|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
61-508 |
3.95e-119 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 362.17 E-value: 3.95e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 61 VLQLCITIVSYIGFLFFIHWGLVVLGILASIPAFIIQYKFGYSnfnLNRLQSGLMREASYINSLFR-NKQSIKEIKLFRS 139
Cdd:COG1132 142 LVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLLVLRLFGRR---LRKLFRRVQEALAELNGRLQeSLSGIRVVKAFGR 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 140 GNFLINRWRKLTTSNNKKILKLFFKQNWANIGLDSLTAVLYSMSAVLMVWLLKLGKMNIGSFVSTAQAIQGLQGTVNQTS 219
Cdd:COG1132 219 EERELERFREANEELRRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 220 HLLASLFESNLYIKDFFDFIEYQNEDDAKKEKLEKnianKSDTANISLKHVYFKYPlSNGYSLKDINLEIKDKEKVAIVG 299
Cdd:COG1132 299 NVLNQLQRALASAERIFELLDEPPEIPDPPGAVPL----PPVRGEIEFENVSFSYP-GDRPVLKDISLTIPPGETVALVG 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 300 HNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENIALS--DISQidnlNEIKQT 377
Cdd:COG1132 374 PSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGrpDATD----EEVEEA 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 378 AFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK 457
Cdd:COG1132 450 AKAAQAHEFIEALPDGYDTVVGE---RGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGR 526
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2105575177 458 TAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYNMYMTQAK 508
Cdd:COG1132 527 TTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFG 577
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
8-507 |
2.68e-112 |
|
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: 348.75 E-value: 2.68e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 8 MELKLNLKLGNMIIEKSLNSPFFYFD---MPEFYNhQFRINNYGHSFLrpISNSMHVLQLCITIVSYIGFLFFIHWGLVV 84
Cdd:COG2274 223 LGQRIDLRLSSRFFRHLLRLPLSFFEsrsVGDLAS-RFRDVESIREFL--TGSLLTALLDLLFVLIFLIVLFFYSPPLAL 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 85 LGILASIPAFIIQYKFGYSNFNLNRLQSGLM-REASYINSLFRNkqsIKEIKLFRSGNFLINRWRKLTTSNNKKILKLFF 163
Cdd:COG2274 300 VVLLLIPLYVLLGLLFQPRLRRLSREESEASaKRQSLLVETLRG---IETIKALGAESRFRRRWENLLAKYLNARFKLRR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 164 KQNWANIGLDSLTAVLYSMSAVLMVWLLKLGKMNIGSFVstaqAIQGLQGT----VNQTSHLLASLFESNLYIKDFFDFI 239
Cdd:COG2274 377 LSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLI----AFNILSGRflapVAQLIGLLQRFQDAKIALERLDDIL 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 240 EYQNEDDAKKEKLEKnianKSDTANISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPT 319
Cdd:COG2274 453 DLPPEREEGRSKLSL----PRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 320 AGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENIALSDiSQIDnLNEIKQTAFLSGADSFIEALPNGYDTtlg 399
Cdd:COG2274 529 SGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD-PDAT-DEEIIEAARLAGLHDFIEALPMGYDT--- 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 400 KVLPNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLK 479
Cdd:COG2274 604 VVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLD 683
|
490 500
....*....|....*....|....*...
gi 2105575177 480 DGQILEEGSHKELMALKGEYYNMYMTQA 507
Cdd:COG2274 684 KGRIVEDGTHEELLARKGLYAELVQQQL 711
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
236-497 |
4.23e-73 |
|
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: 241.97 E-value: 4.23e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 236 FDFIEYQNEDDAKKEKleknIANKSDTANISLKHVYFKYPlSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGL 315
Cdd:COG4988 312 FALLDAPEPAAPAGTA----PLPAAGPPSIELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 316 YKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENIALS--DISQidnlNEIKQTAFLSGADSFIEALPNG 393
Cdd:COG4988 387 LPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGrpDASD----EELEAALEAAGLDEFVAALPDG 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 394 YDTTLGKvlpNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMAD 473
Cdd:COG4988 463 LDTPLGE---GGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQAD 539
|
250 260
....*....|....*....|....
gi 2105575177 474 RIIHLKDGQILEEGSHKELMALKG 497
Cdd:COG4988 540 RILVLDDGRIVEQGTHEELLAKNG 563
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
265-503 |
1.23e-71 |
|
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: 227.88 E-value: 1.23e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYALSVKENIA--LSDISQidnlNEIKQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSI 422
Cdd:cd03251 81 VSQDVFLFNDTVAENIAygRPGATR----EEVEEAARAANAHEFIMELPEGYDTVIGE---RGVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 423 FKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYNM 502
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
.
gi 2105575177 503 Y 503
Cdd:cd03251 234 H 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
265-506 |
2.31e-71 |
|
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: 227.42 E-value: 2.31e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYS-LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVS 343
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPiLKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 344 VVFQDFVRYALSVKENIALSDISQIDNlnEIKQTAFLSGADSFIEALPNGYDTTLGkvlPNSIDISGGQWQRIALARSIF 423
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATDE--EVEEAAKKANIHDFIMSLPDGYDTLVG---ERGSQLSGGQKQRIAIARALL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 424 KKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYNMY 503
Cdd:cd03249 156 RNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLV 235
|
...
gi 2105575177 504 MTQ 506
Cdd:cd03249 236 KAQ 238
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
265-482 |
6.13e-70 |
|
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: 221.10 E-value: 6.13e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYALSVKENIalsdisqidnlneikqtaflsgadsfiealpngydttlgkvlpnsidISGGQWQRIALARSIFK 424
Cdd:cd03228 81 VPQDPFLFSGTIRENI-----------------------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 425 KSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQ 482
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
263-497 |
6.73e-70 |
|
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: 223.26 E-value: 6.73e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 263 ANISLKHVYFKYPlSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYV 342
Cdd:cd03254 1 GEIEFENVNFSYD-EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 343 SVVFQDFVRYALSVKENIALSDisQIDNLNEIKQTAFLSGADSFIEALPNGYDTTLGkvlPNSIDISGGQWQRIALARSI 422
Cdd:cd03254 80 GVVLQDTFLFSGTIMENIRLGR--PNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLG---ENGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 423 FKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKG 497
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
265-503 |
1.13e-69 |
|
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: 233.12 E-value: 1.13e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYALSVKENIAL-----SDisqidnlNEIKQTAFLSGADSFIEALPNGYDTTLGkvlPNSIDISGGQWQRIALA 419
Cdd:COG4987 414 VPQRPHLFDTTLRENLRLarpdaTD-------EELWAALERVGLGDWLAALPDGLDTWLG---EGGRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 420 RSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEY 499
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRY 563
|
....
gi 2105575177 500 YNMY 503
Cdd:COG4987 564 RQLY 567
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
265-506 |
1.84e-69 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 222.36 E-value: 1.84e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYALSVKENIALSDISQidNLNEIKQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFK 424
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGM--SMERVIEAAKLAGAHDFISELPEGYDTIVGE---QGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 425 KSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYNMYM 504
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQ 235
|
..
