLEQVglppSFLDRYPhQ--------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 452 gvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneyLVQ-EALDRLMD-----GRTVLVIAHRLSTIknANM---V 522
Cdd:COG1124 139 ---LSGGQRQRVAIARALILEPELLLLDEPTSALDV----SVQaEILNLLKDlreerGLTYLFVSHDLAVV--AHLcdrV 209
|
250 260 270
....*....|....*....|....*....|.
gi 767912302 523 AVLDQGKITEYGKHEELLSKPNGIY-RKLMN 552
Cdd:COG1124 210 AVMQNGRIVEELTVADLLAGPKHPYtRELLA 240
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
313-534 |
1.85e-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: 1.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKIG 392
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFSCSIAENIaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekGVLLSGGQKQRIAIARALLKN 472
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL------------------------------------------GRRFSGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912302 473 PKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYG 534
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
11-295 |
2.39e-45 |
|
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: 162.24 E-value: 2.39e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 11 FFLGKIIDVIYTNPTVDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTR-- 88
Cdd:cd18578 30 ILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAGERLTRRLRKLAFRAILRQDIAWFDDPEns 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 89 TGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSL 168
Cdd:cd18578 110 TGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 169 AQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMT 248
Cdd:cd18578 190 EESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYT 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767912302 249 VGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPK 295
Cdd:cd18578 270 FEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPE 316
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
313-543 |
4.28e-45 |
|
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: 159.39 E-value: 4.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 392
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFS-CSIAENIAYgadDPSSVTAEEIQRVAEVANAVAFIRNFPQGF-NTVVGEkgvlLSGGQKQRIAIARALL 470
Cdd:cd03295 79 YVIQQIGLFPhMTVEENIAL---VPKLLKWPKEKIRERADELLALVGLDPAEFaDRYPHE----LSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 471 KNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRL-STIKNANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
312-543 |
4.54e-45 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 159.82 E-value: 4.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD--P---ASGTISLDGHDI--RQLNP 384
Cdd:COG1117 11 KIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 385 VWLRSKIGTVSQEPILFSCSIAENIAYGA---DDPSSVTAEEI-----QRVA---EVANavafirnfpqgfntVVGEKGV 453
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSIYDNVAYGLrlhGIKSKSELDEIveeslRKAAlwdEVKD--------------RLKKSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 454 LLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAH------RLStiknaNMVAVLDQ 527
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFYL 228
|
250
....*....|....*.
gi 767912302 528 GKITEYGKHEELLSKP 543
Cdd:COG1117 229 GELVEFGPTEQIFTNP 244
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
314-529 |
4.73e-45 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 158.01 E-value: 4.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 314 EFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 393
Cdd:cd03225 1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 394 VSQEP--ILFSCSIAENIAYGAdDPSSVTAEEI-QRVAEVANAvafirnfpqgfntvVGEKGVL------LSGGQKQRIA 464
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGL-ENLGLPEEEIeERVEEALEL--------------VGLEGLRdrspftLSGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 465 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGK 529
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
312-543 |
5.46e-45 |
|
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: 166.23 E-value: 5.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA---SGTISLDGHDIRQLNPVWLR 388
Cdd:COG1123 4 LLEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 SKIGTVSQEPI--LFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQgfntvvgekgvLLSGGQKQRI 463
Cdd:COG1123 83 RRIGMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVgleRRLDRYPH-----------QLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 464 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELL 540
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEIL 231
|
...
gi 767912302 541 SKP 543
Cdd:COG1123 232 AAP 234
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
313-543 |
6.31e-45 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 158.62 E-value: 6.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI----RQLNPvwLR 388
Cdd:COG1126 2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdskKDINK--LR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 SKIGTVSQEPILFS-CSIAENIAYGaddPSSV------TAEEI-----QRV--AEVANAvafirnFP-Qgfntvvgekgv 453
Cdd:COG1126 77 RKVGMVFQQFNLFPhLTVLENVTLA---PIKVkkmskaEAEERamellERVglADKADA------YPaQ----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 454 lLSGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALDrLM-----DGRTVLVIAHRLSTIKN-ANMVAVLDQ 527
Cdd:COG1126 137 -LSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMrdlakEGMTMVVVTHEMGFAREvADRVVFMDG 211
|
250
....*....|....*.
gi 767912302 528 GKITEYGKHEELLSKP 543
Cdd:COG1126 212 GRIVEEGPPEEFFENP 227
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
312-532 |
8.89e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 157.90 E-value: 8.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPA-RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP----VW 386
Cdd:COG1136 4 LLELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSErelaRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 387 LRSKIGTVSQEPILFSC-SIAENIAYGADdPSSVTAEEI-QRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQ 461
Cdd:COG1136 84 RRRHIGFVFQFFNLLPElTALENVALPLL-LAGVSRKERrERARELLERVglgDRLDHRP-------SQ----LSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912302 462 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITE 532
Cdd:COG1136 152 RVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
311-534 |
1.39e-44 |
|
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: 156.80 E-value: 1.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 311 GALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS 389
Cdd:cd03369 5 GEIEVENLSVRY--APDLPpVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 KIGTVSQEPILFSCSIAENIaygadDP-SSVTAEEIQRVAEVAnavafirnfpqgfntvvgEKGVLLSGGQKQRIAIARA 468
Cdd:cd03369 83 SLTIIPQDPTLFSGTIRSNL-----DPfDEYSDEEIYGALRVS------------------EGGLNLSQGQRQLLCLARA 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 469 LLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYG 534
Cdd:cd03369 140 LLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
313-542 |
2.39e-44 |
|
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: 157.33 E-value: 2.39e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 392
Cdd:COG4555 2 IEVENLSKKYG---KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFS-CSIAENIAYGA---DDPSSVTAEEIQRVAEVANAVAFIrnfpqgfNTVVGEkgvlLSGGQKQRIAIARA 468
Cdd:COG4555 78 VLPDERGLYDrLTVRENIRYFAelyGLFDEELKKRIEELIELLGLEEFL-------DRRVGE----LSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 469 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 542
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
331-483 |
4.43e-44 |
|
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: 153.57 E-value: 4.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 331 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFS-CSIAENI 409
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPrLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912302 410 AYGADDPSSVTAEEIQRVAEVANAVAfIRNFPqgfNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATS 483
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLG-LGDLA---DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
313-511 |
5.52e-44 |
|
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: 155.71 E-value: 5.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYP-ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwlrsKI 391
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIAR 467
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEELLELVglsGFENAYPHQ-----------LSGGMRQRVALAR 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767912302 468 ALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAH 511
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWreTGKTVLLVTH 190
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
312-544 |
5.62e-44 |
|
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: 156.29 E-value: 5.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP---VWLR 388
Cdd:COG1127 5 MIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 SKIGTVSQEPILF-SCSIAENIAYGADDPSSVTAEEI-QRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQRI 463
Cdd:COG1127 82 RRIGMLFQGGALFdSLTVFENVAFPLREHTDLSEAEIrELVLEKLELVglpGAADKMP-------SE----LSGGMRKRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 464 AIARALLKNPKILLLDEATSALD----AENEYLVQEALDRLmdGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEE 538
Cdd:COG1127 151 ALARALALDPEILLYDEPTAGLDpitsAVIDELIRELRDEL--GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
....*.
gi 767912302 539 LLSKPN 544
Cdd:COG1127 229 LLASDD 234
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
313-529 |
2.76e-43 |
|
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: 152.34 E-value: 2.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLN--PVWLRSK 390
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEPILFS-CSIAENIAYGaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARAL 469
Cdd:cd03229 78 IGMVFQDFALFPhLTVLENIALG------------------------------------------LSGGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912302 470 LKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGK 529
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLqaQLGITVVLVTHDLDeAARLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
313-534 |
5.20e-43 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 152.67 E-value: 5.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRsKIG 392
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-PPERR-NIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILF-SCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIARA 468
Cdd:cd03259 76 MVFQDYALFpHLTVAENIAFGLKLRGVPKAEIRARVRELLELVgleGLLNRYPHE-----------LSGGQQQRVALARA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 469 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYG 534
Cdd:cd03259 145 LAREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
312-511 |
6.21e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 154.09 E-value: 6.21e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwlrsK 390
Cdd:COG1116 7 ALELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-----D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFP-QgfntvvgekgvlLSGGQKQRIAI 465
Cdd:COG1116 82 RGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELLELVglaGFEDAYPhQ------------LSGGMRQRVAI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 767912302 466 ARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAH 511
Cdd:COG1116 150 ARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTH 197
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
312-544 |
6.93e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 153.32 E-value: 6.93e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnpvwlRSKI 391
Cdd:COG1121 6 AIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQepilfscsiaeNIAYGADDPSSV------------------TAEEIQRVAEVANAV---AFIrnfpqgfNTVVGE 450
Cdd:COG1121 78 GYVPQ-----------RAEVDWDFPITVrdvvlmgrygrrglfrrpSRADREAVDEALERVgleDLA-------DRPIGE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 451 kgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTI-KNANMVAVLDQG 528
Cdd:COG1121 140 ----LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVrEYFDRVLLLNRG 215
|
250
....*....|....*.
gi 767912302 529 KITeYGKHEELLSKPN 544
Cdd:COG1121 216 LVA-HGPPEEVLTPEN 230
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
313-542 |
1.47e-42 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 153.35 E-value: 1.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVW-LRSKI 391
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEP-ILFSCSIAEN-IAYGaddPSS--VTAEEI-QRVAEVANAV---AFIRNFPQgfntvvgekgvLLSGGQKQRI 463
Cdd:TIGR04520 80 GMVFQNPdNQFVGATVEDdVAFG---LENlgVPREEMrKRVDEALKLVgmeDFRDREPH-----------LLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 464 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLS 541
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
.
gi 767912302 542 K 542
Cdd:TIGR04520 226 Q 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
313-544 |
3.02e-42 |
|
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: 151.50 E-value: 3.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---RS 389
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 KIGTVSQEPILF-SCSIAENIAYGADDPSSVTAEEI-QRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQRIA 464
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVAFPLREHTRLSEEEIrEIVLEKLEAVglrGAEDLYP-------AE----LSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 465 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLS 541
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
...
gi 767912302 542 KPN 544
Cdd:cd03261 227 SDD 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
55-552 |
6.79e-42 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 162.07 E-value: 6.79e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 55 YLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSpn 134
Cdd:PLN03232 972 FWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQLLSTFALIGTVS-- 1049
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 135 laTFVLSVVPPVSII---AVIY----GRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKeMTEIEKYASKVDHVMQ 207
Cdd:PLN03232 1050 --TISLWAIMPLLILfyaAYLYyqstSREVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYDR-MAKINGKSMDNNIRFT 1126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 208 LARKEAfARAGFFGATGLSGNLIVLSVLYkGGLLMGSAHMTVGELSS---FLMYAFWVGISIGGLSSFYSELMKGLGAGG 284
Cdd:PLN03232 1127 LANTSS-NRWLTIRLETLGGVMIWLTATF-AVLRNGNAENQAGFASTmglLLSYTLNITTLLSGVLRQASKAENSLNSVE 1204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 285 RLWELLEREPKLPfneGVILNEKS-----FQGALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVL 358
Cdd:PLN03232 1205 RVGNYIDLPSEAT---AIIENNRPvsgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSML 1279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 359 SLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIaygadDP-SSVTAEEIQRVAEVANAVAFI 437
Cdd:PLN03232 1280 NALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI-----DPfSEHNDADLWEALERAHIKDVI 1354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 438 RNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIK 517
Cdd:PLN03232 1355 DRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTII 1434
|
490 500 510
....*....|....*....|....*....|....*
gi 767912302 518 NANMVAVLDQGKITEYGKHEELLSKPNGIYRKLMN 552
Cdd:PLN03232 1435 DCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
312-544 |
1.51e-41 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 152.94 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRsKI 391
Cdd:COG3842 5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-PPEKR-NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEPILFS-CSIAENIAYGADDpSSVTAEEI-QRVAEVANAV---AFIRNFPQgfntvvgekgvLLSGGQKQRIAIA 466
Cdd:COG3842 80 GMVFQDYALFPhLTVAENVAFGLRM-RGVPKAEIrARVAELLELVgleGLADRYPH-----------QLSGGQQQRVALA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 467 RALLKNPKILLLDEATSALDAEneyL---VQEALDRLMD--GRTVLVIAHRLS---TIknANMVAVLDQGKITEYGKHEE 538
Cdd:COG3842 148 RALAPEPRVLLLDEPLSALDAK---LreeMREELRRLQRelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEE 222
|
....*.
gi 767912302 539 LLSKPN 544
Cdd:COG3842 223 IYERPA 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
313-544 |
1.52e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 149.52 E-value: 1.52e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIG 392
Cdd:COG3840 2 LRLDDLTYRYGDFP-----LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQRIAIARA 468
Cdd:COG3840 75 MLFQENNLFPhLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVglaGLLDRLP-------GQ----LSGGQRQRVALARC 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 469 LLKNPKILLLDEATSALD----AENEYLVQEALDRLmdGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:COG3840 144 LVRKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGE 221
|
.
gi 767912302 544 N 544
Cdd:COG3840 222 P 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
55-550 |
1.95e-41 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 160.67 E-value: 1.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 55 YLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVtenlsdglragaqaSVGISM-MFFVSP 133
Cdd:PLN03130 975 YWLIMSSLYAAKRLHDAMLGSILRAPMSFFHTNPLGRIINRFAKDLGDIDRNV--------------AVFVNMfLGQIFQ 1040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 134 NLATFVL-SVVPPVSIIAVI------YGRYL------RKLTKVtqDSLAQATQLAE--ERIGNVRTVRAFG--KEMTEIE 196
Cdd:PLN03130 1041 LLSTFVLiGIVSTISLWAIMpllvlfYGAYLyyqstaREVKRL--DSITRSPVYAQfgEALNGLSTIRAYKayDRMAEIN 1118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 197 kyASKVDHVMQlarkeafaragfFGATGLSGN---LIVLSVLykGGLL---------MGSAHM--------TVGELssfL 256
Cdd:PLN03130 1119 --GRSMDNNIR------------FTLVNMSSNrwlAIRLETL--GGLMiwltasfavMQNGRAenqaafasTMGLL---L 1179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 257 MYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREPKLPFnegVILNEKS-----FQGALEFKNVHFAYpaRPEVP-I 330
Cdd:PLN03130 1180 SYALNITSLLTAVLRLASLAENSLNAVERVGTYIDLPSEAPL---VIENNRPppgwpSSGSIKFEDVVLRY--RPELPpV 1254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 331 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIa 410
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL- 1333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 411 ygadDP-SSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN 489
Cdd:PLN03130 1334 ----DPfNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912302 490 EYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYRKL 550
Cdd:PLN03130 1410 DALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKM 1470
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
314-534 |
2.57e-41 |
|
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: 146.81 E-value: 2.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 314 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 393
Cdd:cd03214 1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 394 VSQepilfscsiaeniaygaddpssvtaeeiqrVAEVANAVAFIRnfpQGFNTvvgekgvlLSGGQKQRIAIARALLKNP 473
Cdd:cd03214 78 VPQ------------------------------ALELLGLAHLAD---RPFNE--------LSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912302 474 KILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYG 534
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
313-532 |
4.27e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 147.89 E-value: 4.27e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP---VWLRS 389
Cdd:COG2884 2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRreiPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 KIGTVSQE-PILFSCSIAENIAY-----GADDpssvtaEEIQ-RVAEVANAV---AFIRNFPQgfntvvgEkgvlLSGGQ 459
Cdd:COG2884 80 RIGVVFQDfRLLPDRTVYENVALplrvtGKSR------KEIRrRVREVLDLVglsDKAKALPH-------E----LSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 460 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKNANM-VAVLDQGKITE 532
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
313-530 |
6.00e-41 |
|
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: 147.25 E-value: 6.00e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---- 387
Cdd:cd03255 1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 388 RSKIGTVSQE----PILfscSIAENIAYGADDPSSVTAEEIQRVAEVANAVafirNFPQGFNTVVGEkgvlLSGGQKQRI 463
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEELLERV----GLGDRLNHYPSE----LSGGQQQRV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 464 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTIKNANMVAVLDQGKI 530
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
310-540 |
7.11e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 146.29 E-value: 7.11e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 310 QGALEFKNVHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS 389
Cdd:PRK13632 5 SVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 KIGTVSQEP--ILFSCSIAENIAYGADD---PSSVTAEEIQRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIA 464
Cdd:PRK13632 84 KIGIIFQNPdnQFIGATVEDDIAFGLENkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912302 465 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELL 540
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
313-530 |
1.06e-39 |
|
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: 142.54 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 392
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFScsiaeniaygaddpsSVTAEEIqrvaevanavafirnfpqgfntvvgekgVLLSGGQKQRIAIARALLKN 472
Cdd:cd03230 77 YLPEEPSLYE---------------NLTVREN----------------------------LKLSGGMKQRLALAQALLHD 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 473 PKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 530
Cdd:cd03230 114 PELLILDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
2-285 |
7.19e-39 |
|
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: 144.08 E-value: 7.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVIYTNP----TVDYsDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSIL 77
Cdd:cd18547 11 STLLSVLGPYLLGKAIDLIIEGLggggGVDF-SGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 78 RQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYL 157
Cdd:cd18547 90 RLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 158 RKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKeafarAGFFG-----ATGLSGNLIVL 232
Cdd:cd18547 170 QKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFK-----AQFYSgllmpIMNFINNLGYV 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 767912302 233 SVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGAGGR 285
Cdd:cd18547 245 LVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
333-544 |
7.37e-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: 142.09 E-value: 7.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 333 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIGTVSQEPILF-SCSIAENIAY 411
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 412 GADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEY 491
Cdd:cd03299 95 GLKKRKVDKKEIERKVLEIAEML--------GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 492 LVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPN 544
Cdd:cd03299 167 KLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPK 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
313-539 |
2.22e-38 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 141.17 E-value: 2.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPArpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---RS 389
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 KIGTVSQEPILFS-CSIAENIAYGADD--------PSSVTAEEIQRVAEVANAV-----AFIRnfpqgfntvVGEkgvlL 455
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGrrstwrslFGLFPKEEKQRALAALERVglldkAYQR---------ADQ----L 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 456 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTIK-NANMVAVLDQGKITE 532
Cdd:cd03256 146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIVF 225
|
....*..
gi 767912302 533 YGKHEEL 539
Cdd:cd03256 226 DGPPAEL 232
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
2-282 |
3.81e-38 |
|
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: 141.84 E-value: 3.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVIYTNPTVD-YSDNLTRLCL--GLSAV--FLCgaaaNAIRVYLMQtsgqRIVNRLRTSLFSSI 76
Cdd:cd18589 8 SSLGEMAIPYYTGRMTDWIMNKDAPEaFTAAITVMSLltIASAVseFVC----DLIYNITMS----RIHSRLQGLVFAAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 77 LRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRY 156
Cdd:cd18589 80 LRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 157 LRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLY 236
Cdd:cd18589 160 QQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILY 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767912302 237 KGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGLGA 282
Cdd:cd18589 240 YGGQLVTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGS 285
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
2-255 |
6.42e-38 |
|
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: 141.47 E-value: 6.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVIYTNPTVDYsdnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEV 81
Cdd:cd18550 11 SALLGLLPPLLLREIIDDALPQGDLGL---LVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRMSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 82 AFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLT 161
Cdd:cd18550 88 AFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRRRKLT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 162 KVTQDSLAQATQLAEER--IGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGG 239
Cdd:cd18550 168 REQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPALVYWVGG 247
|
250
....*....|....*.
gi 767912302 240 LLMGSAHMTVGELSSF 255
Cdd:cd18550 248 LLVIGGGLTIGTLVAF 263
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
312-530 |
9.25e-38 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.42 E-value: 9.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---R 388
Cdd:COG3638 2 MLELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 SKIGTVSQEPILFS-CSIAENIAYG--ADDP------SSVTAEEIQRVAEVANAV-----AFIRnfpqgfntvVGEkgvl 454
Cdd:COG3638 80 RRIGMIFQQFNLVPrLSVLTNVLAGrlGRTStwrsllGLFPPEDRERALEALERVgladkAYQR---------ADQ---- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 455 LSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-----EYLVQEALDrlmDGRTVLVIAHRLSTIKN-ANMVAVLDQG 528
Cdd:COG3638 147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTarqvmDLLRRIARE---DGITVVVNLHQVDLARRyADRIIGLRDG 223
|
..
gi 767912302 529 KI 530
Cdd:COG3638 224 RV 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
313-543 |
9.45e-38 |
|
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: 141.73 E-value: 9.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDP---ASGTISLDGHDIRQLNPVWLR 388
Cdd:COG0444 2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 S----KIGTVSQEPilFSC---------SIAENIAYGADDPSsvtAEEIQRVAEVANAV------AFIRNFP-Qgfntvv 448
Cdd:COG0444 82 KirgrEIQMIFQDP--MTSlnpvmtvgdQIAEPLRIHGGLSK---AEARERAIELLERVglpdpeRRLDRYPhE------ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 449 gekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneyLVQ-EALDRLMD-----GRTVLVIAHRLSTIKN-ANM 521
Cdd:COG0444 151 ------LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNLLKDlqrelGLAILFITHDLGVVAEiADR 220
|
250 260
....*....|....*....|..
gi 767912302 522 VAVLDQGKITEYGKHEELLSKP 543
Cdd:COG0444 221 VAVMYAGRIVEEGPVEELFENP 242
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
314-530 |
1.21e-37 |
|
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: 138.05 E-value: 1.21e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 314 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnpvwlRSKIGT 393
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 394 VSQEPIL---FSCSIAENIAYGADDPSS----VTAEEIQRVAEVANAV---AFI-RNFpqgfntvvGEkgvlLSGGQKQR 462
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGHKGlfrrLSKADKAKVDEALERVglsELAdRQI--------GE----LSGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 463 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTI-KNANMVAVLDQGKI 530
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELrREGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
2-258 |
2.12e-37 |
|
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: 139.83 E-value: 2.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVIYTNPTVDYSdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEV 81
Cdd:cd18544 11 ATALELLGPLLIKRAIDDYIVPGQGDLQ-GLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 82 AFFDKTRTGELINRLSSDTAllgrSVTENLSDGLRAGAQAS---VGI-SMMFFVSPNLATFVLSVVPPVSIIAVIYGRYL 157
Cdd:cd18544 90 SFFDRTPVGRLVTRVTNDTE----ALNELFTSGLVTLIGDLlllIGIlIAMFLLNWRLALISLLVLPLLLLATYLFRKKS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 158 RKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYK 237
Cdd:cd18544 166 RKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALFRPLVELLSSLALALVLWY 245
|
250 260
....*....|....*....|.
gi 767912302 238 GGLLMGSAHMTVGELSSFLMY 258
Cdd:cd18544 246 GGGQVLSGAVTLGVLYAFIQY 266
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
313-530 |
7.85e-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: 135.74 E-value: 7.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI----RQLNPvwLR 388
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddkKNINE--LR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 SKIGTVSQEPILFS-CSIAENIAYGaddPSSV----------TAEEI-QRV--AEVANAvafirnFPQGfntvvgekgvl 454
Cdd:cd03262 76 QKVGMVFQQFNLFPhLTVLENITLA---PIKVkgmskaeaeeRALELlEKVglADKADA------YPAQ----------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 455 LSGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGK 529
Cdd:cd03262 136 LSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE---LVGEVLDVMKDlaeeGMTMVVVTHEMGFAREvADRVIFMDDGR 212
|
.
gi 767912302 530 I 530
Cdd:cd03262 213 I 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
314-543 |
7.89e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 139.94 E-value: 7.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 314 EFKNVHFAYP-ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS--- 389
Cdd:PRK11153 3 ELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKarr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 KIGTVSQE-PILFSCSIAENIAYgaddP---SSVTAEEI-QRVAEVANAV---AFIRNFP-QgfntvvgekgvlLSGGQK 460
Cdd:PRK11153 83 QIGMIFQHfNLLSSRTVFDNVAL----PlelAGTPKAEIkARVTELLELVglsDKADRYPaQ------------LSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 461 QRIAIARALLKNPKILLLDEATSALDAENeylVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 534
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPAT---TRSILELLKDinrelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQG 223
|
....*....
gi 767912302 535 KHEELLSKP 543
Cdd:PRK11153 224 TVSEVFSHP 232
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
1-258 |
1.43e-36 |
|
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: 137.54 E-value: 1.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIyTNPTVDYSDnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQE 80
Cdd:cd18541 10 LVDLLQLLIPRIIGRAIDAL-TAGTLTASQ-LLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 81 VAFFDKTRTGELINRLSSDTAllgrSVTENLSDGLRAGAQASVG----ISMMFFVSPNLATFVLSVVPPVSIIAVIYGRY 156
Cdd:cd18541 88 PSFYQKNRTGDLMARATNDLN----AVRMALGPGILYLVDALFLgvlvLVMMFTISPKLTLIALLPLPLLALLVYRLGKK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 157 LRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLY 236
Cdd:cd18541 164 IHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLW 243
|
250 260
....*....|....*....|..
gi 767912302 237 KGGLLMGSAHMTVGELSSFLMY 258
Cdd:cd18541 244 YGGRLVIRGTITLGDLVAFNSY 265
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
2-259 |
2.90e-36 |
|
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: 136.87 E-value: 2.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIID--VIYTNPTVDYSDnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQ 79
Cdd:cd18563 11 GTALGLVPPYLTKILIDdvLIQLGPGGNTSL-LLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 80 EVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQAsVGIS-MMFFVSPNLATFVLSVVPPVSIIAVIYGRYLR 158
Cdd:cd18563 90 SLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMI-IGIGvVLFSLNWKLALLVLIPVPLVVWGSYFFWKKIR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 159 KL-TKVTQDSLAQATQLAEErIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYK 237
Cdd:cd18563 169 RLfHRQWRRWSRLNSVLNDT-LPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLGTLIVWYF 247
|
250 260
....*....|....*....|..
gi 767912302 238 GGLLMGSAHMTVGELSSFLMYA 259
Cdd:cd18563 248 GGRQVLSGTMTLGTLVAFLSYL 269
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
312-543 |
1.16e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 134.93 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPEvPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL--LRLYDPASGT-ISLDGHDIRQLNpVW-L 387
Cdd:PRK13640 5 IVEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLIngLLLPDDNPNSkITVDGITLTAKT-VWdI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 388 RSKIGTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVA---FIRNFPQGfntvvgekgvlLSGGQKQR 462
Cdd:PRK13640 83 REKVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGmldYIDSEPAN-----------LSGGQKQR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 463 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELL 540
Cdd:PRK13640 152 VAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231
|
...
