|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-491 |
3.73e-62 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 213.49 E-value: 3.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 4 YILKYKYDNLVHILLLALNAAIFVSASVTLALMTNQLVSKR-IQSFLALLGLEVGLYIIYLVLNYIIAVHQTKLIQKMTL 82
Cdd:COG1132 15 YLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGdLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 83 SIRQSYLSKIIHHSFSEFRKSDIGEHLSVLNNDIQLIESNGFSSIYTLCSTVFTTLFSIIALLSYDVRIVLLAIFLTLCL 162
Cdd:COG1132 95 DLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 163 TYLPKPFTNKMQKSMEKFSQANEELVSGVSDQLYGYADVYYASRKQIFLRQVRSIVEEYIVQKIIFTKRNTSTETLMALF 242
Cdd:COG1132 175 LLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 243 SVAAQMLILLLTGLLIIFGNIAVGTIASVGQISGNIFNSLSTINQLQVTIKSVDPILKKFHDF---------PEDPKTCI 313
Cdd:COG1132 255 GNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELldeppeipdPPGAVPLP 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 314 ATIQDVRFENVSYHFGENA-IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVS 392
Cdd:COG1132 335 PVRGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRR 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 393 NCAYVGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSR----IDEQVSDG--SFSEGQKQRIGLIRAFLKG 466
Cdd:COG1132 415 QIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEAlpdgYDTVVGERgvNLSGGQRQRIAIARALLKD 494
|
490 500
....*....|....*....|....*
gi 1937373637 467 SSVVIFDEATANLDhnnaTRIEHLL 491
Cdd:COG1132 495 PPILILDEATSALD----TETEALI 515
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-523 |
1.81e-57 |
|
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: 203.53 E-value: 1.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 4 YILKYKYDnLVHILLLALNAAIF--VSASVTLALMTNQLVSKRIQSFLALLGLEVGLYIIYLVLNYIiavhQTKLI---- 77
Cdd:COG2274 150 LLRRYRRL-LLQVLLASLLINLLalATPLFTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLL----RSYLLlrlg 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 78 QKMTLSIRQSYLSKIIHHSFSEFRKSDIGEHLSVLNnDIQLIEsNGFSSIY-TLCSTVFTTLFSIIALLSYDVRIVLLAI 156
Cdd:COG2274 225 QRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIR-EFLTGSLlTALLDLLFVLIFLIVLFFYSPPLALVVL 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 157 FLTLCLTYLPKPFTNKMQKSMEKFSQANEELVSGVSDQLYGYADVYYASRKQIFLRQVRSIVEEYIVQKIIFTKRNTSTE 236
Cdd:COG2274 303 LLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLS 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 237 TLMALFSVAAQMLILLLTGLLIIFGNIAVGT-IAS---VGQISG---NIFNSLSTINQLQVTIKSVDPILKKFHDFPEDP 309
Cdd:COG2274 383 TLSGLLQQLATVALLWLGAYLVIDGQLTLGQlIAFnilSGRFLApvaQLIGLLQRFQDAKIALERLDDILDLPPEREEGR 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 310 -KTCIATIQ-DVRFENVSYHFGENA--IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEI 385
Cdd:COG2274 463 sKLSLPRLKgDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQI 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 386 DENSIVSNCAYVGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSR----IDEQVSDG--SFSEGQKQRIGL 459
Cdd:COG2274 543 DPASLRRQIGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEAlpmgYDTVVGEGgsNLSGGQRQRLAI 622
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937373637 460 IRAFLKGSSVVIFDEATANLDHNNATRI-EHLLLSDPNITYITVTHHL--IKenepYFDEIIRLGEG 523
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIIlENLRRLLKGRTVIIIAHRLstIR----LADRIIVLDKG 685
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
97-524 |
4.62e-41 |
|
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: 155.69 E-value: 4.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 97 FSEFRKSDIgehLSVLNNDIQLIEsNGF-SSIYTLCSTVFTTLFSIIALLSYDVRI-VLLAIFLTLCLTYLPKPFTNKMQ 174
Cdd:COG4987 106 LARLRSGDL---LNRLVADVDALD-NLYlRVLLPLLVALLVILAAVAFLAFFSPALaLVLALGLLLAGLLLPLLAARLGR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 175 KSMEKFSQANEELVSGVSDQLYGYADVYYASRKQIFLRQVRSIVEEYIV----QKIIFTKRNTSTETLMALFSVAAqmli 250
Cdd:COG4987 182 RAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAaqrrLARLSALAQALLQLAAGLAVVAV---- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 251 llltgllIIFGNIAVGTiasvGQISGNI-----------FNSLSTI----NQLQVTIKS---VDPIL--KKFHDFPEDPK 310
Cdd:COG4987 258 -------LWLAAPLVAA----GALSGPLlallvlaalalFEALAPLpaaaQHLGRVRAAarrLNELLdaPPAVTEPAEPA 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 311 TcIATIQDVRFENVSYHF--GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDEN 388
Cdd:COG4987 327 P-APGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 389 SIVSNCAYVGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSR----IDEQVSDG--SFSEGQKQRIGLIRA 462
Cdd:COG4987 406 DLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAAlpdgLDTWLGEGgrRLSGGERRRLALARA 485
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937373637 463 FLKGSSVVIFDEATANLDHNNATRIEHLLLS-DPNITYITVTHHLikENEPYFDEIIRLGEGT 524
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLADLLEaLAGRTVLLITHRL--AGLERMDRILVLEDGR 546
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
318-523 |
8.34e-41 |
|
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: 154.92 E-value: 8.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 318 DVRFENVSYHF-GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAY 396
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSR----IDEQVSDGSF--SEGQKQRIGLIRAFLKGSSVV 470
Cdd:COG4988 416 VPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAAlpdgLDTPLGEGGRglSGGQAQRLALARALLRDAPLL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1937373637 471 IFDEATANLDHNNATRIEHLL--LSdPNITYITVTHHLikENEPYFDEIIRLGEG 523
Cdd:COG4988 496 LLDEPTAHLDAETEAEILQALrrLA-KGRTVILITHRL--ALLAQADRILVLDDG 547
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
319-523 |
9.12e-34 |
|
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: 125.57 E-value: 9.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENA--IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAY 396
Cdd:cd03228 1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQTHIYNDTLRNNLtlwneaitdthikealervnllsflsrideqvsdgsFSEGQKQRIGLIRAFLKGSSVVIFDEAT 476
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------LSGGQRQRIAIARALLRDPPILILDEAT 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937373637 477 ANLDHNNATRIEHLLLS-DPNITYITVTHHLikENEPYFDEIIRLGEG 523
Cdd:cd03228 125 SALDPETEALILEALRAlAKGKTVIVIAHRL--STIRDADRIIVLDDG 170
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
320-524 |
8.06e-30 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 116.07 E-value: 8.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 320 RFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYVGS 399
Cdd:COG4619 2 ELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 400 QTHIYNDTLRNNLTLW----NEAITDTHIKEALERVNL-LSFLSRideQVSDgsFSEGQKQRIGLIRAFLKGSSVVIFDE 474
Cdd:COG4619 82 EPALWGGTVRDNLPFPfqlrERKFDRERALELLERLGLpPDILDK---PVER--LSGGERQRLALIRALLLQPDVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1937373637 475 ATANLDHNNATRIEHLL---LSDPNITYITVTHHLIKENEpYFDEIIRLGEGT 524
Cdd:COG4619 157 PTSALDPENTRRVEELLreyLAEEGRAVLWVSHDPEQIER-VADRVLTLEAGR 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
318-524 |
1.33e-28 |
|
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: 113.47 E-value: 1.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 318 DVRFENVSYHFGE-NAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAY 396
Cdd:cd03254 2 EIEFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSRI----DEQVSDGS--FSEGQKQRIGLIRAFLKGSSVV 470
Cdd:cd03254 82 VLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLpngyDTVLGENGgnLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937373637 471 IFDEATANLDHNNATRIEHLLLS-DPNITYITVTHHL--IKENepyfDEIIRLGEGT 524
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKlMKGRTSIIIAHRLstIKNA----DKILVLDDGK 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
318-504 |
3.41e-28 |
|
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: 111.91 E-value: 3.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 318 DVRFENVSYHF--GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCA 395
Cdd:cd03245 2 RIEFRNVSFSYpnQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 396 YVGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSR----IDEQVSDGSF--SEGQKQRIGLIRAFLKGSSV 469
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKhpngLDLQIGERGRglSGGQRQAVALARALLNDPPI 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1937373637 470 VIFDEATANLDHNNATR-IEHLLLSDPNITYITVTH 504
Cdd:cd03245 162 LLLDEPTSAMDMNSEERlKERLRQLLGDKTLIIITH 197
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
319-520 |
7.53e-28 |
|
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: 117.00 E-value: 7.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHF-GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYV 397
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 GSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLS----RIDEQVSDGS--FSEGQKQRIGLIRAFLKGSSVVI 471
Cdd:TIGR02857 402 PQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAalpqGLDTPIGEGGagLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937373637 472 FDEATANLD-HNNATRIEHLLLSDPNITYITVTHHL-IKENepyFDEIIRL 520
Cdd:TIGR02857 482 LDEPTAHLDaETEAEVLEALRALAQGRTVLLVTHRLaLAAL---ADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
318-524 |
5.73e-26 |
|
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: 105.65 E-value: 5.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 318 DVRFENVS--YHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCA 395
Cdd:cd03244 2 DIEFKNVSlrYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 396 YVGSQTHIYNDTLRNNLTLWNEAiTDTHIKEALERVNLLSFLS----RIDEQVSDG--SFSEGQKQRIGLIRAFLKGSSV 469
Cdd:cd03244 82 IIPQDPVLFSGTIRSNLDPFGEY-SDEELWQALERVGLKEFVEslpgGLDTVVEEGgeNLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937373637 470 VIFDEATANLDHNNATRIEHLLLS-DPNITYITVTHHL--IKEnepyFDEIIRLGEGT 524
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREaFKDCTVLTIAHRLdtIID----SDRILVLDKGR 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
319-491 |
4.05e-25 |
|
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: 102.94 E-value: 4.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKlESKEIDENSIVSNCAYVG 398
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG-EPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 SQTHIYND-TLRNNLTLW----NEAITDTHIKEALERVNLLSFLsriDEQVsdGSFSEGQKQRIGLIRAFLKGSSVVIFD 473
Cdd:COG4133 82 HADGLKPElTVRENLRFWaalyGLRADREAIDEALEAVGLAGLA---DLPV--RQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170
....*....|....*...
gi 1937373637 474 EATANLDHNNATRIEHLL 491
Cdd:COG4133 157 EPFTALDAAGVALLAELI 174
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
318-506 |
1.08e-23 |
|
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: 104.36 E-value: 1.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 318 DVRFENVSYHF-GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAY 396
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSRIDEQVS-----DG-SFSEGQKQRIGLIRAFLKGSSVV 470
Cdd:TIGR02868 414 CAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDtvlgeGGaRLSGGERQRLALARALLADAPIL 493
|
170 180 190
....*....|....*....|....*....|....*..
gi 1937373637 471 IFDEATANLDHNNATRIEHLLLS-DPNITYITVTHHL 506
Cdd:TIGR02868 494 LLDEPTEHLDAETADELLEDLLAaLSGRTVVLITHHL 530
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
319-523 |
8.14e-23 |
|
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: 96.92 E-value: 8.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFG--ENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAY 396
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSRIDEQV-----SDGS-FSEGQKQRIGLIRAFLKGSSVV 470
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYdtvigERGVkLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 471 IFDEATANLDhNNATR-----IEHLLlsdPNITYITVTHHL--IKENepyfDEIIRLGEG 523
Cdd:cd03251 161 ILDEATSALD-TESERlvqaaLERLM---KNRTTFVIAHRLstIENA----DRIVVLEDG 212
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
319-523 |
1.00e-22 |
|
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: 96.92 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFG-ENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYV 397
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 GSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNL----LSFLSRIDEQVSDGS--FSEGQKQRIGLIRAFLKGSSVVI 471
Cdd:cd03253 81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIhdkiMRFPDGYDTIVGERGlkLSGGEKQRVAIARAILKNPPILL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1937373637 472 FDEATANLDHNNATRI-EHLLLSDPNITYITVTHHL--IKENepyfDEIIRLGEG 523
Cdd:cd03253 161 LDEATSALDTHTEREIqAALRDVSKGRTTIVIAHRLstIVNA----DKIIVLKDG 211
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
305-524 |
1.11e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 98.36 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 305 FPEDPKTCIA----TIQDVRFenvSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKL 380
Cdd:PRK11160 326 FPTTSTAAADqvslTLNNVSF---TYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 381 ESKEIDENSIVSNCAYVGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERV---NLLSFLSRIDEQVSDG--SFSEGQKQ 455
Cdd:PRK11160 403 PIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVgleKLLEDDKGLNAWLGEGgrQLSGGEQR 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 456 RIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLSD-PNITYITVTHHLIkeNEPYFDEIIRLGEGT 524
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHaQNKTVLMITHRLT--GLEQFDRICVMDNGQ 550
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
320-524 |
2.59e-21 |
|
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: 90.38 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 320 RFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYVGS 399
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 400 qthiyndtlrnnltlwneaitdthikealervnllsflsrideqvsdgsFSEGQKQRIGLIRAFLKGSSVVIFDEATANL 479
Cdd:cd00267 81 -------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1937373637 480 DHNNATRIEHLL--LSDPNITYITVTHHLiKENEPYFDEIIRLGEGT 524
Cdd:cd00267 112 DPASRERLLELLreLAEEGRTVIIVTHDP-ELAELAADRVIVLKDGK 157
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
319-480 |
5.60e-21 |
|
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: 91.83 E-value: 5.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHF---GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCA 395
Cdd:cd03249 1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 396 YVGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLS----RIDEQVSDGSF--SEGQKQRIGLIRAFLKGSSV 469
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMslpdGYDTLVGERGSqlSGGQKQRIAIARALLRNPKI 160
|
170
....*....|.
gi 1937373637 470 VIFDEATANLD 480
Cdd:cd03249 161 LLLDEATSALD 171
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
320-524 |
5.88e-21 |
|
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: 90.99 E-value: 5.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 320 RFENVSYHF--GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYV 397
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 G--SQTHIYNDTLR-------NNLTLwNEAITDTHIKEALERVNLLSFLSRideqvSDGSFSEGQKQRIGLIRAFLKGSS 468
Cdd:cd03225 81 FqnPDDQFFGPTVEeevafglENLGL-PEEEIEERVEEALELVGLEGLRDR-----SPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937373637 469 VVIFDEATANLDHNNATRIEHLL--LSDPNITYITVTHHLiKENEPYFDEIIRLGEGT 524
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLkkLKAEGKTIIIVTHDL-DLLLELADRVIVLEDGK 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
322-524 |
8.76e-20 |
|
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: 88.76 E-value: 8.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGkLESKEIDENSIVSNCAYVGSQT 401
Cdd:COG4555 5 ENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILID-GEDVRKEPREARRQIGVLPDER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 402 HIY-NDTLRNNLTLWNEA--ITDTHIKEALERVN-LLSFLSRIDEQVSDgsFSEGQKQRIGLIRAFLKGSSVVIFDEATA 477
Cdd:COG4555 84 GLYdRLTVRENIRYFAELygLFDEELKKRIEELIeLLGLEEFLDRRVGE--LSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937373637 478 NLDHNNATRI-EHLL-LSDPNITyITVTHHLIKENEPYFDEIIRLGEGT 524
Cdd:COG4555 162 GLDVMARRLLrEILRaLKKEGKT-VLFSSHIMQEVEALCDRVVILHKGK 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
319-523 |
1.02e-19 |
|
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: 86.60 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENA--IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIdENSIVSNCAY 396
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQTHIYNDTLRNNLTLwneaitdthikealervnllsflsrideqvsdgSFSEGQKQRIGLIRAFLKGSSVVIFDEAT 476
Cdd:cd03247 80 LNQRPYLFDTTLRNNLGR---------------------------------RFSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937373637 477 ANLDHNNATRIEHLLLSD-PNITYITVTHHL--IKenepYFDEIIRLGEG 523
Cdd:cd03247 127 VGLDPITERQLLSLIFEVlKDKTLIWITHHLtgIE----HMDKILFLENG 172
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
52-506 |
1.33e-19 |
|
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: 92.50 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 52 LGLeVGLYIIYLVLNYIIAVHQTKLIQKMTLSIRQSYLSKIIHHSFSEFRKSDIGEHLSVLNNDIQLIESNGfSSIYTLC 131
Cdd:TIGR01193 200 IGL-IIAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALA-STILSLF 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 132 STVFTTLFSIIALLSYDVR---IVLLAIFLTLCLTYLPKPFTNKM-QKSMekfsQANEELVSGVSDQLYGYADVYYASRK 207
Cdd:TIGR01193 278 LDMWILVIVGLFLVRQNMLlflLSLLSIPVYAVIIILFKRTFNKLnHDAM----QANAVLNSSIIEDLNGIETIKSLTSE 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 208 QIFLRQVRSIVEEYIVQKIIFTKRNTSTETLMALFSVAAQMLILLLTGLLIIFGNIAVGTIASVGQISGNIFNSLSTINQ 287
Cdd:TIGR01193 354 AERYSKIDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITFNALLSYFLTPLENIIN 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 288 LQ-------VTIKSVDPILKKFHDFpEDPKTCIATIQ---DVRFENVSYHFGENA-IIKGFTQTFKEGGKYAITGCSGSG 356
Cdd:TIGR01193 434 LQpklqaarVANNRLNEVYLVDSEF-INKKKRTELNNlngDIVINDVSYSYGYGSnILSDISLTIKMNSKTTIVGMSGSG 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 357 KSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYVGSQTHIYNDTLRNNLTLWN-EAITDTHIKEALERVNL-- 433
Cdd:TIGR01193 513 KSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAkENVSQDEIWAACEIAEIkd 592
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937373637 434 ------LSFLSRIDEqvSDGSFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLSDPNITYITVTHHL 506
Cdd:TIGR01193 593 dienmpLGYQTELSE--EGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIFVAHRL 669
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
306-525 |
3.62e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.64 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 306 PEDPKTCIATIQD--VRFENVS-YHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLES 382
Cdd:COG4178 348 LPEAASRIETSEDgaLALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGAR 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 383 keidensivsnCAYVGSQTHIYNDTLRNNLTLWN--EAITDTHIKEALERVNLLSFLSRIDEQVS-DGSFSEGQKQRIGL 459
Cdd:COG4178 428 -----------VLFLPQRPYLPLGTLREALLYPAtaEAFSDAELREALEAVGLGHLAERLDEEADwDQVLSLGEQQRLAF 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937373637 460 IRAFLKGSSVVIFDEATANLDHNNATRIEHLLLSD-PNITYITVTHHliKENEPYFDEIIRLGEGTE 525
Cdd:COG4178 497 ARLLLHKPDWLFLDEATSALDEENEAALYQLLREElPGTTVISVGHR--STLAAFHDRVLELTGDGS 561
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
340-506 |
4.93e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 90.29 E-value: 4.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 340 TFKEGGKYAITGCSGSGKSTLLNLLLGNLKdYEGKILFGKLESKEIDENSIVSNCAYVGSQTHIYNDTLRNNLTLWNEAI 419
Cdd:PRK11174 372 TLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDA 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 420 TDTHIKEALERVNLLSFLSR----IDEQVSDGS--FSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLS 493
Cdd:PRK11174 451 SDEQLQQALENAWVSEFLPLlpqgLDTPIGDQAagLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNA 530
|
170
....*....|....