gi 2105575177 505 TQ 506
Cdd:cd03252 236 LQ 237
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
31-502 |
1.61e-65 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 222.28 E-value: 1.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 31 YFDMPEFYnhqFRINNYGHSFLRPISNSMHVLQLCI-----------TIVSYIGFLFFIHWGL-VVLGILASIPAFIIQY 98
Cdd:TIGR02203 97 LLGLPVSF---FDRQPTGTLLSRITFDSEQVASAATdafivlvretlTVIGLFIVLLYYSWQLtLIVVVMLPVLSILMRR 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 99 kFGYSNFNLNRLQSGLMREASYINSlfRNKQSIKEIKLFRSGNFLINRWRKLTTSNNKKILKLffkqNWANIGLDSLTAV 178
Cdd:TIGR02203 174 -VSKRLRRISKEIQNSMGQVTTVAE--ETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKM----TSAGSISSPITQL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 179 LYS--MSAVLMV--WLLKLGKMNIGSFVSTAQAIQGLQGTVNQTSHLlASLFESNLYIKDF-FDFIEYQNEDDAKKEKLE 253
Cdd:TIGR02203 247 IASlaLAVVLFIalFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNV-NAPMQRGLAAAESlFTLLDSPPEKDTGTRAIE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 254 KNianksdTANISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQI 333
Cdd:TIGR02203 326 RA------RGDVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 334 DENELSEYVSVVFQDFVRYALSVKENIALSDISQIDNlNEIKQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQW 413
Cdd:TIGR02203 400 TLASLRRQVALVSQDVVLFNDTIANNIAYGRTEQADR-AEIERALAAAYAQDFVDKLPLGLDTPIGE---NGVLLSGGQR 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 414 QRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELM 493
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
490
....*....|..
gi 2105575177 494 ALKGEY---YNM 502
Cdd:TIGR02203 556 ARNGLYaqlHNM 567
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
265-506 |
1.10e-64 |
|
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: 209.78 E-value: 1.10e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:cd03253 1 IEFENVTFAYD-PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYALSVKENIALSDISQIDNlnEIKQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFK 424
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDE--EVIEAAKAAQIHDKIMRFPDGYDTIVGE---RGLKLSGGEKQRVAIARAILK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 425 KSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYNMYM 504
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWK 234
|
..
gi 2105575177 505 TQ 506
Cdd:cd03253 235 AQ 236
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
264-487 |
4.57e-62 |
|
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: 202.43 E-value: 4.57e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 264 NISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVS 343
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 344 VVFQDFVRYALSVKENIALSDISQIDnlNEIKQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIF 423
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADD--ERILRAAELAGVTDFVNKHPNGLDLQIGE---RGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 424 KKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEG 487
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
59-506 |
5.97e-61 |
|
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: 212.68 E-value: 5.97e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 59 MHVLQLCITIVsYIGFLFFiHWGLVVLGILASIPAFIIqYKFGYSNFNLNRLQSGLMREASYINSLFRNKQSIKEIKLFR 138
Cdd:TIGR01846 258 TVVLDLLFVVV-FLAVMFF-YSPTLTGVVIGSLVCYAL-LSVFVGPILRKRVEDKFERSAAATSFLVESVTGIETIKATA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 139 SGNFLINRWRKLTTSNNKKILKLffkQNWANIGLDSLTAVLYSMSAVLMVWLLKL---GKMNIGSFVstaqAIQGLQGTV 215
Cdd:TIGR01846 335 TEPQFQNRWDRQLAAYVAASFRV---TNLGNIAGQAIELIQKLTFAILLWFGAHLvigGALSPGQLV----AFNMLAGRV 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 216 NQTSHLLASLFEsnlyikdffDF----IEYQNEDDAKKEKLEKNIANKSDTAN----ISLKHVYFKYPLSNGYSLKDINL 287
Cdd:TIGR01846 408 TQPVLRLAQLWQ---------DFqqtgIALERLGDILNSPTEPRSAGLAALPElrgaITFENIRFRYAPDSPEVLSNLNL 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 288 EIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENIALSDiSQ 367
Cdd:TIGR01846 479 DIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCN-PG 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 368 IDnLNEIKQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVF 447
Cdd:TIGR01846 558 AP-FEHVIHAAKLAGAHDFISELPQGYNTEVGE---KGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIM 633
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 448 EKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYNMYMTQ 506
Cdd:TIGR01846 634 RNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLWQQQ 692
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
262-499 |
5.43e-60 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 207.63 E-value: 5.43e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 262 TANISLKHVYFKYPLSNGY-SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSE 340
Cdd:TIGR02204 335 RGEIEFEQVNFAYPARPDQpALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 341 YVSVVFQDFVRYALSVKENIALSDISQIDNlnEIKQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALAR 420
Cdd:TIGR02204 415 RMALVPQDPVLFAASVMENIRYGRPDATDE--EVEAAARAAHAHEFISALPEGYDTYLGE---RGVTLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 421 SIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEY 499
Cdd:TIGR02204 490 AILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLY 568
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
71-497 |
2.70e-57 |
|
type I secretion system ATPase, LssB 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. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 202.40 E-value: 2.70e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 71 YIGFLFFIHWGLVVLGILAS----IPAFIIQYKfgysnfnLNRLQSGLMREASYINS-LFRNKQSIKEIKLFRSGNFLIN 145
Cdd:TIGR03375 276 FLLVIAIIGGPLVWVPLVAIplilLPGLLLQRP-------LSRLAEESMRESAQRNAvLVESLSGLETIKALNAEGRFQR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 146 RWRKLTTSNNKKILKLffkQNWANIgLDSLTAVLYSMSAVLM----VWLLKLGKMNIGSFVS----TAQAIqglqGTVNQ 217
Cdd:TIGR03375 349 RWEQTVAALARSGLKS---RFLSNL-ATNFAQFIQQLVSVAIvvvgVYLISDGELTMGGLIAcvmlSGRAL----APLGQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 218 TSHLLASLFESNLYIKDFFDFIEYQNEDDAKKEKLEKNIANksdtANISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAI 297
Cdd:TIGR03375 421 LAGLLTRYQQAKTALQSLDELMQLPVERPEGTRFLHRPRLQ----GEIEFRNVSFAYPGQETPALDNVSLTIRPGEKVAI 496
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 298 VGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENIALSDiSQIDNlNEIKQT 377
Cdd:TIGR03375 497 IGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYGTLRDNIALGA-PYADD-EEILRA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 378 AFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK 457
Cdd:TIGR03375 575 AELAGVTEFVRRHPDGLDMQIGE---RGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGK 651
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2105575177 458 TAIFISHRLASVKMADRIIHLKDGQILEEGSHKELM-ALKG 497
Cdd:TIGR03375 652 TLVLVTHRTSLLDLVDRIIVMDNGRIVADGPKDQVLeALRK 692
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
265-507 |
1.76e-55 |
|
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: 195.81 E-value: 1.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFkyplsnGYS-----LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELS 339
Cdd:COG5265 358 VRFENVSF------GYDperpiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 340 EYVSVVFQDFVRYALSVKENIALS--DISQidnlNEIKQTAFLSGADSFIEALPNGYDTTLG----KVlpnsidiSGGQW 413
Cdd:COG5265 432 AAIGIVPQDTVLFNDTIAYNIAYGrpDASE----EEVEAAARAAQIHDFIESLPDGYDTRVGerglKL-------SGGEK 500
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 414 QRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELM 493
Cdd:COG5265 501 QRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELL 580
|
250
....*....|....