gi 767912302 541 SKP 543
Cdd:PRK13640 232 SKV 234
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
335-543 |
1.39e-35 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 136.01 E-value: 1.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 335 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP---VWLRSKIGTVSQEPilFSC-----SIA 406
Cdd:COG4608 38 SFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGrelRPLRRRMQMVFQDP--YASlnprmTVG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 407 ENIAYGADDPSSVTAEEIQ-RVAEVANAV----AFIRNFPQGFntvvgekgvllSGGQKQRIAIARALLKNPKILLLDEA 481
Cdd:COG4608 116 DIIAEPLRIHGLASKAERReRVAELLELVglrpEHADRYPHEF-----------SGGQRQRIGIARALALNPKLIVCDEP 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 482 TSALDAEneylVQ-EALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:COG4608 185 VSALDVS----IQaQVLNLLEDlqdelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDELYARP 249
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
329-551 |
1.64e-35 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 133.88 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 329 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAEN 408
Cdd:cd03288 35 PVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 409 IaygaDDPSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 488
Cdd:cd03288 115 L----DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912302 489 NEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYRKLM 551
Cdd:cd03288 191 TENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLV 253
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
316-531 |
3.31e-35 |
|
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: 131.23 E-value: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 316 KNVHFAYPARPEvpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdiRQLNPVWLRSKIGTVS 395
Cdd:cd03226 3 ENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 396 QEP--ILFSCSIAENIAYGADDPSSVtAEEIQRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNP 473
Cdd:cd03226 78 QDVdyQLFTDSVREELLLGLKELDAG-NEQAETVLKDLDLYALKERHPLS-----------LSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 474 KILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGKIT 531
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRELAaQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
313-543 |
3.73e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 135.27 E-value: 3.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIrqlnPVWL---RS 389
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL----FTNLpprER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 KIGTVSQEPILF-SCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFP-QgfntvvgekgvlLSGGQKQRIA 464
Cdd:COG1118 76 RVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEELLELVqleGLADRYPsQ------------LSGGQRQRVA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 465 IARALLKNPKILLLDEATSALDA----ENEYLVQEALDRLmdGRTVLVIAH------RLstiknANMVAVLDQGKITEYG 534
Cdd:COG1118 144 LARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDEL--GGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVG 216
|
....*....
gi 767912302 535 KHEELLSKP 543
Cdd:COG1118 217 TPDEVYDRP 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
332-543 |
4.16e-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: 132.77 E-value: 4.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL----RSKIGTVSQEPILF-SCSIA 406
Cdd:cd03294 41 NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 407 ENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPqgfntvvGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATS 483
Cdd:cd03294 121 ENVAFGLEVQGVPRAEREERAAEALELVgleGWEHKYP-------DE----LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912302 484 ALDAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:cd03294 190 ALDPLIRREMQDELLRLQAelQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
313-534 |
4.99e-34 |
|
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: 128.08 E-value: 4.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevpIFQDFSLSIPSGsVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 392
Cdd:cd03264 1 LQLENLTKRYGKKR---ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILF-SCSIAENIAYGA---DDPSSvtaEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARA 468
Cdd:cd03264 76 YLPQEFGVYpNFTVREFLDYIAwlkGIPSK---EVKARVDEVLELV--------NLGDRAKKKIGSLSGGMRRRVGIAQA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 469 LLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 534
Cdd:cd03264 145 LVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
313-541 |
6.60e-34 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 129.75 E-value: 6.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdiRQLNP--VW-LRS 389
Cdd:PRK13635 6 IRVEHISFRYP-DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEetVWdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 KIGTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIA 464
Cdd:PRK13635 82 QVGMVFQNPdnQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVgmeDFLNREPHR-----------LSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 465 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLS 541
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqkGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFK 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
311-544 |
7.29e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 131.73 E-value: 7.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 311 GALEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSK 390
Cdd:COG3839 2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEPILF-SCSIAENIAYG---ADdpssVTAEEI-QRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQR 462
Cdd:COG3839 77 IAMVFQSYALYpHMTVYENIAFPlklRK----VPKAEIdRRVREAAELLgleDLLDRKPKQ-----------LSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 463 IAIARALLKNPKILLLDEATSALDAEneyLVQEA---LDRLMDGR---TVLV---------IAHRlstiknanmVAVLDQ 527
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDAK---LRVEMraeIKRLHRRLgttTIYVthdqveamtLADR---------IAVMND 209
|
250
....*....|....*..
gi 767912302 528 GKITEYGKHEELLSKPN 544
Cdd:COG3839 210 GRIQQVGTPEELYDRPA 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
313-544 |
1.21e-33 |
|
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: 127.74 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIG 392
Cdd:cd03300 1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIARA 468
Cdd:cd03300 76 TVFQNYALFPhLTVFENIAFGLRLKKLPKAEIKERVAEALDLVqleGYANRKPSQ-----------LSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 469 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKPN 544
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKelGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
312-544 |
6.12e-33 |
|
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: 125.91 E-value: 6.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwLRSKI 391
Cdd:cd03296 2 SIEVRNVSKRFGDFVAL---DDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV--QERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEPILFS-CSIAENIAYG------ADDPSSvtAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQ 461
Cdd:cd03296 77 GFVFQHYALFRhMTVFDNVAFGlrvkprSERPPE--AEIRAKVHELLKLVqldWLADRYPAQ-----------LSGGQRQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 462 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDG---RTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEE 538
Cdd:cd03296 144 RVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDE 223
|
....*.
gi 767912302 539 LLSKPN 544
Cdd:cd03296 224 VYDHPA 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
313-530 |
1.03e-32 |
|
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: 124.83 E-value: 1.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLN----PvWLR 388
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiP-YLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 SKIGTVSQE-PILFSCSIAENIAYgADDPSSVTAEEIQ-RVAEVANAVAF---IRNFPQGfntvvgekgvlLSGGQKQRI 463
Cdd:cd03292 78 RKIGVVFQDfRLLPDRNVYENVAF-ALEVTGVPPREIRkRVPAALELVGLshkHRALPAE-----------LSGGEQQRV 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 464 AIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 530
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
313-551 |
1.18e-32 |
|
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: 131.35 E-value: 1.18e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPAR--------PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLyDPASGTISLDGHDI----- 379
Cdd:COG4172 276 LEARDLKVWFPIKrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLdglsr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 380 RQLNPvwLRSKIGTVSQEPilFSC-----SIAENIAYG--ADDPSSVTAEEIQRVAEVANAV----AFIRNFPQGFntvv 448
Cdd:COG4172 355 RALRP--LRRRMQVVFQDP--FGSlsprmTVGQIIAEGlrVHGPGLSAAERRARVAEALEEVgldpAARHRYPHEF---- 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 449 gekgvllSGGQKQRIAIARALLKNPKILLLDEATSALDAeneyLVQ-EALDRLMD-----GRTVLVIAHRLSTIKN-ANM 521
Cdd:COG4172 427 -------SGGQRQRIAIARALILEPKLLVLDEPTSALDV----SVQaQILDLLRDlqrehGLAYLFISHDLAVVRAlAHR 495
|
250 260 270
....*....|....*....|....*....|.
gi 767912302 522 VAVLDQGKITEYGKHEELLSKPNGIY-RKLM 551
Cdd:COG4172 496 VMVMKDGKVVEQGPTEQVFDAPQHPYtRALL 526
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
312-544 |
2.14e-32 |
|
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: 124.81 E-value: 2.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASG-TISLDGHDIRQLNPVWLRSK 390
Cdd:COG1119 3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVS---QEPILFSCSIAENIAYGADD----PSSVTAEEIQRVAEVANAVAFI----RNFPQgfntvvgekgvlLSGGQ 459
Cdd:COG1119 80 IGLVSpalQLRFPRDETVLDVVLSGFFDsiglYREPTDEQRERARELLELLGLAhladRPFGT------------LSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 460 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNA-NMVAVLDQGKITEYGKH 536
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPK 227
|
....*...
gi 767912302 537 EELLSKPN 544
Cdd:COG1119 228 EEVLTSEN 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
313-543 |
2.71e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 124.43 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNV--HFAyparpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR--QLNPVWLR 388
Cdd:PRK09493 2 IEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 SKIGTVSQEPILFSCSIA-ENIAYGaddP------SSVTAEEIQR-------VAEVANavafirNFPqgfntvvGEkgvl 454
Cdd:PRK09493 77 QEAGMVFQQFYLFPHLTAlENVMFG---PlrvrgaSKEEAEKQARellakvgLAERAH------HYP-------SE---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 455 LSGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALdRLM-----DGRTVLVIAHRLS-TIKNANMVAVLDQG 528
Cdd:PRK09493 137 LSGGQQQRVAIARALAVKPKLMLFDEPTSALDPE---LRHEVL-KVMqdlaeEGMTMVIVTHEIGfAEKVASRLIFIDKG 212
|
250
....*....|....*
gi 767912302 529 KITEYGKHEELLSKP 543
Cdd:PRK09493 213 RIAEDGDPQVLIKNP 227
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
313-541 |
1.15e-31 |
|
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: 121.77 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-VWLRSKI 391
Cdd:cd03224 1 LEVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEPILF-SCSIAENIAYGADD-PSSVTAEEIQRVAEVanavafirnFPqgfntVVGE----KGVLLSGGQKQRIAI 465
Cdd:cd03224 78 GYVPEGRRIFpELTVEENLLLGAYArRRAKRKARLERVYEL---------FP-----RLKErrkqLAGTLSGGEQQMLAI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 466 ARALLKNPKILLLDEATSALdAENeyLVQEALDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELL 540
Cdd:cd03224 144 ARALMSRPKLLLLDEPSEGL-APK--IVEEIFEAIRElrdeGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220
|
.
gi 767912302 541 S 541
Cdd:cd03224 221 A 221
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
63-551 |
1.78e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 130.48 E-value: 1.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 63 RIVNRLRTSLFSSILRQEVAFFDKTR----TGELINRLSSDTALLgRSVTENLSdGLRAgAQASVGISMMFF-----VSP 133
Cdd:PLN03232 367 RVGFRLRSTLVAAIFHKSLRLTHEARknfaSGKVTNMITTDANAL-QQIAEQLH-GLWS-APFRIIVSMVLLyqqlgVAS 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 134 NLATFVLSVVPPVSIIAViygRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEA 213
Cdd:PLN03232 444 LFGSLILFLLIPLQTLIV---RKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQGIRNEELSWFRKAQ 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 214 FARAgfFGATGLSGNLIVLSVLYKGG-LLMGSAHMTVGELSSFLMYAFwVGISIGGLSSFYSELMKGLGAGGRLWELLER 292
Cdd:PLN03232 521 LLSA--FNSFILNSIPVVVTLVSFGVfVLLGGDLTPARAFTSLSLFAV-LRSPLNMLPNLLSQVVNANVSLQRIEELLLS 597
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 293 EPKL-----PFNEGVilneksfqGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDP 367
Cdd:PLN03232 598 EERIlaqnpPLQPGA--------PAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 368 ASGTisldghdirqlnPVWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSvtaeeiqRVAEVANAVAFIRN---FPQGF 444
Cdd:PLN03232 670 AETS------------SVVIRGSVAYVPQVSWIFNATVRENILFGSDFESE-------RYWRAIDVTALQHDldlLPGRD 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 445 NTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLV-QEALDRLMDGRTVLVIAHRLSTIKNANMVA 523
Cdd:PLN03232 731 LTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVfDSCMKDELKGKTRVLVTNQLHFLPLMDRII 810
|
490 500
....*....|....*....|....*...
gi 767912302 524 VLDQGKITEYGKHEElLSKPNGIYRKLM 551
Cdd:PLN03232 811 LVSEGMIKEEGTFAE-LSKSGSLFKKLM 837
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
32-258 |
1.84e-31 |
|
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: 123.78 E-value: 1.84e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 32 LTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENL 111
Cdd:cd18564 53 LLLAAAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 112 SDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKE 191
Cdd:cd18564 133 LPLLTNLLTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGRE 212
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 192 MTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMY 258
Cdd:cd18564 213 EHEERRFARENRKSLRAGLRAARLQALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAY 279
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
333-543 |
1.90e-31 |
|
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: 124.83 E-value: 1.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 333 DFSLSIPSGSVTALVGPSGSGKSTVLSL---LLRlydPASGTISLDGH-----DIRQLNPVWLRSkIGTVSQEPILFS-C 403
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEvlqdsARGIFLPPHRRR-IGYVFQEARLFPhL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 404 SIAENIAYGADD-PSSVTAEEIQRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEAT 482
Cdd:COG4148 93 SVRGNLLYGRKRaPRAERRISFDEVVELLGIGHLLDRRPAT-----------LSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 483 SALDAENEYLVQEALDRLMD--GRTVLVIAH------RLstiknANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:COG4148 162 AALDLARKAEILPYLERLRDelDIPILYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
306-547 |
3.05e-31 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 124.95 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 306 EKSFQGALEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPv 385
Cdd:PRK11607 13 RKALTPLLEIRNLTKSFDGQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 386 wLRSKIGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFirnfpQGFntvVGEKGVLLSGGQKQRIA 464
Cdd:PRK11607 89 -YQRPINMMFQSYALFPhMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHM-----QEF---AKRKPHQLSGGQRQRVA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 465 IARALLKNPKILLLDEATSALDAE----NEYLVQEALDRLmdGRTVLVIAH-RLSTIKNANMVAVLDQGKITEYGKHEEL 539
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDILERV--GVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
....*...
gi 767912302 540 LSKPNGIY 547
Cdd:PRK11607 238 YEHPTTRY 245
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
333-530 |
6.13e-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: 119.52 E-value: 6.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 333 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIGTVSQEPILFS-CSIAENIAY 411
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 412 GADDPSSVTAEEIQRVAEVANAVAFirnfpQGFNTVVGEKgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAEney 491
Cdd:cd03298 94 GLSPGLKLTAEDRQAIEVALARVGL-----AGLEKRLPGE---LSGGERQRVALARVLVRDKPVLLLDEPFAALDPA--- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767912302 492 LVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 530
Cdd:cd03298 163 LRAEMLDLVLDlhaetKMTVLMVTHQPEDAKRlAQRVVFLDNGRI 207
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
313-511 |
6.61e-31 |
|
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: 119.51 E-value: 6.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAypaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 392
Cdd:COG4133 3 LEAENLSCR---RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILF-SCSIAENIAYGAD-DPSSVTAEEIQRVAEVANAVAFIRNFPQgfntvvgekgvLLSGGQKQRIAIARALL 470
Cdd:COG4133 79 YLGHADGLKpELTVRENLRFWAAlYGLRADREAIDEALEAVGLAGLADLPVR-----------QLSAGQKRRVALARLLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767912302 471 KNPKILLLDEATSALDAENEYLVQEALDR-LMDGRTVLVIAH 511
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
312-544 |
1.31e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 120.61 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKI 391
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIA 466
Cdd:PRK13647 82 GLVFQDPddQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVrmwDFRDKPPYH-----------LSYGQKKRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 467 RALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKhEELLSKPN 544
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLhNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTDED 229
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
1-276 |
1.72e-30 |
|
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: 120.65 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIYTNPTVDYsdnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQE 80
Cdd:cd18545 11 LSTAASLAGPYLIKIAIDEYIPNGDLSG---LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 81 VAFFDKTRTGELINRLSSDTallgrsvtENLSDGLRAGAQASVG--------ISMMFFVSPNLATFVLSVVPPVSIIAVI 152
Cdd:cd18545 88 FSFFDSRPVGKILSRVINDV--------NSLSDLLSNGLINLIPdlltlvgiVIIMFSLNVRLALVTLAVLPLLVLVVFL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 153 YGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVL 232
Cdd:cd18545 160 LRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGTA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767912302 233 SVLYKGGLLMGSAHMTVGELSSFLMYA--FWVGISigGLSSFYSEL 276
Cdd:cd18545 240 LVYWYGGKLVLGGAITVGVLVAFIGYVgrFWQPIR--NLSNFYNQL 283
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
313-543 |
1.87e-30 |
|
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: 118.93 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSK-- 390
Cdd:COG0410 4 LEVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL-PPHRIARlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEPILF-SCSIAENI---AYGADDPSSVtAEEIQRVAEVanavafirnFPqgfntVVGE----KGVLLSGGQKQR 462
Cdd:COG0410 80 IGYVPEGRRIFpSLTVEENLllgAYARRDRAEV-RADLERVYEL---------FP-----RLKErrrqRAGTLSGGEQQM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 463 IAIARALLKNPKILLLDEATSALdAENeyLVQE---ALDRLMD-GRTVLV----------IAHRlstiknanmVAVLDQG 528
Cdd:COG0410 145 LAIGRALMSRPKLLLLDEPSLGL-APL--IVEEifeIIRRLNReGVTILLveqnarfaleIADR---------AYVLERG 212
|
250
....*....|....*
gi 767912302 529 KITEYGKHEELLSKP 543
Cdd:COG0410 213 RIVLEGTAAELLADP 227
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
333-544 |
2.22e-30 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 121.76 E-value: 2.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 333 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDG---HDIRQ---LNPVwlRSKIGTVSQEPILFS-CSI 405
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgifLPPE--KRRIGYVFQEARLFPhLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 406 AENIAYG---ADDPSSVTAEEiqRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEAT 482
Cdd:TIGR02142 93 RGNLRYGmkrARPSERRISFE--RVIELLGIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 483 SALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPN 544
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
312-544 |
3.44e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 118.72 E-value: 3.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvWLRSKI 391
Cdd:PRK13548 2 MLEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELARR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 -GTVSQEPIL-FSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFI----RNFPQgfntvvgekgvlLSGGQKQRIAI 465
Cdd:PRK13548 78 rAVLPQHSSLsFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAhlagRDYPQ------------LSGGEQQRVQL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 466 ARALL------KNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLstikN-----ANMVAVLDQGKITE 532
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHerGLAVIVVLHDL----NlaaryADRIVLLHQGRLVA 221
|
250
....*....|..
gi 767912302 533 YGKHEELLSKPN 544
Cdd:PRK13548 222 DGTPAEVLTPET 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-543 |
4.28e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 118.61 E-value: 4.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 330 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH------DIRQLNPVWLRSKIGTVSQEPILFS- 402
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQPNPFPh 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 403 CSIAENIAYGADDPSSVTAEEIQRVAEVA-NAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEA 481
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEEClRKVGLWKEVYDRLNSPASQ----LSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912302 482 TSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTSP 243
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
313-546 |
5.52e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.70 E-value: 5.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPArPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 392
Cdd:PRK13648 8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPI-LFSCSIAE-NIAYGADDpSSVTAEEIQR-VAEVANAVAFI--RNF-PQGfntvvgekgvlLSGGQKQRIAIA 466
Cdd:PRK13648 87 IVFQNPDnQFVGSIVKyDVAFGLEN-HAVPYDEMHRrVSEALKQVDMLerADYePNA-----------LSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 467 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPN 544
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
..
gi 767912302 545 GI 546
Cdd:PRK13648 235 EL 236
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
327-543 |
8.33e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 117.71 E-value: 8.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 327 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRL---YDPA--SGTISLDGHDIRQLNPVWLRSKIGTVSQEP-IL 400
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielYPEArvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 401 FSCSIAENIAYGADDPSSVT--AEEIQRVAEVANAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLL 478
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLVKskKELQERVRWALEKAQLWDEVKDRLDAPAGK----LSGGQQQRLCIARALAFQPEVLLA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912302 479 DEATSALDAENEYLVQEALDRLMDGRTVLVIAH------RLStiknaNMVAVLDQGKITEYGKHEELLSKP 543
Cdd:PRK14247 171 DEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
312-542 |
8.66e-30 |
|
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: 125.06 E-value: 8.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYpARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDpasgtiSLDGHdirqlnpVWLRSKI 391
Cdd:TIGR00957 636 SITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMD------KVEGH-------VHMKGSV 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEPILFSCSIAENIAYGaddpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLK 471
Cdd:TIGR00957 702 AYVPQQAWIQNDSLRENILFG----KALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYS 777
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912302 472 NPKILLLDEATSALDAE-NEYLVQEAL--DRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSK 542
Cdd:TIGR00957 778 NADIYLFDDPLSAVDAHvGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
335-543 |
8.71e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.57 E-value: 8.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 335 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD-----PASGTISLDGHDI--RQLNPVWLRSKIGTVSQEPILFSCSIAE 407
Cdd:PRK14239 25 SLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIysPRTDTVDLRKEIGMVFQQPNPFPMSIYE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 408 NIAYGADDPSSVTAEEIQRVAEVANAVAFIrnfpqgFNTV---VGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSA 484
Cdd:PRK14239 105 NVVYGLRLKGIKDKQVLDEAVEKSLKGASI------WDEVkdrLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912302 485 LDAENEYLVQEALDRLMDGRTVLVIAHRL---STIknANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:PRK14239 179 LDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
313-525 |
8.93e-30 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 116.74 E-value: 8.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 392
Cdd:PRK10247 8 LQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFSCSIAENIAYgaddPSSVTAEEIQRVAEVANAVAFirNFPQgfNTVvgEKGV-LLSGGQKQRIAIARALLK 471
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIF----PWQIRNQQPDPAIFLDDLERF--ALPD--TIL--TKNIaELSGGEKQRISLIRNLQF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 472 NPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTIKNANMVAVL 525
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITL 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
313-544 |
1.43e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 117.91 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpVW-LRSKI 391
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEN-VWdIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFirnfpQGFNTvvgEKGVLLSGGQKQRIAIARAL 469
Cdd:PRK13650 84 GMVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGM-----QDFKE---REPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 470 LKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPN 544
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
324-488 |
2.00e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 115.27 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 324 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDP---ASGTISLDGHDIRQLNPvwLRSKIGTVSQEPIL 400
Cdd:COG4136 10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA--EQRRIGILFQDDLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 401 FS-CSIAENIAYGAddPSSVTAEeiQRVAEVANAVA------FIRNFPqgfNTvvgekgvlLSGGQKQRIAIARALLKNP 473
Cdd:COG4136 88 FPhLSVGENLAFAL--PPTIGRA--QRRARVEQALEeaglagFADRDP---AT--------LSGGQRARVALLRALLAEP 152
|
170
....*....|....*
gi 767912302 474 KILLLDEATSALDAE 488
Cdd:COG4136 153 RALLLDEPFSKLDAA 167
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
332-543 |
4.40e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 116.03 E-value: 4.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD-----PASGTISLDGHDI--RQLNPVWLRSKIGTVSQEPILFSCS 404
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 405 IAENIAYGAD------DPSSVTAEEIQRVA---EVANAVAfirnfpqgfntvvgEKGVLLSGGQKQRIAIARALLKNPKI 475
Cdd:PRK14243 107 IYDNIAYGARingykgDMDELVERSLRQAAlwdEVKDKLK--------------QSGLSLSGGQQQRLCIARAIAVQPEV 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912302 476 LLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRL-STIKNANMVAVLD---------QGKITEYGKHEELLSKP 543
Cdd:PRK14243 173 ILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMqQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSP 250
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
333-547 |
8.33e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 117.51 E-value: 8.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 333 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlnpvwlRS----KIGTVSQEPILFS-CSIAE 407
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSiqqrDICMVFQSYALFPhMSLGE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 408 NIAYGAdDPSSVTAEEI-QRVAEVANAVAFIrnfpqGFntvvGEKGV-LLSGGQKQRIAIARALLKNPKILLLDEATSAL 485
Cdd:PRK11432 98 NVGYGL-KMLGVPKEERkQRVKEALELVDLA-----GF----EDRYVdQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 486 DAENEYLVQEALDRLMD--GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKPNGIY 547
Cdd:PRK11432 168 DANLRRSMREKIRELQQqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRF 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
332-530 |
8.41e-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: 114.46 E-value: 8.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKIGTVS--QEPILF-SCSIAEN 408
Cdd:cd03219 17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELTVLEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 409 IAYGA-------DDPSSVTAEEIQRVAEVANAVAFIRNFPQGfNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEA 481
Cdd:cd03219 96 VMVAAqartgsgLLLARARREEREARERAEELLERVGLADLA-DRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767912302 482 TSALDAEneyLVQEALDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 530
Cdd:cd03219 171 AAGLNPE---ETEELAELIRElrerGITVLLVEHDMDVVMSlADRVTVLDQGRV 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
333-534 |
9.70e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 113.54 E-value: 9.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 333 DFSLSIP---SGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDG---HDIRQ---LNPVwlRSKIGTVSQEPILFS- 402
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKkinLPPQ--QRKIGLVFQQYALFPh 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 403 CSIAENIAYGADDPSSvtAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEAT 482
Cdd:cd03297 90 LNVRENLAFGLKRKRN--REDRISVDELLDLL--------GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 483 SALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYG 534
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
313-534 |
1.43e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 113.12 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIG 392
Cdd:cd03301 1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILF-SCSIAENIAYG---ADDPSSVTAEEIQRVAEVAnavafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARA 468
Cdd:cd03301 76 MVFQNYALYpHMTVYDNIAFGlklRKVPKDEIDERVREVAELL-----------QIEHLLDRKPKQLSGGQRQRVALGRA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 469 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAH-RLSTIKNANMVAVLDQGKITEYG 534
Cdd:cd03301 145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQrlGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
313-541 |
2.94e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 113.57 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 392
Cdd:PRK11231 3 LRTENLTVGYGTKR---ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQ-----EPIlfscSIAENIAYG------------ADDPSSVT-AEEIQRVAEVAnavafirnfpqgfntvvgEKGVL 454
Cdd:PRK11231 80 LLPQhhltpEGI----TVRELVAYGrspwlslwgrlsAEDNARVNqAMEQTRINHLA------------------DRRLT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 455 -LSGGQKQRIAIARALLKNPKILLLDEATSALDAENeylvQEALDRLM-----DGRTVLVIAHRLS-TIKNANMVAVLDQ 527
Cdd:PRK11231 138 dLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINH----QVELMRLMrelntQGKTVVTVLHDLNqASRYCDHLVVLAN 213
|
250
....*....|....
gi 767912302 528 GKITEYGKHEELLS 541
Cdd:PRK11231 214 GHVMAQGTPEEVMT 227
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
313-486 |
2.96e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 116.20 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIG 392
Cdd:PRK09452 15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFS-CSIAENIAYGADdPSSVTAEEIQ-RVAEvanAVAFIR--NFPQgfntvvgEKGVLLSGGQKQRIAIARA 468
Cdd:PRK09452 90 TVFQSYALFPhMTVFENVAFGLR-MQKTPAAEITpRVME---ALRMVQleEFAQ-------RKPHQLSGGQQQRVAIARA 158
|
170
....*....|....*...
gi 767912302 469 LLKNPKILLLDEATSALD 486
Cdd:PRK09452 159 VVNKPKVLLLDESLSALD 176
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
2-275 |
4.49e-28 |
|
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: 113.73 E-value: 4.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVIYTNPTvdySDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEV 81
Cdd:cd18543 11 ATLAGLAIPLLTRRAIDGPIAHGD---RSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 82 AFFDKTRTGELINRLSSDTALLGRSvtenLSDGLRA---GAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLR 158
Cdd:cd18543 88 AFHDRWQSGQLLSRATSDLSLVQRF----LAFGPFLlgnLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 159 KLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKG 238
Cdd:cd18543 164 PASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALG 243
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767912302 239 GLLMGSAHMTVGELSSFLMYAF---WVGISIGGLSSFYSE 275
Cdd:cd18543 244 GWLVANGSLTLGTLVAFSAYLTmlvWPVRMLGWLLAMAQR 283
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
326-528 |
4.58e-28 |
|
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: 111.65 E-value: 4.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 326 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTI----SLDGHDIRQLNPVWLRSKIGTVSQEPILF 401
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 402 SCSIAENIAYGaddpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEA 481
Cdd:cd03290 92 NATVEENITFG----SPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767912302 482 TSALDAE-NEYLVQEALDRLM--DGRTVLVIAHRLSTIKNANMVAVLDQG 528
Cdd:cd03290 168 FSALDIHlSDHLMQEGILKFLqdDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
285-512 |
5.08e-28 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 117.99 E-value: 5.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 285 RLWEL---LEREPKLPFNEGVIlnEKSFQGALEFKNVHFAYPArpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTvlslL 361
Cdd:COG4178 334 RLAGFeeaLEAADALPEAASRI--ETSEDGALALEDLTLRTPD--GRPLLEDLSLSLKPGERLLITGPSGSGKST----L 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 362 LR----LYDPASGTISL-DGHDIrqlnpVWLrskigtvSQEPILFSCSIAENIAYgADDPSSVTAEEIQRV------AEV 430
Cdd:COG4178 406 LRaiagLWPYGSGRIARpAGARV-----LFL-------PQRPYLPLGTLREALLY-PATAEAFSDAELREAleavglGHL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 431 ANAVAFIRNFPQgfntvvgekgvLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIA 510
Cdd:COG4178 473 AERLDEEADWDQ-----------VLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVG 541
|
..