gi 1937373637 494 DPN-ITYITVTHHL 506
Cdd:PRK11174 531 ASRrQTTLMVTHQL 544
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
319-506 |
1.24e-18 |
|
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: 84.83 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHF---GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILfgkLESKEI---DENSIVS 392
Cdd:cd03248 12 VKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVL---LDGKPIsqyEHKYLHS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 393 NCAYVGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSR----IDEQVSD--GSFSEGQKQRIGLIRAFLKG 466
Cdd:cd03248 89 KVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISElasgYDTEVGEkgSQLSGGQKQRVAIARALIRN 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1937373637 467 SSVVIFDEATANLDHNNATRIEHLLLSDP-NITYITVTHHL 506
Cdd:cd03248 169 PQVLILDEATSALDAESEQQVQQALYDWPeRRTVLVIAHRL 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
334-477 |
2.99e-18 |
|
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: 81.54 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 334 IKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYVGSQTHIYND-TLRNNL 412
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937373637 413 TL------WNEAITDTHIKEALERVNLLSFLSR-IDEQVSdgSFSEGQKQRIGLIRAFLKGSSVVIFDEATA 477
Cdd:pfam00005 81 RLglllkgLSKREKDARAEEALEKLGLGDLADRpVGERPG--TLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
319-524 |
8.46e-18 |
|
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: 82.38 E-value: 8.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHF-GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYV 397
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 ----GSQthIYNDTLRN-------NLTLwNEAITDTHIKEALERVNLLSFLSRideqvSDGSFSEGQKQRIGLIRAFLKG 466
Cdd:COG1122 81 fqnpDDQ--LFAPTVEEdvafgpeNLGL-PREEIRERVEEALELVGLEHLADR-----PPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 467 SSVVIFDEATANLDHNNATRIEHLL--LSDPNITYITVTHHLiKENEPYFDEIIRLGEGT 524
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLkrLNKEGKTVIIVTHDL-DLVAELADRVIVLDDGR 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-523 |
3.02e-17 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 81.29 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKI-LFGKLESKeiDENSIvsncAYV 397
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVrLFGKPPRR--ARRRI----GYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 gSQTHIYNDTL--------------RNNLTLWNEAITDTHIKEALERVNLLSFLSRideQVsdGSFSEGQKQRIGLIRAF 463
Cdd:COG1121 81 -PQRAEVDWDFpitvrdvvlmgrygRRGLFRRPSRADREAVDEALERVGLEDLADR---PI--GELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937373637 464 LKGSSVVIFDEATANLDHNNATRIEHLL--LSDPNITYITVTHHL--IKEnepYFDEIIRLGEG 523
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLreLRREGKTILVVTHDLgaVRE---YFDRVLLLNRG 215
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
80-523 |
3.30e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 84.77 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 80 MTLSIRQSYLSKIIHHSFSEFRKSDIGEHLSVLNNDIQLIesngfSSIYTLCSTVFT-----TLFSIIALLSYDVRIVLL 154
Cdd:TIGR00958 232 INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTM-----SRSLSLNVNVLLrnlvmLLGLLGFMLWLSPRLTMV 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 155 AIFLTLCLTYLPKPF-------TNKMQKSMEKFSQANEELVSGVSDQLYGYADVYYASRKQIFLRQVRSIVEEYIVQKII 227
Cdd:TIGR00958 307 TLINLPLVFLAEKVFgkryqllSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAG 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 228 FTkrnTSTEtLMALFSvaaQMLILLLTGLLIIFGNIAVGTIASV----GQISGNIFNSLSTINQLQVTIKSVDPILKKFH 303
Cdd:TIGR00958 387 YL---WTTS-VLGMLI---QVLVLYYGGQLVLTGKVSSGNLVSFllyqEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLD 459
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 304 DFPEDPKTCIATIQDVR----FENVSYHF---GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKIL 376
Cdd:TIGR00958 460 RKPNIPLTGTLAPLNLEglieFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVL 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 377 FGKLESKEIDENSIVSNCAYVGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSR----IDEQVSD-GSF-S 450
Cdd:TIGR00958 540 LDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEfpngYDTEVGEkGSQlS 619
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937373637 451 EGQKQRIGLIRAFLKGSSVVIFDEATANLDhnnaTRIEHLLLSDPN---ITYITVTHHL-IKENEpyfDEIIRLGEG 523
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALD----AECEQLLQESRSrasRTVLLIAHRLsTVERA---DQILVLKKG 689
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
320-520 |
3.91e-17 |
|
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: 80.27 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 320 RFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKI-LFGKleSKEIDENSIvsncAYVg 398
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIrVFGK--PLEKERKRI----GYV- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 SQTHIYNDTL--------------RNNLTLWNEAITDTHIKEALERVNLLSFLSR-IDEqvsdgsFSEGQKQRIGLIRAF 463
Cdd:cd03235 74 PQRRSIDRDFpisvrdvvlmglygHKGLFRRLSKADKAKVDEALERVGLSELADRqIGE------LSGGQQQRVLLARAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937373637 464 LKGSSVVIFDEATANLDHNNATRIEHLL--LSDPNITYITVTHHLiKENEPYFDEIIRL 520
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLreLRREGMTILVVTHDL-GLVLEYFDRVLLL 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
322-524 |
1.44e-16 |
|
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: 77.48 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYVgSQt 401
Cdd:cd03214 3 ENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV-PQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 402 hiyndtlrnnltlwneaitdthikeALERVNLLSFLSRIDEQVSDgsfseGQKQRIGLIRAFLKGSSVVIFDEATANLDH 481
Cdd:cd03214 81 -------------------------ALELLGLAHLADRPFNELSG-----GERQRVLLARALAQEPPILLLDEPTSHLDI 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937373637 482 NNATRIEHLL--LSD-PNITYITVTHHLikeNE--PYFDEIIRLGEGT 524
Cdd:cd03214 131 AHQIELLELLrrLAReRGKTVVMVLHDL---NLaaRYADRVILLKDGR 175
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
318-480 |
2.39e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.99 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 318 DVRFENVS--YHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCA 395
Cdd:PRK11176 341 DIEFRNVTftYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVA 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 396 YVGSQTHIYNDTLRNNLTLwneAITDTHIKEALERVNLLSFLSRIDEQVSDG----------SFSEGQKQRIGLIRAFLK 465
Cdd:PRK11176 421 LVSQNVHLFNDTIANNIAY---ARTEQYSREQIEEAARMAYAMDFINKMDNGldtvigengvLLSGGQRQRIAIARALLR 497
|
170
....*....|....*
gi 1937373637 466 GSSVVIFDEATANLD 480
Cdd:PRK11176 498 DSPILILDEATSALD 512
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
322-504 |
2.50e-16 |
|
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: 76.87 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGENA--IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYVgs 399
Cdd:cd03246 4 ENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 400 qthiyndtlrnnltlwneaitdthikeaLERVNLLSflsridEQVSDGSFSEGQKQRIGLIRAFLKGSSVVIFDEATANL 479
Cdd:cd03246 82 ----------------------------PQDDELFS------GSIAENILSGGQRQRLGLARALYGNPRILVLDEPNSHL 127
|
170 180
....*....|....*....|....*..
gi 1937373637 480 DHNNATRIEHLL--LSDPNITYITVTH 504
Cdd:cd03246 128 DVEGERALNQAIaaLKAAGATRIVIAH 154
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
322-491 |
4.92e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 76.63 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDEnSIVSNCAYVGSQT 401
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 402 HIYND-TLRNNLTLWNE--AITDTHIKEALERVNLLSFlsridEQVSDGSFSEGQKQRIGLIRAFLKGSSVVIFDEATAN 478
Cdd:TIGR01189 83 GLKPElSALENLHFWAAihGGAQRTIEDALAAVGLTGF-----EDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170
....*....|...
gi 1937373637 479 LDHNNATRIEHLL 491
Cdd:TIGR01189 158 LDKAGVALLAGLL 170
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
319-506 |
6.82e-16 |
|
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: 76.84 E-value: 6.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTL------LNLLLGNLKDyEGKILFGKLESKEIDENsIVS 392
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLlrllnrLNDLIPGAPD-EGEVLLDGKDIYDLDVD-VLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 393 NCAYVG---SQTHIYNDTLRNNLTL-------WNEAITDTHIKEALERVNLlsflsriDEQVSD----GSFSEGQKQRIG 458
Cdd:cd03260 79 LRRRVGmvfQKPNPFPGSIYDNVAYglrlhgiKLKEELDERVEEALRKAAL-------WDEVKDrlhaLGLSGGQQQRLC 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937373637 459 LIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLS-DPNITYITVTHHL 506
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAElKKEYTIVIVTHNM 200
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
319-523 |
2.09e-15 |
|
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: 75.22 E-value: 2.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENA----IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVS-- 392
Cdd:cd03255 1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 393 --NCAYVGSQTHIYND-TLRNNLTL--------WNEAITDthIKEALERVNLLSFLSRIDEQVSdGsfseGQKQRIGLIR 461
Cdd:cd03255 81 rrHIGFVFQSFNLLPDlTALENVELplllagvpKKERRER--AEELLERVGLGDRLNHYPSELS-G----GQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937373637 462 AFLKGSSVVIFDEATANLDHNNATRIEHLLLS---DPNITYITVTH-HLIKEnepYFDEIIRLGEG 523
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRElnkEAGTTIVVVTHdPELAE---YADRIIELRDG 216
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
322-504 |
2.22e-15 |
|
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: 76.00 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGE----NAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYV 397
Cdd:COG1124 5 RNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 gSQtHIY---------NDTLRNNLTLWNEAITDTHIKEALERVNL-LSFLSRIDEQVSDgsfseGQKQRIGLIRAFLKGS 467
Cdd:COG1124 85 -FQ-DPYaslhprhtvDRILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSG-----GQRQRVAIARALILEP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1937373637 468 SVVIFDEATANLDHNNATRIEHLLLS---DPNITYITVTH 504
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDlreERGLTYLFVSH 197
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
16-248 |
2.22e-15 |
|
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: 76.82 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 16 ILLLALNAAIFVSASVTLALMTNQLV-----SKRIQSFLALLGLEVGLYIIYLVLNYIIAVHQTKLIQKMTLSIRQSYLS 90
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIddvipAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 91 KIIHHSFSEFRKSDIGEHLSVLNNDIQLIESNGFSSIYTLCSTVFTTLFSIIALLSYDVRIVLLAIFLTLCLTYLPKPFT 170
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937373637 171 NKMQKSMEKFSQANEELVSGVSDQLYGYADVYYASRKQIFLRQVRSIVEEYIVQKIIFTKRNTSTETLMALFSVAAQM 248
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTA 238
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
320-523 |
2.42e-15 |
|
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: 75.68 E-value: 2.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 320 RFENVSYHFGEN-AIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILF-----GKLESKEIdeNSIVSN 393
Cdd:cd03256 2 EVENLSKTYPNGkKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdgtdiNKLKGKAL--RQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 394 CAY-------VGSQTHIYN---------DTLRNNLTLWNEAitDTHI-KEALERVNLLSF-LSRIDEqvsdgsFSEGQKQ 455
Cdd:cd03256 80 IGMifqqfnlIERLSVLENvlsgrlgrrSTWRSLFGLFPKE--EKQRaLAALERVGLLDKaYQRADQ------LSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937373637 456 RIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLS---DPNITYITVTHH--LIKEnepYFDEIIRLGEG 523
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRinrEEGITVIVSLHQvdLARE---YADRIVGLKDG 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
320-524 |
3.63e-15 |
|
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: 74.22 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 320 RFENVSYHFGENA-IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKlesKEIDENSIVSNCAYV- 397
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVm 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 -GSQTHIYNDTLRNNLTLWNEAITD--THIKEALERVNLLSFlsridEQVSDGSFSEGQKQRIGLIRAFLKGSSVVIFDE 474
Cdd:cd03226 78 qDVDYQLFTDSVREELLLGLKELDAgnEQAETVLKDLDLYAL-----KERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1937373637 475 ATANLDHNNATRIEHLL--LSDPNITYITVTH--HLIKEnepYFDEIIRLGEGT 524
Cdd:cd03226 153 PTSGLDYKNMERVGELIreLAAQGKAVIVITHdyEFLAK---VCDRVLLLANGA 203
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
318-506 |
7.27e-15 |
|
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: 73.60 E-value: 7.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 318 DVRFENVSYHFGEN--AIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCA 395
Cdd:cd03369 6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 396 YVGSQTHIYNDTLRNNLTLWNEaITDTHIKEALErvnllsflsrideqVSDG--SFSEGQKQRIGLIRAFLKGSSVVIFD 473
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLDPFDE-YSDEEIYGALR--------------VSEGglNLSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190
....*....|....*....|....*....|....
gi 1937373637 474 EATANLDHNNATRIEHLLLSD-PNITYITVTHHL 506
Cdd:cd03369 151 EATASIDYATDALIQKTIREEfTNSTILTIAHRL 184
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
319-506 |
8.06e-15 |
|
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: 73.69 E-value: 8.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHF----GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFG------------KLES 382
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDgkdllklsrrlrKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 383 KEIdenSIVSNCAY--------VGsqtHIYNDTLRNNLTLWNEAITDTHIKEALERVNLlsflsriDEQVSD---GSFSE 451
Cdd:cd03257 82 KEI---QMVFQDPMsslnprmtIG---EQIAEPLRIHGKLSKKEARKEAVLLLLVGVGL-------PEEVLNrypHELSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937373637 452 GQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLL---SDPNITYITVTHHL 506
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklqEELGLTLLFITHDL 206
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
318-506 |
1.58e-14 |
|
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: 76.32 E-value: 1.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 318 DVRFENVSYHFGENA--IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCA 395
Cdd:TIGR01846 455 AITFENIRFRYAPDSpeVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMG 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 396 YVGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSRI----DEQVSD--GSFSEGQKQRIGLIRAFLKGSSV 469
Cdd:TIGR01846 535 VVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELpqgyNTEVGEkgANLSGGQRQRIAIARALVGNPRI 614
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1937373637 470 VIFDEATANLDHNNatriEHLLLSD-PNI----TYITVTHHL 506
Cdd:TIGR01846 615 LIFDEATSALDYES----EALIMRNmREIcrgrTVIIIAHRL 652
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
329-491 |
2.63e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 71.76 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 329 GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILfgkLESKEIDE--NSIVSNCAYVGSQTHIYND 406
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVL---LNGGPLDFqrDSIARGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 407 -TLRNNLTLWNEAITDTHIKEALERVNLLSFlsridEQVSDGSFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNAT 485
Cdd:cd03231 88 lSVLENLRFWHADHSDEQVEEALARVGLNGF-----EDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA 162
|
....*.