gi 2105575177 494 ALKGEYYNMYMTQA 507
Cdd:COG5265 581 AQGGLYAQMWARQQ 594
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
62-502 |
3.63e-53 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 191.47 E-value: 3.63e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 62 LQLCITIVSYIGFLFFIHWGLVVLGILASIPAFIIQYKFG--YSNFnLNRLQSGLMREasyiNSLFRNKQS-IKEIKLFR 138
Cdd:TIGR00958 283 LRNLVMLLGLLGFMLWLSPRLTMVTLINLPLVFLAEKVFGkrYQLL-SEELQEAVAKA----NQVAEEALSgMRTVRSFA 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 139 SGNFLINRWR-KLTtsnnkKILKLFFKQNWANIGLDSLTAVLYSMSAVLMVW----LLKLGKMNIGSFVS----TAQAIQ 209
Cdd:TIGR00958 358 AEEGEASRFKeALE-----ETLQLNKRKALAYAGYLWTTSVLGMLIQVLVLYyggqLVLTGKVSSGNLVSfllyQEQLGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 210 GLQGTVNQTSHLLASLFESnlyiKDFFDFIEyqneddaKKEKLEKN--IANKSDTANISLKHVYFKYPL-SNGYSLKDIN 286
Cdd:TIGR00958 433 AVRVLSYVYSGMMQAVGAS----EKVFEYLD-------RKPNIPLTgtLAPLNLEGLIEFQDVSFSYPNrPDVPVLKGLT 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 287 LEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENIALSDIS 366
Cdd:TIGR00958 502 FTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTD 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 367 QIDnlNEIKQTAFLSGADSFIEALPNGYDTTLGkvlPNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEaYV 446
Cdd:TIGR00958 582 TPD--EEIMAAAKAANAHDFIMEFPNGYDTEVG---EKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECE-QL 655
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2105575177 447 FEKFRELtENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYNM 502
Cdd:TIGR00958 656 LQESRSR-ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
31-500 |
2.11e-52 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 187.09 E-value: 2.11e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 31 YF----DMPEFYNHQFRINNYGHSFLRPiSNSMHVLQL------CITIVSYIGFL---FFIHWGL-VVLGILASIPAFII 96
Cdd:PRK13657 95 YFeriiQLPLAWHSQRGSGRALHTLLRG-TDALFGLWLefmrehLATLVALVVLLplaLFMNWRLsLVLVVLGIVYTLIT 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 97 QykfgysnFNLNRLQSGLMREASYINSLF-RNKQSIKEIKLFRSgnflINRWRKLTTSNNKKILKLFFKQN-----WANI 170
Cdd:PRK13657 174 T-------LVMRKTKDGQAAVEEHYHDLFaHVSDAIGNVSVVQS----YNRIEAETQALRDIADNLLAAQMpvlswWALA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 171 GLDSLTAVLYSMSAVLMV--WLLKLGKMNIG---SFVSTAQAiqgLQGTVNQTSHLLASLFESNLYIKDFFDFIeyqned 245
Cdd:PRK13657 243 SVLNRAASTITMLAILVLgaALVQKGQLRVGevvAFVGFATL---LIGRLDQVVAFINQVFMAAPKLEEFFEVE------ 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 246 DAKKEKLEKniANKSDTANIS----LKHVYFKYPLSnGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAG 321
Cdd:PRK13657 314 DAVPDVRDP--PGAIDLGRVKgaveFDDVSFSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSG 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 322 NIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENIALSDISQIDNlnEIKQTAFLSGADSFIEALPNGYDTTLGKv 401
Cdd:PRK13657 391 RILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDE--EMRAAAERAQAHDFIERKPDGYDTVVGE- 467
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 402 lpNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDG 481
Cdd:PRK13657 468 --RGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNG 545
|
490
....*....|....*....
gi 2105575177 482 QILEEGSHKELMALKGEYY 500
Cdd:PRK13657 546 RVVESGSFDELVARGGRFA 564
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
265-494 |
1.01e-51 |
|
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: 175.60 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:COG1122 1 IELENLSFSYP-GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQD----FVryALSVKENIALS------DISQIDNLneIKQTAFLSGADSFIEALPNgydttlgkvlpnsiDISGGQWQ 414
Cdd:COG1122 80 VFQNpddqLF--APTVEEDVAFGpenlglPREEIRER--VEEALELVGLEHLADRPPH--------------ELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 415 RIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL-TENKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKEL 492
Cdd:COG1122 142 RVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
|
..
gi 2105575177 493 MA 494
Cdd:COG1122 222 FS 223
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
265-483 |
1.16e-51 |
|
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: 174.99 E-value: 1.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYS--LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY- 341
Cdd:cd03255 1 IELKNLSKTYGGGGEKVqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 ---VSVVFQDF--VRYaLSVKENIALSDISQIDNLNEIKQTAflsgadsfIEALpngydTTLGkvLPNSID-----ISGG 411
Cdd:cd03255 81 rrhIGFVFQSFnlLPD-LTALENVELPLLLAGVPKKERRERA--------EELL-----ERVG--LGDRLNhypseLSGG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 412 QWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASVKMADRIIHLKDGQI 483
Cdd:cd03255 145 QQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
265-486 |
8.86e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 172.92 E-value: 8.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYS--LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELS--- 339
Cdd:COG1136 5 LELRNLTKSYGTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 340 -EYVSVVFQDF--VRYaLSVKENIALSDISQIDNLNEIKQTaflsgADSFIEALpnGydttLGKVL---PNsiDISGGQW 413
Cdd:COG1136 85 rRHIGFVFQFFnlLPE-LTALENVALPLLLAGVSRKERRER-----ARELLERV--G----LGDRLdhrPS--QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 414 QRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL--TENKTAIFISH--RLASvkMADRIIHLKDGQILEE 486
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHdpELAA--RADRVIRLRDGRIVSD 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
236-506 |
7.12e-50 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 180.21 E-value: 7.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 236 FDFIEYQNEDDAKKEKLEKNianksdTANISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGL 315
Cdd:PRK11176 319 FAILDLEQEKDEGKRVIERA------KGDIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 316 YKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENIALSDISQIDNlNEIKQTAFLSGADSFIEALPNGYD 395
Cdd:PRK11176 393 YDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEQYSR-EQIEEAARMAYAMDFINKMDNGLD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 396 TTLGKvlpNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRI 475
Cdd:PRK11176 472 TVIGE---NGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEI 548
|
250 260 270
....*....|....*....|....*....|.