gi 767912302 511 HR 512
Cdd:COG4178 542 HR 543
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
30-552 |
5.32e-28 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 119.50 E-value: 5.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 30 DNLTRLCLGLSAVFLcGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTE 109
Cdd:PTZ00243 996 SAATYLYVYLGIVLL-GTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPM 1074
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 110 NLSDGLRAGAQASVGISMMFFVSPnlatFVLSVVPPVSI----IAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTV 185
Cdd:PTZ00243 1075 SYLYLLQCLFSICSSILVTSASQP----FVLVALVPCGYlyyrLMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATI 1150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 186 RAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKG--GLLMGSAHMTVGELSSFLMYAF--- 260
Cdd:PTZ00243 1151 TAYGKAHLVMQEALRRLDVVYSCSYLENVANRWLGVRVEFLSNIVVTVIALIGviGTMLRATSQEIGLVSLSLTMAMqtt 1230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 261 ----W----VGISIGGLSS-----FYS-----ELMKGLGAggrLWELLEREPKLPFN-EGVILNEKSF----------QG 311
Cdd:PTZ00243 1231 atlnWlvrqVATVEADMNSverllYYTdevphEDMPELDE---EVDALERRTGMAADvTGTVVIEPASptsaaphpvqAG 1307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYpaRPEVP-IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSK 390
Cdd:PTZ00243 1308 SLVFEGVQMRY--REGLPlVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ 1385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEPILFSCSIAENIaygadDP-SSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARAL 469
Cdd:PTZ00243 1386 FSMIPQDPVLFDGTVRQNV-----DPfLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARAL 1460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 470 LK-NPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYR 548
Cdd:PTZ00243 1461 LKkGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFH 1540
|
....
gi 767912302 549 KLMN 552
Cdd:PTZ00243 1541 SMVE 1544
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1-273 |
1.00e-27 |
|
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: 113.02 E-value: 1.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIyTNPTVDySDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQE 80
Cdd:cd18778 10 LSTLLGLVPPWLIRELVDLV-TIGSKS-LGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 81 VAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQAsVGIS-MMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRK 159
Cdd:cd18778 88 LRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTL-VGVAiILFSINPKLALLTLIPIPFLALGAWLYSKKVRP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 160 LTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGG 239
Cdd:cd18778 167 RYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVLVLGFGG 246
|
250 260 270
....*....|....*....|....*....|....
gi 767912302 240 LLMGSAHMTVGELSSFLMYafwvgisiggLSSFY 273
Cdd:cd18778 247 RLVLAGELTIGDLVAFLLY----------LGLFY 270
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
2-258 |
1.02e-27 |
|
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: 112.97 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIID--VIYTNPTVdysdnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQ 79
Cdd:cd18546 11 DTAASLAGPLLVRYGIDsgVRAGDLGV-----LLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 80 EVAFFDKTRTGELINRLSSDTAllgrSVTENLSDGLRAGAQAS---VGIS-MMFFVSPNLATFVLSVVPPVSIIAVIYGR 155
Cdd:cd18546 86 SLDFHERETSGRIMTRMTSDID----ALSELLQTGLVQLVVSLltlVGIAvVLLVLDPRLALVALAALPPLALATRWFRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 156 YLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVL 235
Cdd:cd18546 162 RSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIYFPGVELLGNLATAAVL 241
|
250 260
....*....|....*....|...
gi 767912302 236 YKGGLLMGSAHMTVGELSSFLMY 258
Cdd:cd18546 242 LVGAWRVAAGTLTVGVLVAFLLY 264
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
332-530 |
1.21e-27 |
|
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: 111.67 E-value: 1.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvWLRSKIGtVS---QEPILF-SCSIAE 407
Cdd:COG0411 21 DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPP-HRIARLG-IArtfQNPRLFpELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 408 NIAYGAD------------DPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKI 475
Cdd:COG0411 99 NVLVAAHarlgrgllaallRLPRARREEREARERAEELLERV-----GLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912302 476 LLLDEATSALDAEneyLVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 530
Cdd:COG0411 174 LLLDEPAAGLNPE---ETEELAELIRRlrderGITILLIEHDMDLVMGlADRIVVLDFGRV 231
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
332-530 |
1.59e-27 |
|
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: 110.00 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWlrSKIGTVSQEPILF-SCSIAENIA 410
Cdd:cd03268 17 DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIGALIEAPGFYpNLTARENLR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 411 YGADDPsSVTAEEIQRVAEVAnavafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENE 490
Cdd:cd03268 95 LLARLL-GIRKKRIDEVLDVV-----------GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 767912302 491 YLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKI 530
Cdd:cd03268 163 KELRELILSLRDqGITVLISSHLLSEIqKVADRIGIINKGKL 204
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
1-258 |
1.66e-27 |
|
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: 112.16 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQE 80
Cdd:cd18549 13 LIAALDLVFPLIVRYIIDDLLPSKNLR---LILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQKLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 81 VAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKL 160
Cdd:cd18549 90 FSFFDNNKTGQLMSRITNDLFDISELAHHGPEDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 161 TKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVmQLARKEAF-ARAGFFGATGLSGNLIVLSVLYKGG 239
Cdd:cd18549 170 FRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGNDRF-LESKKKAYkAMAYFFSGMNFFTNLLNLVVLVAGG 248
|
250
....*....|....*....
gi 767912302 240 LLMGSAHMTVGELSSFLMY 258
Cdd:cd18549 249 YFIIKGEITLGDLVAFLLY 267
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
312-511 |
1.83e-27 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 111.49 E-value: 1.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPA-RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlnPVWLRsk 390
Cdd:COG4525 3 MLTVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 iGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFirnfpQGFntvvGEKGVL-LSGGQKQRIAIARA 468
Cdd:COG4525 79 -GVVFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEELLALVGL-----ADF----ARRRIWqLSGGMRQRVGIARA 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767912302 469 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAH 511
Cdd:COG4525 149 LAADPRFLLMDEPFGALDALTREQMQELLLDVWQrtGKGVFLITH 193
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
313-534 |
2.92e-27 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 108.79 E-value: 2.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARP---EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL--LRLYDPASGTISLDGHDIRqlnPVWL 387
Cdd:cd03213 4 LSFRNLTVTVKSSPsksGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 388 RSKIGTVSQEPILFSC-SIAENIAYGAddpssvtaeEIQRvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIA 466
Cdd:cd03213 81 RKIIGYVPQDDILHPTlTVRETLMFAA---------KLRG----------------------------LSGGERKRVSIA 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912302 467 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLST--IKNANMVAVLDQGKITEYG 534
Cdd:cd03213 124 LELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
313-531 |
2.93e-27 |
|
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: 107.51 E-value: 2.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSKI 391
Cdd:cd03216 1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdARRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQepilfscsiaeniaygaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvlLSGGQKQRIAIARALLK 471
Cdd:cd03216 78 AMVYQ----------------------------------------------------------LSVGERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912302 472 NPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKIT 531
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRLRAqGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
313-530 |
3.52e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 110.56 E-value: 3.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVH--FaYPARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRS 389
Cdd:COG1101 2 LELKNLSktF-NPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 K-IGTVSQEPILFSC---SIAEN--IAYGADDP----SSVTAEEIQRVAEvanavaFIRNFPQGF----NTVVGekgvLL 455
Cdd:COG1101 80 KyIGRVFQDPMMGTApsmTIEENlaLAYRRGKRrglrRGLTKKRRELFRE------LLATLGLGLenrlDTKVG----LL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912302 456 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKI 530
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
324-552 |
4.20e-27 |
|
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: 110.28 E-value: 4.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 324 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVW---LRSKIGTVSQEpil 400
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQD--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 401 fscsiaeniAYGADDPSSvTAEEI-----------------QRVAEVANAVAF----IRNFPQGFntvvgekgvllSGGQ 459
Cdd:TIGR02769 97 ---------SPSAVNPRM-TVRQIigeplrhltsldeseqkARIAELLDMVGLrsedADKLPRQL-----------SGGQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 460 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKH 536
Cdd:TIGR02769 156 LQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDV 235
|
250
....*....|....*.
gi 767912302 537 EELLSKPNGIYRKLMN 552
Cdd:TIGR02769 236 AQLLSFKHPAGRNLQS 251
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
312-532 |
7.50e-27 |
|
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: 108.68 E-value: 7.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYP-ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLN----PVW 386
Cdd:COG4181 8 IIELRGLTKTVGtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 387 LRSKIGTVSQ-EPILFSCSIAENIAY-----GADDPSSVTAEEIQRV--AEVANAvafirnFPQGfntvvgekgvlLSGG 458
Cdd:COG4181 88 RARHVGFVFQsFQLLPTLTALENVMLplelaGRRDARARARALLERVglGHRLDH------YPAQ-----------LSGG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 459 QKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKITE 532
Cdd:COG4181 151 EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRerGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
330-543 |
1.08e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 111.33 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 330 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwlRS-KIGTVSQEPILFS-CSIAE 407
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDrKVGFVFQHYALFRhMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 408 NIAYGA------DDPSSvtAEEIQRVAEVANAVAFIR---NFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLL 478
Cdd:PRK10851 94 NIAFGLtvlprrERPNA--AAIKAKVTQLLEMVQLAHladRYPAQ-----------LSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912302 479 DEATSALDAEneylVQEALDRLMdgR---------TVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:PRK10851 161 DEPFGALDAQ----VRKELRRWL--RqlheelkftSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREP 228
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
10-266 |
1.23e-26 |
|
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: 109.80 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 10 PFFLGKIIDVIYTNPTVDYsdnLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRT 89
Cdd:cd18548 19 PTLMADIIDEGIANGDLSY---ILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKFGT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 90 GELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLA 169
Cdd:cd18548 96 SSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 170 QATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTV 249
Cdd:cd18548 176 RLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQV 255
|
250
....*....|....*..
gi 767912302 250 GELSSFLMYAFWVGISI 266
Cdd:cd18548 256 GDLVAFINYLMQILMSL 272
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
313-544 |
1.57e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 109.34 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYpaRPEVPiFQ-----DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI------RQ 381
Cdd:PRK13634 3 ITFQKVEHRY--QYKTP-FErralyDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkknKK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 382 LNPvwLRSKIGTVSQ--EPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVL-LSGG 458
Cdd:PRK13634 80 LKP--LRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELV--------GLPEELLARSPFeLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 459 QKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGK 535
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHkeKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGT 229
|
....*....
gi 767912302 536 HEELLSKPN 544
Cdd:PRK13634 230 PREIFADPD 238
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
315-533 |
2.08e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.85 E-value: 2.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 315 FKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhDIRqlnpvwlrskIGTV 394
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 395 SQEPILFS-CSIAENIAYGADDPSSVTAE-------------------EIQ-------------RVAEVANAVafirNFP 441
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELRALEAEleeleaklaepdedlerlaELQeefealggweaeaRAEEILSGL----GFP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 442 QG-FNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-----EYLVQEaldrlmDGrTVLVIAH-R-- 512
Cdd:COG0488 143 EEdLDRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNY------PG-TVLVVSHdRyf 211
|
250 260
....*....|....*....|.
gi 767912302 513 LSTIknANMVAVLDQGKITEY 533
Cdd:COG0488 212 LDRV--ATRILELDRGKLTLY 230
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
312-537 |
3.15e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 107.41 E-value: 3.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI---RQLNP---V 385
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEkaiR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 386 WLRSKIGTVSQE----PILfscSIAENIAygaDDPSSV---TAEEIQRVAEVANAVAFIRNFPQGFNtvvgekgVLLSGG 458
Cdd:COG4161 79 LLRQKVGMVFQQynlwPHL---TVMENLI---EAPCKVlglSKEQAREKAMKLLARLRLTDKADRFP-------LHLSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 459 QKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKH 536
Cdd:COG4161 146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFArKVASQVVYMEKGRIIEQGDA 225
|
.
gi 767912302 537 E 537
Cdd:COG4161 226 S 226
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
312-535 |
3.88e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.91 E-value: 3.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPA-RP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI------RQLN 383
Cdd:PRK13649 2 GINLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsknKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 384 PVwlRSKIGTVSQ--EPILFSCSIAENIAYGADDpSSVTAEEIQRVA-EVANAVAFIRNFpqgFNTVVGEkgvlLSGGQK 460
Cdd:PRK13649 82 QI--RKKVGLVFQfpESQLFEETVLKDVAFGPQN-FGVSQEEAEALArEKLALVGISESL---FEKNPFE----LSGGQM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 461 QRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGK 535
Cdd:PRK13649 152 RRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
312-539 |
4.81e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.65 E-value: 4.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSK 390
Cdd:COG1129 4 LLEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRdAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEPILFSC-SIAENIAYGADDPSSVT---AEEIQRVAEVANAVafirnfpqGFN----TVVGEkgvlLSGGQKQR 462
Cdd:COG1129 81 IAIIHQELNLVPNlSVAENIFLGREPRRGGLidwRAMRRRARELLARL--------GLDidpdTPVGD----LSVAQQQL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 463 IAIARALLKNPKILLLDEATSAL-DAENEYLVqEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEEL 539
Cdd:COG1129 149 VEIARALSRDARVLILDEPTASLtEREVERLF-RIIRRLKAqGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
313-542 |
5.03e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 107.87 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPE---VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVW-LR 388
Cdd:PRK13633 5 IKCKNVSYKYESNEEsteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 SKIGTVSQEP--ILFSCSIAENIAYGADDpSSVTAEEIQ-RVAEVANAVA---FIRNFPQgfntvvgekgvLLSGGQKQR 462
Cdd:PRK13633 85 NKAGMVFQNPdnQIVATIVEEDVAFGPEN-LGIPPEEIReRVDESLKKVGmyeYRRHAPH-----------LLSGGQKQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 463 IAIARALLKNPKILLLDEATSALDAENEylvQEALDRLMD-----GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHE 537
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGR---REVVNTIKElnkkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
....*
gi 767912302 538 ELLSK 542
Cdd:PRK13633 230 EIFKE 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
334-541 |
6.65e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 106.20 E-value: 6.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 334 FSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIGTVSQEPILFS-CSIAENIAYG 412
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 413 ADDPSSVTAEEIQRVAEVANAVaFIRNFpqgFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDA--ENE 490
Cdd:PRK10771 96 LNPGLKLNAAQREKLHAIARQM-GIEDL---LARLPGQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPalRQE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767912302 491 YLvqEALDRLMDGR--TVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLS 541
Cdd:PRK10771 168 ML--TLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
332-531 |
7.65e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.89 E-value: 7.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-VWLRSKIGTVSQEPILF-SCSIAENI 409
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrDAIALGIGMVHQHFMLVpNLTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 410 AYGADDPSSV---TAEEIQRVAEVANAVafirnfpqGF----NTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEAT 482
Cdd:COG3845 102 VLGLEPTKGGrldRKAARARIRELSERY--------GLdvdpDAKVED----LSVGEQQRVEILKALYRGARILILDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767912302 483 SALDAeneylvQEAlDRLMD--------GRTVLVIAHRLSTIK-NANMVAVLDQGKIT 531
Cdd:COG3845 170 AVLTP------QEA-DELFEilrrlaaeGKSIIFITHKLREVMaIADRVTVLRRGKVV 220
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
330-542 |
8.53e-26 |
|
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: 106.86 E-value: 8.53e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 330 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDpASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENI 409
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 410 aygadDPSSV-TAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 488
Cdd:cd03289 98 -----DPYGKwSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767912302 489 NEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSK 542
Cdd:cd03289 173 TYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
37-539 |
8.95e-26 |
|
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: 111.04 E-value: 8.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 37 LGLSAVFLcgaAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVtENLSDGLR 116
Cdd:COG4615 55 AGLLVLLL---LSRLASQLLLTRLGQHAVARLRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAF-VRLPELLQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 117 AGAQASVGISMMFFVSPNLATFVLSVVppvSIIAVIYGRYLRKLTKvtqdSLAQATQLAEERIGNVRTV----------R 186
Cdd:COG4615 131 SVALVLGCLAYLAWLSPPLFLLTLVLL---GLGVAGYRLLVRRARR----HLRRAREAEDRLFKHFRALlegfkelklnR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 187 AFGKEMTEiEKYASKVDHVMQLaRKEAFAragFFGATGLSGNLIVLSVLykGGLLMGSAHMTVGELSSFLMYA----FWV 262
Cdd:COG4615 204 RRRRAFFD-EDLQPTAERYRDL-RIRADT---IFALANNWGNLLFFALI--GLILFLLPALGWADPAVLSGFVlvllFLR 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 263 GiSIGGLSSFYSELMKGLGAGGRLWEL---LEREPKLPFNEGVILNEKSFQgALEFKNVHFAYPARPEVPIFQ--DFSLS 337
Cdd:COG4615 277 G-PLSQLVGALPTLSRANVALRKIEELelaLAAAEPAAADAAAPPAPADFQ-TLELRGVTYRYPGEDGDEGFTlgPIDLT 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 338 IPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFscsiaENIaYGADDPs 417
Cdd:COG4615 355 IRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLF-----DRL-LGLDGE- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 418 sVTAEEIQ---RVAEVANAVAFirnfpqgfntvvgEKGVL----LSGGQKQRIAIARALLKNPKILLLDEATSALDAEN- 489
Cdd:COG4615 428 -ADPARARellERLELDHKVSV-------------EDGRFsttdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFr 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 490 EYLVQEALDRLMD-GRTVLVIAH---------RLstIKnanmvavLDQGKITEYGKHEEL 539
Cdd:COG4615 494 RVFYTELLPELKArGKTVIAISHddryfdladRV--LK-------MDYGKLVELTGPAAL 544
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
313-530 |
1.25e-25 |
|
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: 104.89 E-value: 1.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIG 392
Cdd:cd03263 1 LQIRNLTKTYK-KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFS-CSIAENIAYGAddpsSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIAIARALLK 471
Cdd:cd03263 79 YCPQFDALFDeLTVREHLRFYA----RLKGLPKSEIKEEVELLLRVLGLTDKANKRART----LSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 472 NPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKI 530
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKL 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
336-543 |
1.36e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.60 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 336 LSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV--------WLRSKIGTVSQEPILFSC-SIA 406
Cdd:PRK11264 24 LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSLsqqkglirQLRQHVGFVFQNFNLFPHrTVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 407 ENIAYGaddPSSVTAEEiqRVAEVANAVAFIRNfpqgfntvVGEKGV------LLSGGQKQRIAIARALLKNPKILLLDE 480
Cdd:PRK11264 104 ENIIEG---PVIVKGEP--KEEATARARELLAK--------VGLAGKetsyprRLSGGQQQRVAIARALAMRPEVILFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912302 481 ATSALDAEneyLVQEALDRLM----DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:PRK11264 171 PTSALDPE---LVGEVLNTIRqlaqEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFADP 235
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
322-550 |
1.64e-25 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 111.79 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 322 YPARPEVpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTisldghdirqlnpVWLRSKIGTVSQEPILF 401
Cdd:PTZ00243 668 FELEPKV-LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGR-------------VWAERSIAYVPQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 402 SCSIAENIAYGADDpssvTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEA 481
Cdd:PTZ00243 734 NATVRGNILFFDEE----DAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 482 TSALDAE-NEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPngIYRKL 550
Cdd:PTZ00243 810 LSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS--LYATL 877
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
330-543 |
1.99e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 105.95 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 330 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASG-----TISLDGHDIRQLNPVW-LRSKIGTVSQEPILFSC 403
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLeFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 404 SIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATS 483
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWD---AVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912302 484 ALDAENEYLVQEALDRLMDGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
313-530 |
2.66e-25 |
|
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: 103.99 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAY-PARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKI 391
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALL 470
Cdd:cd03266 81 GFVSDSTGLYDrLTARENLEYFAGLYGLKGDELTARLEELADRL--------GMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912302 471 KNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 530
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRV 214
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
330-543 |
2.77e-25 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 105.05 E-value: 2.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 330 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR-------QLNPV------WLRSKIGTVSQ 396
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKVAdknqlrLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 397 EPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFPQGfntvvgEKGVLLSGGQKQRIAIARALLKNPKI 475
Cdd:PRK10619 100 HFNLWShMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQG------KYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912302 476 LLLDEATSALDAEneyLVQEALdRLM-----DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:PRK10619 174 LLFDEPTSALDPE---LVGEVL-RIMqqlaeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNP 243
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
313-541 |
3.05e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 105.56 E-value: 3.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpVW-LRSKI 391
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN-VWnLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTvvgEKGVLLSGGQKQRIAIARAL 469
Cdd:PRK13642 84 GMVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNML-----DFKT---REPARLSGGQKQRVAVAGII 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912302 470 LKNPKILLLDEATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLS 541
Cdd:PRK13642 156 ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
67-542 |
4.30e-25 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 110.39 E-value: 4.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 67 RLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLR-----AGAQASVGIsmmffvspnLATFVLS 141
Cdd:TIGR01271 959 RLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQltlivLGAIFVVSV---------LQPYIFI 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 142 VVPPVSIIAVIYGRY-LRKLTKVTQDSLAQATQLAEERIGNVR---TVRAFGKE---------------------MTEIE 196
Cdd:TIGR01271 1030 AAIPVAVIFIMLRAYfLRTSQQLKQLESEARSPIFSHLITSLKglwTIRAFGRQsyfetlfhkalnlhtanwflyLSTLR 1109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 197 KYASKVDHVMQLarkeafaragFFGAtglsgnLIVLSVLYKG------GLLMGSAHMtvgeLSSFLMYAFWVGISIGGLS 270
Cdd:TIGR01271 1110 WFQMRIDIIFVF----------FFIA------VTFIAIGTNQdgegevGIILTLAMN----ILSTLQWAVNSSIDVDGLM 1169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 271 SFYSELMKGLGAGGRLWELLEREPKLPFNEGVILNEKSFQ------GALEFKNVHFAYPARPEVpIFQDFSLSIPSGSVT 344
Cdd:TIGR01271 1170 RSVSRVFKFIDLPQEEPRPSGGGGKYQLSTVLVIENPHAQkcwpsgGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRV 1248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 345 ALVGPSGSGKSTVLSLLLRLYDpASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIaygadDP-SSVTAEE 423
Cdd:TIGR01271 1249 GLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNL-----DPyEQWSDEE 1322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 424 IQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDG 503
Cdd:TIGR01271 1323 IWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSN 1402
|
490 500 510
....*....|....*....|....*....|....*....
gi 767912302 504 RTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSK 542
Cdd:TIGR01271 1403 CTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
312-544 |
4.38e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 105.30 E-value: 4.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYParPEVPI----FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR----QLN 383
Cdd:PRK13641 2 SIKFENVDYIYS--PGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgNKN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 384 PVWLRSKIGTVSQ--EPILFSCSIAENIAYGaddPSSVTAEEiQRVAEvaNAVAFIRNFpqGFNTVVGEKGVL-LSGGQK 460
Cdd:PRK13641 80 LKKLRKKVSLVFQfpEAQLFENTVLKDVEFG---PKNFGFSE-DEAKE--KALKWLKKV--GLSEDLISKSPFeLSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 461 QRIAIARALLKNPKILLLDEATSALDAEN-EYLVQEALDRLMDGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEE 538
Cdd:PRK13641 152 RRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKE 231
|
....*.
gi 767912302 539 LLSKPN 544
Cdd:PRK13641 232 IFSDKE 237
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
312-537 |
4.78e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 103.94 E-value: 4.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH-----------DIR 380
Cdd:PRK11124 2 SIQLNGINCFYGAHQ---ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfdfsktpsdkAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 381 QLnpvwlRSKIGTVSQE----PILfscSIAENI------AYGADDPSSVT-AEEI---QRVAEVANAvafirnFPQGfnt 446
Cdd:PRK11124 79 EL-----RRNVGMVFQQynlwPHL---TVQQNLieapcrVLGLSKDQALArAEKLlerLRLKPYADR------FPLH--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 447 vvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAV 524
Cdd:PRK11124 142 --------LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVArKTASRVVY 213
|
250
....*....|...
gi 767912302 525 LDQGKITEYGKHE 537
Cdd:PRK11124 214 MENGHIVEQGDAS 226
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
313-539 |
5.27e-25 |
|
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: 103.37 E-value: 5.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL-RSKI 391
Cdd:TIGR03410 1 LEVSNLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRVAEVanavafirnFPQGFnTVVGEKGVLLSGGQKQRIAIARALL 470
Cdd:TIGR03410 78 AYVPQGREIFPrLTVEENLLTGLAALPRRSRKIPDEIYEL---------FPVLK-EMLGRRGGDLSGGQQQQLAIARALV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912302 471 KNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEEL 539
Cdd:TIGR03410 148 TRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAegGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
332-547 |
5.65e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 107.04 E-value: 5.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS----KIGTVSQEPILFS-CSIA 406
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPhMTVL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 407 ENIAYGAdDPSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALD 486
Cdd:PRK10070 125 DNTAFGM-ELAGINAEERREKALDALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912302 487 AENEYLVQEALDRLM--DGRTVLVIAHRL-STIKNANMVAVLDQGKITEYGKHEELLSKPNGIY 547
Cdd:PRK10070 197 PLIRTEMQDELVKLQakHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
313-542 |
1.13e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 103.77 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH--DIRQLNPVWLRSK 390
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEP--ILFSCSIAENIAYGADDpSSVTAEEIQRVAEVA---NAVAFIRNFPQGFntvvgekgvlLSGGQKQRIAI 465
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVN-LKLPEDEVRKRVDNAlkrTGIEHLKDKPTHC----------LSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 466 ARALLKNPKILLLDEATSALD----AENEYLVQEALDRLmdGRTVLVIAHRLSTIK-NANMVAVLDQGKITEYGKHEELL 540
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVF 230
|
..