gi 1937373637 486 RIEHLL 491
Cdd:cd03231 163 RFAEAM 168
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
319-504 |
6.38e-14 |
|
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: 70.64 E-value: 6.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFG--KLESKEIDENSIVSNCAY 396
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQTHIY-NDTLRNNLTL-------WNEAITDTHIKEALERVNLLSFlsridEQVSDGSFSEGQKQRIGLIRAFLKGSS 468
Cdd:cd03262 81 VFQQFNLFpHLTVLENITLapikvkgMSKAEAEERALELLEKVGLADK-----ADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 1937373637 469 VVIFDEATANLDHNNATRIEHLL--LSDPNITYITVTH 504
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMkdLAEEGMTMVVVTH 193
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
135-480 |
8.75e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.84 E-value: 8.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 135 FTTLFSIIALL----SYDVR-----IVLLAIFLtlCLTYLPKPFTNKMQKSMEKFsqaNEELVSGVSDQLYGYADVYYAS 205
Cdd:PRK13657 138 LATLVALVVLLplalFMNWRlslvlVVLGIVYT--LITTLVMRKTKDGQAAVEEH---YHDLFAHVSDAIGNVSVVQSYN 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 206 RKQIFLRQVRSIVEEYI-VQKIIFT--------KRNTSTETLMALFSVAAQMLILlltglliifGNIAVGTIASvgqisg 276
Cdd:PRK13657 213 RIEAETQALRDIADNLLaAQMPVLSwwalasvlNRAASTITMLAILVLGAALVQK---------GQLRVGEVVA------ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 277 niFNSLST--INQL-QV-----TIKSVDPILKKFHDF---------PEDPKTCIATIQDVRFENVSYHF-GENAIIKGFT 338
Cdd:PRK13657 278 --FVGFATllIGRLdQVvafinQVFMAAPKLEEFFEVedavpdvrdPPGAIDLGRVKGAVEFDDVSFSYdNSRQGVEDVS 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 339 QTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYVGSQTHIYNDTLRNNLTLWNEA 418
Cdd:PRK13657 356 FEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPD 435
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937373637 419 ITDTHIKEALERVNLLSFLSR----IDEQVSD--GSFSEGQKQRIGLIRAFLKGSSVVIFDEATANLD 480
Cdd:PRK13657 436 ATDEEMRAAAERAQAHDFIERkpdgYDTVVGErgRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
311-523 |
1.12e-13 |
|
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: 73.40 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 311 TCIATIQDVRfenVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKD---YEGKILFGKLESKEIDE 387
Cdd:COG1123 2 TPLLEVRDLS---VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 388 NSIVSNCAYVG----SQ---THIYND---TLRNNLTLWNEAitDTHIKEALERVNLLSFLSRIDEQvsdgsFSEGQKQRI 457
Cdd:COG1123 79 ALRGRRIGMVFqdpmTQlnpVTVGDQiaeALENLGLSRAEA--RARVLELLEAVGLERRLDRYPHQ-----LSGGQRQRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1937373637 458 GLIRAFLKGSSVVIFDEATANLDHNNATRIEHL---LLSDPNITYITVTHHLiKENEPYFDEIIRLGEG 523
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLlreLQRERGTTVLLITHDL-GVVAEIADRVVVMDDG 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
319-506 |
1.30e-13 |
|
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: 70.59 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENA--IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAY 396
Cdd:cd03252 1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSRIDEQVSD------GSFSEGQKQRIGLIRAFLKGSSVV 470
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTivgeqgAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1937373637 471 IFDEATANLDHNNatriEHLLLSD-----PNITYITVTHHL 506
Cdd:cd03252 161 IFDEATSALDYES----EHAIMRNmhdicAGRTVIIIAHRL 197
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
319-522 |
2.43e-13 |
|
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: 69.64 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGEN-AIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYV 397
Cdd:cd03295 1 IEFENVTKRYGGGkKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 GSQTHIY-NDTLRNNLTL------WNEAITDTHIKEALERVNL--LSFLSRIDEQVSDGsfsegQKQRIGLIRAFLKGSS 468
Cdd:cd03295 81 IQQIGLFpHMTVEENIALvpkllkWPKEKIRERADELLALVGLdpAEFADRYPHELSGG-----QQQRVGVARALAADPP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937373637 469 VVIFDEATANLD-------HNNATRIEHLLlsdpNITYITVTHHLikenepyfDEIIRLGE 522
Cdd:cd03295 156 LLLMDEPFGALDpitrdqlQEEFKRLQQEL----GKTIVFVTHDI--------DEAFRLAD 204
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
319-523 |
2.56e-13 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 69.30 E-value: 2.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENA----IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFG-----KLESKEIDE-- 387
Cdd:COG1136 5 LELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqdisSLSERELARlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 388 NSivsncaYVG--SQTH--IYNDTLRNNLTL------WNEAITDTHIKEALERVNLLSFLSRIDEQVSdGsfseGQKQRI 457
Cdd:COG1136 85 RR------HIGfvFQFFnlLPELTALENVALplllagVSRKERRERARELLERVGLGDRLDHRPSQLS-G----GQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937373637 458 GLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLS---DPNITYITVTH--HLIKenepYFDEIIRLGEG 523
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnrELGTTIVMVTHdpELAA----RADRVIRLRDG 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
319-506 |
2.99e-13 |
|
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: 68.70 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGK--LESKEIDENSIvsncAY 396
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdVTGVPPERRNI----GM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQ----THIyndTLRNN------LTLWNEAITDTHIKEALERVNLLSFLSRIDEQVSdGsfseGQKQRIGLIRAFLKG 466
Cdd:cd03259 77 VFQDyalfPHL---TVAENiafglkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELS-G----GQQQRVALARALARE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937373637 467 SSVVIFDEATANLDHNNATRIEHLL---LSDPNITYITVTHHL 506
Cdd:cd03259 149 PSLLLLDEPLSALDAKLREELREELkelQRELGITTIYVTHDQ 191
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
319-523 |
3.85e-13 |
|
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: 67.42 E-value: 3.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEiDENSIVSNCAYVG 398
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 SQTHIYndtlrNNLTLWneaitdthikEALErvnllsflsrideqvsdgsFSEGQKQRIGLIRAFLKGSSVVIFDEATAN 478
Cdd:cd03230 80 EEPSLY-----ENLTVR----------ENLK-------------------LSGGMKQRLALAQALLHDPELLILDEPTSG 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1937373637 479 LDHNNATRIEHLL--LSDPNITYITVTHHLiKENEPYFDEIIRLGEG 523
Cdd:cd03230 126 LDPESRREFWELLreLKKEGKTILLSSHIL-EEAERLCDRVAILNNG 171
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
319-506 |
4.98e-13 |
|
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: 68.68 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKIL-FGK--LESKEIDENSIVSNCA 395
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLiDGEdiSGLSEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 396 YVGSQTHIYNDT---------LRNNLTLWNEAITDThIKEALERVNLlsflsRIDEQVSDGSFSEGQKQRIGLIRAFLKG 466
Cdd:cd03261 81 MLFQSGALFDSLtvfenvafpLREHTRLSEEEIREI-VLEKLEAVGL-----RGAEDLYPAELSGGMKKRVALARALALD 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937373637 467 SSVVIFDEATANLDHNNATRIEHLLLS---DPNITYITVTHHL 506
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLIRSlkkELGLTSIMVTHDL 197
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
320-520 |
9.62e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 67.82 E-value: 9.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 320 RFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFgklESKEIDENS------IVSN 393
Cdd:PRK10247 9 QLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLF---EGEDISTLKpeiyrqQVSY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 394 CAyvgsQT-HIYNDTLRNNLTL-W---NEAITDTHIKEALERVNL-LSFLS-RIDEqvsdgsFSEGQKQRIGLIRAFLKG 466
Cdd:PRK10247 86 CA----QTpTLFGDTVYDNLIFpWqirNQQPDPAIFLDDLERFALpDTILTkNIAE------LSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937373637 467 SSVVIFDEATANLD-HN--NATRIEHLLLSDPNITYITVTHHliKENEPYFDEIIRL 520
Cdd:PRK10247 156 PKVLLLDEITSALDeSNkhNVNEIIHRYVREQNIAVLWVTHD--KDEINHADKVITL 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
319-506 |
9.87e-13 |
|
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: 70.32 E-value: 9.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHF-----GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFG-----KLESKEIDEn 388
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkdltKLSRRSLRE- 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 389 sIVSNCAYV-----GS----QT--HIYNDTLRNnLTLWNEAITDTHIKEALERVNL-LSFLSRideqvSDGSFSEGQKQR 456
Cdd:COG1123 340 -LRRRVQMVfqdpySSlnprMTvgDIIAEPLRL-HGLLSRAERRERVAELLERVGLpPDLADR-----YPHELSGGQRQR 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1937373637 457 IGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLS---DPNITYITVTHHL 506
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlqrELGLTYLFISHDL 465
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
319-480 |
1.29e-12 |
|
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: 70.23 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHF-GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLlnlllgnlkdyeGKILFGKLESKE----IDENSI--- 390
Cdd:COG5265 358 VRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTL------------ARLLFRFYDVTSgrilIDGQDIrdv 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 391 --VSNCAYVG--SQ-THIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSR----IDEQVSDGSF--SEGQKQRIGL 459
Cdd:COG5265 426 tqASLRAAIGivPQdTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESlpdgYDTRVGERGLklSGGEKQRVAI 505
|
170 180
....*....|....*....|.
gi 1937373637 460 IRAFLKGSSVVIFDEATANLD 480
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALD 526
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
16-474 |
1.40e-12 |
|
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: 69.83 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 16 ILLLALnAAIFVSASVTLALMT--NQLVSKRIQSFLALLGLEVGLYIIYLVLNYIIAVHQTKLIQKMTLSIRQSYLSKII 93
Cdd:COG4615 14 LLLLAL-LLGLLSGLANAGLIAliNQALNATGAALARLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRLRLSRRIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 94 HHSFSEFRKsdIGEH--LSVLNNDIQLIeSNGFSSIYTLCSTVFTTLFSII--ALLSYDV-RIVLLAIFLTLCLTYLpkp 168
Cdd:COG4615 93 AAPLERLER--IGAArlLAALTEDVRTI-SQAFVRLPELLQSVALVLGCLAylAWLSPPLfLLTLVLLGLGVAGYRL--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 169 FTNKMQKSMEKFSQANEELVSGVSDQLYGyadvyyasRKQIFLRQVRS--IVEEYIVQKIIfTKRNTSTETlMALFSVAa 246
Cdd:COG4615 167 LVRRARRHLRRAREAEDRLFKHFRALLEG--------FKELKLNRRRRraFFDEDLQPTAE-RYRDLRIRA-DTIFALA- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 247 qmlillltgllIIFGNI----AVGTI---------ASVGQISG-------------NIFNSLSTINQLQVTIKSVDPILK 300
Cdd:COG4615 236 -----------NNWGNLlffaLIGLIlfllpalgwADPAVLSGfvlvllflrgplsQLVGALPTLSRANVALRKIEELEL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 301 KF-----HDFPEDPKTCIATIQDVRFENVSYHFGENAIIKGFT-----QTFKEGGKYAITGCSGSGKSTLLnlllgnlkd 370
Cdd:COG4615 305 ALaaaepAAADAAAPPAPADFQTLELRGVTYRYPGEDGDEGFTlgpidLTIRRGELVFIVGGNGSGKSTLA--------- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 371 yegKILFG---------KLESKEIDENSIvsncayvgsqthiynDTLRNNLTlwneAI-TDTHIKEAL---------ERV 431
Cdd:COG4615 376 ---KLLTGlyrpesgeiLLDGQPVTADNR---------------EAYRQLFS----AVfSDFHLFDRLlgldgeadpARA 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1937373637 432 N-LLSFLsRIDEQVS--DGSF-----SEGQKQRIGLIRAFLKGSSVVIFDE 474
Cdd:COG4615 434 ReLLERL-ELDHKVSveDGRFsttdlSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
319-523 |
2.54e-12 |
|
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: 67.03 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLL-GNLKDYEGKI-LFG-KLESKEIDEnsIVSNCA 395
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITgDLPPTYGNDVrLFGeRRGGEDVWE--LRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 396 YVGSQTHIY---NDTLRN--------NLTLWNEaITDTHIKEALERVNLLSFLSRIDEQVsdGSFSEGQKQRIGLIRAFL 464
Cdd:COG1119 82 LVSPALQLRfprDETVLDvvlsgffdSIGLYRE-PTDEQRERARELLELLGLAHLADRPF--GTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937373637 465 KGSSVVIFDEATANLDHNNA----TRIEHlLLSDPNITYITVTHHLikeNE--PYFDEIIRLGEG 523
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARelllALLDK-LAAEGAPTLVLVTHHV---EEipPGITHVLLLKDG 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
323-504 |
5.87e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 65.70 E-value: 5.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 323 NVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDY-----EGKILfgkLESKEIDENSIVSNCAYV 397
Cdd:PRK14247 8 DLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVY---LDGQDIFKMDVIELRRRV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 GSQTHIYNDTlrNNLTLW--------------NEAITDTHIKEALERVNLLsflsridEQVSD------GSFSEGQKQRI 457
Cdd:PRK14247 85 QMVFQIPNPI--PNLSIFenvalglklnrlvkSKKELQERVRWALEKAQLW-------DEVKDrldapaGKLSGGQQQRL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937373637 458 GLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLS-DPNITYITVTH 504
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLElKKDMTIVLVTH 203
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
320-520 |
6.69e-12 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 65.16 E-value: 6.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 320 RFENVSYHFGEnaIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGkleSKEIDENSI----VSnca 395
Cdd:COG3840 3 RLDDLTYRYGD--FPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWN---GQDLTALPPaerpVS--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 396 yvgsqtHIYND-------TLRNNLTLwneAITD---------THIKEALERVNLLSFLSRIDEQVSdGsfseGQKQRIGL 459
Cdd:COG3840 75 ------MLFQEnnlfphlTVAQNIGL---GLRPglkltaeqrAQVEQALERVGLAGLLDRLPGQLS-G----GQRQRVAL 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937373637 460 IRAFLKGSSVVIFDEATANLDhnNATRIEHLLL-----SDPNITYITVTHHLikenepyfDEIIRL 520
Cdd:COG3840 141 ARCLVRKRPILLLDEPFSALD--PALRQEMLDLvdelcRERGLTVLMVTHDP--------EDAARI 196
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
315-504 |
8.44e-12 |
|
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: 65.32 E-value: 8.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 315 TIQD--VRFENvsyhfGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVS 392
Cdd:cd03288 21 KIHDlcVRYEN-----NLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 393 NCAYVGSQTHIYNDTLRNNLTLwNEAITDTHIKEALERVNLLSFLSRI----DEQVSDG--SFSEGQKQRIGLIRAFLKG 466
Cdd:cd03288 96 RLSIILQDPILFSGSIRFNLDP-ECKCTDDRLWEALEIAQLKNMVKSLpgglDAVVTEGgeNFSVGQRQLFCLARAFVRK 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1937373637 467 SSVVIFDEATANLDHNNATRIEHLLLSD-PNITYITVTH 504
Cdd:cd03288 175 SSILIMDEATASIDMATENILQKVVMTAfADRTVVTIAH 213
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
319-524 |
9.62e-12 |
|
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: 63.75 E-value: 9.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGkleskeidensivsncayvG 398
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILID-------------------G 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 SQTHIYNDTLRNNltlwneaitDTHIKEALERVNLLSFLSRIDeQVSDGsFSEGQKQRIGLIRAFLKGSSVVIFDEATAN 478
Cdd:cd03229 62 EDLTDLEDELPPL---------RRRIGMVFQDFALFPHLTVLE-NIALG-LSGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937373637 479 LDHNNATRIEHLLLS---DPNITYITVTHHLiKENEPYFDEIIRLGEGT 524
Cdd:cd03229 131 LDPITRREVRALLKSlqaQLGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
319-524 |
1.52e-11 |
|
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: 63.64 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQ-----TFKEGGKYAITGCSGSGKSTLLNLllgnlkdyegkiLFGKLESKEiDENSIVSN 393
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLkdinlEVPKGELVAIVGPVGSGKSSLLSA------------LLGELEKLS-GSVSVPGS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 394 CAYVGSQTHIYNDTLRNNLtLWNEAITDTHIKEALERVNLLSFLsridEQVSDG----------SFSEGQKQRIGLIRAF 463
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENI-LFGKPFDEERYEKVIKACALEPDL----EILPDGdlteigekgiNLSGGQKQRISLARAV 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937373637 464 LKGSSVVIFDEATANLDHNNATRI-EHLLLSDP--NITYITVTHHLikENEPYFDEIIRLGEGT 524
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGRHIfENCILGLLlnNKTRILVTHQL--QLLPHADQIVVLDNGR 204
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
319-506 |
2.18e-11 |
|
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: 66.89 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFEN--VSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAY 396
Cdd:TIGR00957 1285 VEFRNycLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQTHIYNDTLRNNLTLWNEaITDTHIKEALERVNLLSFLS----RIDEQVSDG--SFSEGQKQRIGLIRAFLKGSSVV 470
Cdd:TIGR00957 1365 IPQDPVLFSGSLRMNLDPFSQ-YSDEEVWWALELAHLKTFVSalpdKLDHECAEGgeNLSVGQRQLVCLARALLRKTKIL 1443
|
170 180 190
....*....|....*....|....*....|....*..
gi 1937373637 471 IFDEATANLDHNNATRIEHLLLSD-PNITYITVTHHL 506
Cdd:TIGR00957 1444 VLDEATAAVDLETDNLIQSTIRTQfEDCTVLTIAHRL 1480
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
319-504 |
2.26e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.13 E-value: 2.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILfgkLESKEIDENSIVSN--CAY 396
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIF---IDGEDVTHRSIQQRdiCMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQTHIYNDTLRNN-------LTLWNEAITdTHIKEALERVNLLSFLSRIDEQVSDGsfsegQKQRIGLIRAFLKGSSV 469
Cdd:PRK11432 84 FQSYALFPHMSLGENvgyglkmLGVPKEERK-QRVKEALELVDLAGFEDRYVDQISGG-----QQQRVALARALILKPKV 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 1937373637 470 VIFDEATANLDHN--NATRiEHL--LLSDPNITYITVTH 504
Cdd:PRK11432 158 LLFDEPLSNLDANlrRSMR-EKIreLQQQFNITSLYVTH 195
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
319-523 |
2.44e-11 |
|
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: 62.17 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGEN-AIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKIlfGKLESKEIdensivsncAYV 397
Cdd:cd03223 1 IELENLSLATPDGrVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--GMPEGEDL---------LFL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 GSQTHIYNDTLRNNLTL-WNEAitdthikealervnllsflsrideqvsdgsFSEGQKQRIGLIRAFLKGSSVVIFDEAT 476
Cdd:cd03223 70 PQRPYLPLGTLREQLIYpWDDV------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937373637 477 ANLDHNNATRIeHLLLSDPNITYITVTHHliKENEPYFDEIIRL-GEG 523
Cdd:cd03223 120 SALDEESEDRL-YQLLKELGITVISVGHR--PSLWKFHDRVLDLdGEG 164
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-506 |
2.85e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.54 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 13 LVHILLLA--LNAAIFVSASVTLALMTNQLVSKRIQSflallglevGLYI-IYLVLNY-IIAVHQTKLIQKMTLSIRQS- 87
Cdd:PLN03232 913 VVMILLVCylTTEVLRVSSSTWLSIWTDQSTPKSYSP---------GFYIvVYALLGFgQVAVTFTNSFWLISSSLHAAk 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 88 -----YLSKIIHHSFSEFRKSDIGEHLSVLNNDIQLIESNGFSSIYTLCSTVFTtLFSIIALLSYDVRIVLLAIFLTLCL 162
Cdd:PLN03232 984 rlhdaMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFMNQLWQ-LLSTFALIGTVSTISLWAIMPLLIL 1062
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 163 TYLPKPFTNKMQKSMEKF-SQANEELVSGVSDQLYGYADVyyasRKQIFLRQVRSIVEEYIVQKIIFTKRNTSTETLMA- 240
Cdd:PLN03232 1063 FYAAYLYYQSTSREVRRLdSVTRSPIYAQFGEALNGLSSI----RAYKAYDRMAKINGKSMDNNIRFTLANTSSNRWLTi 1138
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 241 -LFSVAAQMLILLLTGLLIIFGNIA--VGTIASVGQI---SGNIFNSLSTI----NQLQVTIKSVDPIlKKFHDFPEDPK 310
Cdd:PLN03232 1139 rLETLGGVMIWLTATFAVLRNGNAEnqAGFASTMGLLlsyTLNITTLLSGVlrqaSKAENSLNSVERV-GNYIDLPSEAT 1217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 311 TCIATIQDV---------RFENV--SYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGK 379
Cdd:PLN03232 1218 AIIENNRPVsgwpsrgsiKFEDVhlRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD 1297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 380 LESKEIDENSIVSNCAYVGSQTHIYNDTLRNNLTLWNEAiTDTHIKEALERVNLLSFLSR----IDEQVSDG--SFSEGQ 453
Cdd:PLN03232 1298 CDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEH-NDADLWEALERAHIKDVIDRnpfgLDAEVSEGgeNFSVGQ 1376
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1937373637 454 KQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLSD-PNITYITVTHHL 506
Cdd:PLN03232 1377 RQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEfKSCTMLVIAHRL 1430
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
319-504 |
3.04e-11 |
|
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: 63.41 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNcayvg 398
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVN----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 sqTHIYNDTLRNNLTLW------------NEAITDTHIKEALERVNLLSFLSRIDEQVSDgsfseGQKQRIGLIRAFLKG 466
Cdd:cd03300 76 --TVFQNYALFPHLTVFeniafglrlkklPKAEIKERVAEALDLVQLEGYANRKPSQLSG-----GQQQRVAIARALVNE 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1937373637 467 SSVVIFDEATANLDhnnATRIEHLLLSDPN------ITYITVTH 504
Cdd:cd03300 149 PKVLLLDEPLGALD---LKLRKDMQLELKRlqkelgITFVFVTH 189
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
40-480 |
3.34e-11 |
|
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: 65.45 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 40 LVSKRIQSFLALLGLEVGLYIIYLVLNYIiavhQTKLIQKMTLSIRQSYLSKIIHHSFS---EFRKSDIGEHLSVLNNDI 116
Cdd:TIGR01842 37 LTSGSVPTLLMLTVLALGLYLFLGLLDAL----RSFVLVRIGEKLDGALNQPIFAASFSatlRRGSGDGLQALRDLDQLR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 117 QLIESNGfssIYTLCSTVFTTLFsIIALLSYDVRIVLLAIFLTLC---LTYLPKPFTNK-MQKSMEKFSQANEELVSGVS 192
Cdd:TIGR01842 113 QFLTGPG---LFAFFDAPWMPIY-LLVCFLLHPWIGILALGGAVVlvgLALLNNRATKKpLKEATEASIRANNLADSALR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 193 DqlygyADVYYA--SRKQIFLRQVRSiVEEYIVQKIIFTKRNTSTETLMALFSVAAQMLILLLTGLLIIFGNIAVGT-IA 269
Cdd:TIGR01842 189 N-----AEVIEAmgMMGNLTKRWGRF-HSKYLSAQSAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMmIA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 270 S---VGQISGNIFNSLSTINQLQVTIKSVDPILKKFHDFPE-DPKTCIATIQ-DVRFENVSY-HFGENA-IIKGFTQTFK 342
Cdd:TIGR01842 263 GsilVGRALAPIDGAIGGWKQFSGARQAYKRLNELLANYPSrDPAMPLPEPEgHLSVENVTIvPPGGKKpTLRGISFSLQ 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 343 EGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYVGSQTHIYNDTLRNNLTLWNEAITDT 422
Cdd:TIGR01842 343 AGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFGENADPE 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937373637 423 HIKEA--LERVN--LLSFLSRIDEQVSDG--SFSEGQKQRIGLIRAFLKGSSVVIFDEATANLD 480
Cdd:TIGR01842 423 KIIEAakLAGVHelILRLPDGYDTVIGPGgaTLSGGQRQRIALARALYGDPKLVVLDEPNSNLD 486
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
319-523 |
3.61e-11 |
|
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: 63.52 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYVg 398
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 SQTHIYNDTL-------------RNNLTLWNEAitDTHI-KEALERVNLLSFLSRIDEQVSDgsfseGQKQRIGLIRAFL 464
Cdd:COG1120 81 PQEPPAPFGLtvrelvalgryphLGLFGRPSAE--DREAvEEALERTGLEHLADRPVDELSG-----GERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937373637 465 KGSSVVIFDEATANLDHNNATRIEHL---LLSDPNITYITVTHHLikeNEP--YFDEIIRLGEG 523
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELlrrLARERGRTVVMVLHDL---NLAarYADRLVLLKDG 214
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
322-480 |
3.63e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.58 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKIlfgKLESKEIDENSIVSNCAYVGSQT 401
Cdd:PRK13539 6 EDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI---KLDGGDIDDPDVAEACHYLGHRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 402 HIyNDTL--RNNLTLWNE--AITDTHIKEALERVNllsfLSRIdEQVSDGSFSEGQKQRIGLIRAFLKGSSVVIFDEATA 477
Cdd:PRK13539 83 AM-KPALtvAENLEFWAAflGGEELDIAAALEAVG----LAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156
|
...