gi 2105575177 476 IHLKDGQILEEGSHKELMALKGEYYNMYMTQ 506
Cdd:PRK11176 549 LVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
69-502 |
1.25e-49 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 181.31 E-value: 1.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 69 VSYIGFLFFIHWGLVVLGILASIPAFIIqykFGYSNFNLNRLQSGLMREASYINSL-FRNKQSIKEIKLFRSGNFLINRW 147
Cdd:TIGR03797 264 LLNLGLMFYYSWKLALVAVALALVAIAV---TLVLGLLQVRKERRLLELSGKISGLtVQLINGISKLRVAGAENRAFARW 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 148 RKLTTsnnkKILKLFFK-QNWANiGLDSLTAVL--YSMSAV--LMVWLLKLGKMNIGSFVS--TA--QAIQGLQGTVNQT 218
Cdd:TIGR03797 341 AKLFS----RQRKLELSaQRIEN-LLTVFNAVLpvLTSAALfaAAISLLGGAGLSLGSFLAfnTAfgSFSGAVTQLSNTL 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 219 SHLLA--SLFESNLYIkdffdfIEYQNEDDAkkeklekniaNKSD----TANISLKHVYFKYPLSNGYSLKDINLEIKDK 292
Cdd:TIGR03797 416 ISILAviPLWERAKPI------LEALPEVDE----------AKTDpgklSGAIEVDRVTFRYRPDGPLILDDVSLQIEPG 479
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 293 EKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENIALSDISQIDnln 372
Cdd:TIGR03797 480 EFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLD--- 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 373 EIKQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRE 452
Cdd:TIGR03797 557 EAWEAARMAGLAEDIRAMPMGMHTVISE---GGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLER 633
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2105575177 453 LteNKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYNM 502
Cdd:TIGR03797 634 L--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQL 681
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
266-482 |
1.36e-49 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 169.57 E-value: 1.36e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 266 SLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVV 345
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 346 FQD----FVryALSVKENIALS----DISQIDNLNEIKQTAFLSGADSFIEALPNgydtTLgkvlpnsidiSGGQWQRIA 417
Cdd:cd03225 81 FQNpddqFF--GPTVEEEVAFGlenlGLPEEEIEERVEEALELVGLEGLRDRSPF----TL----------SGGQKQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 418 LARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL-TENKTAIFISHRLASVK-MADRIIHLKDGQ 482
Cdd:cd03225 145 IAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLeLADRVIVLEDGK 211
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
71-494 |
4.02e-49 |
|
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: 177.54 E-value: 4.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 71 YIGFLFFIHwglVVLGILASIPAFIIqykFGYSNFNlNRLQSGLMREAS--------YINSLFRNKQSIKEIKLFRSgnf 142
Cdd:TIGR01842 132 YLLVCFLLH---PWIGILALGGAVVL---VGLALLN-NRATKKPLKEATeasirannLADSALRNAEVIEAMGMMGN--- 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 143 LINRWRKLttsnNKKILKLFFKQNWANIGLDSLTAVLYSM--SAVLMV--WLLKLGKMNIGSFVS----TAQAIQGLQGT 214
Cdd:TIGR01842 202 LTKRWGRF----HSKYLSAQSAASDRAGMLSNLSKYFRIVlqSLVLGLgaYLAIDGEITPGMMIAgsilVGRALAPIDGA 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 215 VNQTSHLLASLfESNLYIKDFFDfiEYQNEDDAKKekleknIANKSDTanISLKHVYFKYPLSNGYSLKDINLEIKDKEK 294
Cdd:TIGR01842 278 IGGWKQFSGAR-QAYKRLNELLA--NYPSRDPAMP------LPEPEGH--LSVENVTIVPPGGKKPTLRGISFSLQAGEA 346
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 295 VAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENIALSDisqiDNLN-- 372
Cdd:TIGR01842 347 LAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIARFG----ENADpe 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 373 EIKQTAFLSGADSFIEALPNGYDTTLGkvlPNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRE 452
Cdd:TIGR01842 423 KIIEAAKLAGVHELILRLPDGYDTVIG---PGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKA 499
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2105575177 453 LTENK-TAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMA 494
Cdd:TIGR01842 500 LKARGiTVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
71-494 |
1.80e-48 |
|
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: 176.09 E-value: 1.80e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 71 YIGFLFFIHWglvVLGILASIPAFIIqykFGYSNFNlNRLQSGLMREAS--------YINSLFRNKQSIkeiklfRS--- 139
Cdd:COG4618 146 FLAVLFLFHP---LLGLLALVGALVL---VALALLN-ERLTRKPLKEANeaairanaFAEAALRNAEVI------EAmgm 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 140 GNFLINRWRKLttsnNKKILKLFFKQNWANIGLDSLTAVL-YSM-SAVLMV--WLLKLGKMNIG---------------- 199
Cdd:COG4618 213 LPALRRRWQRA----NARALALQARASDRAGGFSALSKFLrLLLqSAVLGLgaYLVIQGEITPGamiaasilmgralapi 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 200 --------SFVSTAQAIQGLQGtvnqtshLLASLfesnlyikdffdfieyqnEDDAKKEKLEKnianksDTANISLKHVY 271
Cdd:COG4618 289 eqaiggwkQFVSARQAYRRLNE-------LLAAV------------------PAEPERMPLPR------PKGRLSVENLT 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 272 FKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVR 351
Cdd:COG4618 338 VVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVEL 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 352 YALSVKENIA-LSDIsqidNLNEIKQTAFLSGADSFIEALPNGYDTTLGkvlPNSIDISGGQWQRIALARSIFKKSKLII 430
Cdd:COG4618 418 FDGTIAENIArFGDA----DPEKVVAAAKLAGVHEMILRLPDGYDTRIG---EGGARLSGGQRQRIGLARALYGDPRLVV 490
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 431 LDEPTAALDPKTEAYVFEKFREL-TENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMA 494
Cdd:COG4618 491 LDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
265-478 |
1.07e-47 |
|
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: 173.24 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGySLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYALSVKENIALSDISQIDNlnEIKQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFK 424
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARPDASDA--EIREALERAGLDEFVAALPQGLDTPIGE---GGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 425 KSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHL 478
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
259-503 |
9.02e-47 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 171.55 E-value: 9.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 259 KSDTANISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENEL 338
Cdd:PRK11160 333 AADQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 339 SEYVSVVFQDFVRYALSVKENIALSDisqiDNLNEIKQTAFLS--GADSFIEAlPNGYDTTLGkvlpnsiD----ISGGQ 412
Cdd:PRK11160 413 RQAISVVSQRVHLFSATLRDNLLLAA----PNASDEALIEVLQqvGLEKLLED-DKGLNAWLG-------EggrqLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 413 WQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK11160 481 QRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQEL 560
|
250
....*....|.
gi 2105575177 493 MALKGEYYNMY 503
Cdd:PRK11160 561 LAQQGRYYQLK 571
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
50-503 |
9.93e-47 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 173.39 E-value: 9.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 50 SFLRPISNSMHVLQLCITIVSYIGFLFFIHWGLVVLGILASIPAF---IIQYKFGYSNFNLNRLQSGLMREASYINSLfr 126
Cdd:TIGR01193 264 SIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVYaviIILFKRTFNKLNHDAMQANAVLNSSIIEDL-- 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 127 nkQSIKEIKLFRSGNFlinRWRKLTTSNnKKILKLFFKQNWANIGLDSLTAVLYSMSAVLMVW----LLKLGKMNIGS-- 200
Cdd:TIGR01193 342 --NGIETIKSLTSEAE---RYSKIDSEF-GDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWtgayLVMRGKLTLGQli 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 201 --------FVSTAQAIQGLQGTVNQTSHLLASLFESNLYIKDFFDfieyqneddaKKEKLEKNIANksdtANISLKHVYF 272
Cdd:TIGR01193 416 tfnallsyFLTPLENIINLQPKLQAARVANNRLNEVYLVDSEFIN----------KKKRTELNNLN----GDIVINDVSY 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 273 KYPLsNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRY 352
Cdd:TIGR01193 482 SYGY-GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIF 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 353 ALSVKENIALSDISQIDNlNEIKQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFKKSKLIILD 432
Cdd:TIGR01193 561 SGSILENLLLGAKENVSQ-DEIWAACEIAEIKDDIENMPLGYQTELSE---EGSSISGGQKQRIALARALLTDSKVLILD 636
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105575177 433 EPTAALDPKTEAYVFEKFRELTEnKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYNMY 503
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
265-487 |
1.27e-46 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 162.29 E-value: 1.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYS--LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY- 341
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 --VSVVFQDFVRY---ALSVKENIA--LSDISQIDNLNEIKQTAFL-----SGADSFIEALPNgydttlgkvlpnsiDIS 409
Cdd:cd03257 82 keIQMVFQDPMSSlnpRMTIGEQIAepLRIHGKLSKKEARKEAVLLllvgvGLPEEVLNRYPH--------------ELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 410 GGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASVK-MADRIIHLKDGQILEE 486
Cdd:cd03257 148 GGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAkIADRVAVMYAGKIVEE 227
|
.
gi 2105575177 487 G 487
Cdd:cd03257 228 G 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
265-494 |
3.74e-46 |
|
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: 161.30 E-value: 3.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplsNGYS-LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY-- 341
Cdd:COG1127 6 IEVRNLTKSF---GDRVvLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 -VSVVFQDfvrYAL----SVKENIAL-----SDISQidnlNEIKQTAflsgadsfiealpngyDTTLGKV-LPNSID--- 407
Cdd:COG1127 83 rIGMLFQG---GALfdslTVFENVAFplrehTDLSE----AEIRELV----------------LEKLELVgLPGAADkmp 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 408 --ISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASV-KMADRIIHLKDGQ 482
Cdd:COG1127 140 seLSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAfAIADRVAVLADGK 219
|
250
....*....|..