gi 767912302 541 SK 542
Cdd:PRK13636 231 AE 232
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
316-538 |
1.21e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.97 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 316 KNVHFAY-PARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI--RQLNPVWLRSKI 391
Cdd:PRK13637 6 ENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRKKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEP--ILFSCSIAENIAYGaddPSS--VTAEEIQ-RVAEVANAVAFirnfpqGFNTVVGEKGVLLSGGQKQRIAIA 466
Cdd:PRK13637 86 GLVFQYPeyQLFEETIEKDIAFG---PINlgLSEEEIEnRVKRAMNIVGL------DYEDYKDKSPFELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 467 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEE 538
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
10-556 |
1.24e-24 |
|
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: 109.23 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 10 PFFLGKIIDVIytNPTVDYSDNLT-RLCLGLSAVFLcgaaanaIRVYLMQTSG---QRIVNRLRTSLFSSI----LRQEV 81
Cdd:TIGR01271 100 PLLLGRIIASY--DPFNAPEREIAyYLALGLCLLFI-------VRTLLLHPAIfglHHLGMQMRIALFSLIykktLKLSS 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 82 AFFDKTRTGELINRLSSDTALLGRSVtenlsdglraGAQASVGIS------MMFFVSPNLATFVLSVVPPVSIIAVIYGR 155
Cdd:TIGR01271 171 RVLDKISTGQLVSLLSNNLNKFDEGL----------ALAHFVWIAplqvilLMGLIWELLEVNGFCGLGFLILLALFQAC 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 156 YLRKLTKVTQDSLAQATQ---LAEERIGNVRTVRAFGKE--MTEIEKYASKVDhvMQLARKEAFARAGFFGATGLSGNLI 230
Cdd:TIGR01271 241 LGQKMMPYRDKRAGKISErlaITSEIIENIQSVKAYCWEeaMEKIIKNIRQDE--LKLTRKIAYLRYFYSSAFFFSGFFV 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 231 VLSVLYKGGLLMGSAHMTVGELSSFLMYafwVGISI-----GGLSSFYSELmkglGAGGRLWELLER------EPKLPFN 299
Cdd:TIGR01271 319 VFLSVVPYALIKGIILRRIFTTISYCIV---LRMTVtrqfpGAIQTWYDSL----GAITKIQDFLCKeeyktlEYNLTTT 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 300 EGVILN-------------EKSFQGALEFK------NVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSL 360
Cdd:TIGR01271 392 EVEMVNvtaswdegigelfEKIKQNNKARKqpngddGLFFSNFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMM 471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 361 LLRLYDPASGTISLDGhdirqlnpvwlrsKIGTVSQEPILFSCSIAENIAYGaddpssVTAEEIqRVAEVANAVAF---I 437
Cdd:TIGR01271 472 IMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNIIFG------LSYDEY-RYTSVIKACQLeedI 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 438 RNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEA-LDRLMDGRTVLVIAHRLSTI 516
Cdd:TIGR01271 532 ALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKEIFEScLCKLMSNKTRILVTSKLEHL 611
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 767912302 517 KNANMVAVLDQGKITEYGKHEELLSKPNGIYRKLMNKQSF 556
Cdd:TIGR01271 612 KKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLGLEAF 651
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
285-553 |
1.30e-24 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 109.06 E-value: 1.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 285 RLWELLERE-----PKLPFNEGvilneksfQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLS 359
Cdd:PLN03130 590 RLEELLLAEervllPNPPLEPG--------LPAISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLIS 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 360 LLLRLYDPASGTIsldghdirqlnpVWLRSKIGTVSQEPILFSCSIAENIAYGADdpssVTAEEIQRVAEVANAVAFIRN 439
Cdd:PLN03130 662 AMLGELPPRSDAS------------VVIRGTVAYVPQVSWIFNATVRDNILFGSP----FDPERYERAIDVTALQHDLDL 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 440 FPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneYLVQEALDRL----MDGRTVLVIAHRLST 515
Cdd:PLN03130 726 LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA---HVGRQVFDKCikdeLRGKTRVLVTNQLHF 802
|
250 260 270
....*....|....*....|....*....|....*....
gi 767912302 516 IKNANMVAVLDQGKITEYGKHEELLSkpNG-IYRKLMNK 553
Cdd:PLN03130 803 LSQVDRIILVHEGMIKEEGTYEELSN--NGpLFQKLMEN 839
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
312-543 |
2.03e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 102.61 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYpARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD-----PASGTISLDGHDI--RQLNP 384
Cdd:PRK14267 4 AIETVNLRVYY-GSNHV--IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 385 VWLRSKIGTVSQEPILFS-CSIAENIAYGADDPSSVTA-EEIQRVAEVA-NAVAFIRNFPQGFNTVVGEkgvlLSGGQKQ 461
Cdd:PRK14267 81 IEVRREVGMVFQYPNPFPhLTIYDNVAIGVKLNGLVKSkKELDERVEWAlKKAALWDEVKDRLNDYPSN----LSGGQRQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 462 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHR-LSTIKNANMVAVLDQGKITEYGKHEELL 540
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
|
...
gi 767912302 541 SKP 543
Cdd:PRK14267 237 ENP 239
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
335-543 |
2.28e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 103.89 E-value: 2.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 335 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI-----------RQ------------LNPvwlRSKI 391
Cdd:PRK11308 35 SFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadpeaqkllRQkiqivfqnpygsLNP---RKKV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEPILFscsiaeNIAYGAddpssvtAEEIQRVAEVANAVA----FIRNFPQGFntvvgekgvllSGGQKQRIAIAR 467
Cdd:PRK11308 112 GQILEEPLLI------NTSLSA-------AERREKALAMMAKVGlrpeHYDRYPHMF-----------SGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 468 ALLKNPKILLLDEATSALDAEneylVQ-EALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELL 540
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVS----VQaQVLNLMMDlqqelGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIF 243
|
...
gi 767912302 541 SKP 543
Cdd:PRK11308 244 NNP 246
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
313-552 |
2.42e-24 |
|
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: 106.69 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKN--VHFAYPARpEVPIFQDFSLSIPSGSVTALVGPSGSGKS-TVLSLLlRLYDP----ASGTISLDGHDIRQLNPV 385
Cdd:COG4172 7 LSVEDlsVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 386 WLR----SKIGTVSQEPI-----LFSCS--IAENIA--YGADDpssvtAEEIQRVAEVANAVAfIRN-------FP-Qgf 444
Cdd:COG4172 85 ELRrirgNRIAMIFQEPMtslnpLHTIGkqIAEVLRlhRGLSG-----AAARARALELLERVG-IPDperrldaYPhQ-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 445 ntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAeneyLVQ-EALDRLMD-----GRTVLVIAHRLSTIKN 518
Cdd:COG4172 157 ----------LSGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaQILDLLKDlqrelGMALLLITHDLGVVRR 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 767912302 519 -ANMVAVLDQGKITEYGKHEELLSKPNGIY-RKLMN 552
Cdd:COG4172 223 fADRVAVMRQGEIVEQGPTAELFAAPQHPYtRKLLA 258
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
329-556 |
4.97e-24 |
|
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: 101.86 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 329 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlnpvwlrsKIGTVSQEPILFSCSIAEN 408
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 409 IAYGaddpssVTAEEIqRVAEVANAVAF---IRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSAL 485
Cdd:cd03291 118 IIFG------VSYDEY-RYKSVVKACQLeedITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912302 486 DAENEYLVQEA-LDRLMDGRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPNGIYRKLMNKQSF 556
Cdd:cd03291 191 DVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDTF 262
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
313-546 |
5.67e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 101.69 E-value: 5.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPEVpiFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL--RSK 390
Cdd:PRK13639 2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEP--ILFSCSIAENIAYGADDpSSVTAEEIQ-RVAEVANAVAFirnfpQGFNTVVGEKgvlLSGGQKQRIAIAR 467
Cdd:PRK13639 80 VGIVFQNPddQLFAPTVEEDVAFGPLN-LGLSKEEVEkRVKEALKAVGM-----EGFENKPPHH---LSGGQKKRVAIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 468 ALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKPNG 545
Cdd:PRK13639 151 ILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
|
.
gi 767912302 546 I 546
Cdd:PRK13639 231 I 231
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
321-525 |
8.32e-24 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.85 E-value: 8.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 321 AYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHdiRQLNPVWLRSKIgtvsqePIL 400
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG--ARVAYVPQRSEV------PDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 401 FSCSIAENIAYG------------ADDPSSVTaEEIQRV--AEVANAVafirnfpqgfntvVGEkgvlLSGGQKQRIAIA 466
Cdd:NF040873 70 LPLTVRDLVAMGrwarrglwrrltRDDRAAVD-DALERVglADLAGRQ-------------LGE----LSGGQRQRALLA 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 467 RALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKNANMVAVL 525
Cdd:NF040873 132 QGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
291-533 |
1.07e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.76 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 291 EREPKLPFNEGVILNEKsfqgALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASG 370
Cdd:COG0488 298 DKTVEIRFPPPERLGKK----VLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 371 TISLdGHDIrqlnpvwlrsKIGTVSQEPILFSC--SIAENIAYGADDpssvtAEEIQrvaevanavafIRNFPQGFN--- 445
Cdd:COG0488 371 TVKL-GETV----------KIGYFDQHQEELDPdkTVLDELRDGAPG-----GTEQE-----------VRGYLGRFLfsg 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 446 ----TVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLmDGrTVLVIAH-R--LSTIkn 518
Cdd:COG0488 424 ddafKPVGV----LSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHdRyfLDRV-- 495
|
250
....*....|....*
gi 767912302 519 ANMVAVLDQGKITEY 533
Cdd:COG0488 496 ATRILEFEDGGVREY 510
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
327-511 |
1.23e-23 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 99.43 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 327 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH----DIRQLNPVWL----RSKIGTVSQep 398
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPREIlalrRRTIGYVSQ-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 399 ilFSCSIaeniaygaddPSsVTAEEIqrVAE------VANAVAFIR--------NFPQGF-----NTvvgekgvlLSGGQ 459
Cdd:COG4778 101 --FLRVI----------PR-VSALDV--VAEpllergVDREEARARarellarlNLPERLwdlppAT--------FSGGE 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 460 KQRIAIARALLKNPKILLLDEATSALDAENE----YLVQEALDRlmdGRTVLVIAH 511
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRavvvELIEEAKAR---GTAIIGIFH 210
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
312-543 |
1.47e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.11 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPAS-----GTISLDGHDI--RQLNP 384
Cdd:PRK14258 7 AIKVNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 385 VWLRSKIGTVSQEPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAfirNFPQGFNTVVGEKGVLLSGGQKQRIA 464
Cdd:PRK14258 84 NRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDA---DLWDEIKHKIHKSALDLSGGQQQRLC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 465 IARALLKNPKILLLDEATSALDA----ENEYLVQEAldRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQ-----GKITEYG 534
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSL--RLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVEFG 238
|
....*....
gi 767912302 535 KHEELLSKP 543
Cdd:PRK14258 239 LTKKIFNSP 247
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
324-532 |
1.98e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 99.76 E-value: 1.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 324 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQL--------------------- 382
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnraqrkafrrdiqmvfqdsis 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 383 --NPvwlRSKIGTVSQEPILFSCSIAEniaygaddpssvtAEEIQRVAEVANAV----AFIRNFPQGfntvvgekgvlLS 456
Cdd:PRK10419 101 avNP---RKTVREIIREPLRHLLSLDK-------------AERLARASEMLRAVdlddSVLDKRPPQ-----------LS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 457 GGQKQRIAIARALLKNPKILLLDEATSALDAeneYLVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKI 530
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDL---VLQAGVIRLLKKlqqqfGTACLFITHDLRLVERfCQRVMVMDNGQI 230
|
..
gi 767912302 531 TE 532
Cdd:PRK10419 231 VE 232
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
313-534 |
2.21e-23 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 97.98 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAypaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRL--YDPASGTISLDGHDIRQLnPVWLRSK 390
Cdd:cd03217 1 LEIKDLHVS---VGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDL-PPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IG-TVS-QEPIlfscsiaeniaygaddpssvtaeeiqRVAEVANAvAFIRNFPQGFntvvgekgvllSGGQKQRIAIARA 468
Cdd:cd03217 77 LGiFLAfQYPP--------------------------EIPGVKNA-DFLRYVNEGF-----------SGGEKKRNEILQL 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 469 LLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAH--RLSTIKNANMVAVLDQGKITEYG 534
Cdd:cd03217 119 LLLEPDLAILDEPDSGLDIDALRLVAEVINKLREeGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
327-543 |
3.19e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 101.84 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 327 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPIL-FSCSI 405
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 406 AENIAYG---------ADDPSSVTAeeIQRVAEVANAVAFIrnfPQGFNTvvgekgvlLSGGQKQRIAIARALLKNPKIL 476
Cdd:PRK09536 95 RQVVEMGrtphrsrfdTWTETDRAA--VERAMERTGVAQFA---DRPVTS--------LSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 477 LLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDdGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
333-539 |
4.71e-23 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 97.44 E-value: 4.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 333 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIGTVSQEPILFSCSIA-ENIAY 411
Cdd:cd03265 18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLSVDDELTGwENLYI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 412 GADDPSSVTAEEIQRVAEVANAVAF-------IRNFpqgfntvvgekgvllSGGQKQRIAIARALLKNPKILLLDEATSA 484
Cdd:cd03265 97 HARLYGVPGAERRERIDELLDFVGLleaadrlVKTY---------------SGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 767912302 485 LDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEEL 539
Cdd:cd03265 162 LDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
324-511 |
5.51e-23 |
|
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: 97.73 E-value: 5.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 324 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL---LRLYDPASGTISLDGhdiRQLNPVWLRSKIGTVSQEPIL 400
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 401 FSC-SIAENIAYGADDPSSVTAEEIQRVAEVA----NAVAfirnfpqgfNTVVGEKGVL-LSGGQKQRIAIARALLKNPK 474
Cdd:cd03234 93 LPGlTVRETLTYTAILRLPRKSSDAIRKKRVEdvllRDLA---------LTRIGGNLVKgISGGERRRVSIAVQLLWDPK 163
|
170 180 190
....*....|....*....|....*....|....*...
gi 767912302 475 ILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAH 511
Cdd:cd03234 164 VLILDEPTSGLDSFTALNLVSTLSQLArRNRIVILTIH 201
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
315-543 |
1.40e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 99.72 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 315 FKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwlRSKIGTV 394
Cdd:PRK11000 6 LRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 395 SQEPILFS-CSIAENIAYGADDPSSVTAEEIQRV---AEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALL 470
Cdd:PRK11000 81 FQSYALYPhLSVAENMSFGLKLAGAKKEEINQRVnqvAEVLQLAHLLDRKPKA-----------LSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 471 KNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAH-RLSTIKNANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAALRVQMRIEISRLHKrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLELYHYP 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
313-551 |
2.72e-22 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 100.55 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARP--------EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPASGTISLDGHDIRQLNP 384
Cdd:PRK15134 276 LDVEQLQVAFPIRKgilkrtvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 385 ---VWLRSKIGTVSQEPilFSC-----SIAENIAYG--ADDPSSVTAEEIQRVAEVANAV----AFIRNFPQGFntvvge 450
Cdd:PRK15134 355 rqlLPVRHRIQVVFQDP--NSSlnprlNVLQIIEEGlrVHQPTLSAAQREQQVIAVMEEVgldpETRHRYPAEF------ 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 451 kgvllSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTV--LVIAHRLSTIKN-ANMVAVLDQ 527
Cdd:PRK15134 427 -----SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQ 501
|
250 260
....*....|....*....|....*
gi 767912302 528 GKITEYGKHEELLSKPNGIY-RKLM 551
Cdd:PRK15134 502 GEVVEQGDCERVFAAPQQEYtRQLL 526
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
313-544 |
3.46e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.59 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTI---SLDGHDIRQLNPVwlRS 389
Cdd:PRK13644 2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSKLQGI--RK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 KIGTVSQEP--ILFSCSIAENIAYGaddPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTVVGEKGVLLSGGQKQRIAIAR 467
Cdd:PRK13644 78 LVGIVFQNPetQFVGRTVEEDLAFG---PENLCLPPIEIRKRVDRALAEI-----GLEKYRHRSPKTLSGGQGQCVALAG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912302 468 ALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPN 544
Cdd:PRK13644 150 ILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEkGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
336-543 |
4.12e-22 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 98.02 E-value: 4.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 336 LSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH---DIRQlnPVWL---RSKIGTVSQEPILFS-CSIAEN 408
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEK--GICLppeKRRIGYVFQDARLFPhYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 409 IAYGAddpSSVTAEEIQRVAEVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 488
Cdd:PRK11144 97 LRYGM---AKSMVAQFDKIVALLGIEPLLDRYPGS-----------LSGGEKQRVAIGRALLTAPELLLMDEPLASLDLP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 489 NEYLVQEALDRLmdGRTV----LVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:PRK11144 163 RKRELLPYLERL--AREInipiLYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
313-542 |
5.47e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.34 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYpaRPEVPIFQ----DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDghDI--------R 380
Cdd:PRK13643 2 IKFEKVNYTY--QPNSPFASralfDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIvvsstskqK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 381 QLNPVwlRSKIGTVSQEP--ILFSCSIAENIAYGADDpSSVTAEEIQRV-AEVANAVAFIRNFPQgfntvvgEKGVLLSG 457
Cdd:PRK13643 78 EIKPV--RKKVGVVFQFPesQLFEETVLKDVAFGPQN-FGIPKEKAEKIaAEKLEMVGLADEFWE-------KSPFELSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 458 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGK 535
Cdd:PRK13643 148 GQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
....*..
gi 767912302 536 HEELLSK 542
Cdd:PRK13643 228 PSDVFQE 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
287-554 |
5.94e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.84 E-value: 5.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 287 WELLEREPKLPFNEGVILNEKSFQGALEFKNVHfayparpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYD 366
Cdd:PRK13631 5 FMKKKLKVPNPLSDDIILRVKNLYCVFDEKQEN-------ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 367 PASGTISLD----GHDIRQLNPVW------------LRSKIGTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVA 428
Cdd:PRK13631 78 SKYGTIQVGdiyiGDKKNNHELITnpyskkiknfkeLRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 429 EVANAVA----FIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEY-LVQEALDRLMDG 503
Cdd:PRK13631 158 FYLNKMGlddsYLERSPFG-----------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANN 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 504 RTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEEL-----------------------LSKPNGIYRKLMNKQ 554
Cdd:PRK13631 227 KTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIftdqhiinstsiqvprviqvindLIKKDPKYKKLYQKQ 301
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
312-511 |
6.53e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 95.15 E-value: 6.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdIRQLNPVWLRski 391
Cdd:PRK11248 1 MLQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG--KPVEGPGAER--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQ-EPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFirnfpQGFntvvGEKGVL-LSGGQKQRIAIARAL 469
Cdd:PRK11248 73 GVVFQnEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGL-----EGA----EKRYIWqLSGGQRQRVGIARAL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767912302 470 LKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAH 511
Cdd:PRK11248 144 AANPQLLLLDEPFGALDAFTREQMQTLLLKLWqeTGKQVLLITH 187
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
313-554 |
1.52e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 94.52 E-value: 1.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAY------PARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH--------- 377
Cdd:COG4167 5 LEVRNLSKTFkyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHkleygdyky 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 378 ---DIR--------QLNPvwlRSKIGTVSQEPILFScsiaeniaygaddpSSVTAEE-IQRVAEVANAVAFIRN----FP 441
Cdd:COG4167 85 rckHIRmifqdpntSLNP---RLNIGQILEEPLRLN--------------TDLTAEErEERIFATLRLVGLLPEhanfYP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 442 QgfntvvgekgvLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE------NEYL-VQEALdrlmdGRTVLVIAHRLS 514
Cdd:COG4167 148 H-----------MLSSGQKQRVALARALILQPKIIIADEALAALDMSvrsqiiNLMLeLQEKL-----GISYIYVSQHLG 211
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767912302 515 TIKN-ANMVAVLDQGKITEYGKHEELLSKP-NGIYRKLMNKQ 554
Cdd:COG4167 212 IVKHiSDKVLVMHQGEVVEYGKTAEVFANPqHEVTKRLIESH 253
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
330-541 |
1.54e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 94.28 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 330 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEpilfscsiaeni 409
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN------------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 410 aygADDPSSVTAEEIQRVAEVANAVAFIRNFPQ------------GFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILL 477
Cdd:PRK10253 90 ---ATTPGDITVQELVARGRYPHQPLFTRWRKEdeeavtkamqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 478 LDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLS 541
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
41-282 |
2.06e-21 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 95.04 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 41 AVFLCGAAANAIRVYLMQTS-----GQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGL 115
Cdd:cd18558 62 AYYYLIIGAIVLITAYIQGSfwglaAGRQTKKIRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 116 RAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEI 195
Cdd:cd18558 142 QNIATFGTGFIIGFIRGWKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 196 EKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSE 275
Cdd:cd18558 222 TRYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVFFSVLIGAFSAGQQVPSIEA 301
|
....*..
gi 767912302 276 LMKGLGA 282
Cdd:cd18558 302 FANARGA 308
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
312-540 |
2.74e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 94.49 E-value: 2.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKI 391
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVV---DGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQ----EPilfSCSIAENIA-----YGaddpssVTAEEIQrvAEVANAVAFIRnFPQGFNTVVGEkgvlLSGGQKQR 462
Cdd:PRK13537 83 GVVPQfdnlDP---DFTVRENLLvfgryFG------LSAAAAR--ALVPPLLEFAK-LENKADAKVGE----LSGGMKRR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 463 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQG-KITEyGKHEEL 539
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGrKIAE-GAPHAL 225
|
.
gi 767912302 540 L 540
Cdd:PRK13537 226 I 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
314-544 |
2.79e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 93.22 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 314 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGT 393
Cdd:COG4604 3 EIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 394 VSQEPILfscsiaeniaygaddPSSVTAEEIqrvaevanaVAFIRnFP--QGFNTVVGEKGV--------L--------- 454
Cdd:COG4604 80 LRQENHI---------------NSRLTVREL---------VAFGR-FPysKGRLTAEDREIIdeaiayldLedladryld 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 455 -LSGGQKQRIAIARALLKNPKILLLDEATSALDAenEYLVQ--EALDRLMD--GRTVLVIAHRLstiknaNMVAV----- 524
Cdd:COG4604 135 eLSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM--KHSVQmmKLLRRLADelGKTVVIVLHDI------NFASCyadhi 206
|
250 260
....*....|....*....|..
gi 767912302 525 --LDQGKITEYGKHEELLSKPN 544
Cdd:COG4604 207 vaMKDGRVVAQGTPEEIITPEV 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
313-511 |
3.20e-21 |
|
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: 89.82 E-value: 3.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlnpvwlrskig 392
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS---------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 tvsqepilfscsiAENIAYgaddpssvtaeeiqrvaevanavafirnFPQgfntvvgekgvlLSGGQKQRIAIARALLKN 472
Cdd:cd03221 62 -------------TVKIGY----------------------------FEQ------------LSGGEKMRLALAKLLLEN 88
|
170 180 190
....*....|....*....|....*....|....*....
gi 767912302 473 PKILLLDEATSALDAENEYLVQEALDRLmdGRTVLVIAH 511
Cdd:cd03221 89 PNLLLLDEPTNHLDLESIEALEEALKEY--PGTVILVSH 125
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
313-534 |
7.89e-21 |
|
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: 90.80 E-value: 7.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpvwlRSKIG 392
Cdd:cd03269 1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILF-SCSIAENIAYGADdPSSVTAEEIQRVAEvanavAFIRNFPQG--FNTVVGEkgvlLSGGQKQRIAIARAL 469
Cdd:cd03269 74 YLPEERGLYpKMKVIDQLVYLAQ-LKGLKKEEARRRID-----EWLERLELSeyANKRVEE----LSKGNQQKVQFIAAV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 470 LKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYG 534
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIRELARaGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
312-555 |
8.18e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 91.68 E-value: 8.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYP-------------------ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTI 372
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 373 SLDGhdirqlNPVWL-------------RskigtvsqEPILFSCSIaeniaYGaddpssVTAEEI-QRVAEVanaVAF-- 436
Cdd:COG1134 84 EVNG------RVSALlelgagfhpeltgR--------ENIYLNGRL-----LG------LSRKEIdEKFDEI---VEFae 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 437 IRNFpqgFNTVVGekgvLLSGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALDRLMD----GRTVLVIAHR 512
Cdd:COG1134 136 LGDF---IDQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAA---FQKKCLARIRElresGRTVIFVSHS 205
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767912302 513 LSTIKN-ANMVAVLDQGKITEYGKHEELLSKpngiYRKLMNKQS 555
Cdd:COG1134 206 MGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA----YEALLAGRE 245
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
329-543 |
8.25e-21 |
|
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: 91.45 E-value: 8.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 329 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSK--IGTVSQEPILF-SCSI 405
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-PMHKRARlgIGYLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 406 AENIaYGADDPSSVTAEEIQRVAEvanavAFIRNFpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSAL 485
Cdd:cd03218 93 EENI-LAVLEIRGLSKKEREEKLE-----ELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912302 486 D----AENEYLVQEALDRlmdGRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:cd03218 165 DpiavQDIQKIIKILKDR---GIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
313-511 |
8.48e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.33 E-value: 8.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---- 387
Cdd:PRK10535 5 LELKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 388 RSKIGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQRvaevanAVAFIRNFpqGFNTVVGEKGVLLSGGQKQRIAIA 466
Cdd:PRK10535 85 REHFGFIFQRYHLLShLTAAQNVEVPAVYAGLERKQRLLR------AQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 767912302 467 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAH 511
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTH 202
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
313-480 |
8.51e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.63 E-value: 8.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSK-- 390
Cdd:COG1137 4 LEAENLVKSYGKRTVV---KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHL-PMHKRARlg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEPILF-SCSIAENIaYGADDPSSVTAEEIQRVAEvanavAFIRNFpqGFNTVVGEKGVLLSGGQKQRIAIARAL 469
Cdd:COG1137 80 IGYLPQEASIFrKLTVEDNI-LAVLELRKLSKKEREERLE-----ELLEEF--GITHLRKSKAYSLSGGERRRVEIARAL 151
|
170
....*....|.
gi 767912302 470 LKNPKILLLDE 480
Cdd:COG1137 152 ATNPKFILLDE 162
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
41-259 |
9.06e-21 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 93.01 E-value: 9.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 41 AVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQ 120
Cdd:cd18565 62 AAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSIIRVVVT 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 121 ASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYAS 200
Cdd:cd18565 142 VLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVAD 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 201 KVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLL------MGSAHMTVGELSSFLMYA 259
Cdd:cd18565 222 ASEEYRDANWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWvldgppLFTGTLTVGTLVTFLFYT 286
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
307-534 |
9.09e-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: 91.05 E-value: 9.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 307 KSFQGALEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlNPVW 386
Cdd:cd03220 14 KGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 387 LrskIG-TVSQEP-------ILFSCSIaeniaYGADDpssvtaeeiqrvAEVANAVAFIRNF---PQGFNTVVGEkgvlL 455
Cdd:cd03220 88 L---LGlGGGFNPeltgrenIYLNGRL-----LGLSR------------KEIDEKIDEIIEFselGDFIDLPVKT----Y 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 456 SGGQKQRIAIARALLKNPKILLLDEATSALDAEneyLVQEALDRLM----DGRTVLVIAHRLSTIKN-ANMVAVLDQGKI 530
Cdd:cd03220 144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAA---FQEKCQRRLRellkQGKTVILVSHDPSSIKRlCDRALVLEKGKI 220
|
....
gi 767912302 531 TEYG 534
Cdd:cd03220 221 RFDG 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
313-551 |
1.95e-20 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 92.46 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKN--VHF------AYPARPEVPI--FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQL 382
Cdd:PRK15079 9 LEVADlkVHFdikdgkQWFWQPPKTLkaVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 383 NPV-WL--RSKIGTVSQEPiLFSC----SIAENIAygadDP-----SSVTAEEI-QRVAEVANAVAFIRN----FPQGFn 445
Cdd:PRK15079 89 KDDeWRavRSDIQMIFQDP-LASLnprmTIGEIIA----EPlrtyhPKLSRQEVkDRVKAMMLKVGLLPNlinrYPHEF- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 446 tvvgekgvllSGGQKQRIAIARALLKNPKILLLDEATSALD----AENEYLVQEaLDRLMdGRTVLVIAHRLSTIKN-AN 520
Cdd:PRK15079 163 ----------SGGQCQRIGIARALILEPKLIICDEPVSALDvsiqAQVVNLLQQ-LQREM-GLSLIFIAHDLAVVKHiSD 230
|
250 260 270
....*....|....*....|....*....|..