gi 1937373637 478 NLD 480
Cdd:PRK13539 157 ALD 159
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
319-524 |
4.70e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 65.09 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLnlllgnlkdyegKILFGKLESkeiDENSIVsncayVG 398
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLL------------KLLAGELEP---DSGTVK-----LG 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 SQTHI-Y----NDTLRNNLTLW------NEAITDTHIKEALERvnllsFL---SRIDEQVsdGSFSEGQKQRIGLIRAFL 464
Cdd:COG0488 376 ETVKIgYfdqhQEELDPDKTVLdelrdgAPGGTEQEVRGYLGR-----FLfsgDDAFKPV--GVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937373637 465 KGSSVVIFDEATANLDHNNATRIEHLLLSDPNiTYITVTHhlikenEPYF-----DEIIRLGEGT 524
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALDDFPG-TVLLVSH------DRYFldrvaTRILEFEDGG 506
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
319-509 |
5.01e-11 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 62.38 E-value: 5.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGEN-AIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIvsncAY- 396
Cdd:COG2884 2 IRFENVSKRYPGGrEALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREI----PYl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 ---VGS--QTH--IYNDTLRNNLTL------WNEAITDTHIKEALERVNLLSFLSRIDEQVSDGsfsegQKQRIGLIRAF 463
Cdd:COG2884 78 rrrIGVvfQDFrlLPDRTVYENVALplrvtgKSRKEIRRRVREVLDLVGLSDKAKALPHELSGG-----EQQRVAIARAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1937373637 464 LKGSSVVIFDEATANLDHNNATRIEHLL--LSDPNITYITVTH--HLIKE 509
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLeeINRRGTTVLIATHdlELVDR 202
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
16-506 |
1.11e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.97 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 16 ILLLALNAAIFVSASVTLALMTNQLVSKRIQSflalLGLEVGLYIIYLVLNYIIAV-H--QTKLIQKMTLSI----RQSY 88
Cdd:PRK10790 29 VLMLWVAAAAEVSGPLLISYFIDNMVAKGNLP----LGLVAGLAAAYVGLQLLAAGlHyaQSLLFNRAAVGVvqqlRTDV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 89 LSKIIHHSFSEFRKSDIGEHLSVLNNDIQLIESngfssIY-TLCSTVFTTLFSI----IALLSYDVRIVLLA--IF---L 158
Cdd:PRK10790 105 MDAALRQPLSAFDTQPVGQLISRVTNDTEVIRD-----LYvTVVATVLRSAALIgamlVAMFSLDWRMALVAimIFpavL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 159 TLCLTY--LPKPFTNKMQKSMEKFSQANEELVSGVSdqlygyadVYyasrkQIFLRQVRsiveeyivqkiiFTKR----- 231
Cdd:PRK10790 180 VVMVIYqrYSTPIVRRVRAYLADINDGFNEVINGMS--------VI-----QQFRQQAR------------FGERmgeas 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 232 ----NTSTETL----------MALFSVAaqmlilLLTGLLIIFGNIAVGTIAsVGQISGNIfNSLSTINQLQVTIKSVDP 297
Cdd:PRK10790 235 rshyMARMQTLrldgfllrplLSLFSAL------ILCGLLMLFGFSASGTIE-VGVLYAFI-SYLGRLNEPLIELTTQQS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 298 ILKK----------FHDFPEDP-KTCIATIQ--DVRFENVSYHF-GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNL 363
Cdd:PRK10790 307 MLQQavvagervfeLMDGPRQQyGNDDRPLQsgRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 364 LLGNLKDYEGKILFGKLESKEIDENSIVSNCAYVGSQTHIYNDTLRNNLTLWNEaITDTHIKEALERVNLLSFL------ 437
Cdd:PRK10790 387 LMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELArslpdg 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937373637 438 --SRIDEQVSdgSFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLL-LSDPNITYITVTHHL 506
Cdd:PRK10790 466 lyTPLGEQGN--NLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALaAVREHTTLVVIAHRL 535
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
319-524 |
2.13e-10 |
|
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: 60.31 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILF-GKLESKEIDENSIVSncAYV 397
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdGKSYQKNIEALRRIG--ALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 GSQTHIYNDTLRNNLTLWNEA--ITDTHIKEALERVNLlsflsRIDEQVSDGSFSEGQKQRIGLIRAFLKGSSVVIFDEA 475
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLlgIRKKRIDEVLDVVGL-----KDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937373637 476 TANLDHNNATRIEHLLLS--DPNITyITVTHHLIKENEPYFDEIIRLGEGT 524
Cdd:cd03268 154 TNGLDPDGIKELRELILSlrDQGIT-VLISSHLLSEIQKVADRIGIINKGK 203
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
322-504 |
1.18e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.09 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLK-----DYEGKI-LFGK-LESKEIDENSIVSNC 394
Cdd:PRK14267 8 VNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVrLFGRnIYSPDVDPIEVRREV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 395 AYVGSQTH------IYNDT---LRNNLTLWNEAITDTHIKEALERVNLLSflsRIDEQVSD--GSFSEGQKQRIGLIRAF 463
Cdd:PRK14267 88 GMVFQYPNpfphltIYDNVaigVKLNGLVKSKKELDERVEWALKKAALWD---EVKDRLNDypSNLSGGQRQRLVIARAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1937373637 464 LKGSSVVIFDEATANLDHNNATRIEHLLLS-DPNITYITVTH 504
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFElKKEYTIVLVTH 206
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
329-523 |
1.22e-09 |
|
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: 61.11 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 329 GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKIlfgkleskeidenSIVSNCAYVGSQTHIYNDTL 408
Cdd:TIGR00957 649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHV-------------HMKGSVAYVPQQAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 409 RNNLtLWNEAITDTHIKEALERVNLLSFLSRI--DEQVSDG----SFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHN 482
Cdd:TIGR00957 716 RENI-LFGKALNEKYYQQVLEACALLPDLEILpsGDRTEIGekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1937373637 483 NATRI-EHLLLSD---PNITYITVTHHLikENEPYFDEIIRLGEG 523
Cdd:TIGR00957 795 VGKHIfEHVIGPEgvlKNKTRILVTHGI--SYLPQVDVIIVMSGG 837
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
340-506 |
1.36e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 59.08 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 340 TFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFG--KLE-------SKEI-----DENSIVSNCAYVGSqthIYN 405
Cdd:COG4167 35 TLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINghKLEygdykyrCKHIrmifqDPNTSLNPRLNIGQ---ILE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 406 DTLRNNlTLWNEAITDTHIKEALERVNLLSFLSRIDEQVsdgsFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNAT 485
Cdd:COG4167 112 EPLRLN-TDLTAEEREERIFATLRLVGLLPEHANFYPHM----LSSGQKQRVALARALILQPKIIIADEALAALDMSVRS 186
|
170 180
....*....|....*....|....
gi 1937373637 486 RIEHLLLS---DPNITYITVTHHL 506
Cdd:COG4167 187 QIINLMLElqeKLGISYIYVSQHL 210
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
322-491 |
1.53e-09 |
|
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: 57.97 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGENAIIKGFTQTFkEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEiDENSIVSNCAYVGSQT 401
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 402 HIY-NDTLRNNLTL--WNEAITDTHIK----EALERVNLLSFLSRideqvSDGSFSEGQKQRIGLIRAFLKGSSVVIFDE 474
Cdd:cd03264 82 GVYpNFTVREFLDYiaWLKGIPSKEVKarvdEVLELVNLGDRAKK-----KIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170
....*....|....*..
gi 1937373637 475 ATANLDHNNATRIEHLL 491
Cdd:cd03264 157 PTAGLDPEERIRFRNLL 173
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
323-523 |
1.77e-09 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 59.86 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 323 NVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYVGSQTH 402
Cdd:PRK09536 8 DLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 403 I-YNDTLR-----------NNLTLWNEAiTDTHIKEALERVNLLSFLSRideqvSDGSFSEGQKQRIGLIRAFLKGSSVV 470
Cdd:PRK09536 88 LsFEFDVRqvvemgrtphrSRFDTWTET-DRAAVERAMERTGVAQFADR-----PVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1937373637 471 IFDEATANLDHNNATRIEHLL--LSDPNITYITVTHHLiKENEPYFDEIIRLGEG 523
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVrrLVDDGKTAVAAIHDL-DLAARYCDELVLLADG 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
319-509 |
3.17e-09 |
|
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: 57.21 E-value: 3.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENA----IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIV--- 391
Cdd:cd03258 2 IELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRkar 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 392 SNCAYVGSQTHIYND-TLRNNLTLWNEaITDTHIKEALERVN-LLSFLSRID-EQVSDGSFSEGQKQRIGLIRAFLKGSS 468
Cdd:cd03258 82 RRIGMIFQHFNLLSSrTVFENVALPLE-IAGVPKAEIEERVLeLLELVGLEDkADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1937373637 469 VVIFDEATANLDHNNATRIEHLLLS---DPNITYITVTH--HLIKE 509
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDinrELGLTIVLITHemEVVKR 206
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
323-524 |
5.70e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 323 NVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFgkleskEIDENSIVSNCAYVgsqth 402
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV------DVPDNQFGREASLI----- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 403 iyndtlrnnltlwnEAIT-DTHIKEALERVNL--LS----FLSRIDEqvsdgsFSEGQKQRIGLIRAFLKGSSVVIFDEA 475
Cdd:COG2401 104 --------------DAIGrKGDFKDAVELLNAvgLSdavlWLRRFKE------LSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1937373637 476 TANLDHNNATRIE---HLLLSDPNITYITVTHH--LIKENEPyfDEIIRLGEGT 524
Cdd:COG2401 164 CSHLDRQTAKRVArnlQKLARRAGITLVVATHHydVIDDLQP--DLLIFVGYGG 215
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
319-480 |
6.13e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGEN--AIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAY 396
Cdd:PLN03130 1238 IKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQTHIYNDTLRNNLTLWNEAiTDTHIKEALERVNLLSFLSR----IDEQVSDG--SFSEGQKQRIGLIRAFLKGSSVV 470
Cdd:PLN03130 1318 IPQAPVLFSGTVRFNLDPFNEH-NDADLWESLERAHLKDVIRRnslgLDAEVSEAgeNFSVGQRQLLSLARALLRRSKIL 1396
|
170
....*....|
gi 1937373637 471 IFDEATANLD 480
Cdd:PLN03130 1397 VLDEATAAVD 1406
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
17-191 |
7.35e-09 |
|
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: 57.05 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 17 LLLALNAAIFVSAS--VTLALM---TNQLVSKRIQSFLALLGLE-VGLYIIYLVLNYIIAVHQTKLIQKMTLSIRQSYLS 90
Cdd:cd18552 1 LALAILGMILVAATtaALAWLLkplLDDIFVEKDLEALLLVPLAiIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 91 KIIHHSFSEFRKSDIGEHLSVLNNDIQLIESNGFSSIYTLCSTVFTTLFSIIALLSYDVRIVLLAiFLTLCLTYLP---- 166
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIA-LVVLPLAALPirri 159
|
170 180
....*....|....*....|....*....
gi 1937373637 167 ----KPFTNKMQKSMEKFSQANEELVSGV 191
Cdd:cd18552 160 gkrlRKISRRSQESMGDLTSVLQETLSGI 188
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
319-524 |
9.09e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 56.68 E-value: 9.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFK--EGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKL-----ESKEIDEN-SI 390
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNipKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQaitddNFEKLRKHiGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 391 V---SNCAYVGSqTHIYNDT--LRNNLTLWNEAITDthIKEALERVNLLSflsRIDEQVSdgSFSEGQKQRIGLIRAFLK 465
Cdd:PRK13648 88 VfqnPDNQFVGS-IVKYDVAfgLENHAVPYDEMHRR--VSEALKQVDMLE---RADYEPN--ALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937373637 466 GSSVVIFDEATANLD---HNNATRIEHLLLSDPNITYITVTHHLIKENEPyfDEIIRLGEGT 524
Cdd:PRK13648 160 NPSVIILDEATSMLDpdaRQNLLDLVRKVKSEHNITIISITHDLSEAMEA--DHVIVMNKGT 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
318-504 |
1.08e-08 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 57.01 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 318 DVRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTllnlllgnlkdyEGKILFG-----KLESKEidensivS 392
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTllrmiagledptSGEILIGgrdvtDLPPKD-------R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 393 NCAYVgSQT-----HIyndTLRNNLTL------WNEAITDTHIKEALERVNLLSFLSRIDEQVSdGsfseGQKQRIGLIR 461
Cdd:COG3839 76 NIAMV-FQSyalypHM---TVYENIAFplklrkVPKAEIDRRVREAAELLGLEDLLDRKPKQLS-G----GQRQRVALGR 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1937373637 462 AFLKGSSVVIFDEATANLDHN--NATRIE-HLLLSDPNITYITVTH 504
Cdd:COG3839 147 ALVREPKVFLLDEPLSNLDAKlrVEMRAEiKRLHRRLGTTTIYVTH 192
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
319-521 |
1.35e-08 |
|
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: 55.17 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENA----IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFgklESKEIDENSivSNC 394
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLV---DGEPVTGPG--PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 395 AYVgSQthiyNDTL------RNNLTL------WNEAITDTHIKEALERVNLLSFLSRIDEQVSDGsfsegQKQRIGLIRA 462
Cdd:cd03293 76 GYV-FQ----QDALlpwltvLDNVALglelqgVPKAEARERAEELLELVGLSGFENAYPHQLSGG-----MRQRVALARA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937373637 463 FLKGSSVVIFDEATANLDHNNATRIEHLLL---SDPNITYITVTHHLikenepyfDEIIRLG 521
Cdd:cd03293 146 LAVDPDVLLLDEPFSALDALTREQLQEELLdiwRETGKTVLLVTHDI--------DEAVFLA 199
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
319-504 |
1.56e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 55.48 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFG--KLESKEIDENSIVSNCAY 396
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDglKVNDPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQTHIYndtlrNNLT-LWNEAITDTHI------------KEALERVNLlsfLSRIDEQVSDgsFSEGQKQRIGLIRAF 463
Cdd:PRK09493 82 VFQQFYLF-----PHLTaLENVMFGPLRVrgaskeeaekqaRELLAKVGL---AERAHHYPSE--LSGGQQQRVAIARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1937373637 464 LKGSSVVIFDEATANLDHNnaTRIEHLL----LSDPNITYITVTH 504
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPE--LRHEVLKvmqdLAEEGMTMVIVTH 194
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
16-292 |
1.73e-08 |
|
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: 55.87 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 16 ILLLALNAAIFVSASVTLALMTNQLVSKRIQS-------FLALLGLEVGLYIIYLVLNYIIAVHQTKLIQKMTLSIRQSY 88
Cdd:cd18547 5 IILAIISTLLSVLGPYLLGKAIDLIIEGLGGGggvdfsgLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 89 LSKIIHHSFSEFRKSDIGEHLSVLNNDIQLIeSNGFS-SIYTLCSTVFTTLFSIIALLSYDVRIVLLAIFLTLCLTYLPK 167
Cdd:cd18547 85 FEKLQRLPLSYFDTHSHGDIMSRVTNDVDNI-SQALSqSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 168 PFTNKMQKSmekFSQANEELvsGvsdQLYGYADVYYASRK--QIFLRqvrsivEEYIVQKiiFTKRNTstetlmALFSVA 245
Cdd:cd18547 164 FIAKRSQKY---FRKQQKAL--G---ELNGYIEEMISGQKvvKAFNR------EEEAIEE--FDEINE------ELYKAS 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937373637 246 --AQMLILLLTGLLIIFGN------------------IAVGTIAS----VGQISGNIFNSLSTINQLQVTI 292
Cdd:cd18547 222 fkAQFYSGLLMPIMNFINNlgyvlvavvggllvingaLTVGVIQAflqySRQFSQPINQISQQINSLQSAL 292
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
334-506 |
1.76e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 334 IKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKIL-------FG--KLESKEI-----DENSIVSNCAYVGs 399
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLiddhplhFGdySYRSQRIrmifqDPSTSLNPRQRIS- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 400 qtHIYNDTLRNNLTLWNEAiTDTHIKEALERVNLLSflsridEQVS--DGSFSEGQKQRIGLIRAFLKGSSVVIFDEATA 477
Cdd:PRK15112 108 --QILDFPLRLNTDLEPEQ-REKQIIETLRQVGLLP------DHASyyPHMLAPGQKQRLGLARALILRPKVIIADEALA 178
|
170 180 190
....*....|....*....|....*....|..