gi 2105575177 483 ILEEGSHKELMA 494
Cdd:COG1127 220 IIAEGTPEELLA 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
265-487 |
3.83e-46 |
|
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: 159.02 E-value: 3.83e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcQIDENELSEYVSV 344
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-SDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 vfqdfvryalsvkenialsdisqidnlneIKQTAFLsgadsfiealpngYDTTLGKVLpnSIDISGGQWQRIALARSIFK 424
Cdd:cd03247 80 -----------------------------LNQRPYL-------------FDTTLRNNL--GRRFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 425 KSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEG 487
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
265-496 |
1.31e-45 |
|
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: 160.67 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCqIDEN--ELSEYV 342
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL-DEENlwEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 343 SVVFQD----FVryALSVKENIALSdisqIDNLN----EIKQ----TAFLSGADSFIEALPNgydttlgkvlpnsiDISG 410
Cdd:TIGR04520 80 GMVFQNpdnqFV--GATVEDDVAFG----LENLGvpreEMRKrvdeALKLVGMEDFRDREPH--------------LLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 411 GQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL--TENKTAIFISHRLASVKMADRIIHLKDGQILEEGS 488
Cdd:TIGR04520 140 GQKQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLnkEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGT 219
|
....*...
gi 2105575177 489 HKELMALK 496
Cdd:TIGR04520 220 PREIFSQV 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
265-494 |
4.23e-45 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 165.85 E-value: 4.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYS---LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY 341
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGvraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 ---VSVVFQD-----FVRyaLSVKENIALS-DISQIDNLNEIKQTAflsgadsfiealpngyDTTLGKV-LPNSI----- 406
Cdd:COG1123 341 rrrVQMVFQDpysslNPR--MTVGDIIAEPlRLHGLLSRAERRERV----------------AELLERVgLPPDLadryp 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 407 -DISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASVK-MADRIIHLKDGQ 482
Cdd:COG1123 403 hELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRyIADRVAVMYDGR 482
|
250
....*....|..
gi 2105575177 483 ILEEGSHKELMA 494
Cdd:COG1123 483 IVEDGPTEEVFA 494
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
265-506 |
1.66e-44 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 165.66 E-value: 1.66e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYpLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:PRK10790 341 IDIDNVSFAY-RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYALSVKENIALS-DIS--QIDNLNEIKQTAflsgadSFIEALPNGYDTTLGKVLPNsidISGGQWQRIALARS 421
Cdd:PRK10790 420 VQQDPVVLADTFLANVTLGrDISeeQVWQALETVQLA------ELARSLPDGLYTPLGEQGNN---LSVGQKQLLALARV 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 422 IFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYN 501
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQ 570
|
....*
gi 2105575177 502 MYMTQ 506
Cdd:PRK10790 571 MYQLQ 575
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
264-488 |
2.17e-44 |
|
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: 156.11 E-value: 2.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 264 NISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVS 343
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 344 VVFQDFVRYALSVKENIalsdisqiDNLN-----EIKQTAFLSGADSFIEALPNGYDTtlgKVLPNSIDISGGQWQRIAL 418
Cdd:cd03244 82 IIPQDPVLFSGTIRSNL--------DPFGeysdeELWQALERVGLKEFVESLPGGLDT---VVEEGGENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 419 ARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGS 488
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
285-503 |
4.80e-44 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 164.25 E-value: 4.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 285 INLEIKDKEKVAIVGHNGSGKTTLIQLIIGlYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENIALSD 364
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 365 ISQIDNlnEIKQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEA 444
Cdd:PRK11174 448 PDASDE--QLQQALENAWVSEFLPLLPQGLDTPIGD---QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 445 YVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYNMY 503
Cdd:PRK11174 523 LVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLL 581
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
265-483 |
1.52e-43 |
|
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: 153.78 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPL-SNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVS 343
Cdd:cd03248 12 VKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 344 VVFQDFVRYALSVKENIA--LSDISqidnLNEIKQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARS 421
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAygLQSCS----FECVKEAAQKAHAHSFISELASGYDTEVGE---KGSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2105575177 422 IFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQI 483
Cdd:cd03248 165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
265-494 |
3.24e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 150.60 E-value: 3.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQiDENELSEYVSV 344
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYA-LSVKENIALsdisqIDNLNEIKQTAFLSGADSFIEA--LPNGYDTTLGKvlpnsidISGGQWQRIALARS 421
Cdd:COG1131 78 VPQEPALYPdLTVRENLRF-----FARLYGLPRKEARERIDELLELfgLTDAADRKVGT-------LSGGMKQRLGLALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 422 IFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFIS-HRLASV-KMADRIIHLKDGQILEEGSHKELMA 494
Cdd:COG1131 146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
265-494 |
3.89e-42 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 150.34 E-value: 3.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY--- 341
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLrrr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 VSVVFQD---FVryALSVKENIA--------LSDiSQIDNLNEIKQTAF-LSGADsfiEALPngydttlgkvlpnsIDIS 409
Cdd:cd03261 79 MGMLFQSgalFD--SLTVFENVAfplrehtrLSE-EEIREIVLEKLEAVgLRGAE---DLYP--------------AELS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 410 GGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASV-KMADRIIHLKDGQILEE 486
Cdd:cd03261 139 GGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAE 218
|
....*...
gi 2105575177 487 GSHKELMA 494
Cdd:cd03261 219 GTPEELRA 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
265-483 |
6.04e-42 |
|
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: 147.75 E-value: 6.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYALSVKENIalsdisqidnlneikqtaflsgadsfiealpngydttlgkvlpnsidISGGQWQRIALARSIFK 424
Cdd:cd03246 81 LPQDDELFSGSIAENI-----------------------------------------------LSGGQRQRLGLARALYG 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 425 KSKLIILDEPTAALDPKTEAYVFEKFRELTE-NKTAIFISHRLASVKMADRIIHLKDGQI 483
Cdd:cd03246 114 NPRILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
265-491 |
6.70e-42 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 149.43 E-value: 6.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlsNGYS-LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY-- 341
Cdd:COG2884 2 IRFENVSKRYP--GGREaLSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 -VSVVFQDFvR--YALSVKENIALS-DISQIDNlNEIKQTAF-------LSG-ADSFIEALpngydttlgkvlpnsidiS 409
Cdd:COG2884 80 rIGVVFQDF-RllPDRTVYENVALPlRVTGKSR-KEIRRRVRevldlvgLSDkAKALPHEL------------------S 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 410 GGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFI-SHRLASV-KMADRIIHLKDGQILEEG 487
Cdd:COG2884 140 GGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIaTHDLELVdRMPKRVLELEDGRLVRDE 219
|
....