gi 767912302 521 MVAVLDQGKITEYGKHEELLSKPNGIYRK-LM 551
Cdd:PRK15079 231 RVLVMYLGHAVELGTYDEVYHNPLHPYTKaLM 262
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
308-553 |
2.26e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.61 E-value: 2.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 308 SFQGALEFKNVHFAYPARP--EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASG-TISLD---GHDIRQ 381
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDyaiPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 382 LNPVW-LRSKIGTVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFpqgfntvVGEKGVLLSGG 458
Cdd:PRK13645 82 IKEVKrLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDY-------VKRSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 459 QKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYG- 534
Cdd:PRK13645 155 QKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGs 234
|
250 260
....*....|....*....|....*...
gi 767912302 535 -----KHEELLSK----PNGIYrKLMNK 553
Cdd:PRK13645 235 pfeifSNQELLTKieidPPKLY-QLMYK 261
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
333-539 |
2.44e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 91.71 E-value: 2.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 333 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpvwlRSKIGTVSQEPILF-SCSIAENIAY 411
Cdd:COG4152 19 DVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYpKMKVGEQLVY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 412 -----GaddpssVTAEEIQR----------VAEVANAvafirnfpqgfntVVGEkgvlLSGGQKQRIAIARALLKNPKIL 476
Cdd:COG4152 95 larlkG------LSKAEAKRradewlerlgLGDRANK-------------KVEE----LSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 477 LLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEEL 539
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
312-537 |
2.70e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.20 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlNPV-----W 386
Cdd:PRK13536 41 AIDLAGVSKSYGDKAVV---NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG------VPVpararL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 387 LRSKIGTVSQEPIL-FSCSIAEN-IAYGAddPSSVTAEEIQRVaeVANAVAFIRnFPQGFNTVVGEkgvlLSGGQKQRIA 464
Cdd:PRK13536 112 ARARIGVVPQFDNLdLEFTVRENlLVFGR--YFGMSTREIEAV--IPSLLEFAR-LESKADARVSD----LSGGMKRRLT 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 465 IARALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQG-KITEYGKHE 537
Cdd:PRK13536 183 LARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVLEAGrKIAEGRPHA 258
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
3-286 |
2.75e-20 |
|
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: 91.35 E-value: 2.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 3 SVISMSAPFFLGKIIDVIYTNptvDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVA 82
Cdd:cd18570 15 TLLGIAGSFFFQILIDDIIPS---GDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKHLLKLPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 83 FFDKTRTGELINRLsSDT----ALLGRSVTENLSDGLragaQASVGISMMFFVSPNLATFVLSVVPpvsIIAVIYGRYLR 158
Cdd:cd18570 92 FFETRKTGEIISRF-NDAnkirEAISSTTISLFLDLL----MVIISGIILFFYNWKLFLITLLIIP---LYILIILLFNK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 159 KLTKVTQDSLAQATQLAE---ERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVL 235
Cdd:cd18570 164 PFKKKNREVMESNAELNSyliESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIGSLLIL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 767912302 236 YKGGLLMGSAHMTVGELSSFL-MYAFWVGiSIGGLSSFYSELMKGLGAGGRL 286
Cdd:cd18570 244 WIGSYLVIKGQLSLGQLIAFNaLLGYFLG-PIENLINLQPKIQEAKVAADRL 294
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
313-537 |
3.77e-20 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 89.74 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHfaypARPE-VPIFQDFSLSIPSGSVTALVGPSGSGKSTvLSLLL---RLYDPASGTISLDGHDIRQLnPVWLR 388
Cdd:COG0396 1 LEIKNLH----VSVEgKEILKGVNLTIKPGEVHAIMGPNGSGKST-LAKVLmghPKYEVTSGSILLDGEDILEL-SPDER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 SK--IGTVSQEPILFS-CSIAE--NIAYGADDPSSVTAEE-IQRVAEVANAVafirNFPQGF-----NtvVGekgvlLSG 457
Cdd:COG0396 75 ARagIFLAFQYPVEIPgVSVSNflRTALNARRGEELSAREfLKLLKEKMKEL----GLDEDFldryvN--EG-----FSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 458 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAH--RLSTIKNANMVAVLDQGKITEYG 534
Cdd:COG0396 144 GEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSG 223
|
...
gi 767912302 535 KHE 537
Cdd:COG0396 224 GKE 226
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
327-551 |
5.99e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 93.77 E-value: 5.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 327 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI-----RQLNPvwLRSKIGTVSQEPILf 401
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlspGKLQA--LRRDIQFIFQDPYA- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 402 SCSIAENIAYGADDPSSVTA-----EEIQRVAEVANAVAFIRN----FPQGFntvvgekgvllSGGQKQRIAIARALLKN 472
Cdd:PRK10261 413 SLDPRQTVGDSIMEPLRVHGllpgkAAAARVAWLLERVGLLPEhawrYPHEF-----------SGGQRQRICIARALALN 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 473 PKILLLDEATSALDAEneyLVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPNGI 546
Cdd:PRK10261 482 PKVIIADEAVSALDVS---IRGQIINLLLDlqrdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQHP 558
|
....*.
gi 767912302 547 Y-RKLM 551
Cdd:PRK10261 559 YtRKLM 564
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
324-511 |
6.49e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.01 E-value: 6.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 324 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTvsQEPILFSC 403
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGH--RNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 404 SIAENIA-----YGADDPSsvtaeeiqrVAEVANAVAF--IRNFPQGFntvvgekgvlLSGGQKQRIAIARALLKNPKIL 476
Cdd:PRK13539 89 TVAENLEfwaafLGGEELD---------IAAALEAVGLapLAHLPFGY----------LSAGQKRRVALARLLVSNRPIW 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 767912302 477 LLDEATSALDAENEYLVQEAL-DRLMDGRTVLVIAH 511
Cdd:PRK13539 150 ILDEPTAALDAAAVALFAELIrAHLAQGGIVIAATH 185
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
332-511 |
7.35e-20 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 88.68 E-value: 7.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLrskigTVSQEPILFS-CSIAENIA 410
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 411 YgADDPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENE 490
Cdd:TIGR01184 77 L-AVDRVLPDLSKSERRAIVEEHIALV-----GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180
....*....|....*....|...
gi 767912302 491 YLVQEALDRLMD--GRTVLVIAH 511
Cdd:TIGR01184 151 GNLQEELMQIWEehRVTVLMVTH 173
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
313-541 |
1.03e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 88.41 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSK-- 390
Cdd:PRK10895 4 LTAKNLAKAYKGRRVV---EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-PLHARARrg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEPILFS-CSIAENIAYGADDPSSVTAEEIQ-RVAEVANA--VAFIRNfpqgfntvvgEKGVLLSGGQKQRIAIA 466
Cdd:PRK10895 80 IGYLPQEASIFRrLSVYDNLMAVLQIRDDLSAEQREdRANELMEEfhIEHLRD----------SMGQSLSGGERRRVEIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 467 RALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRL-STIKNANMVAVLDQGKITEYGKHEELLS 541
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
331-530 |
1.09e-19 |
|
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: 86.72 E-value: 1.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 331 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-VWLRSKIGTVSQEP----ILFSCSI 405
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRkregLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 406 AENIAYGaddpssvtaeeiqrvaevanavafirnfpqgfntvvgekgVLLSGGQKQRIAIARALLKNPKILLLDEATSAL 485
Cdd:cd03215 96 AENIALS----------------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 767912302 486 DAENEYLVQEALDRLMD-GRTVLVIahrlST-----IKNANMVAVLDQGKI 530
Cdd:cd03215 136 DVGAKAEIYRLIRELADaGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
313-526 |
1.21e-19 |
|
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: 86.05 E-value: 1.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPArpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHdirqlnpvwlrSKIG 392
Cdd:cd03223 1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEPILFSCSIAENIAYGADDpssvtaeeiqrvaevanavafirnfpqgfntvvgekgvLLSGGQKQRIAIARALLKN 472
Cdd:cd03223 68 FLPQRPYLPLGTLREQLIYPWDD--------------------------------------VLSGGEQQRLAFARLLLHK 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 473 PKILLLDEATSALDAENE-YLVQEALDRLMdgrTVLVIAHRLSTIKNANMVAVLD 526
Cdd:cd03223 110 PKFVFLDEATSALDEESEdRLYQLLKELGI---TVISVGHRPSLWKFHDRVLDLD 161
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
313-530 |
1.37e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 88.58 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTIsLDG----HDIRQlnpvwlr 388
Cdd:PRK11247 13 LLLNAVSKRYGERT---VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGtaplAEARE------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 sKIGTVSQEPILFSC-SIAENIAYGaddpssVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIAR 467
Cdd:PRK11247 82 -DTRLMFQDARLLPWkKVIDNVGLG------LKGQWRDAALQALAAV--------GLADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 468 ALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKI 530
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwqQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
313-544 |
1.90e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.68 E-value: 1.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAY-PARP-EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI------RQLNP 384
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkdKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 385 VwlRSKIGTVSQ--EPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNfpqgfntVVGEKGVLLSGGQKQR 462
Cdd:PRK13646 83 V--RKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRD-------VMSQSPFQMSGGQMRK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 463 IAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEEL 539
Cdd:PRK13646 154 IAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKEL 233
|
....*
gi 767912302 540 LSKPN 544
Cdd:PRK13646 234 FKDKK 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
313-538 |
1.96e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.24 E-value: 1.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPEVPIFQDFSLSipSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV---WLRS 389
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGVTFHMR--PGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 KIGTVSQEP-ILFSCSIAENIAYgaddP---SSVTAEEIQR-VAEVANAVAFI---RNFPqgfntvvgekgVLLSGGQKQ 461
Cdd:PRK10908 80 QIGMIFQDHhLLMDRTVYDNVAI----PliiAGASGDDIRRrVSAALDKVGLLdkaKNFP-----------IQLSGGEQQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 462 RIAIARALLKNPKILLLDEATSALDAEneylVQEALDRLMD-----GRTVLVIAHRLSTIKNANM-VAVLDQGKITEyGK 535
Cdd:PRK10908 145 RVGIARAVVNKPAVLLADEPTGNLDDA----LSEGILRLFEefnrvGVTVLMATHDIGLISRRSYrMLTLSDGHLHG-GV 219
|
...
gi 767912302 536 HEE 538
Cdd:PRK10908 220 GGE 222
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
316-540 |
3.58e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 87.54 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 316 KNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVS 395
Cdd:PRK10575 15 RNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 396 QE-PILFSCSIAENIA------YGAddPSSVTAEEIQRVAEvanAVAFIRNFPQGFNTVVGekgvlLSGGQKQRIAIARA 468
Cdd:PRK10575 92 QQlPAAEGMTVRELVAigrypwHGA--LGRFGAADREKVEE---AISLVGLKPLAHRLVDS-----LSGGERQRAWIAML 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 469 LLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAhrlsTIKNANMVA-------VLDQGKITEYGKHEELL 540
Cdd:PRK10575 162 VAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA----VLHDINMAArycdylvALRGGEMIAQGTPAELM 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
313-544 |
3.63e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.94 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYpaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIG 392
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQEP--ILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALL 470
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML--------GLEELRDRVPHHLSGGEKKRVAIAGVIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 471 KNPKILLLDEATSALDAENeylVQEALDRLMD-----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPN 544
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQG---VKELIDFLNDlpetyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
330-514 |
3.88e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.79 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 330 IFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQL---NPVWLRS-KIGTVSQ-EPILFSCS 404
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNqKLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 405 IAENIAYGADDPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSA 484
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAV--------GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
|
170 180 190
....*....|....*....|....*....|..
gi 767912302 485 LDAENEYLVQEALDRL--MDGRTVLVIAHRLS 514
Cdd:PRK11629 176 LDARNADSIFQLLGELnrLQGTAFLVVTHDLQ 207
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
329-548 |
9.37e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.60 E-value: 9.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 329 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH--DIRQLNPVWLRSKIGTVSQEP--ILFSCS 404
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPeqQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 405 IAENIAYGADDPSSVTAEEIQRVAEVANAVAfirnfPQGFNTvvgEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSA 484
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVD-----AQHFRH---QPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 485 LDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPNGIYR 548
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTEAMEQ 232
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
327-512 |
1.01e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 85.01 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 327 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLY--DPASGTISLDGHDIrqlnpvwlrskigtvSQEpilfsCS 404
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQF---------------GRE-----AS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 405 IAENIaygADDPSSVTAEEIQRVAEVANAVAFIRNFPQgfntvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSA 484
Cdd:COG2401 102 LIDAI---GRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190
....*....|....*....|....*....|
gi 767912302 485 LDAENEYLVQEALDRLMD--GRTVLVIAHR 512
Cdd:COG2401 167 LDRQTAKRVARNLQKLARraGITLVVATHH 196
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
336-530 |
1.25e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 85.83 E-value: 1.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 336 LSIPSGSVTALVGPSGSGKSTVLSLLLRLY--DPASGT-ISLDGH----------DIRQLnpvwlRSKIGTVSQEPILFS 402
Cdd:PRK09984 25 LNIHHGEMVALLGPSGSGKSTLLRHLSGLItgDKSAGShIELLGRtvqregrlarDIRKS-----RANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 403 -CSIAENIAYGA--DDP------SSVTAEEIQRVAEVANAVAFIRNFPQGFNTvvgekgvlLSGGQKQRIAIARALLKNP 473
Cdd:PRK09984 100 rLSVLENVLIGAlgSTPfwrtcfSWFTREQKQRALQALTRVGMVHFAHQRVST--------LSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 474 KILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLS-TIKNANMVAVLDQGKI 530
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDInqNDGITVVVTLHQVDyALRYCERIVALRQGHV 231
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
4-259 |
2.45e-18 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 85.59 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 4 VISMSAPFFLGKIID-VIytnPTVDYsDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVA 82
Cdd:cd18567 16 LFALASPLYLQLVIDeVI---VSGDR-DLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 83 FFDKTRTGELINRLSS-DT--ALLGRSVTENLSDGLragaQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRK 159
Cdd:cd18567 92 YFEKRHLGDIVSRFGSlDEiqQTLTTGFVEALLDGL----MAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 160 LTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGG 239
Cdd:cd18567 168 ATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARWLNLLVDAINADIRLQRLQILFSAANGLLFGLENILVIYLGA 247
|
250 260
....*....|....*....|
gi 767912302 240 LLMGSAHMTVGELSSFLMYA 259
Cdd:cd18567 248 LLVLDGEFTVGMLFAFLAYK 267
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
312-487 |
2.58e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.44 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKNVHFAYPARpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSkI 391
Cdd:PRK11650 3 GLKLQAVRKSYDGK--TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPA-DRD-I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 392 GTVSQEPILFS-CSIAENIAYGADDpSSVTAEEI-QRVAEVANAV---AFIRNFPQGfntvvgekgvlLSGGQKQRIAIA 466
Cdd:PRK11650 79 AMVFQNYALYPhMSVRENMAYGLKI-RGMPKAEIeERVAEAARILelePLLDRKPRE-----------LSGGQRQRVAMG 146
|
170 180
....*....|....*....|.
gi 767912302 467 RALLKNPKILLLDEATSALDA 487
Cdd:PRK11650 147 RAIVREPAVFLFDEPLSNLDA 167
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
313-541 |
2.89e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.52 E-value: 2.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARP--EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISL---DGHDIRQLNPVW- 386
Cdd:PRK13651 3 IKVKNIVKIFNKKLptELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 387 --------------------LRSKIGTVSQ--EPILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFPQG- 443
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQRs 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 444 -FNtvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRL-STIKNAN 520
Cdd:PRK13651 163 pFE---------LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLdNVLEWTK 233
|
250 260
....*....|....*....|.
gi 767912302 521 MVAVLDQGKITEYGKHEELLS 541
Cdd:PRK13651 234 RTIFFKDGKIIKDGDTYDILS 254
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
334-544 |
4.50e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.74 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 334 FSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPASGTISLDGHDIRQLNPVWLRSKIGTVSQE-PILFSCSIAENIAYG 412
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYLALH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 413 AdDPSSVTAEEIQRVAEVANAVAFI----RNFPQgfntvvgekgvlLSGGQKQRIAIARALLK-----NP--KILLLDEA 481
Cdd:COG4138 94 Q-PAGASSEAVEQLLAQLAEALGLEdklsRPLTQ------------LSGGEWQRVRLAAVLLQvwptiNPegQLLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 482 TSALD-AEneylvQEALDRLMD-----GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKPN 544
Cdd:COG4138 161 MNSLDvAQ-----QAALDRLLRelcqqGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGETAEVMTPEN 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
326-517 |
2.07e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.22 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 326 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-VWLRSKIGTVSQE-PILFSC 403
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHkLAAQLGIGIIYQElSVIDEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 404 SIAENIAYGADDPSSVTAEEI---QRVAEVANAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDE 480
Cdd:PRK09700 96 TVLENLYIGRHLTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDE 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 767912302 481 ATSAL-DAENEYLVQeALDRLM-DGRTVLVIAHRLSTIK 517
Cdd:PRK09700 172 PTSSLtNKEVDYLFL-IMNQLRkEGTAIVYISHKLAEIR 209
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
313-539 |
2.15e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKIG 392
Cdd:PRK15439 12 LCARSISKQYSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 T--VSQEPILF-SCSIAENIAYGADDPSSVTAEEIQRVAEVanavafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARAL 469
Cdd:PRK15439 88 IylVPQEPLLFpNLSVKENILFGLPKRQASMQKMKQLLAAL------------GCQLDLDSSAGSLEVADRQIVEILRGL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912302 470 LKNPKILLLDEATSALD-AENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEEL 539
Cdd:PRK15439 156 MRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
334-544 |
2.58e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 81.52 E-value: 2.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 334 FSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPASGTISLDGHDIRQLNPVWLRSKIGTVSQE-PILFSCSIAENIA-Y 411
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPFAMPVFQYLTlH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 412 GADdpSSVTAEEIQRVAEVANAVAFIRNFPQGFNTvvgekgvlLSGGQKQRIAIARALLK-----NP--KILLLDEATSA 484
Cdd:PRK03695 94 QPD--KTRTEAVASALNEVAEALGLDDKLGRSVNQ--------LSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 485 LDAENeylvQEALDRLMD-----GRTVLVIAHRLS-TIKNANMVAVLDQGKITEYGKHEELLSKPN 544
Cdd:PRK03695 164 LDVAQ----QAALDRLLSelcqqGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
319-531 |
3.12e-17 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 81.22 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 319 HFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHD--IRQLNpvwLRSKIGTV-- 394
Cdd:cd03267 25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVpwKRRKK---FLRRIGVVfg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 395 SQEPILFSCSIAENIA-----YGADDpssvtAEEIQRVAEVANAVafirNFPQGFNTVVGEkgvlLSGGQKQRIAIARAL 469
Cdd:cd03267 102 QKTQLWWDLPVIDSFYllaaiYDLPP-----ARFKKRLDELSELL----DLEELLDTPVRQ----LSLGQRMRAEIAAAL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 470 LKNPKILLLDEATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTI-KNANMVAVLDQGKIT 531
Cdd:cd03267 169 LHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRLL 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
333-552 |
3.73e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 84.37 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 333 DFSLSIPSGSVTALVGPSGSGKS-TVLSLLLRLYDPA----SGTISLDGHDIRQLNPVWLR----SKIGTVSQEPILfSC 403
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRgvrgNKIAMIFQEPMV-SL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 404 SIAENIAYGADDPSSV---------TAEEIQ---RVAeVANAVAFIRNFPQGfntvvgekgvlLSGGQKQRIAIARALLK 471
Cdd:PRK15134 106 NPLHTLEKQLYEVLSLhrgmrreaaRGEILNcldRVG-IRQAAKRLTDYPHQ-----------LSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 472 NPKILLLDEATSALD----AENEYLVQEALDRLmdGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPNGI 546
Cdd:PRK15134 174 RPELLIADEPTTALDvsvqAQILQLLRELQQEL--NMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFSAPTHP 251
|
....*..
gi 767912302 547 Y-RKLMN 552
Cdd:PRK15134 252 YtQKLLN 258
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
326-543 |
6.44e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.51 E-value: 6.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 326 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA----SGTISLDGhdiRQLNPVWLRSK-IGTVSQEP-- 398
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDG---KPVAPCALRGRkIATIMQNPrs 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 399 ------ILFSCSIAENIAYGADDPSSVTAEEIQRVAeVANAVAFIRNFPqgFNtvvgekgvlLSGGQKQRIAIARALLKN 472
Cdd:PRK10418 91 afnplhTMHTHARETCLALGKPADDATLTAALEAVG-LENAARVLKLYP--FE---------MSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912302 473 PKILLLDEATSALDAENEYLVQEALDRLMDGRT--VLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNAP 232
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
324-488 |
8.87e-17 |
|
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: 78.94 E-value: 8.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 324 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSC 403
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 404 SIAENIAYGADDPSSVtaeeiQRVAEVANAVAFIRNFPQgfnTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATS 483
Cdd:TIGR01189 89 SALENLHFWAAIHGGA-----QRTIEDALAAVGLTGFED---LPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
....*
gi 767912302 484 ALDAE 488
Cdd:TIGR01189 157 ALDKA 161
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
310-516 |
9.02e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 9.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 310 QGALEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLR 388
Cdd:PRK11288 2 SPYLSFDGIGKTFPG---VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 389 SKIGTVSQE----PILfscSIAENI-------AYGADDPSSVTAEEIQRVAEVANAVAfirnfPqgfNTVVGEkgvlLSG 457
Cdd:PRK11288 79 AGVAIIYQElhlvPEM---TVAENLylgqlphKGGIVNRRLLNYEAREQLEHLGVDID-----P---DTPLKY----LSI 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912302 458 GQKQRIAIARALLKNPKILLLDEATSALDA-ENEYLVQeALDRLMD-GRTVLVIAHRLSTI 516
Cdd:PRK11288 144 GQRQMVEIAKALARNARVIAFDEPTSSLSArEIEQLFR-VIRELRAeGRVILYVSHRMEEI 203
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
325-541 |
9.60e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.56 E-value: 9.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 325 RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLrLYDPA----SGTISLDGHDIrqlNPVWLRSKIGTVSQEPIL 400
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPI---DAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 401 F-SCSIAENIAYGAD--DPSSVTAEE-IQRVAEVANAVAFIRnfpqGFNTVVGEKGVL--LSGGQKQRIAIARALLKNPK 474
Cdd:TIGR00955 111 IpTLTVREHLMFQAHlrMPRRVTKKEkRERVDEVLQALGLRK----CANTRIGVPGRVkgLSGGERKRLAFASELLTDPP 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 475 ILLLDEATSALDAENEYLVQEALDRL-MDGRTVLVIAHRLST--IKNANMVAVLDQGKITEYGKHEELLS 541
Cdd:TIGR00955 187 LLFCDEPTSGLDSFMAYSVVQVLKGLaQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
2-277 |
1.33e-16 |
|
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: 80.33 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEV 81
Cdd:cd18782 14 VQLLGLANPLLFQVIIDKVLVQQDLA---TLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 82 AFFDKTRTGELINRLSS-DTA---LLGRSVTENLSdglraGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYL 157
Cdd:cd18782 91 GFFDKRPVGELSTRISElDTIrgfLTGTALTTLLD-----VLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 158 RKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYK 237
Cdd:cd18782 166 RRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNKLSSLLVLWV 245
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 767912302 238 GGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELM 277
Cdd:cd18782 246 GAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQ 285
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
5-259 |
1.67e-16 |
|
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: 80.16 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 5 ISMSAPFFLGKIIDVIYTNPTVDYSDNLTRLCLGLSAVFLCGAAANA----IRVYLMQTSGQRIVNRLRTSLFSSILRQE 80
Cdd:cd18554 14 IPLLLPLILKYIVDDVIQGSSLTLDEKVYKLFTIIGIMFFIFLILRPpveyYRQYFAQWIANKILYDIRKDLFDHLQKLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 81 VAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLaTFVLSVVPPVSIIAV--IYGRyLR 158
Cdd:cd18554 94 LRYYANNRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKL-TFVSLVIFPFYILAVkyFFGR-LR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 159 KLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKG 238
Cdd:cd18554 172 KLTKERSQALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFA 251
|
250 260
....*....|....*....|.
gi 767912302 239 GLLMGSAHMTVGELSSFLMYA 259
Cdd:cd18554 252 AYLVIEGNLTVGTLVAFVGYM 272
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
313-533 |
4.34e-16 |
|
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: 76.51 E-value: 4.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYP-ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA--SGTISLDGhdiRQLNPVWLRS 389
Cdd:cd03232 4 LTWKNLNYTVPvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILING---RPLDKNFQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 kIGTVSQEPILFSCSiaeniaygaddpssvTAEEIQRVAevanavAFIRNfpqgfntvvgekgvlLSGGQKQRIAIARAL 469
Cdd:cd03232 81 -TGYVEQQDVHSPNL---------------TVREALRFS------ALLRG---------------LSVEQRKRLTIGVEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 470 LKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLS--TIKNANMVAVLDQGKITEY 533
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADsGQAILCTIHQPSasIFEKFDRLLLLKRGGKTVY 190
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
331-531 |
4.50e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.83 E-value: 4.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 331 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSKIGTVS----QEPILFSCSI 405
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdAIRAGIAYVPedrkGEGLVLDLSI 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 406 AENIAYGADDPSSvTAEEIQRVAEVANAVAFIRNF---PQGFNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEAT 482
Cdd:COG1129 348 RENITLASLDRLS-RGGLLDRRRERALAEEYIKRLrikTPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912302 483 SALD--AENEylVQEALDRLMD-GRTVLVI----------AHRlstiknanmVAVLDQGKIT 531
Cdd:COG1129 423 RGIDvgAKAE--IYRLIRELAAeGKAVIVIsselpellglSDR---------ILVMREGRIV 473
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
324-497 |
4.95e-16 |
|
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: 76.76 E-value: 4.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 324 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILFSC 403
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 404 SIAENIAYGADDPSSVTAEEIqrVAEVanavafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATS 483
Cdd:cd03231 89 SVLENLRFWHADHSDEQVEEA--LARV------------GLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170
....*....|....
gi 767912302 484 ALDAENEYLVQEAL 497
Cdd:cd03231 155 ALDKAGVARFAEAM 168
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
329-555 |
7.31e-16 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.60 E-value: 7.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 329 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIrQLNPVWLRSKIGTVSQEPILFS-CSIAE 407
Cdd:TIGR01257 944 PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 408 NIAYGADDPSSvTAEEIQRVAEvanavAFIRNfpQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDA 487
Cdd:TIGR01257 1023 HILFYAQLKGR-SWEEAQLEME-----AMLED--TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDP 1094
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 488 ENEYLVQEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKIteYGKHEELLSKP---NGIY----RKLMNKQS 555
Cdd:TIGR01257 1095 YSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRL--YCSGTPLFLKNcfgTGFYltlvRKMKNIQS 1168
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
313-552 |
7.50e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.88 E-value: 7.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAypaRPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWL---RS 389
Cdd:PRK11831 8 VDMRGVSFT---RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 KIGTVSQEPILFS-CSIAENIAYgaddPssvTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARA 468
Cdd:PRK11831 85 RMSMLFQSGALFTdMNVFDNVAY----P---LREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 469 LLKNPKILLLDEATSALDAeneyLVQEALDRLMD------GRTVLVIAHR----LSTIKNANMVAvlDQgKITEYGKHEE 538
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDP----ITMGVLVKLISelnsalGVTCVVVSHDvpevLSIADHAYIVA--DK-KIVAHGSAQA 230
|
250
....*....|....