gi 1937373637 478 NLDHNNATRIEHLLL---SDPNITYITVTHHL 506
Cdd:PRK15112 179 SLDMSMRSQLINLMLelqEKQGISYIYVTQHL 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
319-506 |
1.86e-08 |
|
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: 55.37 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILF-----GKLESKEIDEnsIVSN 393
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdgqdiTGLSEKELYE--LRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 394 CAYV--GSqthiyndTLRNNLTLW-------------NEAITDTHIKEALERVNLLSFLSRIDEQVSdGsfseGQKQRIG 458
Cdd:COG1127 84 IGMLfqGG-------ALFDSLTVFenvafplrehtdlSEAEIRELVLEKLELVGLPGAADKMPSELS-G----GMRKRVA 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1937373637 459 LIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLS---DPNITYITVTHHL 506
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRElrdELGLTSVVVTHDL 202
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
319-506 |
1.86e-08 |
|
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: 55.51 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHF--GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEID---------- 386
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEEnlweirkkvg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 387 ------ENSIVSNcayvgsqthiyndTLRN-------NLTLWNEAItDTHIKEALERVNLLSFLSRIDEQVSdGsfseGQ 453
Cdd:TIGR04520 81 mvfqnpDNQFVGA-------------TVEDdvafgleNLGVPREEM-RKRVDEALKLVGMEDFRDREPHLLS-G----GQ 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 454 KQRIGL--IRAfLKgSSVVIFDEATANLDHNnaTRIE-----HLLLSDPNITYITVTHHL 506
Cdd:TIGR04520 142 KQRVAIagVLA-MR-PDIIILDEATSMLDPK--GRKEvletiRKLNKEEGITVISITHDM 197
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
303-480 |
1.95e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.90 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 303 HDFPEDPKtcIATIQDVRFENVSYHFGENAI-IKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILfgkLE 381
Cdd:PRK10522 309 AEFPRPQA--FPDWQTLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEIL---LD 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 382 SKEIDENSIVsncAY------VGSQTHIYNDTLRNNltlwNEAITDTHIKEALERVNLLSFLSRIDEQVSDGSFSEGQKQ 455
Cdd:PRK10522 384 GKPVTAEQPE---DYrklfsaVFTDFHLFDQLLGPE----GKPANPALVEKWLERLKMAHKLELEDGRISNLKLSKGQKK 456
|
170 180
....*....|....*....|....*
gi 1937373637 456 RIGLIRAFLKGSSVVIFDEATANLD 480
Cdd:PRK10522 457 RLALLLALAEERDILLLDEWAADQD 481
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
319-521 |
2.77e-08 |
|
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: 53.20 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLnlllgnlkdyegKILFGKLEskeIDENSIVSNcayvG 398
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLM------------KILSGLYK---PDSGEILVD----G 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 SQTHIYNdtlrnnltlwneaitdthIKEALER----VNLLSFlsrideqvsdgsfseGQKQRIGLIRAFLKGSSVVIFDE 474
Cdd:cd03216 62 KEVSFAS------------------PRDARRAgiamVYQLSV---------------GERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1937373637 475 ATANLDhnnATRIEHLL-----LSDPNITYITVTHHLikenepyfDEIIRLG 521
Cdd:cd03216 109 PTAALT---PAEVERLFkvirrLRAQGVAVIFISHRL--------DEVFEIA 149
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
319-504 |
2.99e-08 |
|
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: 54.18 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFG-----KLESKEIDENSIVSN 393
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvtDLPPKDRDIAMVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 394 CAYVGSQThIYnDTLRNNLTLWN--EAITDTHIKEALERVNLLSFLSRIDEQVSDgsfseGQKQRIGLIRAFLKGSSVVI 471
Cdd:cd03301 81 YALYPHMT-VY-DNIAFGLKLRKvpKDEIDERVREVAELLQIEHLLDRKPKQLSG-----GQRQRVALGRAIVREPKVFL 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 1937373637 472 FDEATANLDH--NNATRIE-HLLLSDPNITYITVTH 504
Cdd:cd03301 154 MDEPLSNLDAklRVQMRAElKRLQQRLGTTTIYVTH 189
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
318-524 |
3.14e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 56.26 E-value: 3.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 318 DVRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYV 397
Cdd:PRK10789 315 DVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVV 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 GSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSRI----DEQVSDGS--FSEGQKQRIGLIRAFLKGSSVVI 471
Cdd:PRK10789 395 SQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLpqgyDTEVGERGvmLSGGQKQRISIARALLLNAEILI 474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937373637 472 FDEATANLDhnnaTRIEHLLLSD-----PNITYITVTHHLIKENEPyfDEIIRLGEGT 524
Cdd:PRK10789 475 LDDALSAVD----GRTEHQILHNlrqwgEGRTVIISAHRLSALTEA--SEILVMQHGH 526
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
16-191 |
3.23e-08 |
|
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: 54.96 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 16 ILLLALNAAIFVSASVTLALMTNQLVSKRIQSFLAL---LGLEVGLYIIYLVLNYIIAVHQTKLIQKMTLSIRQSYLSKI 92
Cdd:pfam00664 5 ILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALnvySLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLFKKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 93 IHHSFSEFRKSDIGEHLSVLNNDIQLIESNGFSSIYTLCSTVFTTLFSIIALLSYDVRIVLLAIFLTLCLTYLP------ 166
Cdd:pfam00664 85 LRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSavfaki 164
|
170 180
....*....|....*....|....*.
gi 1937373637 167 -KPFTNKMQKSMEKFSQANEELVSGV 191
Cdd:pfam00664 165 lRKLSRKEQKAVAKASSVAEESLSGI 190
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
13-295 |
3.53e-08 |
|
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: 55.14 E-value: 3.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 13 LVHILLLALNAAIF-VSASVTLALMTNQLVSKRIQSFLALLGLEV-GLYIIYLVLNYIiavhQTKLI----QKMTLSIRQ 86
Cdd:cd18570 4 LILILLLSLLITLLgIAGSFFFQILIDDIIPSGDINLLNIISIGLiLLYLFQSLLSYI----RSYLLlklsQKLDIRLIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 87 SYLSKIIH--HSFSEFRKSdiGEHLSVLNnDIQLIESNGFSSIYTLCSTVFTTLFSIIALLSYDVR---IVLLAIFLTLC 161
Cdd:cd18570 80 GYFKHLLKlpLSFFETRKT--GEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKlflITLLIIPLYIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 162 LTYL-PKPFTNKMQKSMEKFSQANEELVSGVSdqlyGYADVYYASRKQIFLRQVRSIVEEYIVQKIIFTKRNTSTETLMA 240
Cdd:cd18570 157 IILLfNKPFKKKNREVMESNAELNSYLIESLK----GIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKG 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1937373637 241 LFSVAAQMLILLLTGLLIIFGNIAVGTIASVGQISGNIFNSLSTINQLQVTIKSV 295
Cdd:cd18570 233 LISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEA 287
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
319-524 |
3.69e-08 |
|
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: 54.04 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIikGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLE-----------SKEIDE 387
Cdd:cd03298 1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDvtaappadrpvSMLFQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 388 NSIVSNCayvgsqTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSRIDEQVSDGsfsegQKQRIGLIRAFLKGS 467
Cdd:cd03298 79 NNLFAHL------TVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGG-----ERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937373637 468 SVVIFDEATANLDhnNATRIEHLLL-----SDPNITYITVTHHlIKENEPYFDEIIRLGEGT 524
Cdd:cd03298 148 PVLLLDEPFAALD--PALRAEMLDLvldlhAETKMTVLMVTHQ-PEDAKRLAQRVVFLDNGR 206
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
327-506 |
4.63e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 54.20 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 327 HFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSivsncayvgSQTHIYND 406
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKD---------GQLKVADK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 407 T----LRNNLT-------LWNEAITDTHIKEALERVNLLS----------FLSR--IDEQVSDG---SFSEGQKQRIGLI 460
Cdd:PRK10619 85 NqlrlLRTRLTmvfqhfnLWSHMTVLENVMEAPIQVLGLSkqeareravkYLAKvgIDERAQGKypvHLSGGQQQRVSIA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937373637 461 RAFLKGSSVVIFDEATANLDHNNATRIEHLL--LSDPNITYITVTHHL 506
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMqqLAEEGKTMVVVTHEM 212
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
319-504 |
5.21e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 54.23 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENV--SYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKI-LFGKLESKE----IDEN-SI 390
Cdd:PRK13632 8 IKVENVsfSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIkIDGITISKEnlkeIRKKiGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 391 V---SNCAYVGSqthiyndTLRNNLT--LWNEAIT----DTHIKEALERVNLLSFLSRIDEqvsdgSFSEGQKQRIGLIR 461
Cdd:PRK13632 88 IfqnPDNQFIGA-------TVEDDIAfgLENKKVPpkkmKDIIDDLAKKVGMEDYLDKEPQ-----NLSGGQKQRVAIAS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1937373637 462 AFLKGSSVVIFDEATANLDHNNATRIEHLLLS---DPNITYITVTH 504
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrkTRKKTLISITH 201
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
329-504 |
6.96e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.24 E-value: 6.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 329 GEN--AIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKI-LFGKLESKEIDENSIVSNCAYVGS--QTHI 403
Cdd:PRK10584 19 GEHelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVsLVGQPLHQMDEEARAKLRAKHVGFvfQSFM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 404 YNDTL--RNNLTL------WNEAITDTHIKEALERVNLLSFLSRIDEQVSDGsfsegQKQRIGLIRAFLKGSSVVIFDEA 475
Cdd:PRK10584 99 LIPTLnaLENVELpallrgESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGG-----EQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|..
gi 1937373637 476 TANLDHNNATRIEHLLLS---DPNITYITVTH 504
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSlnrEHGTTLILVTH 205
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
316-506 |
7.79e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.50 E-value: 7.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 316 IQDVRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLK-----DYEGKI-LFGK-LESKEIDEN 388
Cdd:PRK14258 5 IPAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVeFFNQnIYERRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 389 SIVSNCAYVGSQTHIYNDTLRNNLTL------WNEAIT-DTHIKEALERVNLLSFL-SRIDEQVSDgsFSEGQKQRIGLI 460
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYgvkivgWRPKLEiDDIVESALKDADLWDEIkHKIHKSALD--LSGGQQQRLCIA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937373637 461 RAFLKGSSVVIFDEATANLDHNNATRIEHLLLSDP---NITYITVTHHL 506
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrsELTMVIVSHNL 211
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
319-523 |
1.15e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 53.09 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNL---KDYEGKI-LFGKLESKE----IDENSI 390
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIeLLGRTVQREgrlaRDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 391 VSNCAYVGSQTHIYND-TLRNNLTL--------------WNEAITDTHIKEALERVNLLSFLSridEQVSdgSFSEGQKQ 455
Cdd:PRK09984 85 RANTGYIFQQFNLVNRlSVLENVLIgalgstpfwrtcfsWFTREQKQRALQALTRVGMVHFAH---QRVS--TLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937373637 456 RIGLIRAFLKGSSVVIFDEATANLDHNNAtRIEHLLLSDPNIT---YITVTHHLIKENEPYFDEIIRLGEG 523
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESA-RIVMDTLRDINQNdgiTVVVTLHQVDYALRYCERIVALRQG 229
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
319-506 |
1.59e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 52.71 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENA--IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKIlfgKLESKEIDENSIVSNCAY 396
Cdd:PRK13635 6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTI---TVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VG-------SQ---THIYNDT---LRNNLTLWNEAITdtHIKEALERVNLLSFLSRideqvSDGSFSEGQKQRIGLIRAF 463
Cdd:PRK13635 83 VGmvfqnpdNQfvgATVQDDVafgLENIGVPREEMVE--RVDQALRQVGMEDFLNR-----EPHRLSGGQKQRVAIAGVL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937373637 464 LKGSSVVIFDEATANLDhnNATRIE-----HLLLSDPNITYITVTHHL 506
Cdd:PRK13635 156 ALQPDIIILDEATSMLD--PRGRREvletvRQLKEQKGITVLSITHDL 201
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
319-524 |
1.61e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 52.86 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFG-----ENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLE------SKEIDE 387
Cdd:PRK13646 3 IRFDNVSYTYQkgtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITithktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 388 NSIVSNCAYVGSQTHIYNDTLRNNLtLWNEAITDTHIKEALERVN--LLSF-LSRIDEQVSDGSFSEGQKQRIGLIRAFL 464
Cdd:PRK13646 83 VRKRIGMVFQFPESQLFEDTVEREI-IFGPKNFKMNLDEVKNYAHrlLMDLgFSRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937373637 465 KGSSVVIFDEATANLDHNNATRIEHLLLS---DPNITYITVTHHLiKENEPYFDEIIRLGEGT 524
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqtDENKTIILVSHDM-NEVARYADEVIVMKEGS 223
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
322-517 |
1.66e-07 |
|
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: 51.99 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGK-ILFGKLESKEIDEnsIVSNCAYVGSQ 400
Cdd:cd03265 4 ENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRaTVAGHDVVREPRE--VRRRIGIVFQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 401 THIYND-TLRNNLTL--------WNEAitDTHIKEALERVNLLSFLsriDEQVSdgSFSEGQKQRIGLIRAFLKGSSVVI 471
Cdd:cd03265 82 LSVDDElTGWENLYIharlygvpGAER--RERIDELLDFVGLLEAA---DRLVK--TYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937373637 472 FDEATANLD-HNNATRIEHL--LLSDPNITyITVTHHLIKENEPYFDEI 517
Cdd:cd03265 155 LDEPTIGLDpQTRAHVWEYIekLKEEFGMT-ILLTTHYMEEAEQLCDRV 202
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
319-521 |
2.50e-07 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 52.01 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHF----GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILfgkLESKEIDENSivSNC 394
Cdd:COG1116 8 LELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVL---VDGKPVTGPG--PDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 395 AYVGsQthiyNDTL------RNNLTL------WNEAITDTHIKEALERVNLLSFLSRIDEQVSdGsfseGQKQRIGLIRA 462
Cdd:COG1116 83 GVVF-Q----EPALlpwltvLDNVALglelrgVPKAERRERARELLELVGLAGFEDAYPHQLS-G----GMRQRVAIARA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937373637 463 FLKGSSVVIFDEATANLDHNNATRIEHLLLS---DPNITYITVTHHLikenepyfDEIIRLG 521
Cdd:COG1116 153 LANDPEVLLMDEPFGALDALTRERLQDELLRlwqETGKTVLFVTHDV--------DEAVFLA 206
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
325-504 |
2.56e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 52.00 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 325 SYHFGENAIiKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILfgkLESKEI--DENSIVSNCAYVG---- 398
Cdd:PRK13639 10 SYPDGTEAL-KGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVL---IKGEPIkyDKKSLLEVRKTVGivfq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 -SQTHIYNDTLRN-------NLTLWNEAItDTHIKEALERVNLLSFlsridEQVSDGSFSEGQKQRIGLIRAFLKGSSVV 470
Cdd:PRK13639 86 nPDDQLFAPTVEEdvafgplNLGLSKEEV-EKRVKEALKAVGMEGF-----ENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 1937373637 471 IFDEATANLDHNNATRIEHLL--LSDPNITYITVTH 504
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLydLNKEGITIIISTH 195
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
319-523 |
2.74e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 51.41 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVS-YHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFG-----KLESKEIDenSIVS 392
Cdd:PRK10908 2 IRFEHVSkAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghditRLKNREVP--FLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 393 NCAYVGSQTHIYND-TLRNN----LTLWNEAITDT--HIKEALERVNLLSFLSRIDEQVSDgsfseGQKQRIGLIRAFLK 465
Cdd:PRK10908 80 QIGMIFQDHHLLMDrTVYDNvaipLIIAGASGDDIrrRVSAALDKVGLLDKAKNFPIQLSG-----GEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937373637 466 GSSVVIFDEATANLDHNNATRIEHLL--LSDPNITYITVTHHL-IKENEPYfdEIIRLGEG 523
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFeeFNRVGVTVLMATHDIgLISRRSY--RMLTLSDG 213
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
319-480 |
2.96e-07 |
|
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: 53.02 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGklESKEIdensivsncAYVG 398
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVKL---------AYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 sQTHiynDTLRNNLTLWnEAITD--THIKEALERVNLLSFLSRI-----DEQVSDGSFSEGQKQRIGLIRAFLKGSSVVI 471
Cdd:TIGR03719 392 -QSR---DALDPNKTVW-EEISGglDIIKLGKREIPSRAYVGRFnfkgsDQQKKVGQLSGGERNRVHLAKTLKSGGNVLL 466
|
....*....
gi 1937373637 472 FDEATANLD 480
Cdd:TIGR03719 467 LDEPTNDLD 475
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
316-506 |
2.96e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.49 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 316 IQDVRFENVSYHFGENA---IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLES-KEIDENSIV 391
Cdd:PTZ00265 380 IKKIQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNlKDINLKWWR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 392 SNCAYVGSQTHIYNDTLRNNL--TLWN----------------------------------------------------- 416
Cdd:PTZ00265 460 SKIGVVSQDPLLFSNSIKNNIkySLYSlkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsneliemrk 539
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 417 --EAITDTHIKEALERVNLLSFLSRIDEQV-----SDGS-FSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIE 488
Cdd:PTZ00265 540 nyQTIKDSEVVDVSKKVLIHDFVSALPDKYetlvgSNASkLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQ 619
|
250 260
....*....|....*....|.