gi 2105575177 488 SHKE 491
Cdd:COG2884 220 ARGV 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
265-494 |
1.41e-41 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 155.83 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTA---GNIFLEGKDLCQIDENELSEY 341
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 VSVVFQDFVRY--ALSVKENIALSDISQIDNLNEIKQTAFLSGADSFIEALPNGYDTTLgkvlpnsidiSGGQWQRIALA 419
Cdd:COG1123 85 IGMVFQDPMTQlnPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQL----------SGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 420 RSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKELMA 494
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
265-483 |
2.02e-41 |
|
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: 146.39 E-value: 2.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlsNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcQIDENELSEYVSV 344
Cdd:cd03230 1 IEVRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYA-LSVKENIALSdisqidnlneikqtaflsgadsfiealpngydttlgkvlpnsidisGGQWQRIALARSIF 423
Cdd:cd03230 78 LPEEPSLYEnLTVRENLKLS----------------------------------------------GGMKQRLALAQALL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2105575177 424 KKSKLIILDEPTAALDPKTEAYVFEKFRELT-ENKTAIFISHRLASV-KMADRIIHLKDGQI 483
Cdd:cd03230 112 HDPELLILDEPTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
265-493 |
6.53e-41 |
|
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: 147.50 E-value: 6.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlsNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:COG1120 2 LEAENLSVGYG--GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDF-VRYALSVKENIAL--------------SDISQIDNLneIKQTaflsGADSFIEALpngYDTtlgkvlpnsidIS 409
Cdd:COG1120 80 VPQEPpAPFGLTVRELVALgryphlglfgrpsaEDREAVEEA--LERT----GLEHLADRP---VDE-----------LS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 410 GGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELT--ENKTAIFISH--RLASvKMADRIIHLKDGQILE 485
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAreRGRTVVMVLHdlNLAA-RYADRLVLLKDGRIVA 218
|
....*...
gi 2105575177 486 EGSHKELM 493
Cdd:COG1120 219 QGPPEEVL 226
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
266-487 |
1.44e-40 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 144.50 E-value: 1.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 266 SLKHVYFKYPlsNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVV 345
Cdd:cd03214 1 EVENLSVGYG--GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 346 FQdfvryalsvkeniALSDIsQIDNLneikqtaflsgADSFIEALpngydttlgkvlpnsidiSGGQWQRIALARSIFKK 425
Cdd:cd03214 79 PQ-------------ALELL-GLAHL-----------ADRPFNEL------------------SGGERQRVLLARALAQE 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2105575177 426 SKLIILDEPTAALDPKTEAYVFEKFRELT--ENKTAIFISH--RLASvKMADRIIHLKDGQILEEG 487
Cdd:cd03214 116 PPILLLDEPTSHLDIAHQIELLELLRRLAreRGKTVVMVLHdlNLAA-RYADRVILLKDGRIVAQG 180
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
266-482 |
6.63e-40 |
|
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: 141.61 E-value: 6.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 266 SLKHVYFKYPlsNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVV 345
Cdd:cd00267 1 EIENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 346 FQdfvryalsvkenialsdisqidnlneikqtaflsgadsfiealpngydttlgkvlpnsidISGGQWQRIALARSIFKK 425
Cdd:cd00267 79 PQ------------------------------------------------------------LSGGQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 426 SKLIILDEPTAALDPKTEAYVFEKFRELT-ENKTAIFISHRLASVKMA-DRIIHLKDGQ 482
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
265-492 |
6.79e-40 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 145.67 E-value: 6.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKY----PLSNgYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSE 340
Cdd:TIGR04521 1 IKLKNVSYIYqpgtPFEK-KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 341 Y---VSVVFQdFVRYAL---SVKENIA-------LSDisqidnlNEIKQTAFlsgadsfiEALPN-GYDTTLGKVLPnsI 406
Cdd:TIGR04521 80 LrkkVGLVFQ-FPEHQLfeeTVYKDIAfgpknlgLSE-------EEAEERVK--------EALELvGLDEEYLERSP--F 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 407 DISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL--TENKTAIFISHRLASV-KMADRIIHLKDGQI 483
Cdd:TIGR04521 142 ELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLhkEKGLTVILVTHSMEDVaEYADRVIVMHKGKI 221
|
....*....
gi 2105575177 484 LEEGSHKEL 492
Cdd:TIGR04521 222 VLDGTPREV 230
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
265-495 |
1.08e-39 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 145.16 E-value: 1.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQ------------DFVRYALsvkENIALSDISQIDNLNE-IKQTaflsGADSFIEALPNgydttlgkvlpnsiDISGG 411
Cdd:PRK13635 86 VFQnpdnqfvgatvqDDVAFGL---ENIGVPREEMVERVDQaLRQV----GMEDFLNREPH--------------RLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 412 QWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASVKMADRIIHLKDGQILEEGSH 489
Cdd:PRK13635 145 QKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTP 224
|
....*.
gi 2105575177 490 KELMAL 495
Cdd:PRK13635 225 EEIFKS 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
282-436 |
3.10e-38 |
|
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: 137.01 E-value: 3.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQD-FVRYALSVKENI 360
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDpQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 361 ALSDISQidnlnEIKQTAFLSGADSFIEALPNGY--DTTLGKvlpNSIDISGGQWQRIALARSIFKKSKLIILDEPTA 436
Cdd:pfam00005 81 RLGLLLK-----GLSKREKDARAEEALEKLGLGDlaDRPVGE---RPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
258-496 |
4.53e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 140.51 E-value: 4.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 258 NKSDTANISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE 337
Cdd:PRK13632 1 IKNKSVMIKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 338 LSEYVSVVFQD----FVryALSVKENIALSDISQIDNLNEIKQ----TAFLSGADSFIEALPNgydttlgkvlpnsiDIS 409
Cdd:PRK13632 81 IRKKIGIIFQNpdnqFI--GATVEDDIAFGLENKKVPPKKMKDiiddLAKKVGMEDYLDKEPQ--------------NLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 410 GGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL--TENKTAIFISHRLASVKMADRIIHLKDGQILEEG 487
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLrkTRKKTLISITHDMDEAILADKVIVFSEGKLIAQG 224
|
....*....
gi 2105575177 488 SHKELMALK 496
Cdd:PRK13632 225 KPKEILNNK 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
265-482 |
7.59e-38 |
|
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: 136.93 E-value: 7.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlsNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDEN--ELSEYV 342
Cdd:cd03229 1 LELKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 343 SVVFQDFVRYA-LSVKENIALSdisqidnlneikqtaflsgadsfiealpngydttlgkvlpnsidISGGQWQRIALARS 421
Cdd:cd03229 79 GMVFQDFALFPhLTVLENIALG--------------------------------------------LSGGQQQRVALARA 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 422 IFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN--KTAIFISHRLASV-KMADRIIHLKDGQ 482
Cdd:cd03229 115 LAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAaRLADRVVVLRDGK 178
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
265-487 |
2.08e-37 |
|
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: 136.88 E-value: 2.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlsNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSeyVSV 344
Cdd:cd03259 1 LELKGLSKTYG--SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN--IGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYA-LSVKENIAL------SDISQIDNlnEIKQTAFLSGADSFIEALPNGydttlgkvlpnsidISGGQWQRIA 417
Cdd:cd03259 77 VFQDYALFPhLTVAENIAFglklrgVPKAEIRA--RVRELLELVGLEGLLNRYPHE--------------LSGGQQQRVA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 418 LARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN--KTAIFISHRLA-SVKMADRIIHLKDGQILEEG 487
Cdd:cd03259 141 LARALAREPSLLLLDEPLSALDAKLREELREELKELQRElgITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
265-494 |
2.53e-37 |
|
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: 137.63 E-value: 2.53e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNG--YSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYV 342
Cdd:COG1124 2 LEVRNLSVSYGQGGRrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 343 SVVFQDFvrYA-----LSVKEniALSDISQIDNLNEIKQTaflsgadsfIEALpngydttLGKV-LPNSI------DISG 410
Cdd:COG1124 82 QMVFQDP--YAslhprHTVDR--ILAEPLRIHGLPDREER---------IAEL-------LEQVgLPPSFldryphQLSG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 411 GQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASV-KMADRIIHLKDGQILEEG 487
Cdd:COG1124 142 GQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEEL 221
|
....*..