gi 767912302 539 LLSKPNGIYRKLMN 552
Cdd:PRK11831 231 LQANPDPRVRQFLD 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
284-531 |
1.61e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.30 E-value: 1.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 284 GRlwELLEREPKLPFNEGVILneksfqgaLEFKNVHfaYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLR 363
Cdd:COG3845 239 GR--EVLLRVEKAPAEPGEVV--------LEVENLS--VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAG 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 364 LYDPASGTISLDGHDIRQLNPVWLR-SKIGTVSQEPILFSC----SIAENIAYGA-DDPSSVTAEEIQRVAEVANAVAFI 437
Cdd:COG3845 307 LRPPASGSIRLDGEDITGLSPRERRrLGVAYIPEDRLGRGLvpdmSVAENLILGRyRRPPFSRGGFLDRKAIRAFAEELI 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 438 RNF---PQGFNTVVGekgvLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVI---- 509
Cdd:COG3845 387 EEFdvrTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDaGAAVLLIsedl 462
|
250 260
....*....|....*....|....*...
gi 767912302 510 ------AHRlstiknanmVAVLDQGKIT 531
Cdd:COG3845 463 deilalSDR---------IAVMYEGRIV 481
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
313-535 |
2.01e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 76.07 E-value: 2.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlnpvW-----L 387
Cdd:PRK11614 6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD----WqtakiM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 388 RSKIGTVSQEPILFS-CSIAENIAYG---ADdpSSVTAEEIQRVAEVanavafirnFPQGFNTVVGEKGVLlSGGQKQRI 463
Cdd:PRK11614 79 REAVAIVPEGRRVFSrMTVEENLAMGgffAE--RDQFQERIKWVYEL---------FPRLHERRIQRAGTM-SGGEQQML 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 464 AIARALLKNPKILLLDEATSALDAeneYLVQEALDRLM----DGRTVLVIAhrlstiKNANMVAVL-DQGKITEYGK 535
Cdd:PRK11614 147 AIGRALMSQPRLLLLDEPSLGLAP---IIIQQIFDTIEqlreQGMTIFLVE------QNANQALKLaDRGYVLENGH 214
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
1-276 |
3.33e-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: 349984 [Multi-domain] Cd Length: 295 Bit Score: 76.36 E-value: 3.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIYTNPTVDysdNLTRLclglSAVFLCGAAANAIRVYLMQTSGQRI---VNR-LRTSLFSSI 76
Cdd:cd18540 13 LVALLDAVFPLLTKYAIDHFITPGTLD---GLTGF----ILLYLGLILIQALSVFLFIRLAGKIemgVSYdLRKKAFEHL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 77 LRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRY 156
Cdd:cd18540 86 QTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQKK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 157 L----RKLTKVTqdslAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVL 232
Cdd:cd18540 166 IlkayRKVRKIN----SRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 767912302 233 SVLYKGGLLMGSAHMTVGELSSFLMYA---FWvgiSIGGLSSFYSEL 276
Cdd:cd18540 242 LVLWYGGILVLAGAITIGTLVAFISYAtqfFE---PIQQLARVLAEL 285
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
341-541 |
4.35e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.38 E-value: 4.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 341 GSVTALVGPSGSGKSTVLSLLL-RLYDPA-SGTISLDGhdiRQLNPVWLRsKIGTVSQEPILFS-CSIAENIAYGA--DD 415
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANN---RKPTKQILK-RTGFVTQDDILYPhLTVRETLVFCSllRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 416 PSSVTAEEIQRVAEvanAVAFIRNFPQGFNTVVGEKGVL-LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEY-LV 493
Cdd:PLN03211 170 PKSLTKQEKILVAE---SVISELGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYrLV 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767912302 494 QEALDRLMDGRTVLVIAHRLST--IKNANMVAVLDQGKITEYGKHEELLS 541
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
331-551 |
7.59e-15 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 74.58 E-value: 7.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 331 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDiRQLNPVW----------LRSKIGTVSQEP-- 398
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD-GQLRDLYalseaerrrlLRTEWGFVHQHPrd 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 399 -ILFSCSIAENI-----AYGADDPSSVTAEEIQRVAEVANAVAFIRNFPQGFntvvgekgvllSGGQKQRIAIARALLKN 472
Cdd:PRK11701 101 gLRMQVSAGGNIgerlmAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTF-----------SGGMQQRLQIARNLVTH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 473 PKILLLDEATSALDAEneylVQEaldRLMD---------GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 542
Cdd:PRK11701 170 PRLVFMDEPTGGLDVS----VQA---RLLDllrglvrelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQVLDD 242
|
....*....
gi 767912302 543 PNGIYRKLM 551
Cdd:PRK11701 243 PQHPYTQLL 251
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
317-549 |
1.73e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 76.43 E-value: 1.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 317 NVHFaYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP--VWLRSK---- 390
Cdd:PRK10261 19 NIAF-MQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRqvIELSEQsaaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 --------IGTVSQEPI-----LFScsIAENIAYGADDPSSVTAEEiqRVAEVANAVAFIRnFPQGfNTVVGEKGVLLSG 457
Cdd:PRK10261 98 mrhvrgadMAMIFQEPMtslnpVFT--VGEQIAESIRLHQGASREE--AMVEAKRMLDQVR-IPEA-QTILSRYPHQLSG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 458 GQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRT--VLVIAHRLSTIKN-ANMVAVLDQGKITEYG 534
Cdd:PRK10261 172 GMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQGEAVETG 251
|
250
....*....|....*
gi 767912302 535 KHEELLSKPNGIYRK 549
Cdd:PRK10261 252 SVEQIFHAPQHPYTR 266
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
331-544 |
2.77e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 331 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlnpVWLRSKIGTVSQ-EPILFSCSI-AEN 408
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLVAYVPQsEEVDWSFPVlVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 409 IA----YGADDPSSVTAEEIQRVAEVANAVAFIRNFPqgfNTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSA 484
Cdd:PRK15056 100 VVmmgrYGHMGWLRRAKKRDRQIVTAALARVDMVEFR---HRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912302 485 LDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMVAVLDQGKITEYGKHEELLSKPN 544
Cdd:PRK15056 173 VDVKTEARIISLLRELRDeGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAEN 233
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
313-534 |
2.82e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 72.75 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLL--RLYDPASGTISLDGHDIRQLNPVwLRSK 390
Cdd:CHL00131 8 LEIKNLHASVN---ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghPAYKILEGDILFKGESILDLEPE-ERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGT------------VSQEPILFSCSIAENIAYGADDPSSVTAEEI--QRVAEVANAVAFI-RNFPQGFntvvgekgvll 455
Cdd:CHL00131 84 LGIflafqypieipgVSNADFLRLAYNSKRKFQGLPELDPLEFLEIinEKLKLVGMDPSFLsRNVNEGF----------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 456 SGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAH--RLSTIKNANMVAVLDQGKITE 532
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTsENSIILITHyqRLLDYIKPDYVHVMQNGKIIK 232
|
..
gi 767912302 533 YG 534
Cdd:CHL00131 233 TG 234
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
325-543 |
6.09e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.13 E-value: 6.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 325 RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVSQEPILfSCS 404
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPST-SLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 405 IAENIAYGADDP----SSVTAEEI-QRVAEVANAVAFIRN----FPQgfntvvgekgvLLSGGQKQRIAIARALLKNPKI 475
Cdd:PRK15112 102 PRQRISQILDFPlrlnTDLEPEQReKQIIETLRQVGLLPDhasyYPH-----------MLAPGQKQRLGLARALILRPKV 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 476 LLLDEATSALDAEneylVQEALDRLM------DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKP 543
Cdd:PRK15112 171 IIADEALASLDMS----MRSQLINLMlelqekQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
334-543 |
9.01e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.63 E-value: 9.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 334 FSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPaSGTIS-----LDGHDIRQLNPV----WLRSKIGTVSQEPIlfSCS 404
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD-NWHVTadrfrWNGIDLLKLSPRerrkIIGREIAMIFQEPS--SCL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 405 iaeniaygadDPSSVTAEEIqrvAEVANAVAFIRNFPQGFNTV----------VG---EKGVL------LSGGQKQRIAI 465
Cdd:COG4170 103 ----------DPSAKIGDQL---IEAIPSWTFKGKWWQRFKWRkkraiellhrVGikdHKDIMnsypheLTEGECQKVMI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 466 ARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 542
Cdd:COG4170 170 AMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnqLQGTSILLISHDLESISQwADTITVLYCGQTVESGPTEQILKS 249
|
.
gi 767912302 543 P 543
Cdd:COG4170 250 P 250
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
335-546 |
9.23e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.17 E-value: 9.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 335 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLnPVWLRSKIGTVS--QEPILF-SCSIAEN--I 409
Cdd:PRK11300 25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIARMGVVRtfQHVRLFrEMTVIENllV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 410 AYGADDPSSVTA-------------EEIQRVAEVANAVafirnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKIL 476
Cdd:PRK11300 104 AQHQQLKTGLFSgllktpafrraesEALDRAATWLERV--------GLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912302 477 LLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKPNGI 546
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPDVI 248
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
9-259 |
9.39e-14 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 72.15 E-value: 9.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 9 APFFLGKIIDVIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTR 88
Cdd:cd18588 21 TPLFFQVIIDKVLVHRSLS---TLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFESRQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 89 TGELINRL------------SSDTALLgrsvtenlsDGLRAGaqasVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRY 156
Cdd:cd18588 98 VGDTVARVrelesirqfltgSALTLVL---------DLVFSV----VFLAVMFYYSPTLTLIVLASLPLYALLSLLVTPI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 157 LRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASkvdhvmQLAR--KEAFARAGFFGATGLSGNLI---- 230
Cdd:cd18588 165 LRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEE------LLARyvKASFKTANLSNLASQIVQLIqklt 238
|
250 260
....*....|....*....|....*....
gi 767912302 231 VLSVLYKGGLLMGSAHMTVGELSSFLMYA 259
Cdd:cd18588 239 TLAILWFGAYLVMDGELTIGQLIAFNMLA 267
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
340-526 |
1.13e-13 |
|
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: 68.55 E-value: 1.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 340 SGSVTALVGPSGSGKSTVLSLLLRLYDPASGT-ISLDGHDIRQLNPVWLRskigtvsqepilfscsiaeniaygaddpss 418
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 419 vtaeeiqrvaevanavafirnfpqgfNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALD 498
Cdd:smart00382 51 --------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104
|
170 180 190
....*....|....*....|....*....|....*
gi 767912302 499 RLMD-------GRTVLVIAHRLSTIKNANMVAVLD 526
Cdd:smart00382 105 LRLLlllksekNLTVILTTNDEKDLGPALLRRRFD 139
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
327-486 |
1.37e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.19 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 327 EVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP---VWLRSK-IGTVSQEPILFS 402
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAKhVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 403 CSIA-ENIAYgaddPSSVTAEEIQRVAEvaNAVAFIRNFpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEA 481
Cdd:PRK10584 102 TLNAlENVEL----PALLRGESSRQSRN--GAKALLEQL--GLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
....*
gi 767912302 482 TSALD 486
Cdd:PRK10584 174 TGNLD 178
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
326-532 |
1.55e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 72.90 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 326 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPA---SGTISLDG-----HDIRQLNpvwlRSKIGTVSQE 397
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevcrfKDIRDSE----ALGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 398 ----PILfscSIAENI-------AYGADDPSSVTAEEIQRVAEVAnavafIRNFPQgfnTVVGEKGVllsgGQKQRIAIA 466
Cdd:NF040905 87 laliPYL---SIAENIflgneraKRGVIDWNETNRRARELLAKVG-----LDESPD---TLVTDIGV----GKQQLVEIA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912302 467 RALLKNPKILLLDEATSAL-DAENEYLvqeaLDRLMD----GRTVLVIAHRLSTI-KNANMVAVLDQGKITE 532
Cdd:NF040905 152 KALSKDVKLLILDEPTAALnEEDSAAL----LDLLLElkaqGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
333-553 |
1.61e-13 |
|
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: 70.51 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 333 DFSLSIPSGS-----VTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIrQLNPVWLRSKI-GTVSQepILFScsia 406
Cdd:cd03237 12 EFTLEVEGGSiseseVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKADYeGTVRD--LLSS---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 407 eniaygaDDPSSVTAEEIQrvAEVANAVAFIRNFPQGFNTvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALD 486
Cdd:cd03237 85 -------ITKDFYTHPYFK--TEIAKPLQIEQILDREVPE--------LSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 487 AENEYLVQEALDRLMDG--RTVLVIAHRLSTIKN-ANMVAVLDqGKITEYGkheeLLSKPNGIyRKLMNK 553
Cdd:cd03237 148 VEQRLMASKVIRRFAENneKTAFVVEHDIIMIDYlADRLIVFE-GEPSVNG----VANPPQSL-RSGMNR 211
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
313-512 |
1.70e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.59 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDI--------RQLNP 384
Cdd:PRK13540 2 LDVIELDFDYH---DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkkdlctyqKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 385 VWLRSKIgtvsqEPILfscSIAENIAYgaDDPSSVTAEEIQRVAEVANAVAFIrNFPQGfntvvgekgvLLSGGQKQRIA 464
Cdd:PRK13540 79 VGHRSGI-----NPYL---TLRENCLY--DIHFSPGAVGITELCRLFSLEHLI-DYPCG----------LLSSGQKRQVA 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767912302 465 IARALLKNPKILLLDEATSALDAEN-EYLVQEALDRLMDGRTVLVIAHR 512
Cdd:PRK13540 138 LLRLWMSKAKLWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
313-529 |
1.96e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.65 E-value: 1.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYdPA---SGTISLDG-----HDIRQLNp 384
Cdd:PRK13549 6 LEMKNITKTFGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGeelqaSNIRDTE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 385 vwlRSKIGTVSQEPILFS-CSIAENIAYGAD-------DPSSVTAEEIQRVAEVANAVafirnfpqGFNTVVGEkgvlLS 456
Cdd:PRK13549 81 ---RAGIAIIHQELALVKeLSVLENIFLGNEitpggimDYDAMYLRAQKLLAQLKLDI--------NPATPVGN----LG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 457 GGQKQRIAIARALLKNPKILLLDEATSAL-DAENEYLvqeaLDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGK 529
Cdd:PRK13549 146 LGQQQLVEIAKALNKQARLLILDEPTASLtESETAVL----LDIIRDlkahGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
310-516 |
2.13e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 72.73 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 310 QGALEFKNVHFAYPArpeVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwlRS 389
Cdd:PRK10762 2 QALLQLKGIDKAFPG---VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGP---KS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 390 K----IGTVSQE-PILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEkgvlLSGGQKQRIA 464
Cdd:PRK10762 76 SqeagIGIIHQElNLIPQLTIAENIFLGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGE----LSIGEQQMVE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 465 IARALLKNPKILLLDEATSAL-DAENEYL---VQEALDRlmdGRTVLVIAHRLSTI 516
Cdd:PRK10762 152 IAKVLSFESKVIIMDEPTDALtDTETESLfrvIRELKSQ---GRGIVYISHRLKEI 204
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
317-534 |
4.75e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.47 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 317 NVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLL-RLYDPA-------SGTISLDGHDIRQLNPVWL- 387
Cdd:PRK13547 3 TADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 388 --RSKIGTVSQEPILFScsiAENIAYGADDPSSVTAEEIQR----VAEVANAVAfirnfpqGFNTVVGEKGVLLSGGQKQ 461
Cdd:PRK13547 83 rlRAVLPQAAQPAFAFS---AREIVLLGRYPHARRAGALTHrdgeIAWQALALA-------GATALVGRDVTTLSGGELA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 462 RIAIARALLK---------NPKILLLDEATSALDAENEYLVQEALDRLM-DGRT-VLVIAHRLS-TIKNANMVAVLDQGK 529
Cdd:PRK13547 153 RVQFARVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLArDWNLgVLAIVHDPNlAARHADRIAMLADGA 232
|
....*
gi 767912302 530 ITEYG 534
Cdd:PRK13547 233 IVAHG 237
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
4-277 |
5.07e-13 |
|
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: 69.90 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 4 VISMSAPFFLGKIID--VIYTNptvdySDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEV 81
Cdd:cd18568 16 LLGLALPLFTQIILDrvLVHKN-----ISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSLPL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 82 AFFDKTRTGELINRLSSD---TALLGRSVTENLSDGLragaQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLR 158
Cdd:cd18568 91 SFFASRKVGDIITRFQENqkiRRFLTRSALTTILDLL----MVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSSPKLK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 159 KL-TKVTQDSLAQATQLAEErIGNVRTVRAFGKEMTEI----EKYASKVDHVMQLARKEAFARAgffgATGLSGNLIVLS 233
Cdd:cd18568 167 RNsREIFQANAEQQSFLVEA-LTGIATIKALAAERPIRwrweNKFAKALNTRFRGQKLSIVLQL----ISSLINHLGTIA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 767912302 234 VLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELM 277
Cdd:cd18568 242 VLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGLWDELQ 285
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
332-522 |
7.85e-13 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 68.80 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVL------SLLLRLYdpASGTISLDGHDIRQLNPVwlrSKIGTVSQEPI------ 399
Cdd:cd03271 12 KNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypALARRLH--LKKEQPGNHDRIEGLEHI---DKVIVIDQSPIgrtprs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 400 --------------LFsCSIAE----------------NIAygadDPSSVTAEEiqrvaevanAVAFIRNFPQGFNTV-- 447
Cdd:cd03271 87 npatytgvfdeireLF-CEVCKgkrynretlevrykgkSIA----DVLDMTVEE---------ALEFFENIPKIARKLqt 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 448 ----------VGEKGVLLSGGQKQRIAIARALLK---NPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRL 513
Cdd:cd03271 153 lcdvglgyikLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkGNTVVVIEHNL 232
|
....*....
gi 767912302 514 STIKNANMV 522
Cdd:cd03271 233 DVIKCADWI 241
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
313-542 |
1.01e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.77 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARP-EV-PIfqdfSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSK 390
Cdd:PRK10522 323 LELRNVTFAYQDNGfSVgPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEPILFScsiaENIAYGADDPSSVTAEEIQRVAEVANAVAFirnfpQGfNTVVGEKgvlLSGGQKQRIAIARALL 470
Cdd:PRK10522 399 FSAVFTDFHLFD----QLLGPEGKPANPALVEKWLERLKMAHKLEL-----ED-GRISNLK---LSKGQKKRLALLLALA 465
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 471 KNPKILLLDEATSALDAE-NEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMVAVLDQGKITE-YGKHEELLSK 542
Cdd:PRK10522 466 EERDILLLDEWAADQDPHfRREFYQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
325-488 |
1.06e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 1.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 325 RPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRS--KIGTVS------- 395
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllYLGHQPgiktelt 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 396 -QEPILFSCSIAENiaygADDpssvtaeeiqrvAEVANAVAfirnfpqgfntVVGEKGVL------LSGGQKQRIAIARA 468
Cdd:PRK13538 91 aLENLRFYQRLHGP----GDD------------EALWEALA-----------QVGLAGFEdvpvrqLSAGQQRRVALARL 143
|
170 180
....*....|....*....|
gi 767912302 469 LLKNPKILLLDEATSALDAE 488
Cdd:PRK13538 144 WLTRAPLWILDEPFTAIDKQ 163
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
1-204 |
1.58e-12 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 68.30 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIYTNPTVDYSDNLTRLCLGLsavFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQE 80
Cdd:cd18580 10 LLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALL---VLASVLLVLLRWLLFVLAGLRASRRLHDKLLRSVLRAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 81 VAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPnlatFVLSVVPPVSIIAVIYGRY---- 156
Cdd:cd18580 87 MSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSP----YFLIVLPPLLVVYYLLQRYylrt 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 767912302 157 ---LRKLtkvtqDSLAQA---TQLAEErIGNVRTVRAFGKEMTEIEKYASKVDH 204
Cdd:cd18580 163 srqLRRL-----ESESRSplySHFSET-LSGLSTIRAFGWQERFIEENLRLLDA 210
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
313-515 |
2.28e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 69.58 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLdGHDIrqlnpvwlrsKIG 392
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQ--EPILFSCSIAENIAYGADdpssvtaeeIQRVAEVA-NAVAFIRNFpqGFNTVVGEKGV-LLSGGQKQRIAIARA 468
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGGLD---------IIKLGKREiPSRAYVGRF--NFKGSDQQKKVgQLSGGERNRVHLAKT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 767912302 469 LLKNPKILLLDEATSALDAENEYLVQEALDRLmdGRTVLVIAH------RLST 515
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
313-542 |
3.23e-12 |
|
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: 69.06 E-value: 3.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL--LRLYDPASGTISLDGHDIRQLNPVWLRSK 390
Cdd:TIGR03269 1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHVALCEKCGYVERPSK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTvsqepilfSCSIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNFP-QGFNTVV-------------GEKGVL-- 454
Cdd:TIGR03269 78 VGE--------PCPVCGGTLEPEEVDFWNLSDKLRRRIRKRIAIMLQRTFAlYGDDTVLdnvlealeeigyeGKEAVGra 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 455 -------------------LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRL 513
Cdd:TIGR03269 150 vdliemvqlshrithiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWP 229
|
250 260 270
....*....|....*....|....*....|
gi 767912302 514 STIKNANMVAV-LDQGKITEYGKHEELLSK 542
Cdd:TIGR03269 230 EVIEDLSDKAIwLENGEIKEEGTPDEVVAV 259
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
332-542 |
3.62e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.42 E-value: 3.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRsKIGTV----SQ----EPILFSC 403
Cdd:COG4586 39 DDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFAR-RIGVVfgqrSQlwwdLPAIDSF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 404 SIAENIaYGADDpssvtAEEIQRVAEvanavafirnfpqgFNTVVGEKGVL------LSGGQKQRIAIARALLKNPKILL 477
Cdd:COG4586 118 RLLKAI-YRIPD-----AEYKKRLDE--------------LVELLDLGELLdtpvrqLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912302 478 LDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 542
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
315-487 |
5.14e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 64.98 E-value: 5.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 315 FKNVHF-AYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL---LRLYDPASGTISLDGHDIRqlnpvwlrsK 390
Cdd:cd03233 6 WRNISFtTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIPYK---------E 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQEPILFScsiaeniayGADD--PSSVTAEEIQRVAEVANAVAFIRnfpqgfntvvgekGVllSGGQKQRIAIARA 468
Cdd:cd03233 77 FAEKYPGEIIYV---------SEEDvhFPTLTVRETLDFALRCKGNEFVR-------------GI--SGGERKRVSIAEA 132
|
170
....*....|....*....
gi 767912302 469 LLKNPKILLLDEATSALDA 487
Cdd:cd03233 133 LVSRASVLCWDNSTRGLDS 151
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
326-535 |
7.93e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.21 E-value: 7.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 326 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVL-SLLLRLYD---PASGTISLDGHDIRQLNPvWLRSKIGTVSQEPILF 401
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTDGfhiGVEGVITYDGITPEEIKK-HYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 402 -SCSIAENIAYGA------DDPSSVTAEEiqRVAEVANAVAFIRNFPQGFNTVVGE---KGVllSGGQKQRIAIARALLK 471
Cdd:TIGR00956 151 pHLTVGETLDFAArcktpqNRPDGVSREE--YAKHIADVYMATYGLSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLG 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767912302 472 NPKILLLDEATSALDAENEYLVQEALD---RLMDGrTVLVIAHRLS--TIKNANMVAVLDQGKITEYGK 535
Cdd:TIGR00956 227 GAKIQCWDNATRGLDSATALEFIRALKtsaNILDT-TPLVAIYQCSqdAYELFDKVIVLYEGYQIYFGP 294
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
321-511 |
1.01e-11 |
|
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: 67.27 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 321 AYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTisldghdirqlnpVWLRS--KIGTVSQEP 398
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE-------------ARPQPgiKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 399 IL-FSCSIAENIAYGADDpssvTAEEIQRVAEVANAVAfirNFPQGFNTVVGEKGVL----------------------- 454
Cdd:TIGR03719 78 QLdPTKTVRENVEEGVAE----IKDALDRFNEISAKYA---EPDADFDKLAAEQAELqeiidaadawdldsqleiamdal 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912302 455 -----------LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLmDGrTVLVIAH 511
Cdd:TIGR03719 151 rcppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH 216
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
333-547 |
1.32e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.90 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 333 DFSLSIPSGSVTALVGPSGSGKS-TVLSL--LLRLYDPASGTISLDGHDI-----RQLNPvwLRS-KIGTVSQEPIlfsC 403
Cdd:PRK09473 34 DLNFSLRAGETLGIVGESGSGKSqTAFALmgLLAANGRIGGSATFNGREIlnlpeKELNK--LRAeQISMIFQDPM---T 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 404 SIaeniaygadDPSSVTAEEIQRV----AEVANAVAF------------------IRNFPQGFntvvgekgvllSGGQKQ 461
Cdd:PRK09473 109 SL---------NPYMRVGEQLMEVlmlhKGMSKAEAFeesvrmldavkmpearkrMKMYPHEF-----------SGGMRQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 462 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEE 538
Cdd:PRK09473 169 RVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMYAGRTMEYGNARD 248
|
....*....
gi 767912302 539 LLSKPNGIY 547
Cdd:PRK09473 249 VFYQPSHPY 257
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
314-511 |
2.61e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.13 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 314 EFKNVHFAYPARPEVpifQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTIsldghdirqlnpvwlrsKIGT 393
Cdd:PRK11147 321 EMENVNYQIDGKQLV---KDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-----------------HCGT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 394 vSQEPILFSC---------SIAENIAYGADDpssVTAEEIQRvaevaNAVAFIRNF---PQGFNTVVGEkgvlLSGGQKQ 461
Cdd:PRK11147 381 -KLEVAYFDQhraeldpekTVMDNLAEGKQE---VMVNGRPR-----HVLGYLQDFlfhPKRAMTPVKA----LSGGERN 447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 767912302 462 RIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRlMDGrTVLVIAH 511
Cdd:PRK11147 448 RLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDS-YQG-TVLLVSH 495
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
335-541 |
2.69e-11 |
|
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: 65.98 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 335 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISL----DGHDIRQLNPVwLRSK----IGTVSQEPILFS-CSI 405
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRakryIGILHQEYDLYPhRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 406 AENI--AYGADDPSsvtaeeiqrvaEVANAVAFIRNFPQGFNTVVGEKgVL------LSGGQKQRIAIARALLKNPKILL 477
Cdd:TIGR03269 383 LDNLteAIGLELPD-----------ELARMKAVITLKMVGFDEEKAEE-ILdkypdeLSEGERHRVALAQVLIKEPRIVI 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 478 LDEATSALDAENEYLVQEAL--DRLMDGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLS 541
Cdd:TIGR03269 451 LDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
316-513 |
3.37e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 316 KNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGhdirqlnpvwlRSKIGTVS 395
Cdd:PRK09544 8 ENVSVSFGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-----------KLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 396 QEpILFSCSIAENIAYGADDPSSVTAEEIQRVAEVANAvAFIRNFPQgfntvvgEKgvlLSGGQKQRIAIARALLKNPKI 475
Cdd:PRK09544 74 QK-LYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQA-GHLIDAPM-------QK---LSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 767912302 476 LLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRL 513
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDL 181
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
341-516 |
3.58e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.29 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 341 GSVTALVGPSGSGKSTVLSLLLRLYDPA---SGTISLDGhdiRQLNPVWLRSkIGTVSQEPI-LFSCSIAENIAYGA--D 414
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTGvitGGDRLVNG---RPLDSSFQRS-IGYVQQQDLhLPTSTVRESLRFSAylR 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 415 DPSSVTAEEIQRVAEvanAVAFIRNFPQGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILL-LDEATSALDAENEYLV 493
Cdd:TIGR00956 865 QPKSVSKSEKMEYVE---EVIKLLEMESYADAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSI 941
|
170 180
....*....|....*....|....