gi 1937373637 489 HL---LLSDPNITYITVTHHL 506
Cdd:PTZ00265 620 KTinnLKGNENRITIIIAHRL 640
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
317-524 |
3.36e-07 |
|
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: 50.63 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 317 QDVRFENVSY------HFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLL--GNLKDYEGKILfgkLESKEIDEN 388
Cdd:cd03213 2 VTLSFRNLTVtvksspSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVL---INGRPLDKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 389 SIVSNCAYVGSqthiyNDTLRNNLTlwneaitdthIKEALERVNLLSflsrideqvsdgSFSEGQKQRIGLIRAFLKGSS 468
Cdd:cd03213 79 SFRKIIGYVPQ-----DDILHPTLT----------VRETLMFAAKLR------------GLSGGERKRVSIALELVSNPS 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1937373637 469 VVIFDEATANLDHNNATRIEHLL--LSDPNITYITVTHHLIKENEPYFDEIIRLGEGT 524
Cdd:cd03213 132 LLFLDEPTSGLDSSSALQVMSLLrrLADTGRTIICSIHQPSSEIFELFDKLLLLSQGR 189
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
403-523 |
4.44e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.86 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 403 IYNDTLRNNLTLWNEAiTDTHIKEALERVNLLSFLSR----IDEQVSDG--SFSEGQKQRIGLIRAFLK-GSSVVIFDEA 475
Cdd:PTZ00243 1395 LFDGTVRQNVDPFLEA-SSAEVWAALELVGLRERVASesegIDSRVLEGgsNYSVGQRQLMCMARALLKkGSGFILMDEA 1473
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1937373637 476 TANLDHNNATRIEHLLLSD-PNITYITVTHHLikENEPYFDEIIRLGEG 523
Cdd:PTZ00243 1474 TANIDPALDRQIQATVMSAfSAYTVITIAHRL--HTVAQYDKIIVMDHG 1520
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
344-523 |
4.97e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 52.67 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 344 GGKYAITGCSGSGKSTLLNLllgnlkdyegkiLFGKLESKEIDENSIVSNCAYVGSQTHIYNDTLRNNLTL--------W 415
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISA------------MLGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFgsdfeserY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 416 NEAITDTHIKEALErvnLLSFLSRIDEQVSDGSFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLSD- 494
Cdd:PLN03232 711 WRAIDVTALQHDLD---LLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSCMKDe 787
|
170 180 190
....*....|....*....|....*....|
gi 1937373637 495 -PNITYITVTHHLikENEPYFDEIIRLGEG 523
Cdd:PLN03232 788 lKGKTRVLVTNQL--HFLPLMDRIILVSEG 815
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
332-506 |
5.50e-07 |
|
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: 50.96 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 332 AIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENS----------IVSNC-AYVGSQ 400
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrrafrrdvqlVFQDSpSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 401 T---HIYNDTLRNnLTLWNEAITDTHIKEALERVNLLS-FLSRIDEQvsdgsFSEGQKQRIGLIRAFLKGSSVVIFDEAT 476
Cdd:TIGR02769 105 MtvrQIIGEPLRH-LTSLDESEQKARIAELLDMVGLRSeDADKLPRQ-----LSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190
....*....|....*....|....*....|...
gi 1937373637 477 ANLD-HNNATRIEHL--LLSDPNITYITVTHHL 506
Cdd:TIGR02769 179 SNLDmVLQAVILELLrkLQQAFGTAYLFITHDL 211
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
322-504 |
7.15e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFG-KLE-------SKEID-ENSIVS 392
Cdd:PRK11147 323 ENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGtKLEvayfdqhRAELDpEKTVMD 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 393 NCAYvGSQTHIYNDTLRNNLTLWNEAItdTHIKEALERVNLLSflsrideqvsdGsfseGQKQRIGLIRAFLKGSSVVIF 472
Cdd:PRK11147 403 NLAE-GKQEVMVNGRPRHVLGYLQDFL--FHPKRAMTPVKALS-----------G----GERNRLLLARLFLKPSNLLIL 464
|
170 180 190
....*....|....*....|....*....|....*..
gi 1937373637 473 DEATANLDhnnatrIEHL-----LLSDPNITYITVTH 504
Cdd:PRK11147 465 DEPTNDLD------VETLelleeLLDSYQGTVLLVSH 495
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
17-192 |
7.58e-07 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 50.89 E-value: 7.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 17 LLLALnaaifVSASVTLA--LMTNQLVSK--RIQSFLALLGLEVGLYIIYLVLN----YIIAvhqtKLIQKMTLSIRQSY 88
Cdd:cd18551 5 LLLSL-----LGTAASLAqpLLVKNLIDAlsAGGSSGGLLALLVALFLLQAVLSalssYLLG----RTGERVVLDLRRRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 89 LSKIIHHSFSEFRKSDIGEHLSVLNNDIQLIE---SNGFSSiytLCSTVFTTLFSIIALLSYDVR--IVLLAIFLTLCLT 163
Cdd:cd18551 76 WRRLLRLPVSFFDRRRSGDLVSRVTNDTTLLReliTSGLPQ---LVTGVLTVVGAVVLMFLLDWVltLVTLAVVPLAFLI 152
|
170 180
....*....|....*....|....*....
gi 1937373637 164 YLpkPFTNKMQKSMEKFSQANEELVSGVS 192
Cdd:cd18551 153 IL--PLGRRIRKASKRAQDALGELSAALE 179
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
319-506 |
7.72e-07 |
|
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: 49.97 E-value: 7.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILF-GKLESKEIDEN--------- 388
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFdGKPLDIAARNRigylpeerg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 389 -----SIVSNCAYVGSQTHIYNDTLRNNLTLWneaitdthikeaLERVNLLSFLSRIDEQVsdgsfSEGQKQRIGLIRAF 463
Cdd:cd03269 81 lypkmKVIDQLVYLAQLKGLKKEEARRRIDEW------------LERLELSEYANKRVEEL-----SKGNQQKVQFIAAV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1937373637 464 LKGSSVVIFDEATANLDHNNATRIEHLL--LSDPNITYITVTHHL 506
Cdd:cd03269 144 IHDPELLILDEPFSGLDPVNVELLKDVIreLARAGKTVILSTHQM 188
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
322-505 |
8.39e-07 |
|
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: 49.83 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLkDYE---GKILFGK--LESKEIDENSivsncay 396
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHP-KYEvteGEILFKGedITDLPPEERA------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 vgsqthiyndtlRNNLTL-WNEAItdthikeALERVNLLSFLSRIDEqvsdgSFSEGQKQRIGLIRAFLKGSSVVIFDEA 475
Cdd:cd03217 76 ------------RLGIFLaFQYPP-------EIPGVKNADFLRYVNE-----GFSGGEKKRNEILQLLLLEPDLAILDEP 131
|
170 180 190
....*....|....*....|....*....|..
gi 1937373637 476 TANLDHNNATRIEHLL--LSDPNITYITVTHH 505
Cdd:cd03217 132 DSGLDIDALRLVAEVInkLREEGKSVLIITHY 163
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
319-504 |
9.62e-07 |
|
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: 50.03 E-value: 9.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSivSNCAYVG 398
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE--RNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 SQTHIYND-TLRNNL----------TLWNEAITDTHIKEALERVNLLSFLSRIDEQVSDgsfseGQKQRIGLIRAFLKGS 467
Cdd:cd03296 81 QHYALFRHmTVFDNVafglrvkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSG-----GQRQRVALARALAVEP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1937373637 468 SVVIFDEATANLDhnnaTRIEHLLLS-------DPNITYITVTH 504
Cdd:cd03296 156 KVLLLDEPFGALD----AKVRKELRRwlrrlhdELHVTTVFVTH 195
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
319-504 |
9.72e-07 |
|
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: 48.21 E-value: 9.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLnlllgnlkdyegKILFGKLEskeidensivsncAYVG 398
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLL------------KLIAGELE-------------PDEG 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 SQTHIyndtlrnnltlwneaitdthikealERVNLLSFlsridEQvsdgsFSEGQKQRIGLIRAFLKGSSVVIFDEATAN 478
Cdd:cd03221 56 IVTWG-------------------------STVKIGYF-----EQ-----LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180
....*....|....*....|....*.
gi 1937373637 479 LDHNNATRIEHLLLSDPNiTYITVTH 504
Cdd:cd03221 101 LDLESIEALEEALKEYPG-TVILVSH 125
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
349-524 |
1.19e-06 |
|
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: 49.64 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 349 ITGCSGSGKSTLLNLLLGNLKDYEGKILFG-KLESKEIDENSIVSN---CAYVGSQTHIYNDTLRNNLTLWN-------E 417
Cdd:cd03290 32 IVGQVGCGKSSLLLAILGEMQTLEGKVHWSnKNESEPSFEATRSRNrysVAYAAQKPWLLNATVEENITFGSpfnkqryK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 418 AITDTHIKEAleRVNLLSFLSRIDEQVSDGSFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNAtriEHL------- 490
Cdd:cd03290 112 AVTDACSLQP--DIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS---DHLmqegilk 186
|
170 180 190
....*....|....*....|....*....|....
gi 1937373637 491 LLSDPNITYITVTHHLikENEPYFDEIIRLGEGT 524
Cdd:cd03290 187 FLQDDKRTLVLVTHKL--QYLPHADWIIAMKDGS 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
424-504 |
1.65e-06 |
|
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: 48.94 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 424 IKEALERVNLLSFLSRIDEQVSDGsfsegQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLL--LSDPNITYIT 501
Cdd:cd03292 117 VPAALELVGLSHKHRALPAELSGG-----EQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLkkINKAGTTVVV 191
|
...
gi 1937373637 502 VTH 504
Cdd:cd03292 192 ATH 194
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
319-504 |
2.16e-06 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 48.86 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLnlllgnlkdyegKIL-------FGKLE--------SK 383
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLL------------RVLnllemprSGTLNiagnhfdfSK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 384 EIDENSIVS---NCAYVGSQTHIY-NDTLRNNLT---------LWNEAITDThiKEALERVNLLSFLSRIDEQVSDGsfs 450
Cdd:PRK11124 71 TPSDKAIRElrrNVGMVFQQYNLWpHLTVQQNLIeapcrvlglSKDQALARA--EKLLERLRLKPYADRFPLHLSGG--- 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1937373637 451 egQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLL--LSDPNITYITVTH 504
Cdd:PRK11124 146 --QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIreLAETGITQVIVTH 199
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
373-506 |
2.27e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.80 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 373 GKILFGKLESKEIDENSIVSNCAYVGSQTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSRIDEQVSDG----- 447
Cdd:PTZ00265 1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNvgpyg 1356
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937373637 448 -SFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLL---SDPNITYITVTHHL 506
Cdd:PTZ00265 1357 kSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdikDKADKTIITIAHRI 1419
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
319-523 |
3.08e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 48.83 E-value: 3.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENA-IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLES---KEIDENSIVSNC 394
Cdd:PRK13644 2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdfSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 395 AYVGSQTHIYNDTLRNNLTLWNE--AITDTHIKE----ALERVNLLSFLSRideqvSDGSFSEGQKQRIGLIRAFLKGSS 468
Cdd:PRK13644 82 VFQNPETQFVGRTVEEDLAFGPEnlCLPPIEIRKrvdrALAEIGLEKYRHR-----SPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1937373637 469 VVIFDEATANLDHNNAT----RIEHLLLSDPNITYItvTHHLikENEPYFDEIIRLGEG 523
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIavleRIKKLHEKGKTIVYI--THNL--EELHDADRIIVMDRG 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
342-521 |
3.30e-06 |
|
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: 48.79 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 342 KEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFG-------------KLESKEID----------ENSIVSNCAYVG 398
Cdd:cd03294 48 REGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgqdiaamsrkelrELRRKKISmvfqsfallpHRTVLENVAFGL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 SQTHIyndtlrnnltlwNEAITDTHIKEALERVNLLSFL-SRIDEqvsdgsFSEGQKQRIGLIRAFLKGSSVVIFDEATA 477
Cdd:cd03294 128 EVQGV------------PRAEREERAAEALELVGLEGWEhKYPDE------LSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1937373637 478 NLDHNNATRIEHLLL---SDPNITYITVTHHLikenepyfDEIIRLG 521
Cdd:cd03294 190 ALDPLIRREMQDELLrlqAELQKTIVFITHDL--------DEALRLG 228
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
333-524 |
3.48e-06 |
|
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: 48.04 E-value: 3.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 333 IIKGFTQTFKEGGKYAITGCSGSGKSTllNLLLGNLKDYEGKILFGK--LESKEIDENSIVSNCAYVgSQthiyNDTLRN 410
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTT--LLDAISGRVEGGGTTSGQilFNGQPRKPDQFQKCVAYV-RQ----DDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 411 NLT----------LWNEAITDTHIKEALERVNLLSFLSriDEQVSD---GSFSEGQKQRIGLIRAFLKGSSVVIFDEATA 477
Cdd:cd03234 95 GLTvretltytaiLRLPRKSSDAIRKKRVEDVLLRDLA--LTRIGGnlvKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937373637 478 NLDHNNATRIEHLL--LSDPNITYITVTHHLIKENEPYFDEIIRLGEGT 524
Cdd:cd03234 173 GLDSFTALNLVSTLsqLARRNRIVILTIHQPRSDLFRLFDRILLLSSGE 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
348-506 |
3.61e-06 |
|
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: 48.06 E-value: 3.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 348 AITGCSGSGKSTLLNLLLGNLKDYEGKILFGKL----ESKEIDENSIVSNCAYVGSQTHIY-NDTLRNNLTLWNEAITDT 422
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYALFpHLNVRENLAFGLKRKRNR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 423 HIK----EALERVNLLSFLSRIDEQVSDGsfsegQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLL---LSDP 495
Cdd:cd03297 107 EDRisvdELLDLLGLDHLLNRYPAQLSGG-----EKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELkqiKKNL 181
|
170
....*....|.
gi 1937373637 496 NITYITVTHHL 506
Cdd:cd03297 182 NIPVIFVTHDL 192
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
320-523 |
5.23e-06 |
|
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: 47.75 E-value: 5.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 320 RFENVSYHFgenAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKIlfgkleskEIDENSIVSNCAYVGS 399
Cdd:cd03266 10 RFRDVKKTV---QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFA--------TVDGFDVVKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 400 QTHIYNDT--LRNNLTLWN--EAITDTH-IK--EALERVNLLSFLSRIDE--QVSDGSFSEGQKQRIGLIRAFLKGSSVV 470
Cdd:cd03266 79 RLGFVSDStgLYDRLTAREnlEYFAGLYgLKgdELTARLEELADRLGMEEllDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1937373637 471 IFDEATANLD--HNNATR--IEHLLLSDPNITYITvthHLIKENEPYFDEIIRLGEG 523
Cdd:cd03266 159 LLDEPTTGLDvmATRALRefIRQLRALGKCILFST---HIMQEVERLCDRVVVLHRG 212
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
424-506 |
5.52e-06 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 47.96 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 424 IKEALERVNLLSFLSRideQVsdGSFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLL--LSDPNITYIT 501
Cdd:PRK15056 123 VTAALARVDMVEFRHR---QI--GELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLreLRDEGKTMLV 197
|
....*
gi 1937373637 502 VTHHL 506
Cdd:PRK15056 198 STHNL 202
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
319-504 |
6.11e-06 |
|
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: 48.98 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHF--GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAY 396
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQTHIYNDTLRNNLTLWNEAiTDTHIKEALERVNL----LSFLSRIDEQVSDGSF--SEGQKQRIGLIRAFLKGSSVV 470
Cdd:COG4618 411 LPQDVELFDGTIAENIARFGDA-DPEKVVAAAKLAGVhemiLRLPDGYDTRIGEGGArlSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1937373637 471 IFDEATANLDH------NNAtrIEHllLSDPNITYITVTH 504
Cdd:COG4618 490 VLDEPNSNLDDegeaalAAA--IRA--LKARGATVVVITH 525
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
16-191 |
6.35e-06 |
|
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: 47.94 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 16 ILLLALNAAIFVSASVTLALMTNQLV-SKRIQSFLALLGLEVGLYIIYLVLNYIIAVHQTKLIQKMTLSIRQSYLSKIIH 94
Cdd:cd18557 2 LLFLLISSAAQLLLPYLIGRLIDTIIkGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 95 HSFSEFRKSDIGEHLSVLNNDIQLIESNGFSSIYTLCSTVFTTLFSIIAL--LSYDVRIVLLAIF-----LTLCLTYLPK 167
Cdd:cd18557 82 QEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILfiLSWKLTLVLLLVIpllliASKIYGRYIR 161
|
170 180
....*....|....*....|....
gi 1937373637 168 PFTNKMQKSMEKFSQANEELVSGV 191
Cdd:cd18557 162 KLSKEVQDALAKAGQVAEESLSNI 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
321-504 |
6.82e-06 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 48.52 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 321 FENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLnlllgnlkdyegKILFGKLESkeiDENSIV--SNC--AY 396
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLL------------KILAGELEP---DSGEVSipKGLriGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VgSQTHIYNDtlrnNLTLWNEAIT-DTHIKEALERVNLLSFL---------------------------SRI-------- 440
Cdd:COG0488 66 L-PQEPPLDD----DLTVLDTVLDgDAELRALEAELEELEAKlaepdedlerlaelqeefealggweaeARAeeilsglg 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 441 ------DEQVSDgsFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLSDPNiTYITVTH 504
Cdd:COG0488 141 fpeedlDRPVSE--LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG-TVLVVSH 207
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
319-481 |
8.84e-06 |
|
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: 46.73 E-value: 8.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVS--YHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLnlllgnlkdyegKILFGKLESKE----IDENSIVS 392
Cdd:cd03263 1 LQIRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTL------------KMLTGELRPTSgtayINGYSIRT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 393 NCAYVgsQTHI-Y---NDTLRNNLTLW------------NEAITDTHIKEALERVNLLSFLsriDEQVSDgsFSEGQKQR 456
Cdd:cd03263 69 DRKAA--RQSLgYcpqFDALFDELTVRehlrfyarlkglPKSEIKEEVELLLRVLGLTDKA---NKRART--LSGGMKRK 141
|
170 180
....*....|....*....|....*
gi 1937373637 457 IGLIRAFLKGSSVVIFDEATANLDH 481
Cdd:cd03263 142 LSLAIALIGGPSVLLLDEPTSGLDP 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
318-480 |
1.08e-05 |
|
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: 48.37 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 318 DVRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDyEGKILFGKLESKEIDENSIVSNCAYV 397
Cdd:TIGR01271 1219 DVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 GSQTHIYNDTLRNNLTLWnEAITDTHIKEALERVNLLS----FLSRIDEQVSDGSF--SEGQKQRIGLIRAFLKGSSVVI 471
Cdd:TIGR01271 1298 PQKVFIFSGTFRKNLDPY-EQWSDEEIWKVAEEVGLKSvieqFPDKLDFVLVDGGYvlSNGHKQLMCLARSILSKAKILL 1376
|
....*....