gi 2105575177 488 SHKELMA 494
Cdd:COG1124 222 TVADLLA 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
265-492 |
2.92e-37 |
|
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: 136.93 E-value: 2.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYK-----PTAGNIFLEGKDLCQIDEN--E 337
Cdd:cd03260 1 IELRDLNVYY--GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 338 LSEYVSVVFQDFVRYALSVKENIA----LSDISQIDNLNEIKQTAfLSGAdsfieALP-NGYDTTLGKVLpnsidiSGGQ 412
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVAyglrLHGIKLKEELDERVEEA-LRKA-----ALWdEVKDRLHALGL------SGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 413 WQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVK-MADRIIHLKDGQILEEGSHKE 491
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 2105575177 492 L 492
Cdd:cd03260 227 I 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
265-483 |
5.70e-37 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 135.71 E-value: 5.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:COG4619 1 LELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYALSVKENIALSDISQIDNLNEIKQTAFLSgadsfiealpngydtTLGkvLPNSI------DISGGQWQRIAL 418
Cdd:COG4619 79 VPQEPALWGGTVRDNLPFPFQLRERKFDRERALELLE---------------RLG--LPPDIldkpveRLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 419 ARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL--TENKTAIFISHRLASVK-MADRIIHLKDGQI 483
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIErVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
267-491 |
1.28e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 137.10 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 267 LKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLC--QIDENELSEYVSV 344
Cdd:PRK13637 8 LTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQdFVRYAL---SVKENIALS----DISQIDNLNEIKQTAFLSGADsfiealpngYDTTLGKvlpNSIDISGGQWQRIA 417
Cdd:PRK13637 88 VFQ-YPEYQLfeeTIEKDIAFGpinlGLSEEEIENRVKRAMNIVGLD---------YEDYKDK---SPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 418 LARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKE 491
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
260-466 |
2.57e-36 |
|
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: 141.34 E-value: 2.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 260 SDTANISLKHVYFKYPLSNGySLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELS 339
Cdd:TIGR02868 330 LGKPTLELRDLSAGYPGAPP-VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 340 EYVSVVFQDFVRYALSVKENIALSDISQIDnlNEIKQTAFLSGADSFIEALPNGYDTTLGkvlPNSIDISGGQWQRIALA 419
Cdd:TIGR02868 409 RRVSVCAQDAHLFDTTVRENLRLARPDATD--EELWAALERVGLADWLRALPDGLDTVLG---EGGARLSGGERQRLALA 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2105575177 420 RSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRL 466
Cdd:TIGR02868 484 RALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
265-482 |
4.81e-36 |
|
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: 132.98 E-value: 4.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYS---LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKdlcqidenelsey 341
Cdd:cd03250 1 ISVEDASFTWDSGEQETsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 VSVVFQD-FVRYAlSVKENIALSdiSQIDN--LNE-IKQTAFLsgADsfIEALPNGYDTTLGKvlpNSIDISGGQWQRIA 417
Cdd:cd03250 68 IAYVSQEpWIQNG-TIRENILFG--KPFDEerYEKvIKACALE--PD--LEILPDGDLTEIGE---KGINLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 418 LARSIFKKSKLIILDEPTAALDPKTEAYVFEK--FRELTENKTAIFISHRLASVKMADRIIHLKDGQ 482
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
265-483 |
5.57e-36 |
|
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: 133.04 E-value: 5.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQ--IDENELSEYV 342
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 343 SVVFQDFVRYA-LSVKENIALsdiSQIDNLNEIKQtaflsgadsfiEALPNGYDtTLGKV-LPNSID-----ISGGQWQR 415
Cdd:cd03262 79 GMVFQQFNLFPhLTVLENITL---APIKVKGMSKA-----------EAEERALE-LLEKVgLADKADaypaqLSGGQQQR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 416 IALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELT-ENKTAIFISHRLA-SVKMADRIIHLKDGQI 483
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAeEGMTMVVVTHEMGfAREVADRVIFMDDGRI 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
265-486 |
1.06e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 133.68 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYS--LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcqideNELSEYV 342
Cdd:COG1116 8 LELRGVSKRFPTGGGGVtaLDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV-----TGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 343 SVVFQDfvrYAL----SVKENIALS-DISQIDNlNEIKQTA--FLS--GADSFIEALPNgydttlgkvlpnsiDISGGQW 413
Cdd:COG1116 83 GVVFQE---PALlpwlTVLDNVALGlELRGVPK-AERRERAreLLElvGLAGFEDAYPH--------------QLSGGMR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 414 QRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL--TENKTAIFISHRLA-SVKMADRIIHLKD--GQILEE 486
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDeAVFLADRVVVLSArpGRIVEE 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
265-498 |
1.08e-35 |
|
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: 133.06 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcQIDENELSEYVSV 344
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-RKEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYA-LSVKENIALsdisqIDNLNEIKQTAFLSGADSFIEA--LPNGYDTTLGKvlpnsidISGGQWQRIALARS 421
Cdd:COG4555 79 LPDERGLYDrLTVRENIRY-----FAELYGLFDEELKKRIEELIELlgLEEFLDRRVGE-------LSTGMKKKVALARA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 422 IFKKSKLIILDEPTAALDPKTEAYVFEKFREL-TENKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKELMALKGE 498
Cdd:COG4555 147 LVHDPKVLLLDEPTNGLDVMARRLLREILRALkKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
265-487 |
2.60e-35 |
|
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: 131.22 E-value: 2.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlsNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSeyVSV 344
Cdd:cd03301 1 VELENVTKRFG--NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD--IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYA-LSVKENIAL---SDISQIDNLNE-IKQTAFLSGadsfIEALPNGYDTTLgkvlpnsidiSGGQWQRIALA 419
Cdd:cd03301 77 VFQNYALYPhMTVYDNIAFglkLRKVPKDEIDErVREVAELLQ----IEHLLDRKPKQL----------SGGQRQRVALG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105575177 420 RSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN--KTAIFISH-RLASVKMADRIIHLKDGQILEEG 487
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlgTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
272-506 |
2.91e-35 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 139.08 E-value: 2.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 272 FKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVR 351
Cdd:PRK10789 321 FTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 352 YALSVKENIALS--DISQidnlNEIKQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFKKSKLI 429
Cdd:PRK10789 401 FSDTVANNIALGrpDATQ----QEIEHVARLASVHDDILRLPQGYDTEVGE---RGVMLSGGQKQRISIARALLLNAEIL 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 430 ILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYNMYMTQ 506
Cdd:PRK10789 474 ILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQ 550
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
265-494 |
1.28e-34 |
|
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: 130.01 E-value: 1.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNG--YSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY- 341
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 --VSVVFQDF-VRYALSVKENIALSdiSQIDNL--NEIKQTAF----LSGADSFIEALPNgydttlgkvlpnsiDISGGQ 412
Cdd:cd03258 82 rrIGMIFQHFnLLSSRTVFENVALP--LEIAGVpkAEIEERVLelleLVGLEDKADAYPA--------------QLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 413 WQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASVK-MADRIIHLKDGQILEEGSH 489
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKrICDRVAVMEKGEVVEEGTV 225
|
....*
gi 2105575177 490 KELMA 494
Cdd:cd03258 226 EEVFA 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
265-483 |
1.36e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.21 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKY---PLsngysLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQiDENELSeY 341
Cdd:COG1121 7 IELENLTVSYggrPV-----LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-ARRRIG-Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 V---SVVFQDFvryALSVKENIAL--------------SDISQIDNLneIKQTaflsGADSFIealpngyDTTLGkvlpn 404
Cdd:COG1121 80 VpqrAEVDWDF---PITVRDVVLMgrygrrglfrrpsrADREAVDEA--LERV----GLEDLA-------DRPIG----- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 405 siDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELT-ENKTAIFISHRLASV-KMADRIIHLKDGQ 482
Cdd:COG1121 139 --ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVrEYFDRVLLLNRGL 216
|
.