gi 767912302 494 QEALDRLMD-GRTVLVIAHRLSTI 516
Cdd:TIGR00956 942 CKLMRKLADhGQAILCTIHQPSAI 965
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
333-486 |
4.81e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 333 DFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSKIGTVSQEP----ILFSCSIAE 407
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdGLANGIVYISEDRkrdgLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 408 NIAYGADDPSSVTAEEIQRVAEVANAVAFIRNF----PqGFNTVVGekgvLLSGGQKQRIAIARALLKNPKILLLDEATS 483
Cdd:PRK10762 350 NMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFniktP-SMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
...
gi 767912302 484 ALD 486
Cdd:PRK10762 425 GVD 427
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
281-526 |
5.57e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 65.16 E-value: 5.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 281 GAGGRLWELLEREPKLPFNEGVIlneksfqgalEFKNVHFAYPARpEVPIfQDFSLSIPSGSVTALVGPSGSGKSTVLSL 360
Cdd:TIGR00954 430 REGGRNSNLVPGRGIVEYQDNGI----------KFENIPLVTPNG-DVLI-ESLSFEVPSGNNLLICGPNGCGKSSLFRI 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 361 LLRLYDPASGTISLDGhdirqlnpvwlRSKIGTVSQEPILFSCSIAENIAYgaddPSSV---------TAEEIQRVAEVA 431
Cdd:TIGR00954 498 LGELWPVYGGRLTKPA-----------KGKLFYVPQRPYMTLGTLRDQIIY----PDSSedmkrrglsDKDLEQILDNVQ 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 432 NAVAFIRNfpQGFNTVVGEKGVLlSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLmdGRTVLVIAH 511
Cdd:TIGR00954 563 LTHILERE--GGWSAVQDWMDVL-SGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSH 637
|
250
....*....|....*
gi 767912302 512 RLSTIKNANMVAVLD 526
Cdd:TIGR00954 638 RKSLWKYHEYLLYMD 652
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
321-488 |
9.79e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 9.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 321 AYParPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTisldghdirqlnpVWLRS--KIGTVSQEP 398
Cdd:PRK11819 15 VVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE-------------ARPAPgiKVGYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 399 IL-FSCSIAENIAYGADDpssvTAEEIQRVAEVANAVAfirNFPQGFNTVVGEKGVL----------------------- 454
Cdd:PRK11819 80 QLdPEKTVRENVEEGVAE----VKAALDRFNEIYAAYA---EPDADFDALAAEQGELqeiidaadawdldsqleiamdal 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 767912302 455 -----------LSGGQKQRIAIARALLKNPKILLLDEATSALDAE 488
Cdd:PRK11819 153 rcppwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE 197
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
333-516 |
1.31e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 1.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 333 DFSLSIPSGS-----VTALVGPSGSGKSTVLSLLLRLYDPASGTISLDghdIR-QLNPVWLRSKI-GTVSQepilFSCSI 405
Cdd:PRK13409 352 DFSLEVEGGEiyegeVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKiSYKPQYIKPDYdGTVED----LLRSI 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 406 AENIAygaddpSSVTAEEIQRvaevanavafirnfPQGFNTV----VGEkgvlLSGGQKQRIAIARALLKNPKILLLDEA 481
Cdd:PRK13409 425 TDDLG------SSYYKSEIIK--------------PLQLERLldknVKD----LSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190
....*....|....*....|....*....|....*..
gi 767912302 482 TSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTI 516
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI 517
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
313-536 |
2.32e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 60.96 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYParpEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLL--RLYDPASGTISLDGHDIRQLNP------ 384
Cdd:PRK09580 2 LSIKDLHVSVE---DKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPedrage 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 385 -VWLR----SKIGTVSQEPILfSCSIAENIAYGADDP------SSVTAEEIQRVAEVANAVAfiRNFPQGFntvvgekgv 453
Cdd:PRK09580 79 gIFMAfqypVEIPGVSNQFFL-QTALNAVRSYRGQEPldrfdfQDLMEEKIALLKMPEDLLT--RSVNVGF--------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 454 llSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDG-RTVLVIAH--RLSTIKNANMVAVLDQGKI 530
Cdd:PRK09580 147 --SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRI 224
|
....*.
gi 767912302 531 TEYGKH 536
Cdd:PRK09580 225 VKSGDF 230
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
331-516 |
3.53e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.49 E-value: 3.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 331 FQDFSLSIPSGS-----VTALVGPSGSGKSTVLSLLLRLYDPASGTISLDghdirqLN----PVWLRSKI-GTVSQepIL 400
Cdd:COG1245 351 YGGFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------LKisykPQYISPDYdGTVEE--FL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 401 FScsiaeniAYGADDPSSVTAEEIQRvaevanavafirnfPQGFNTVVgEKGVL-LSGGQKQRIAIARALLKNPKILLLD 479
Cdd:COG1245 423 RS-------ANTDDFGSSYYKTEIIK--------------PLGLEKLL-DKNVKdLSGGELQRVAIAACLSRDADLYLLD 480
|
170 180 190
....*....|....*....|....*....|....*....
gi 767912302 480 EATSALDAENEYLVQEALDRLMDGR--TVLVIAHRLSTI 516
Cdd:COG1245 481 EPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI 519
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
317-539 |
3.93e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.66 E-value: 3.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 317 NVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLlrlydpaSGTISLD------GHDIR----QLNPVw 386
Cdd:PRK11147 5 SIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdgriiyEQDLIvarlQQDPP- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 387 lRSKIGTVsqepilFScSIAENIAYGAD--------------DPSSVTAEEIQRVAEV---ANAvafiRNFPQGFNTVVG 449
Cdd:PRK11147 77 -RNVEGTV------YD-FVAEGIEEQAEylkryhdishlvetDPSEKNLNELAKLQEQldhHNL----WQLENRINEVLA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 450 EKGV-------LLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-EYLvqEALdrLMDGRTVLV-IAHRLSTIKN-A 519
Cdd:PRK11147 145 QLGLdpdaalsSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiEWL--EGF--LKTFQGSIIfISHDRSFIRNmA 220
|
250 260
....*....|....*....|....*....
gi 767912302 520 NMVAVLDQGKITEY---------GKHEEL 539
Cdd:PRK11147 221 TRIVDLDRGKLVSYpgnydqyllEKEEAL 249
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
44-210 |
5.35e-10 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 60.56 E-value: 5.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 44 LCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQASV 123
Cdd:cd18604 54 LLSVLLGTLRYLLFFFGSLRASRKLHERLLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLV 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 124 GISMMFFVSPnlaTFVLsvvpPVSIIAVIYGRYLRKLTKVTQD-----SLAQA---TQLAEERIGNVrTVRAFGKEMTEI 195
Cdd:cd18604 134 ILIAIVVVSP---AFLL----PAVVLAALYVYIGRLYLRASRElkrleSVARSpilSHFGETLAGLV-TIRAFGAEERFI 205
|
170
....*....|....*
gi 767912302 196 EKYASKVDHVMQLAR 210
Cdd:cd18604 206 EEMLRRIDRYSRAFR 220
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
335-547 |
7.97e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.59 E-value: 7.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 335 SLSIPSGSVTALVGPSGSGKSTVLSLLLRL----YDPASGTISLDGHDIRQLNPVWLRSKIG-TVS---QEPIlfSCSia 406
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRKLVGhNVSmifQEPQ--SCL-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 407 eniaygadDPS-SVTAEEIQ--------------------RVAEVANAVAF------IRNFPQGfntvvgekgvlLSGGQ 459
Cdd:PRK15093 103 --------DPSeRVGRQLMQnipgwtykgrwwqrfgwrkrRAIELLHRVGIkdhkdaMRSFPYE-----------LTEGE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 460 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRL--MDGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKH 536
Cdd:PRK15093 164 CQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnqNNNTTILLISHDLQMLsQWADKINVLYCGQTVETAPS 243
|
250
....*....|.
gi 767912302 537 EELLSKPNGIY 547
Cdd:PRK15093 244 KELVTTPHHPY 254
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
313-533 |
8.15e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 61.41 E-value: 8.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTI--------------SLDGHD 378
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLD 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 379 IrqlnpvwlrskigtvSQEPILFscsiaeniaygaddpssvtaeeiqrvaevanavaFIRNFP----QGFNTVVGEKGV- 453
Cdd:PLN03073 587 L---------------SSNPLLY----------------------------------MMRCFPgvpeQKLRAHLGSFGVt 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 454 ---------LLSGGQKQRIAIARALLKNPKILLLDEATSALDAEN-EYLVQEALdrLMDGrTVLVIAHRLSTIKNA-NMV 522
Cdd:PLN03073 618 gnlalqpmyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAvEALIQGLV--LFQG-GVLMVSHDEHLISGSvDEL 694
|
250
....*....|.
gi 767912302 523 AVLDQGKITEY 533
Cdd:PLN03073 695 WVVSEGKVTPF 705
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
4-257 |
8.48e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 59.90 E-value: 8.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 4 VISMSAPFFLGKIIDVIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAF 83
Cdd:cd18566 16 ILALATPLFILQVYDRVIPNESIP---TLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 84 FDKTRTGELINRLSSdtallgrsvTENLSDGLrAGAQASVGISM---------MFFVSPNLATFVLSVVPPVSIIAVIYG 154
Cdd:cd18566 93 FEREPSGAHLERLNS---------LEQIREFL-TGQALLALLDLpfvliflglIWYLGGKLVLVPLVLLGLFVLVAILLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 155 RYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKY----ASKVDHVMQLARKEAFARAGFFGATGLSGnLI 230
Cdd:cd18566 163 PILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYerlqANAAYAGFKVAKINAVAQTLGQLFSQVSM-VA 241
|
250 260
....*....|....*....|....*..
gi 767912302 231 VLSVlykGGLLMGSAHMTVGELSSFLM 257
Cdd:cd18566 242 VVAF---GALLVINGDLTVGALIACTM 265
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
335-547 |
1.12e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.14 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 335 SLSIPSGSVTALVGPSGSGKStVLSL-LLRLYD-PA---SGTISLDGHDIRQLNPVWLRSKIGT----VSQEPILfSCSI 405
Cdd:PRK11022 27 SYSVKQGEVVGIVGESGSGKS-VSSLaIMGLIDyPGrvmAEKLEFNGQDLQRISEKERRNLVGAevamIFQDPMT-SLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 406 AENIAYGADDPSSV-----TAEEIQRVAEVANAVAF------IRNFPQGfntvvgekgvlLSGGQKQRIAIARALLKNPK 474
Cdd:PRK11022 105 CYTVGFQIMEAIKVhqggnKKTRRQRAIDLLNQVGIpdpasrLDVYPHQ-----------LSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 475 ILLLDEATSALDAENEYLVQEALDRLM--DGRTVLVIAHRLSTI-KNANMVAVLDQGKITEYGKHEELLSKPNGIY 547
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRAPRHPY 249
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
335-536 |
1.61e-09 |
|
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: 60.22 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 335 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPAS--GTISLDGHDIRQLNPVWLRSK-IGTVSQEPILF-SCSIAENIA 410
Cdd:TIGR02633 21 DLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVpELSVAENIF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 411 YGAD--DPSSVT--AEEIQRVAEVANAVafirNFPQGFNT-VVGEKGvllsGGQKQRIAIARALLKNPKILLLDEATSAL 485
Cdd:TIGR02633 101 LGNEitLPGGRMayNAMYLRAKNLLREL----QLDADNVTrPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767912302 486 -DAENEYLVQEALDRLMDGRTVLVIAHRLSTIKnanmvAVLDQGKITEYGKH 536
Cdd:TIGR02633 173 tEKETEILLDIIRDLKAHGVACVYISHKLNEVK-----AVCDTICVIRDGQH 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
331-526 |
2.08e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 331 FQDFSLSIPS-GSVTALVGPSGSGKSTVLSLLlrlydpaSGTI--SLDGHDIrqlNPVW---LRSKIGTVSQEpiLFSCS 404
Cdd:PRK13409 88 FKLYGLPIPKeGKVTGILGPNGIGKTTAVKIL-------SGELipNLGDYEE---EPSWdevLKRFRGTELQN--YFKKL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 405 IAENIAygaddpssvTAEEIQRVAEVANAVafirnfpQGfnTV------VGEKGVL-------------------LSGGQ 459
Cdd:PRK13409 156 YNGEIK---------VVHKPQYVDLIPKVF-------KG--KVrellkkVDERGKLdevverlglenildrdiseLSGGE 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 460 KQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLstiknanmvAVLD 526
Cdd:PRK13409 218 LQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL---------AVLD 275
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
341-514 |
2.41e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.24 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 341 GSVTALVGPSGSGKSTVLSLLL--RLYDPASGTISLDGHDIRQLNpvwlRSKIGTVSQEPILFS--CSIAENIAYGA--D 414
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGFPKKQET----FARISGYCEQNDIHSpqVTVRESLIYSAflR 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 415 DPSSVTAEEIQR-VAEVANAVAfIRNFPqgfNTVVGEKGVL-LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYL 492
Cdd:PLN03140 982 LPKEVSKEEKMMfVDEVMELVE-LDNLK---DAIVGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1057
|
170 180
....*....|....*....|...
gi 767912302 493 VQEALDRLMD-GRTVLVIAHRLS 514
Cdd:PLN03140 1058 VMRTVRNTVDtGRTVVCTIHQPS 1080
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
313-530 |
3.78e-09 |
|
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: 59.07 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPA-SGTISLDGHDIRQLNPV-WLRSK 390
Cdd:TIGR02633 258 LEARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAqAIRAG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 391 IGTVSQE-------PILfscSIAENIAYGA----------DDPSSVTA--EEIQRVaEVANAVAFIrnfPQGfntvvgek 451
Cdd:TIGR02633 338 IAMVPEDrkrhgivPIL---GVGKNITLSVlksfcfkmriDAAAELQIigSAIQRL-KVKTASPFL---PIG-------- 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 452 gvLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGK 529
Cdd:TIGR02633 403 --RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVLGlSDRVLVIGEGK 480
|
.
gi 767912302 530 I 530
Cdd:TIGR02633 481 L 481
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
324-511 |
5.14e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 56.40 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 324 ARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNpvwlRSK-IGTVSQEPILFS 402
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 403 -CSIAENIAYgaddPSSVTAEEIQRVAEVANAVAFIRNFPQgfnTVVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEA 481
Cdd:PRK13543 96 dLSTLENLHF----LCGLHGRRAKQMPGSALAIVGLAGYED---TLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180 190
....*....|....*....|....*....|.
gi 767912302 482 TSALDAENEYLVQEALD-RLMDGRTVLVIAH 511
Cdd:PRK13543 165 YANLDLEGITLVNRMISaHLRGGGAALVTTH 195
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
314-518 |
5.67e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.49 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 314 EFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLL-----------LRLYDPASG---TIsldgHDI 379
Cdd:PRK10938 262 VLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysndLTLFGRRRGsgeTI----WDI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 380 RQlnpvwlrsKIGTVSQEPIL---FSCSIAENIAYGADDPSSVtaeeIQRVAEVANAVAfirnfPQ-----GFNTVVGEK 451
Cdd:PRK10938 335 KK--------HIGYVSSSLHLdyrVSTSVRNVILSGFFDSIGI----YQAVSDRQQKLA-----QQwldilGIDKRTADA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 452 GVL-LSGGQkQRIA-IARALLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLV------------IAHRLSTI 516
Cdd:PRK10938 398 PFHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLIsEGETQLLfvshhaedapacITHRLEFV 476
|
..
gi 767912302 517 KN 518
Cdd:PRK10938 477 PD 478
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
284-531 |
7.69e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.02 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 284 GRlwELLEREPKLPFNEGVILneksfqgaLEFKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLR 363
Cdd:PRK13549 241 GR--ELTALYPREPHTIGEVI--------LEVRNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 364 LYDPAS-GTISLDGHDIRQLNPV-WLRSKIGTVSQE-------PILfscSIAENIAYGA----------DDPSSVTA--E 422
Cdd:PRK13549 311 AYPGRWeGEIFIDGKPVKIRNPQqAIAQGIAMVPEDrkrdgivPVM---GVGKNITLAAldrftggsriDDAAELKTilE 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 423 EIQRVaEVANAVAFIRnfpqgfntvVGEkgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEY--------LVQ 494
Cdd:PRK13549 388 SIQRL-KVKTASPELA---------IAR----LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYeiyklinqLVQ 453
|
250 260 270
....*....|....*....|....*....|....*...
gi 767912302 495 EaldrlmdGRTVLVIAHRLSTIKN-ANMVAVLDQGKIT 531
Cdd:PRK13549 454 Q-------GVAIIVISSELPEVLGlSDRVLVMHEGKLK 484
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
331-526 |
1.03e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 331 FQDFSLSIP-SGSVTALVGPSGSGKSTVLSLLlrlydpaSGtisldghdirQLNPvwlrsKIGTVSQEP----IL--FSC 403
Cdd:COG1245 88 FRLYGLPVPkKGKVTGILGPNGIGKSTALKIL-------SG----------ELKP-----NLGDYDEEPswdeVLkrFRG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 404 SIAENiaYgaddpssvtaeeIQRVAE----VANAVAFIRNFPQGFNTVVG-------EKGVL------------------ 454
Cdd:COG1245 146 TELQD--Y------------FKKLANgeikVAHKPQYVDLIPKVFKGTVRellekvdERGKLdelaeklglenildrdis 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 455 -LSGGQKQRIAIARALLKNPKILLLDEATSALD-------AEneyLVQEALDrlmDGRTVLVIAHRLstiknanmvAVLD 526
Cdd:COG1245 212 eLSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrlnvAR---LIRELAE---EGKYVLVVEHDL---------AILD 276
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
4-276 |
1.34e-08 |
|
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: 56.36 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 4 VISMSAPFFLGKIIDVIYTNPTVDYSDNLTrlcLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAF 83
Cdd:cd18555 16 LLTLLIPILTQYVIDNVIVPGNLNLLNVLG---IGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFFEHLLKLPYSF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 84 FDKTRTGELINRLSSDTA---LLGRSVTENLSDGLRAGaqasVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKL 160
Cdd:cd18555 93 FENRSSGDLLFRANSNVYirqILSNQVISLIIDLLLLV----IYLIYMLYYSPLLTLIVLLLGLLIVLLLLLTRKKIKKL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 161 TK--VTQDSLAQATQLaeERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFaRAGFFG--ATGLS--GNLIVLSV 234
Cdd:cd18555 169 NQeeIVAQTKVQSYLT--ETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKER-LSNILNsiSSSIQfiAPLLILWI 245
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 767912302 235 lykGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSEL 276
Cdd:cd18555 246 ---GAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQF 284
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
294-511 |
2.13e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 294 PKLPFNEGvilnEKSFQGALEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTIS 373
Cdd:PRK15064 305 PFIRFEQD----KKLHRNALEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 374 ldghdirqlnpvWlrskigtvsqepilfscsiAEN--IAYGADDPSSVTAEEIqrvaevaNAVAFIRNF--PQGFNTVVg 449
Cdd:PRK15064 378 ------------W-------------------SENanIGYYAQDHAYDFENDL-------TLFDWMSQWrqEGDDEQAV- 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767912302 450 eKGVL----------------LSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDrLMDGrTVLVIAH 511
Cdd:PRK15064 419 -RGTLgrllfsqddikksvkvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALE-KYEG-TLIFVSH 493
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
331-531 |
2.74e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.60 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 331 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVwLRSKIGTV-----SQEPILF-SCS 404
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYlDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 405 IAENIaygaddpSSVTAEE----IQRVAEVANAVAFIRNFPQGFNTVvgEKGV-LLSGGQKQRIAIARALLKNPKILLLD 479
Cdd:PRK15439 358 LAWNV-------CALTHNRrgfwIKPARENAVLERYRRALNIKFNHA--EQAArTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 480 EATSALD--AENE-YLVQEALDRlmDGRTVLVIAHRLSTI-KNANMVAVLDQGKIT 531
Cdd:PRK15439 429 EPTRGVDvsARNDiYQLIRSIAA--QNVAVLFISSDLEEIeQMADRVLVMHQGEIS 482
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
332-519 |
2.99e-08 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 53.48 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRlydpASGTISLDGhdirqLNPVWLRSKIGTVSQEPILfscsIAENIAY 411
Cdd:cd03238 12 QNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----ASGKARLIS-----FLPKFSRNKLIFIDQLQFL----IDVGLGY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 412 gaddpssvtaeeiqrvaevanavafirnfpqgfnTVVGEKGVLLSGGQKQRIAIARALLKNPK--ILLLDEATSALDAEN 489
Cdd:cd03238 79 ----------------------------------LTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|.
gi 767912302 490 EYLVQEALDRLMD-GRTVLVIAHRLSTIKNA 519
Cdd:cd03238 125 INQLLEVIKGLIDlGNTVILIEHNLDVLSSA 155
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
326-529 |
3.11e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.28 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 326 PEVPIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIR-QLNPVWLRSKIGTVSQE-PILFSC 403
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQElNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 404 SIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIrnfpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATS 483
Cdd:PRK10982 89 SVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDEL-----DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTS 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 767912302 484 AL-DAENEYLVQeALDRLMD-GRTVLVIAHRLSTI-KNANMVAVLDQGK 529
Cdd:PRK10982 164 SLtEKEVNHLFT-IIRKLKErGCGIVYISHKMEEIfQLCDEITILRDGQ 211
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
332-522 |
3.99e-08 |
|
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: 56.17 E-value: 3.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLL------RLYdpASGTISLDGHDIRQLNPVwlrSKIGTVSQEPI------ 399
Cdd:TIGR00630 625 KNITVSIPLGLFTCITGVSGSGKSTLINDTLypalanRLN--GAKTVPGRYTSIEGLEHL---DKVIHIDQSPIgrtprs 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 400 --------------LFscsiAE----------------NIAYGA----------------DDPSSVTAE----------- 422
Cdd:TIGR00630 700 npatytgvfdeireLF----AEtpeakvrgytpgrfsfNVKGGRceacqgdgvikiemhfLPDVYVPCEvckgkrynret 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 423 -EIQ----RVAEVAN-----AVAFIRNFPQ-----------GFNTV-VGEKGVLLSGGQKQRIAIARALLK---NPKILL 477
Cdd:TIGR00630 776 lEVKykgkNIADVLDmtveeAYEFFEAVPSisrklqtlcdvGLGYIrLGQPATTLSGGEAQRIKLAKELSKrstGRTLYI 855
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 767912302 478 LDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMV 522
Cdd:TIGR00630 856 LDEPTTGLHFDDIKKLLEVLQRLVDkGNTVVVIEHNLDVIKTADYI 901
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
453-550 |
4.24e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 53.34 E-value: 4.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 453 VLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD--GRTVLVIAHRLSTIKNANMVAVLDQGKI 530
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVFEGEP 149
|
90 100
....*....|....*....|
gi 767912302 531 TEYGKHEELLSKPNGIYRKL 550
Cdd:cd03222 150 GVYGIASQPKGTREGINRFL 169
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
332-531 |
4.49e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 55.69 E-value: 4.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPvwlRSKI--GTV------SQEPILFSC 403
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSP---RDAIraGIMlcpedrKAEGIIPVH 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 404 SIAENIAYGADDPSSVTAEEIQRVAEVANAVAFIRNF----PQGfntvvGEKGVLLSGGQKQRIAIARALLKNPKILLLD 479
Cdd:PRK11288 347 SVADNINISARRHHLRAGCLINNRWEAENADRFIRSLniktPSR-----EQLIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 480 EATSALD--AENE-YLVQEALDRlmDGRTVLVIAHRL-STIKNANMVAVLDQGKIT 531
Cdd:PRK11288 422 EPTRGIDvgAKHEiYNVIYELAA--QGVAVLFVSSDLpEVLGVADRIVVMREGRIA 475
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
331-514 |
6.99e-08 |
|
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: 53.91 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 331 FQDFSLSIP-SGSVTALVGPSGSGKSTVLSLLlrlydpaSGTI--SLDGHDIrqlNPVW---LRSKIGTVSQEpilFSCS 404
Cdd:cd03236 15 FKLHRLPVPrEGQVLGLVGPNGIGKSTALKIL-------AGKLkpNLGKFDD---PPDWdeiLDEFRGSELQN---YFTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 405 IAENIAYGADDPSSV----------TAEEIQRVAEvanavafiRNFPQGFNTVVGEKGVL------LSGGQKQRIAIARA 468
Cdd:cd03236 82 LLEGDVKVIVKPQYVdlipkavkgkVGELLKKKDE--------RGKLDELVDQLELRHVLdrnidqLSGGELQRVAIAAA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 767912302 469 LLKNPKILLLDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLS 514
Cdd:cd03236 154 LARDADFYFFDEPSSYLDIKQRLNAARLIRELAeDDNYVLVVEHDLA 200
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
3-259 |
1.42e-07 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 53.29 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 3 SVISMSAPFFLGKIIDVIYTNPTVDysdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVA 82
Cdd:cd18783 15 HVLALAPPIFFQIVIDKVLVHQSYS---TLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLLSLPID 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 83 FFDKTRTGELINRLSSDTALlgRS-VTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLT 161
Cdd:cd18783 92 FFERTPAGVLTKHMQQIERI--RQfLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 162 KVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLL 241
Cdd:cd18783 170 QALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYL 249
|
250
....*....|....*...
gi 767912302 242 MGSAHMTVGELSSFLMYA 259
Cdd:cd18783 250 VFAGSLTVGALIAFNMLA 267
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
332-532 |
1.85e-07 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.63 E-value: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPV-WLRSKIGTVSQ---EPILFS-CSIA 406
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLdAVKKGMAYITEsrrDNGFFPnFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 407 ENIA-------------YGADDPSsvtaeEIQRVAEVANAVAFIRNfpQGFNTVVGEkgvlLSGGQKQRIAIARALLKNP 473
Cdd:PRK09700 360 QNMAisrslkdggykgaMGLFHEV-----DEQRTAENQRELLALKC--HSVNQNITE----LSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912302 474 KILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNA-NMVAVLDQGKITE 532
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADdGKVILMVSSELPEIITVcDRIAVFCEGRLTQ 489
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
343-511 |
2.03e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.84 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 343 VTALVGPSGSGKSTVLSLLLrlydpasgtISLDGHDIRQLNPVWLRSKIgtvsqepilfsCSIAENIAYGADDPSSVTAE 422
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALK---------YALTGELPPNSKGGAHDPKL-----------IREGEVRAQVKLAFENANGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 423 E--IQRVAEVANAVAFIRnfpQG-FNTVVGEKGVLLSGGQKQ------RIAIARALLKNPKILLLDEATSALDAENeylV 493
Cdd:cd03240 84 KytITRSLAILENVIFCH---QGeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEEN---I 157
|
170 180
....*....|....*....|....