gi 1937373637 472 FDEATANLD 480
Cdd:TIGR01271 1377 LDEPSAHLD 1385
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
323-480 |
1.16e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.48 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 323 NVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFgklESKEIDENSivsnCAY------ 396
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILF---ERQSIKKDL----CTYqkqlcf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 397 VGSQTHIyndtlRNNLTLWNEAITDTHIK----EALERVNLLSFLSRIDEQVsdGSFSEGQKQRIGLIRAFLKGSSVVIF 472
Cdd:PRK13540 79 VGHRSGI-----NPYLTLRENCLYDIHFSpgavGITELCRLFSLEHLIDYPC--GLLSSGQKRQVALLRLWMSKAKLWLL 151
|
....*...
gi 1937373637 473 DEATANLD 480
Cdd:PRK13540 152 DEPLVALD 159
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
318-504 |
1.17e-05 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 47.40 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 318 DVRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTllnlllgnlkdyEGKILfgkleskeIDENSIVS----- 392
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTllrmiagfetpdSGRIL--------LDGRDVTGlppek 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 393 -NCAYVgSQthiyNDTLRNNLTLW------------NEAITDTHIKEALERVNLLSFLSRIDEQVSdGsfseGQKQRIGL 459
Cdd:COG3842 77 rNVGMV-FQ----DYALFPHLTVAenvafglrmrgvPKAEIRARVAELLELVGLEGLADRYPHQLS-G----GQQQRVAL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1937373637 460 IRAFLKGSSVVIFDEATANLDHN--NATRIEhL--LLSDPNITYITVTH 504
Cdd:COG3842 147 ARALAPEPRVLLLDEPLSALDAKlrEEMREE-LrrLQRELGITFIYVTH 194
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
319-480 |
1.44e-05 |
|
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: 46.77 E-value: 1.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLkDYEGKILFGKLESKEIDENSIVSNCAYVG 398
Cdd:cd03289 5 VKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSVPLQKWRKAFGVIP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 SQTHIYNDTLRNNLTLwNEAITDTHIKEALERVNLLS----FLSRIDEQVSDGSF--SEGQKQRIGLIRAFLKGSSVVIF 472
Cdd:cd03289 84 QKVFIFSGTFRKNLDP-YGKWSDEEIWKVAEEVGLKSvieqFPGQLDFVLVDGGCvlSHGHKQLMCLARSVLSKAKILLL 162
|
....*...
gi 1937373637 473 DEATANLD 480
Cdd:cd03289 163 DEPSAHLD 170
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
332-506 |
1.48e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 46.60 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 332 AIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILF-----GKLESKEI------------DENSIVSNC 394
Cdd:PRK10419 26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrgeplAKLNRAQRkafrrdiqmvfqDSISAVNPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 395 AYVGSqthIYNDTLRNNLTLwNEAITDTHIKEALERVNL-LSFLSRIDEQVSDGsfsegQKQRIGLIRAFLKGSSVVIFD 473
Cdd:PRK10419 106 KTVRE---IIREPLRHLLSL-DKAERLARASEMLRAVDLdDSVLDKRPPQLSGG-----QLQRVCLARALAVEPKLLILD 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1937373637 474 EATANLD-HNNATRIEHL--LLSDPNITYITVTHHL 506
Cdd:PRK10419 177 EAVSNLDlVLQAGVIRLLkkLQQQFGTACLFITHDL 212
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
328-506 |
1.88e-05 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 45.69 E-value: 1.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 328 FGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLnlllgnlkdyegKILFGKLE----SKEIDENSIVsncAYVGSQTHI 403
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLL------------KVLAGVLRptsgTVRRAGGARV---AYVPQRSEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 404 yNDTL----RNNLT--------LWNEAITDTH--IKEALERVNLLSFLSRideqvSDGSFSEGQKQRIGLIRAFLKGSSV 469
Cdd:NF040873 67 -PDSLpltvRDLVAmgrwarrgLWRRLTRDDRaaVDDALERVGLADLAGR-----QLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 1937373637 470 VIFDEATANLDHNNATRIEHLL--LSDPNITYITVTHHL 506
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLaeEHARGATVVVVTHDL 179
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
309-523 |
2.24e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 46.33 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 309 PKTCIATIQDVRFenvSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLlnlllgnlkdyeGKILFGKLESKEIDEN 388
Cdd:PRK13640 1 MKDNIVEFKHVSF---TYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTI------------SKLINGLLLPDDNPNS 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 389 SIVSNCAYVGSQThIYNDTLRNNLTLWNE------AITDTHIKEALE-----RVNLLSFLSRIDEQVSDGSF-------- 449
Cdd:PRK13640 66 KITVDGITLTAKT-VWDIREKVGIVFQNPdnqfvgATVGDDVAFGLEnravpRPEMIKIVRDVLADVGMLDYidsepanl 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937373637 450 SEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHL---LLSDPNITYITVTHHLIKENEPyfDEIIRLGEG 523
Cdd:PRK13640 145 SGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLirkLKKKNNLTVISITHDIDEANMA--DQVLVLDDG 219
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
23-191 |
2.25e-05 |
|
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: 46.31 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 23 AAIFVSASVTLALMTNQLVSKR----------IQSFLALLGLEVGLYIIYLVLNYIIAVHQTKLIQKMTLSIRQSYLSKI 92
Cdd:cd18545 4 LALLLMLLSTAASLAGPYLIKIaideyipngdLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 93 IHHSFSEFRKSDIGEHLSVLNNDIQLIeSNGFSS-IYTLCSTVFTTLFSIIALLSYDVRIVLLAI----FLTLCLTYLPK 167
Cdd:cd18545 84 QKLSFSFFDSRPVGKILSRVINDVNSL-SDLLSNgLINLIPDLLTLVGIVIIMFSLNVRLALVTLavlpLLVLVVFLLRR 162
|
170 180
....*....|....*....|....*..
gi 1937373637 168 PFTNKMQKSMEKFSQAN---EELVSGV 191
Cdd:cd18545 163 RARKAWQRVRKKISNLNaylHESISGI 189
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
334-522 |
2.40e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 46.24 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 334 IKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEG--KILFGKLESKEIDENSIVSNCAYVGSQTHIYNDTLRNN 411
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 412 LT--LWNEAITD----THIKEALERVNLLSFLSRideqvSDGSFSEGQKQRIGLIRAFLKGSSVVIFDEATANLD---HN 482
Cdd:PRK13642 103 VAfgMENQGIPReemiKRVDEALLAVNMLDFKTR-----EPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDptgRQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1937373637 483 NATRIEHLLLSDPNITYITVTHHLIKENEPYFDEIIRLGE 522
Cdd:PRK13642 178 EIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGE 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
327-505 |
4.50e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 45.04 E-value: 4.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 327 HFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYE------GKILFGKLESKEIDENSIVSNCAYVGSQ 400
Cdd:PRK14246 19 YINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIFQIDAIKLRKEVGMVFQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 401 THIY-NDTLRNNLT--LWNEAITDTH-----IKEALERVNLLSFL-SRIDEQVSdgSFSEGQKQRIGLIRAFLKGSSVVI 471
Cdd:PRK14246 99 PNPFpHLSIYDNIAypLKSHGIKEKReikkiVEECLRKVGLWKEVyDRLNSPAS--QLSGGQQQRLTIARALALKPKVLL 176
|
170 180 190
....*....|....*....|....*....|....*
gi 1937373637 472 FDEATANLDHNNATRIEHLLLSDPN-ITYITVTHH 505
Cdd:PRK14246 177 MDEPTSMIDIVNSQAIEKLITELKNeIAIVIVSHN 211
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
319-524 |
7.04e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 44.84 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHF--GENAIiKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGkleSKEID--ENSIVSNC 394
Cdd:PRK13636 6 LKVEELNYNYsdGTHAL-KGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFD---GKPIDysRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 395 AYVGS----------QTHIYNDTlrnNLTLWNEAITDTHIKEALERVNLLSFLSRIDEQVSDgSFSEGQKQRIGLIRAFL 464
Cdd:PRK13636 82 ESVGMvfqdpdnqlfSASVYQDV---SFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTH-CLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937373637 465 KGSSVVIFDEATANLDHNNATRIEHLLLS---DPNITYITVTHHLikENEP-YFDEIIRLGEGT 524
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqkELGLTIIIATHDI--DIVPlYCDNVFVMKEGR 219
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
325-504 |
7.23e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.49 E-value: 7.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 325 SYHFGEN--AIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVS----NCAYVG 398
Cdd:PRK10535 13 SYPSGEEqvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrreHFGFIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 SQTHIYND-TLRNNLTLwnEAI-TDTHIKEALERVN-LLSFL---SRIDEQVSdgSFSEGQKQRIGLIRAFLKGSSVVIF 472
Cdd:PRK10535 93 QRYHLLSHlTAAQNVEV--PAVyAGLERKQRLLRAQeLLQRLgleDRVEYQPS--QLSGGQQQRVSIARALMNGGQVILA 168
|
170 180 190
....*....|....*....|....*....|....
gi 1937373637 473 DEATANLDHNNATRIEHLL--LSDPNITYITVTH 504
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILhqLRDRGHTVIIVTH 202
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
425-504 |
7.44e-05 |
|
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: 44.35 E-value: 7.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 425 KEALERVNLLSFLSRIDEQVSDGsfsegQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLS---DPNITYIT 501
Cdd:COG4181 128 RALLERVGLGHRLDHYPAQLSGG-----EQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFElnrERGTTLVL 202
|
...
gi 1937373637 502 VTH 504
Cdd:COG4181 203 VTH 205
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
319-523 |
9.19e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 44.46 E-value: 9.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENA-----IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSN 393
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 394 CA------------------YVGSQTHIYNDTLRNNLTLWNEAI----TDTHIKEA--LERVNL-LSFLSRideqvSDGS 448
Cdd:PRK13631 102 NPyskkiknfkelrrrvsmvFQFPEYQLFKDTIEKDIMFGPVALgvkkSEAKKLAKfyLNKMGLdDSYLER-----SPFG 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937373637 449 FSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLSDP--NITYITVTHHLIKENEpYFDEIIRLGEG 523
Cdd:PRK13631 177 LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKanNKTVFVITHTMEHVLE-VADEVIVMDKG 252
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
329-506 |
9.54e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 9.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 329 GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDyEGKILFG-----KLESKEI------------DENSIV 391
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDgqplhNLNRRQLlpvrhriqvvfqDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 392 SNCAYVgsqTHIYNDTLRNNLTLWNEAITDTHIKEALERVNLlSFLSRideQVSDGSFSEGQKQRIGLIRAFLKGSSVVI 471
Cdd:PRK15134 376 NPRLNV---LQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGL-DPETR---HRYPAEFSGGQRQRIAIARALILKPSLII 448
|
170 180 190
....*....|....*....|....*....|....*...
gi 1937373637 472 FDEATANLDHNNATRIEHLLLS---DPNITYITVTHHL 506
Cdd:PRK15134 449 LDEPTSSLDKTVQAQILALLKSlqqKHQLAYLFISHDL 486
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
415-520 |
9.97e-05 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 45.01 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 415 WNEAITDThiKEALERVNLlsflsRID--EQVSDgsFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNatrIEHLL- 491
Cdd:COG1129 114 WRAMRRRA--RELLARLGL-----DIDpdTPVGD--LSVAQQQLVEIARALSRDARVLILDEPTASLTERE---VERLFr 181
|
90 100 110
....*....|....*....|....*....|...
gi 1937373637 492 ----LSDPNITYITVTHHLikenepyfDEIIRL 520
Cdd:COG1129 182 iirrLKAQGVAIIYISHRL--------DEVFEI 206
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
329-505 |
1.05e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.86 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 329 GENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLG--NLKDYEGKILFG-----KLESKEIDENSI----------- 390
Cdd:CHL00131 18 NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKgesilDLEPEERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 391 -VSN-----CAYVGSQTHiYNDTLRNNLTLWneaitdTHIKEALERVNL-LSFLSRideQVSDGsFSEGQKQRIGLIRAF 463
Cdd:CHL00131 98 gVSNadflrLAYNSKRKF-QGLPELDPLEFL------EIINEKLKLVGMdPSFLSR---NVNEG-FSGGEKKRNEILQMA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1937373637 464 LKGSSVVIFDEATANLDHNNATRIEHLL--LSDPNITYITVTHH 505
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGInkLMTSENSIILITHY 210
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
333-506 |
1.59e-04 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 43.27 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 333 IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILF-----GKLESK---EIDENSIvsncAYVGSQTHIY 404
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFngqpmSKLSSAakaELRNQKL----GFIYQFHHLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 405 ND-TLRNNLT---LWNEAITDTHIKEALERVNLLSFLSRIDEQVSDgsFSEGQKQRIGLIRAFLKGSSVVIFDEATANLD 480
Cdd:PRK11629 100 PDfTALENVAmplLIGKKKPAEINSRALEMLAAVGLEHRANHRPSE--LSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190
....*....|....*....|....*....|
gi 1937373637 481 HNNATRIEHlLLSDPNI----TYITVTHHL 506
Cdd:PRK11629 178 ARNADSIFQ-LLGELNRlqgtAFLVVTHDL 206
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
349-507 |
1.69e-04 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 42.87 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 349 ITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDEnSIVSNCAYVGSQTHIYND-TLRNNLTlWNEAI----TDTH 423
Cdd:PRK13538 32 IEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD-EYHQDLLYLGHQPGIKTElTALENLR-FYQRLhgpgDDEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 424 IKEALERVNLLSFlsridEQVSDGSFSEGQKQRIGLIRAFLKGSSVVIFDEA-TAnLDHNNATRIEHLL---LSDPNITY 499
Cdd:PRK13538 110 LWEALAQVGLAGF-----EDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPfTA-IDKQGVARLEALLaqhAEQGGMVI 183
|
....*...
gi 1937373637 500 ITvTHHLI 507
Cdd:PRK13538 184 LT-THQDL 190
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
344-524 |
1.87e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.34 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 344 GGKYAITGCSGSGKSTLLNLllgnlkdyegkiLFGKLESKEIDENSIVSNCAYVGSQTHIYNDTLRNNLTL--------W 415
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISA------------MLGELPPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFgspfdperY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 416 NEAITDTHIKEALErvnLLSF--LSRIDEQVSDgsFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLS 493
Cdd:PLN03130 711 ERAIDVTALQHDLD---LLPGgdLTEIGERGVN--ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIK 785
|
170 180 190
....*....|....*....|....*....|...
gi 1937373637 494 DP--NITYITVTHHLikENEPYFDEIIRLGEGT 524
Cdd:PLN03130 786 DElrGKTRVLVTNQL--HFLSQVDRIILVHEGM 816
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
319-504 |
2.07e-04 |
|
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: 44.02 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTlLNLLLGNLKDYE---GKILF------------------ 377
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSV-LMHVLRGMDQYEptsGRIIYhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 378 -------GKLESKEID--------ENSIVSNCAYVGSQTH-IYND--TLRNNLTLWNEA--ITDTHIKEALERVNLLSFL 437
Cdd:TIGR03269 80 epcpvcgGTLEPEEVDfwnlsdklRRRIRKRIAIMLQRTFaLYGDdtVLDNVLEALEEIgyEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 438 SRIDEQVSDgsFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLS---DPNITYITVTH 504
Cdd:TIGR03269 160 HRITHIARD--LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavkASGISMVLTSH 227
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
319-506 |
2.08e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 43.23 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLL-----NLLLGNLKDYEGKILFG--KLESKEID----- 386
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrLNDLIPGFRVEGKVTFHgkNLYAPDVDpvevr 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 387 -------------ENSIVSNCA-------YVGSQTHIYNDTLRNnLTLWNEaitdthIKEALERVNLlsflsrideqvsd 446
Cdd:PRK14243 91 rrigmvfqkpnpfPKSIYDNIAygaringYKGDMDELVERSLRQ-AALWDE------VKDKLKQSGL------------- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1937373637 447 gSFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLS-DPNITYITVTHHL 506
Cdd:PRK14243 151 -SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHElKEQYTIIIVTHNM 210
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
319-506 |
2.08e-04 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 43.10 E-value: 2.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTL------LNLLLGNLKdYEGKILF-GK-LESKEIDEN-- 388
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLlrclnrMNDLIPGAR-VEGEILLdGEdIYDPDVDVVel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 389 ----------------SIVSNCAYvGSQTHIYNDtlRNNLtlwneaitDTHIKEALERVNLLsflsriDEqVSD------ 446
Cdd:COG1117 91 rrrvgmvfqkpnpfpkSIYDNVAY-GLRLHGIKS--KSEL--------DEIVEESLRKAALW------DE-VKDrlkksa 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937373637 447 GSFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLL--LSDpNITYITVTHHL 506
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELIleLKK-DYTIVIVTHNM 213
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
344-504 |
2.72e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 43.69 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 344 GGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILF----------GKLESKEIDENSIVSNcAYVG---SQTHIYN--DTL 408
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFngqridtlspGKLQALRRDIQFIFQD-PYASldpRQTVGDSimEPL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 409 RNNLTLWNEAiTDTHIKEALERVNLL-SFLSRIDEQvsdgsFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRI 487
Cdd:PRK10261 429 RVHGLLPGKA-AAARVAWLLERVGLLpEHAWRYPHE-----FSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQI 502
|
170 180
....*....|....*....|
gi 1937373637 488 EHLLLS---DPNITYITVTH 504
Cdd:PRK10261 503 INLLLDlqrDFGIAYLFISH 522
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
18-191 |
2.77e-04 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 42.85 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 18 LLALNAAIFVSASVTLA--LMTNQLVSKRI-QSFLALLGLEVGLYIIYLVLNYIIAVHQTKLI----QKMTLSIRQSYLS 90
Cdd:cd18550 1 LALVLLLILLSALLGLLppLLLREIIDDALpQGDLGLLVLLALGMVAVAVASALLGVVQTYLSarigQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 91 KIIHHSFSEFRKSDIGEHLSVLNNDIQLIESNGFSSIYTLCSTVFTTLFSIIALLSYDVRIVLLAIfLTLCLTYLP-KPF 169
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSL-VLLPLFVLPtRRV 159
|
170 180 190
....*....|....*....|....*....|.
gi 1937373637 170 TNKMQK----SMEKF----SQANEEL-VSGV 191
Cdd:cd18550 160 GRRRRKltreQQEKLaelnSIMQETLsVSGA 190
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
15-195 |
3.46e-04 |
|
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: 42.82 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 15 HILLLALNAAIFVSAsVTLA--LMTNQLV-----SKRIQSFLALLGLEVGLYIIYLVLNYIIAVHQTKLIQKMTLSIRQS 87
Cdd:cd18549 2 KLFFLDLFCAVLIAA-LDLVfpLIVRYIIddllpSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 88 YLSKIIHHSFSEFRKSDIGEHLSVLNNDIqliesngfSSIYTLCS--------TVFTTLFSIIALLSYDVRIVLLAIFLT 159
Cdd:cd18549 81 LFEHLQKLSFSFFDNNKTGQLMSRITNDL--------FDISELAHhgpedlfiSIITIIGSFIILLTINVPLTLIVFALL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 1937373637 160 LCLTYlpkpFTNKMQKSMEKFSQANEELVSGVSDQL 195
Cdd:cd18549 153 PLMII----FTIYFNKKMKKAFRRVREKIGEINAQL 184
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
322-506 |
3.77e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 42.46 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLL-----------NLLLGNLKDYEGKILFgkleSKEIDENSI 390
Cdd:PRK14239 9 SDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLrsinrmndlnpEVTITGSIVYNGHNIY----SPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 391 VSNCAYVGSQTHIYNDTLRNNLT--LWNEAITDTHI-KEALER-VNLLSFLSRIDEQVSDG--SFSEGQKQRIGLIRAFL 464
Cdd:PRK14239 85 RKEIGMVFQQPNPFPMSIYENVVygLRLKGIKDKQVlDEAVEKsLKGASIWDEVKDRLHDSalGLSGGQQQRVCIARVLA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937373637 465 KGSSVVIFDEATANLDHNNATRIEHLLLS-DPNITYITVTHHL 506
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGlKDDYTMLLVTRSM 207
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
56-191 |
3.79e-04 |
|
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: 42.46 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 56 VGLYIIYLVLNYI-------IAVHQTKliqkmtlSIRQSYLSKIIHHSFSEFRKSDIGEHLSVLNNDIQLIEsNGFS--- 125
Cdd:cd18577 54 VYLGIGSFVLSYIqtacwtiTGERQAR-------RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQ-DGIGekl 125
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1937373637 126 SIYTLCSTVFTTLFsIIAL-LSYDVRIVLLAI--FLTLCLTYLPKPFTNKMQKSMEKFSQAN---EELVSGV 191
Cdd:cd18577 126 GLLIQSLSTFIAGF-IIAFiYSWKLTLVLLATlpLIAIVGGIMGKLLSKYTKKEQEAYAKAGsiaEEALSSI 196
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
424-506 |
4.60e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 41.88 E-value: 4.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 424 IKEALERVNLLSFLSRIDEQVSDGsfsegQKQRIGLIRAFLKGSSVVIFDEATANLDhnNATRIEHL-LLSD----PNIT 498
Cdd:PRK10771 110 LHAIARQMGIEDLLARLPGQLSGG-----QRQRVALARCLVREQPILLLDEPFSALD--PALRQEMLtLVSQvcqeRQLT 182
|
....*...
gi 1937373637 499 YITVTHHL 506
Cdd:PRK10771 183 LLMVSHSL 190
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
322-504 |
4.75e-04 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 41.97 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDEN------------- 388
Cdd:PRK11247 16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDtrlmfqdarllpw 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 389 -SIVSNcayVGSqthiyndTLRNNltlWNEAitdthIKEALERVNLlsfLSRIDEQVSdgSFSEGQKQRIGLIRAFLKGS 467
Cdd:PRK11247 96 kKVIDN---VGL-------GLKGQ---WRDA-----ALQALAAVGL---ADRANEWPA--ALSGGQKQRVALARALIHRP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1937373637 468 SVVIFDEATANLDhnNATRIE--HLLLS---DPNITYITVTH 504
Cdd:PRK11247 153 GLLLLDEPLGALD--ALTRIEmqDLIESlwqQHGFTVLLVTH 192
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
319-523 |
4.85e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 42.03 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKG-----FTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKL------ESKEIDE 387
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFASralfdIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsstsKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 388 NSIVSNCAYVGSQTHIYNDTLRNNLTL--WNEAITDTHIKE-ALERVNLLSfLSRIDEQVSDGSFSEGQKQRIGLIRAFL 464
Cdd:PRK13643 82 VRKKVGVVFQFPESQLFEETVLKDVAFgpQNFGIPKEKAEKiAAEKLEMVG-LADEFWEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1937373637 465 KGSSVVIFDEATANLDHNnaTRIEHLLLSDP----NITYITVThHLIKENEPYFDEIIRLGEG 523
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPK--ARIEMMQLFESihqsGQTVVLVT-HLMDDVADYADYVYLLEKG 220
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
318-524 |
5.52e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 41.93 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 318 DVRFENVSYHFG-----ENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFG-KLESKEIDENSIV 391
Cdd:PRK13634 2 DITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGeRVITAGKKNKKLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 392 SNCAYVG-----SQTHIYNDTLRNNLTL--WNEAITDthiKEALERVNLLSFLSRIDEQVSDGS---FSEGQKQRIGLIR 461
Cdd:PRK13634 82 PLRKKVGivfqfPEHQLFEETVEKDICFgpMNFGVSE---EDAKQKAREMIELVGLPEELLARSpfeLSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1937373637 462 AFLKGSSVVIFDEATANLDHNNATRIEHL---LLSDPNITYITVTHHLiKENEPYFDEIIRLGEGT 524
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMfykLHKEKGLTTVLVTHSM-EDAARYADQIVVMHKGT 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
323-505 |
5.78e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 5.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 323 NVSYhfGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNL-KDYEGK-ILFGKLE-SKEI--DensIVSNCAYV 397
Cdd:PRK10938 267 VVSY--NDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHpQGYSNDlTLFGRRRgSGETiwD---IKKHIGYV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 GSQTHI-Y--NDTLRN--------NLTLWnEAITDTHIKEALERVNLLSflsrIDEQVSDGSF---SEGQkQRIGLI-RA 462
Cdd:PRK10938 342 SSSLHLdYrvSTSVRNvilsgffdSIGIY-QAVSDRQQKLAQQWLDILG----IDKRTADAPFhslSWGQ-QRLALIvRA 415
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1937373637 463 FLKGSSVVIFDEATANLDHNN---ATRIEHLLLSDPNITYITVTHH 505
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLDPLNrqlVRRFVDVLISEGETQLLFVSHH 461
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
351-524 |
8.36e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.46 E-value: 8.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 351 GCSGSGKSTLLNLLLGNLKDYEGKILfgkleskeiDENSIvsncAYVGSQTHIYNDTLRNNLTLWNEAITdthikEALER 430
Cdd:PTZ00243 693 GATGSGKSTLLQSLLSQFEISEGRVW---------AERSI----AYVPQQAWIMNATVRGNILFFDEEDA-----ARLAD 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 431 VNLLSFLSRIDEQVSDG----------SFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRI--EHLLLSDPNIT 498
Cdd:PTZ00243 755 AVRVSQLEADLAQLGGGleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVveECFLGALAGKT 834
|
170 180
....*....|....*....|....*...
gi 1937373637 499 YITVTH--HLIkenePYFDEIIRLGEGT 524
Cdd:PTZ00243 835 RVLATHqvHVV----PRADYVVALGDGR 858
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
323-480 |
1.02e-03 |
|
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: 40.32 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 323 NVSYHFGENA----IIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDY---EGKILFGKLESKEIDEnSIVSNCA 395
Cdd:cd03233 8 NISFTTGKGRskipILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAE-KYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 396 YVGSQthiyndtlrnnltlwneaitDTHIKEALERvNLLSFLSRI--DEQVSdgSFSEGQKQRIGLIRAFLKGSSVVIFD 473
Cdd:cd03233 87 YVSEE--------------------DVHFPTLTVR-ETLDFALRCkgNEFVR--GISGGERKRVSIAEALVSRASVLCWD 143
|
....*..
gi 1937373637 474 EATANLD 480
Cdd:cd03233 144 NSTRGLD 150
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
16-197 |
1.07e-03 |
|
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: 40.96 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 16 ILLLALNAAIFVSASVTLALMTNQLV---------SKRIQSFLALLGLEVGLYIIYLVLNYIIAVHQTKLIQKMTLSIRQ 86
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIddvliqlgpGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 87 SYLSKIIHHSFSEFRKSDIGEHLSVLNNDIQLIE---SNGFSSiytLCSTVFTTLFSIIALLSYDVR---IVLLAIFLTL 160
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQdflSDGLPD---FLTNILMIIGIGVVLFSLNWKlalLVLIPVPLVV 157
|
170 180 190
....*....|....*....|....*....|....*..
gi 1937373637 161 CLTYLpkpFTNKMQKSMEKFSQANEELVSGVSDQLYG 197
Cdd:cd18563 158 WGSYF---FWKKIRRLFHRQWRRWSRLNSVLNDTLPG 191
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
322-505 |
1.20e-03 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 40.54 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTlLNLLLGNLKDYE---GKILFGKLESKEIDENSIVSNCAYVG 398
Cdd:PRK09580 5 KDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKST-LSATLAGREDYEvtgGTVEFKGKDLLELSPEDRAGEGIFMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 SQTHIYNDTLRNNLTLWN--EAITDTHIKEALERVNLLSFLSR-----------IDEQVSDGsFSEGQKQRIGLIRAFLK 465
Cdd:PRK09580 84 FQYPVEIPGVSNQFFLQTalNAVRSYRGQEPLDRFDFQDLMEEkiallkmpedlLTRSVNVG-FSGGEKKRNDILQMAVL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1937373637 466 GSSVVIFDEATANLDHNNATRIEHLL--LSDPNITYITVTHH 505
Cdd:PRK09580 163 EPELCILDESDSGLDIDALKIVADGVnsLRDGKRSFIIVTHY 204
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-511 |
2.30e-03 |
|
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: 40.50 E-value: 2.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 17 LLLALNAAIFVS---ASVTLALMTNQLVSKRIQSFLALLGLEVGLYIIYLVLNYIIAVHQTKLIQKMTLSIRqsylSKII 93
Cdd:TIGR00954 96 GLLILIAFLLVSrtyLSVYVATLDGQIESSIVRRSPRNFAWILFKWFLIAPPASFINSAIKYLLKELKLRFR----VRLT 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 94 HHSFSEFRKSDIGEHLSVLNNDIQLIESNGFSSIYTLCST--------------VFTTLFSII-ALLSYDVRIVLLAIFL 158
Cdd:TIGR00954 172 RYLYSKYLSGFTFYKVSNLDSRIQNPDQLLTQDVEKFCDSvvelysnltkpildVILYSFKLLtALGSVGPAGLFAYLFA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 159 T-LCLTYLPKPF---TNKMQKSMEKFSQANEELVSGvSDQL--------------YGYADVYYASRKQIFLR----QVRS 216
Cdd:TIGR00954 252 TgVVLTKLRPPIgklTVEEQALEGEYRYVHSRLIMN-SEEIafyqgnkveketvmSSFYRLVEHLNLIIKFRfsygFLDN 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 217 IVEEYI--------VQKIIFTKRNTST-----ETLMALFSVAAQMLILLLTglliifgniAVGTIASVG----QISGnIF 279
Cdd:TIGR00954 331 IVAKYTwsavglvaVSIPIFDKTHPAFlemseEELMQEFYNNGRLLLKAAD---------ALGRLMLAGrdmtRLAG-FT 400
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 280 NSLSTINQLQVTIKSVD----------PILKKFHDFPEDPKTCIATIQD--VRFENVSYHFGENAI-IKGFTQTFKEGGK 346
Cdd:TIGR00954 401 ARVDTLLQVLDDVKSGNfkrprveeieSGREGGRNSNLVPGRGIVEYQDngIKFENIPLVTPNGDVlIESLSFEVPSGNN 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 347 YAITGCSGSGKSTLLNLLlgnlkdyeGKI--LFGKLESKEIDENSIvsncaYVGSQTHIYNDTLRNNLT-------LWNE 417
Cdd:TIGR00954 481 LLICGPNGCGKSSLFRIL--------GELwpVYGGRLTKPAKGKLF-----YVPQRPYMTLGTLRDQIIypdssedMKRR 547
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 418 AITDTHIKEALERVNLLSFLSRID--EQVSDGS--FSEGQKQRIGLIRAFLKGSSVVIFDEATanldhnNATRIE----- 488
Cdd:TIGR00954 548 GLSDKDLEQILDNVQLTHILEREGgwSAVQDWMdvLSGGEKQRIAMARLFYHKPQFAILDECT------SAVSVDvegym 621
|
570 580
....*....|....*....|....*
gi 1937373637 489 HLLLSDPNITYITVTHH--LIKENE 511
Cdd:TIGR00954 622 YRLCREFGITLFSVSHRksLWKYHE 646
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
319-482 |
2.76e-03 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 39.71 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKIlfgkleskeidENSIVSNCAYVG 398
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 SQTHIYND---TLRNNLTLwNEAITDTHIKEALERVNLLSFLSRIDEQVSDgsfseGQKQRIGLIRAFLKGSSVVIFDEA 475
Cdd:PRK09544 74 QKLYLDTTlplTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQKLSG-----GETQRVLLARALLNRPQLLVLDEP 147
|
....*..
gi 1937373637 476 TANLDHN 482
Cdd:PRK09544 148 TQGVDVN 154
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
334-522 |
2.94e-03 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 40.02 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 334 IKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKIL-----FGKLESKEIDE------NSIVSNCAYVGSQTH 402
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLidgvdIAKISDAELREvrrkkiAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 403 IYNDTLRNNLTLWNEAITDTHIKEALERVNLLSFLSRIDEQVSDgsfseGQKQRIGLIRAFLKGSSVVIFDEATANLDHN 482
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSG-----GMRQRVGLARALAINPDILLMDEAFSALDPL 198
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1937373637 483 NATRIEHLLL---SDPNITYITVTHHLikenepyfDEIIRLGE 522
Cdd:PRK10070 199 IRTEMQDELVklqAKHQRTIVFISHDL--------DEAMRIGD 233
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
424-506 |
3.33e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 39.71 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 424 IKEALERVNLLSFLSRideqvSDGSFSEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNatRIEHL-----LLSDPNIT 498
Cdd:PRK13650 121 VNEALELVGMQDFKER-----EPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG--RLELIktikgIRDDYQMT 193
|
....*...
gi 1937373637 499 YITVTHHL 506
Cdd:PRK13650 194 VISITHDL 201
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
427-506 |
3.52e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 39.31 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 427 ALERVNLLSFLSRIDEQVSDGSF--SEGQKQRIGLIRAFLKGSSVVIFDEATANLDHNNATRIEHLLLSDPN-ITYITVT 503
Cdd:PRK14271 140 AQARLTEVGLWDAVKDRLSDSPFrlSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrLTVIIVT 219
|
...
gi 1937373637 504 HHL 506
Cdd:PRK14271 220 HNL 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
319-504 |
3.60e-03 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 39.55 E-value: 3.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILfgkLESKEIDE--------NSI 390
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM---LDGQDITHvpaenrhvNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 391 VSNCAYVgsqTHIyndTLRNNLT-------LWNEAITdTHIKEALERVNLLSFLSRIDEQVSDgsfseGQKQRIGLIRAF 463
Cdd:PRK09452 92 FQSYALF---PHM---TVFENVAfglrmqkTPAAEIT-PRVMEALRMVQLEEFAQRKPHQLSG-----GQQQRVAIARAV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937373637 464 LKGSSVVIFDEATANLDH-------NNATRIEHLLlsdpNITYITVTH 504
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYklrkqmqNELKALQRKL----GITFVFVTH 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
319-523 |
4.53e-03 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 38.95 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGE-NAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKIlfgKLESKEIDEnsivSNCAYV 397
Cdd:PRK13647 5 IEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRV---KVMGREVNA----ENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 GSQT---------HIYNDTLRN-------NLTLWNEAItDTHIKEALERVNLLSFLSRIDEQVsdgsfSEGQKQRIGLIR 461
Cdd:PRK13647 78 RSKVglvfqdpddQVFSSTVWDdvafgpvNMGLDKDEV-ERRVEEALKAVRMWDFRDKPPYHL-----SYGQKKRVAIAG 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937373637 462 AFLKGSSVVIFDEATANLDHNNATRIEHLL--LSDPNITYITVTHHLIKENEpYFDEIIRLGEG 523
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILdrLHNQGKTVIVATHDVDLAAE-WADQVIVLKEG 214
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
322-504 |
4.54e-03 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 38.91 E-value: 4.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 322 ENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGKLESKEIDENSIVSNCAYVGSQT 401
Cdd:COG4604 5 KNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQEN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 402 HIyndTLR----------------NNLTLWNEAitdtHIKEALERVNLLSFLSR-IDEqvsdgsFSEGQKQrigliRAFL 464
Cdd:COG4604 85 HI---NSRltvrelvafgrfpyskGRLTAEDRE----IIDEAIAYLDLEDLADRyLDE------LSGGQRQ-----RAFI 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1937373637 465 -----KGSSVVIFDEATANLDHNNATRIEHLL--LSDP-NITYITVTH 504
Cdd:COG4604 147 amvlaQDTDYVLLDEPLNNLDMKHSVQMMKLLrrLADElGKTVVIVLH 194
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
19-155 |
6.27e-03 |
|
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: 38.70 E-value: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 19 LALNAAIFVSASVTLALMTNQLVSKRIQSFLALLGLEVGLYIIYLVLNYIIAVHQTKLIQKMTLSIRQSYLSKIIHHSFS 98
Cdd:cd18565 24 VAIDAVFNGEASFLPLVPASLGPADPRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMA 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 99 EFRKSDIGEHLSVLNNDIQLIE---SNGFSSIYTLcSTVFTTLFSIIALLSYDVRIVLLA 155
Cdd:cd18565 104 FFEDRQTGDLMSVLNNDVNQLErflDDGANSIIRV-VVTVLGIGAILFYLNWQLALVALL 162
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
326-480 |
7.10e-03 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 38.45 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 326 YHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFgklESKEIDEN-----SIVSNCAYV--- 397
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLW---QGKPLDYSkrgllALRQQVATVfqd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 398 GSQTHIYND-------TLRnNLTLWNEAITdTHIKEALERVNLLSFlsridEQVSDGSFSEGQKQRIGLIRAFLKGSSVV 470
Cdd:PRK13638 86 PEQQIFYTDidsdiafSLR-NLGVPEAEIT-RRVDEALTLVDAQHF-----RHQPIQCLSHGQKKRVAIAGALVLQARYL 158
|
170
....*....|
gi 1937373637 471 IFDEATANLD 480
Cdd:PRK13638 159 LLDEPTAGLD 168
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
319-480 |
9.31e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 38.56 E-value: 9.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 319 VRFENVSYHFGENAIIKGFTQTFKEGGKYAITGCSGSGKSTLLNLLLGNLKDYEGKILFGklESKEIdensivsncAYVG 398
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG--ETVKL---------AYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937373637 399 sQTHiynDTLRNNLTLWnEAITD--THIKEALERVNLLSFLSRI-----DEQVSDGSFSEGQKQRIGLIRAFLKGSSVVI 471
Cdd:PRK11819 394 -QSR---DALDPNKTVW-EEISGglDIIKVGNREIPSRAYVGRFnfkggDQQKKVGVLSGGERNRLHLAKTLKQGGNVLL 468
|
....*....
gi 1937373637 472 FDEATANLD 480
Cdd:PRK11819 469 LDEPTNDLD 477
|
|
| |