gi 767912302 494 QEALDRLMD------GRTVLVIAH 511
Cdd:cd03240 158 EESLAEIIEerksqkNFQLIVITH 181
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
1-280 |
2.09e-07 |
|
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: 52.89 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIyTNPTVDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQE 80
Cdd:cd18582 7 LAKLLNVAVPFLLKYAVDAL-SAPASALLAVPLLLLLAYGLARILSSLFNELRDALFARVSQRAVRRLALRVFRHLHSLS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 81 VAFFDKTRTGEL---INRLSsdtallgRSVTENLSdglragaqasvgiSMMFFVSPNLATFVLSVV-------PPVSIIA 150
Cdd:cd18582 86 LRFHLSRKTGALsraIERGT-------RGIEFLLR-------------FLLFNILPTILELLLVCGilwylygWSYALIT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 151 ----VIYGRYLRKLTK---------VTQDSlaQATQLAEERIGNVRTVRAFGKEMTEIEKYaskvDHVMQLARKEAFARA 217
Cdd:cd18582 146 lvtvALYVAFTIKVTEwrtkfrremNEADN--EANAKAVDSLLNYETVKYFNNEEYEAERY----DKALAKYEKAAVKSQ 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 218 GFFGATGLSGNLIV----LSVLYKGGLLMGSAHMTVGELSSFLMYAFWVGISIGGLSSFYSELMKGL 280
Cdd:cd18582 220 TSLALLNIGQALIIslglTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSL 286
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
335-541 |
2.41e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 2.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 335 SLSIPSGSVTALVGPSGSGKSTvLSLLLrlydpaSGTISL-DGHDIRQLNPVWLRS-----KIgtVSQEpilFSCSIAEN 408
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSA-LARAL------AGELPLlSGERQSQFSHITRLSfeqlqKL--VSDE---WQRNNTDM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 409 IAYGADDPSSVTAEEIQ-------RVAEVANAVA----FIRNFPQgfntvvgekgvlLSGGQKQRIAIARALLKNPKILL 477
Cdd:PRK10938 91 LSPGEDDTGRTTAEIIQdevkdpaRCEQLAQQFGitalLDRRFKY------------LSTGETRKTLLCQALMSEPDLLI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 478 LDEATSALDAENEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLS 541
Cdd:PRK10938 159 LDEPFDGLDVASRQQLAELLASLHqSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ 224
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
335-554 |
2.42e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.36 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 335 SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKIGTVsqepilfscsiaENIAYGAD 414
Cdd:PRK13545 44 SFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGI------------ENIELKGL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 415 dPSSVTAEEIQ----RVAEVANAVAFIRnfpQGFNTvvgekgvlLSGGQKQRIAIARALLKNPKILLLDEATSALDaenE 490
Cdd:PRK13545 112 -MMGLTKEKIKeiipEIIEFADIGKFIY---QPVKT--------YSSGMKSRLGFAISVHINPDILVIDEALSVGD---Q 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912302 491 YLVQEALDRLMD----GRTVLVIAHRLSTIKNANMVAV-LDQGKITEYGKHEELLSKPNGIYRKL--MNKQ 554
Cdd:PRK13545 177 TFTKKCLDKMNEfkeqGKTIFFISHSLSQVKSFCTKALwLHYGQVKEYGDIKEVVDHYDEFLKKYnqMSVE 247
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
313-511 |
2.47e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.58 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 313 LEFKNVHFAYPARPevpIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLdGHDIrqlnpvwlrsKIG 392
Cdd:PRK11819 325 IEAENLSKSFGDRL---LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 393 TVSQ--EPILFSCSIAENIAYGADdpssvtaeeIQRVA--EVaNAVAFIRNFpqGFNTVVGEKGV-LLSGGQKQRIAIAR 467
Cdd:PRK11819 391 YVDQsrDALDPNKTVWEEISGGLD---------IIKVGnrEI-PSRAYVGRF--NFKGGDQQKKVgVLSGGERNRLHLAK 458
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 767912302 468 ALLKNPKILLLDEATSALDAENEYLVQEALDRLmdGRTVLVIAH 511
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLDVETLRALEEALLEF--PGCAVVISH 500
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
1-235 |
2.66e-07 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 52.49 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIYTNPTVDYSDNLTrLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQE 80
Cdd:cd18579 8 LEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYL-LALALFLVSLLQSLLLHQYFFLSFRLGMRVRSALSSLIYRKALRLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 81 VAFFDKTRTGELINRLSSDTALLGrSVTENLSDGLRAGAQASVGISMMFFVspnlatFVLSVVPPVSIIAVI--YGRYLR 158
Cdd:cd18579 87 SSARQETSTGEIVNLMSVDVQRIE-DFFLFLHYLWSAPLQIIVALYLLYRL------LGWAALAGLGVLLLLipLQAFLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 159 KLTKVTQDSLAQAT----QLAEERIGNVRTVRAFGKEmteiEKYASKVDHV----MQLARKEAFARAGFFGATGLSGNLI 230
Cdd:cd18579 160 KLISKLRKKLMKATdervKLTNEILSGIKVIKLYAWE----KPFLKRIEELrkkeLKALRKFGYLRALNSFLFFSTPVLV 235
|
....*
gi 767912302 231 VLSVL 235
Cdd:cd18579 236 SLATF 240
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
1-234 |
3.43e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 52.10 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIYTNPTVDYSDNLTRL----CLGLSAVFLCGAAAnairvYLMQTSGQRIVNRLRTSLFSSI 76
Cdd:cd18603 10 LSQAFSVGSNIWLSEWSDDPALNGTQDTEQRDYRLgvygALGLGQAIFVFLGS-----LALALGCVRASRNLHNKLLHNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 77 LRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRAGAQAsvgISMMFFVSPNLATFVLSVVPpvsiIAVIYG-- 154
Cdd:cd18603 85 LRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQV---ISTLVVISISTPIFLVVIIP----LAILYFfi 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 155 --------RYLRKLTKVT--------QDSLAQATqlaeerignvrTVRAFGKEMTEIEKYASKVDHvmqlarkeaFARAG 218
Cdd:cd18603 158 qrfyvatsRQLKRLESVSrspiyshfSETLQGAS-----------TIRAYGVQERFIRESDRRVDE---------NQRAY 217
|
250 260
....*....|....*....|....*
gi 767912302 219 FFGATG---LS------GNLIVLSV 234
Cdd:cd18603 218 YPSIVSnrwLAvrleflGNLIVLFA 242
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
334-522 |
3.48e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.03 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 334 FSLSI---PSgSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLrSKIGtvSQEPILFSCSIAENIA 410
Cdd:PRK13541 17 FDLSItflPS-AITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYC-TYIG--HNLGLKLEMTVFENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 411 YGADDPSSVTAeeiqrvaeVANAVAFIRnfpqgFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENE 490
Cdd:PRK13541 93 FWSEIYNSAET--------LYAAIHYFK-----LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
170 180 190
....*....|....*....|....*....|...
gi 767912302 491 YLVQEALD-RLMDGRTVLVIAHRLSTIKNANMV 522
Cdd:PRK13541 160 DLLNNLIVmKANSGGIVLLSSHLESSIKSAQIL 192
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
449-545 |
4.61e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.04 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 449 GEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLV-QEALDRLMDGRTVLVIAHRLSTIKN-ANMVAVLD 526
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLTTQYMEEAEQlAHELTVID 218
|
90
....*....|....*....
gi 767912302 527 QGKITEYGKHEELLSKPNG 545
Cdd:NF000106 219 RGRVIADGKVDELKTKVGG 237
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
333-486 |
5.09e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.82 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 333 DFSLSIPSGSVTALVGPSGSGKSTVLSLLlrlydpA------SGTISLDGHDI------RQLNPvwlrsKIGTVSQ---- 396
Cdd:NF033858 19 DVSLDIPAGCMVGLIGPDGVGKSSLLSLI------AgarkiqQGRVEVLGGDMadarhrRAVCP-----RIAYMPQglgk 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 397 --EPILfscSIAENIA-----YGADdpssvTAEEIQRVAEVANAV---AFiRNFPQGfntvvgeKgvlLSGGQKQRIAIA 466
Cdd:NF033858 88 nlYPTL---SVFENLDffgrlFGQD-----AAERRRRIDELLRATglaPF-ADRPAG-------K---LSGGMKQKLGLC 148
|
170 180
....*....|....*....|
gi 767912302 467 RALLKNPKILLLDEATSALD 486
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVD 168
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
332-552 |
3.32e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 48.66 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGH-DIRQLNpVWLRSKIGTVsqEPILFSCSIaenIA 410
Cdd:PRK13546 41 DDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEvSVIAIS-AGLSGQLTGI--ENIEFKMLC---MG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 411 YGADDPSSVTAEEIqrvaEVANAVAFIRNFPQGFntvvgekgvllSGGQKQRIAIARALLKNPKILLLDEATSALDaenE 490
Cdd:PRK13546 115 FKRKEIKAMTPKII----EFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD---Q 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 491 YLVQEALDRLMD----GRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSKpngiYRKLMN 552
Cdd:PRK13546 177 TFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK----YEAFLN 239
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
42-204 |
3.69e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 49.07 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 42 VFLCGAAANAI----RVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRA 117
Cdd:cd18605 47 VYGFLAGLNSLftllRAFLFAYGGLRAARRLHNKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 118 GAQASVGISMMFFVSPNLATFVLsvvppvsIIAVIYGRY----------LRKLTKVTQDSLaqATQLAEErIGNVRTVRA 187
Cdd:cd18605 127 LFGLLGYLVVICYQLPWLLLLLL-------PLAFIYYRIqryyratsreLKRLNSVNLSPL--YTHFSET-LKGLVTIRA 196
|
170
....*....|....*..
gi 767912302 188 FGKEMTEIEKYASKVDH 204
Cdd:cd18605 197 FRKQERFLKEYLEKLEN 213
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
11-282 |
4.62e-06 |
|
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: 48.43 E-value: 4.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 11 FFLGKIIDVIYTNptvDYSDNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTG 90
Cdd:cd18561 17 WLLARALARIFAG---GPWEDIMPPLAGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLGPGYLEGERTG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 91 ELINRLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQ 170
Cdd:cd18561 94 ELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDTGRRHWAAYGR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 171 ATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKE---AFARAGFFGATGLSGNLIVLSVLyKGGLLMGSAHM 247
Cdd:cd18561 174 LSAQFLDSLQGMTTLKAFGASKRRGNELAARAEDLRQATMKVlavSLLSSGIMGLATALGTALALGVG-ALRVLGGQLTL 252
|
250 260 270
....*....|....*....|....*....|....*
gi 767912302 248 TVGELSSFLMYAFWvgISIGGLSSFYSELMKGLGA 282
Cdd:cd18561 253 SSLLLILFLSREFF--RPLRDLGAYWHAGYQGISA 285
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
37-203 |
5.28e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 48.37 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 37 LGLSAVFLCGAAanairVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLR 116
Cdd:cd18602 59 LSLGAVILSLVT-----NLAGELAGLRAARRLHDRMLRNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 117 AGAQASVGISMMFFVSPnlaTFVLSVVpPVSIIAVIYGRYLRKLTKVTQ--DSLAQATQLAE--ERIGNVRTVRAFGKEM 192
Cdd:cd18602 134 FLLLCLSAIIVNAIVTP---YFLIALI-PIIIVYYFLQKFYRASSRELQrlDNITKSPVFSHfsETLGGLTTIRAFRQQA 209
|
170
....*....|.
gi 767912302 193 TEIEKYASKVD 203
Cdd:cd18602 210 RFTQQMLELID 220
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
335-520 |
1.01e-05 |
|
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: 45.81 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 335 SLSIPSGSVTALVGPSGSGKSTVLSlllrlydpasgTISLdghdirqlnpvwlrskigtvsqepILFSCSIAENIAYGAD 414
Cdd:cd03227 15 DVTFGEGSLTIITGPNGSGKSTILD-----------AIGL------------------------ALGGAQSATRRRSGVK 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 415 DPSSVTAEEIQrvaevanavaFIRNFPQgfntvvgekgvlLSGGQKQRIAIARAL---LKNPKIL-LLDEATSALDAENE 490
Cdd:cd03227 60 AGCIVAAVSAE----------LIFTRLQ------------LSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDG 117
|
170 180 190
....*....|....*....|....*....|.
gi 767912302 491 YLVQEAL-DRLMDGRTVLVIAHRLSTIKNAN 520
Cdd:cd03227 118 QALAEAIlEHLVKGAQVIVITHLPELAELAD 148
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
455-519 |
1.46e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.10 E-value: 1.46e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767912302 455 LSGGQKQRIAIARALLK--NPKIL-LLDEATSAL---DaeneylVQ---EALDRLMD-GRTVLVIAHRLSTIKNA 519
Cdd:COG0178 827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLhfhD------IRkllEVLHRLVDkGNTVVVIEHNLDVIKTA 895
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
455-519 |
2.10e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 47.37 E-value: 2.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912302 455 LSGGQKQRIAIARALLKNP--KIL-LLDEATSALDAENeylVQ---EALDRLMD-GRTVLVIAHRLSTIKNA 519
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFED---IRkllEVLHRLVDkGNTVVVIEHNLDVIKTA 899
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
332-522 |
3.31e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.33 E-value: 3.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTV----------------LSLLLR-----LYDPA-------SGTISLDGHDIRQlN 383
Cdd:cd03270 12 KNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryvesLSAYARqflgqMDKPDvdsieglSPAIAIDQKTTSR-N 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 384 PvwlRSKIGTVSQ----EPILFScsiaeniaygaddpssvtaeeiqRVAeVANAVAFIRNFPQGFNTVVGEKGVLlSGGQ 459
Cdd:cd03270 91 P---RSTVGTVTEiydyLRLLFA-----------------------RVG-IRERLGFLVDVGLGYLTLSRSAPTL-SGGE 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767912302 460 KQRIAIARALLKNPK--ILLLDEATSAL-DAENEYLVqEALDRLMD-GRTVLVIAHRLSTIKNANMV 522
Cdd:cd03270 143 AQRIRLATQIGSGLTgvLYVLDEPSIGLhPRDNDRLI-ETLKRLRDlGNTVLVVEHDEDTIRAADHV 208
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
329-542 |
3.90e-05 |
|
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: 46.93 E-value: 3.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 329 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQlNPVWLRSKIGTVSQEPILFSCSIAEN 408
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLLTGRE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 409 IAYGADDPSSVTAEEIQRVAEVAnavafIRNFpqGFNTVVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAE 488
Cdd:TIGR01257 2032 HLYLYARLRGVPAEEIEKVANWS-----IQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQ 2104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 767912302 489 NEYLVQEALDRLM-DGRTVLVIAHRLSTIKN-ANMVAVLDQGKITEYGKHEELLSK 542
Cdd:TIGR01257 2105 ARRMLWNTIVSIIrEGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
38-156 |
7.16e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 45.00 E-value: 7.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 38 GLSAVFLCGAAANAIRV-YLMQTSGQRIVNRLrtslFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLR 116
Cdd:cd18601 67 GLTAATFVFGFLRSLLFfHVAVSASKNLHNKM----FASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFLQ 142
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 767912302 117 AGAQASVGISMMFFVSPnlatFVLSVVPPVSIIAVIYGRY 156
Cdd:cd18601 143 LLLQVVGVVLLAVVVNP----WVLIPVIPLVILFLFLRRY 178
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
32-259 |
1.03e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 44.46 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 32 LTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALlgRSV-TEN 110
Cdd:cd18779 41 LGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDLLMRLSSNATI--RELlTSQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 111 LSDGLRAGAQASVGISMMFFVSPNLATFVLSV-VPPVSIIAVIYGRyLRKLTK--VTQDSLAQATQLaeERIGNVRTVRA 187
Cdd:cd18779 119 TLSALLDGTLVLGYLALLFAQSPLLGLVVLGLaALQVALLLATRRR-VRELMAreLAAQAEAQSYLV--EALSGIETLKA 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912302 188 FGKEMTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSSFLMYA 259
Cdd:cd18779 196 SGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLALNALA 267
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
329-486 |
1.32e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.50 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 329 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDirqlnpvwlrsKIGTVSQEPILF-SCSIAE 407
Cdd:PRK15064 15 PLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPNE-----------RLGKLRQDQFAFeEFTVLD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 408 NIAYGADDPSSV-------------TAEEIQRVAEVANAVAFIRNFpqgfnTVVGEKGVLLSG----------------- 457
Cdd:PRK15064 84 TVIMGHTELWEVkqerdriyalpemSEEDGMKVADLEVKFAEMDGY-----TAEARAGELLLGvgipeeqhyglmsevap 158
|
170 180
....*....|....*....|....*....
gi 767912302 458 GQKQRIAIARALLKNPKILLLDEATSALD 486
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
312-509 |
1.41e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 312 ALEFKN--VHfaYPARPEVPIFQDFSLSIPSGSVTALVGPSGSGKsTVL--SLLLRLYDP-ASGTISLDGHDIRqlnpvw 386
Cdd:NF040905 257 VFEVKNwtVY--HPLHPERKVVDDVSLNVRRGEIVGIAGLMGAGR-TELamSVFGRSYGRnISGTVFKDGKEVD------ 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 387 lrskIGTVSQepilfscSIAENIAYGADD------------PSSVTAEEIQRVAE--VANAVAFIR---NFPQGFNT--- 446
Cdd:NF040905 328 ----VSTVSD-------AIDAGLAYVTEDrkgyglnliddiKRNITLANLGKVSRrgVIDENEEIKvaeEYRKKMNIktp 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767912302 447 VVGEKGVLLSGGQKQRIAIARALLKNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVI 509
Cdd:NF040905 397 SVFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAeGKGVIVI 460
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
455-522 |
2.07e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.07e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912302 455 LSGGQKQRIAIARALL---KNPKILLLDEATSALDAENEYLVQEALDRLMD-GRTVLVIAHRLSTIKNANMV 522
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHqGHTVVIIEHNMHVVKVADYV 881
|
|
| ABC_6TM_PrtD_like |
cd18586 |
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ... |
32-252 |
2.26e-04 |
|
Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides
Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 43.36 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 32 LTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENL 111
Cdd:cd18586 41 LLGLTLGMVVLLAFDGLLRQVRSRILQRVGLRLDVELGRRVFRAVLELPLESRPSGYWQQLLRDLDTLRNFLTGPSLFAF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 112 SDGLragaQASVGISMMFFVSPNLATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQLAEERIGNVRTVRAFGKE 191
Cdd:cd18586 121 FDLP----WAPLFLAVIFLIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGML 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912302 192 MTEIEKYASKVDHVMQLARKEAFARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGEL 252
Cdd:cd18586 197 GNLRRRWEARHAETLELQIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGELTIGAL 257
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
341-382 |
2.79e-04 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 41.35 E-value: 2.79e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 767912302 341 GSVTALVGPSGSGKSTVLSlllRLYDPASgTISLDghDIRQL 382
Cdd:COG4639 2 LSLVVLIGLPGSGKSTFAR---RLFAPTE-VVSSD--DIRAL 37
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
456-511 |
2.87e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.70 E-value: 2.87e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767912302 456 SGGQKQRIAIARALLKNPKILLLDEATSALDAE-----NEYLVQEAldrlmdgRTVLVIAH 511
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHavlwlETYLLKWP-------KTFIVVSH 399
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
331-369 |
2.93e-04 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 39.12 E-value: 2.93e-04
10 20 30
....*....|....*....|....*....|....*....
gi 767912302 331 FQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPAS 369
Cdd:pfam13555 12 FDGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
2-211 |
3.71e-04 |
|
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: 42.60 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 2 SSVISMSAPFFLGKIIDVIYTNPTVDYSdNLTRLCLGLSAVFLCGAAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEV 81
Cdd:cd18560 8 GKACNVLAPLFLGRAVNALTLAKVKDLE-SAVTLILLYALLRFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSLSL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 82 AFFDKTRTGELINRLSSDTALLgRSVTENLSDGLRAGAQASVGISMMFFV--SPNLATFVLSVVPPVSIIAVIYGRYLRK 159
Cdd:cd18560 87 DWHLSKKTGEVVRIMDRGTESA-NTLLSYLVFYLVPTLLELIVVSVVFAFhfGAWLALIVFLSVLLYGVFTIKVTEWRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 767912302 160 LTKVTQDSLAQATQLAEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARK 211
Cdd:cd18560 166 FRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVKEYQKSSVK 217
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
329-486 |
4.03e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.18 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 329 PIFQDFSLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP-----------VWLRSKIGTVSQE 397
Cdd:PRK10982 262 PSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNAneainhgfalvTEERRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 398 PILFSCSIAENIAY----GADDPSSVTAEeIQRVAEVANAVAfirnfpQGFNTVVGEkgvlLSGGQKQRIAIARALLKNP 473
Cdd:PRK10982 342 DIGFNSLISNIRNYknkvGLLDNSRMKSD-TQWVIDSMRVKT------PGHRTQIGS----LSGGNQQKVIIGRWLLTQP 410
|
170
....*....|...
gi 767912302 474 KILLLDEATSALD 486
Cdd:PRK10982 411 EILMLDEPTRGID 423
|
|
| RepA |
COG3598 |
RecA-family ATPase [Replication, recombination and repair]; |
338-511 |
5.79e-04 |
|
RecA-family ATPase [Replication, recombination and repair];
Pssm-ID: 442817 [Multi-domain] Cd Length: 313 Bit Score: 42.20 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 338 IPSGSVTALVGPSGSGKST-VLSLLLRLydpASGTiSLDGHDIRQLNPVWLrskigtvsqepilfscsiaeniayGADDP 416
Cdd:COG3598 10 LPEGGVTLLAGPPGTGKSFlALQLAAAV---AAGG-PWLGRRVPPGKVLYL------------------------AAEDD 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 417 ssvtAEEIQ-RVAEVANAVAFIRNFPQG-FNTVVGEKGVLLSGGQKQRIAIARAllKNPKILLLDEATSAL-----DAEN 489
Cdd:COG3598 62 ----RGELRrRLKALGADLGLPFADLDGrLRLLSLAGDLDDTDDLEALERAIEE--EGPDLVVIDPLARVFggdenDAEE 135
|
170 180
....*....|....*....|....
gi 767912302 490 EYLVQEALDRLMD--GRTVLVIAH 511
Cdd:COG3598 136 MRAFLNPLDRLAErtGAAVLLVHH 159
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
38-204 |
7.20e-04 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 41.78 E-value: 7.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 38 GLSAVFLCGAaaNAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTALLGRSVTENLSDGLRA 117
Cdd:cd18599 65 GGSILVILLL--SLIRGFVFVKVTLRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 118 GAQASVGISMMFFVSPnlatFVLSVVPPVSIIAVIYGRYLRKLTKVTQD----------SLAQATqlaeerIGNVRTVRA 187
Cdd:cd18599 143 VLLVVFSLIIIAIVFP----WFLIALIPLAIIFVFLSKIFRRAIRELKRlenisrsplfSHLTAT------IQGLSTIHA 212
|
170
....*....|....*..
gi 767912302 188 FGKEMTEIEKYASKVDH 204
Cdd:cd18599 213 FNKEKEFLSKFKKLLDQ 229
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
39-158 |
1.25e-03 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 40.92 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 39 LSAVFLCGAAanairvYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELINRLSSDTallgRSVTENLSDGLRag 118
Cdd:cd18606 47 LQAIFLFLFG------LLLAYLGIRASKRLHNKALKRVLRAPMSFFDTTPLGRILNRFSKDT----DVLDNELPDSLR-- 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 767912302 119 aQASVGISMMFfvspnlATFVLSVV---------PPVSIIAVIYGRYLR 158
Cdd:cd18606 115 -MFLYTLSSII------GTFILIIIylpwfaialPPLLVLYYFIANYYR 156
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
454-522 |
1.55e-03 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 41.50 E-value: 1.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912302 454 LLSGGQKQRIAIA--RALLK-NPK-ILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANMV 522
Cdd:pfam02463 1077 LLSGGEKTLVALAliFAIQKyKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKL 1149
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
332-547 |
1.60e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 332 QDFSLSIPSGSVTALVGPSGSGKSTVLS---------LLLRLYDPASGTISLDGHDIrqlnPVWLRSKIGT--------- 393
Cdd:PRK00635 1507 QNLNVSAPLHSLVAISGVSGSGKTSLLLegfykqacaLIEKGPSVFSEIIFLDSHPQ----ISSQRSDISTyfdiapslr 1582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 394 -----VSQEPIL------FS-------CSIAENIAYGADDPSSVTAEE----------IQRVA----------------- 428
Cdd:PRK00635 1583 nfyasLTQAKALnisasmFStntkqgqCSDCWGLGYQWIDRAFYALEKrpcptcsgfrIQPLAqevvyegkhfgqllqtp 1662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 429 --EVANAVAFIRNFPQGFNTVV---------GEKGVLLSGGQKQRIAIARALL---KNPKILLLDEATSALDAENEYLVQ 494
Cdd:PRK00635 1663 ieEVAETFPFLKKIQKPLQALIdnglgylplGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALL 1742
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 767912302 495 EALDRLMD-GRTVLVIAHRLSTIKNANMVAVLDQGKiTEYGKHEELLSKPNGIY 547
Cdd:PRK00635 1743 VQLRTLVSlGHSVIYIDHDPALLKQADYLIEMGPGS-GKTGGKILFSGPPKDIS 1795
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
1-111 |
1.95e-03 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 40.32 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 1 MSSVISMSAPFFLGKIIDVIytnpTVDYSDNLTRLCLgLSAVFLCGAAANAIRVYL---MQTSGQ-RIVNRLRTSLFSSI 76
Cdd:cd18556 13 LSSILISISPVILAKITDLL----TSSSSDSYNYIVV-LAALYVITISATKLLGFLslyLQSSLRvELIISISSSYFRYL 87
|
90 100 110
....*....|....*....|....*....|....*...
gi 767912302 77 LRQEVAFFDKTRTGEL---INRLSSDTALLGRSVTENL 111
Cdd:cd18556 88 YEQPKTFFVKENSGDItqrLNQASNDLYTLVRNLSTNI 125
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
331-378 |
2.06e-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: 40.76 E-value: 2.06e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 767912302 331 FQDFSLSIPSGsVTALVGPSGSGKSTVLSLLLRLYDPaSGTISLDGHD 378
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGP-SSSRKFDEED 59
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
343-404 |
3.55e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.68 E-value: 3.55e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767912302 343 VTALVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNPVWLRSKI-GTVSQEPILFSCS 404
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLnGIDPKEPIEFEIS 63
|
|
| Zeta_toxin |
pfam06414 |
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ... |
346-384 |
4.51e-03 |
|
Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.
Pssm-ID: 428926 Cd Length: 192 Bit Score: 38.50 E-value: 4.51e-03
10 20 30
....*....|....*....|....*....|....*....
gi 767912302 346 LVGPSGSGKSTVLSLLLRLYDPASGTISLDGHDIRQLNP 384
Cdd:pfam06414 16 LGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELHP 54
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
442-521 |
4.86e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.88 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767912302 442 QGFNTVVGEKGVL-----LSGGQKQ------RIAIARALLKNPKILLLDEATSALDAENEY----LVQEALDRLMDGRTV 506
Cdd:PRK01156 784 QDFNITVSRGGMVegidsLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTnlkdIIEYSLKDSSDIPQV 863
|
90
....*....|....*
gi 767912302 507 LVIAHRLSTIKNANM 521
Cdd:PRK01156 864 IMISHHRELLSVADV 878
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
454-521 |
5.48e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 38.21 E-value: 5.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767912302 454 LLSGGQKQRIAIAR--ALLK-NPK-ILLLDEATSALDAENEYLVQEALDRLMDGRTVLVIAHRLSTIKNANM 521
Cdd:cd03278 113 LLSGGEKALTALALlfAIFRvRPSpFCVLDEVDAALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADR 184
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
346-367 |
7.63e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 37.13 E-value: 7.63e-03
|
| |