gi 2105575177 483 I 483
Cdd:COG1121 217 V 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
265-486 |
1.85e-34 |
|
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: 129.13 E-value: 1.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGY--SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENelseyV 342
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 343 SVVFQDfvrYAL----SVKENIALSDISQIDNLNEIKQTA--FLS--GADSFIEALPNgydttlgkvlpnsiDISGGQWQ 414
Cdd:cd03293 76 GYVFQQ---DALlpwlTVLDNVALGLELQGVPKAEARERAeeLLElvGLSGFENAYPH--------------QLSGGMRQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 415 RIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL--TENKTAIFISHRLA-SVKMADRIIHL--KDGQILEE 486
Cdd:cd03293 139 RVALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIwrETGKTVLLVTHDIDeAVFLADRVVVLsaRPGRIVAE 215
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
265-492 |
2.07e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 132.53 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcqideNELSEY--- 341
Cdd:COG3842 6 LELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-----TGLPPEkrn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 VSVVFQDfvrYAL----SVKENIA--LsdisQIDNLN--EIKQTAFlsgadsfiEALpngyD----TTLGKVLPNsiDIS 409
Cdd:COG3842 79 VGMVFQD---YALfphlTVAENVAfgL----RMRGVPkaEIRARVA--------ELL----ElvglEGLADRYPH--QLS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 410 GGQWQRIALARSIFKKSKLIILDEPTAALDPK----TEAYVFEKFRELteNKTAIFISHR----LAsvkMADRIIHLKDG 481
Cdd:COG3842 138 GGQQQRVALARALAPEPRVLLLDEPLSALDAKlreeMREELRRLQREL--GITFIYVTHDqeeaLA---LADRIAVMNDG 212
|
250
....*....|.
gi 2105575177 482 QILEEGSHKEL 492
Cdd:COG3842 213 RIEQVGTPEEI 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
282-483 |
2.41e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 130.21 E-value: 2.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVR---YALSVKE 358
Cdd:COG1101 22 LDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKYIGRVFQDPMMgtaPSMTIEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 359 NIALsdisqidnlneikqtAFLSGA-------------DSFIEALpngydTTLGKVLPNSIDI-----SGGQWQRIALAR 420
Cdd:COG1101 102 NLAL---------------AYRRGKrrglrrgltkkrrELFRELL-----ATLGLGLENRLDTkvgllSGGQRQALSLLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2105575177 421 SIFKKSKLIILDEPTAALDPKTEAYVFEKFREL-TENK-TAIFISHRLA-SVKMADRIIHLKDGQI 483
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNlTTLMVTHNMEqALDYGNRLIMMHEGRI 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
282-494 |
3.10e-34 |
|
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: 130.07 E-value: 3.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSE----YVSVVFQDFvryAL--- 354
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSF---ALlph 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 -SVKENIALSDISQIDNLNEIKQTAflsgadsfIEALPN----GYdttlGKVLPNsiDISGGQWQRIALARSIFKKSKLI 429
Cdd:cd03294 117 rTVLENVAFGLEVQGVPRAEREERA--------AEALELvgleGW----EHKYPD--ELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 430 ILDEPTAALDPKTEAYVFEKFRELTEN--KTAIFISHRLA-SVKMADRIIHLKDGQILEEGSHKELMA 494
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAElqKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
263-492 |
8.43e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 130.96 E-value: 8.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 263 ANISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcqideNELSEY- 341
Cdd:COG3839 2 ASLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-----TDLPPKd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 --VSVVFQDfvrYAL----SVKENIALS------DISQIDNlnEIKQTAFLSGadsfIEALpngydttLGKvLPNsiDIS 409
Cdd:COG3839 75 rnIAMVFQS---YALyphmTVYENIAFPlklrkvPKAEIDR--RVREAAELLG----LEDL-------LDR-KPK--QLS 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 410 GGQWQRIALARSIFKKSKLIILDEPTAALDPK----TEAYVFEKFRELteNKTAIFISHR----LAsvkMADRIIHLKDG 481
Cdd:COG3839 136 GGQRQRVALGRALVREPKVFLLDEPLSNLDAKlrveMRAEIKRLHRRL--GTTTIYVTHDqveaMT---LADRIAVMNDG 210
|
250
....*....|.
gi 2105575177 482 QILEEGSHKEL 492
Cdd:COG3839 211 RIQQVGTPEEL 221
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
269-494 |
1.20e-33 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 129.79 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 269 HVYFkyPLSNGY--SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKP---TAGNIFLEGKDLCQIDENELSEY-- 341
Cdd:COG0444 8 KVYF--PTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKELRKIrg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 --VSVVFQDfvryALS-------VKENIALS-DISQIDNLNEIKQTAflsgadsfIEALpngydttlGKV-LPNSIDI-- 408
Cdd:COG0444 86 reIQMIFQD----PMTslnpvmtVGDQIAEPlRIHGGLSKAEARERA--------IELL--------ERVgLPDPERRld 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 409 ------SGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASVK-MADRIIHLK 479
Cdd:COG0444 146 ryphelSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVAeIADRVAVMY 225
|
250
....*....|....*
gi 2105575177 480 DGQILEEGSHKELMA 494
Cdd:COG0444 226 AGRIVEEGPVEELFE 240
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
266-479 |
1.38e-33 |
|
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: 126.49 E-value: 1.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 266 SLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcqIDENELSEYVSVV 345
Cdd:cd03235 1 EVEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--EKERKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 346 FQDFVRYALSVKENIALSDISQIDNLNEIKQtaflSGADSFIEALpngyDTT-LGKVLPNSID-ISGGQWQRIALARSIF 423
Cdd:cd03235 77 RSIDRDFPISVRDVVLMGLYGHKGLFRRLSK----ADKAKVDEAL----ERVgLSELADRQIGeLSGGQQQRVLLARALV 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 424 KKSKLIILDEPTAALDPKTEAYVFEKFRELT-ENKTAIFISHRLASV-KMADRIIHLK 479
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRrEGMTILVVTHDLGLVlEYFDRVLLLN 206
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
265-492 |
1.71e-33 |
|
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: 127.30 E-value: 1.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY--- 341
Cdd:cd03256 1 IEVENLSKTYP-NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 VSVVFQDF---VRyaLSVKENI---ALSDISQIDNL-----NEIKQTAFlsgadsfiEALpngydTTLG---KVLPNSID 407
Cdd:cd03256 80 IGMIFQQFnliER--LSVLENVlsgRLGRRSTWRSLfglfpKEEKQRAL--------AAL-----ERVGlldKAYQRADQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 408 ISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL--TENKTAIFISHRL-ASVKMADRIIHLKDGQIL 484
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVdLAREYADRIVGLKDGRIV 224
|
....*...
gi 2105575177 485 EEGSHKEL 492
Cdd:cd03256 225 FDGPPAEL 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
265-494 |
2.84e-33 |
|
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: 126.65 E-value: 2.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYA-LSVKENIALsdisqIDNLNEIKQTAFLSGADSFIE--ALPngyDTTLGKVLPNsiDISGGQWQRIALARS 421
Cdd:cd03295 80 VIQQIGLFPhMTVEENIAL-----VPKLLKWPKEKIRERADELLAlvGLD---PAEFADRYPH--ELSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2105575177 422 IFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRL-ASVKMADRIIHLKDGQILEEGSHKELMA 494
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
281-492 |
1.35e-32 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 124.72 E-value: 1.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 281 SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY---VSVVFQDFVRYA-LSV 356
Cdd:TIGR02315 17 ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKLrrrIGMIFQHYNLIErLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 KENIALSDISQIDNLNEIKQtaFLSGADSfIEALPNgydttLGKV------LPNSIDISGGQWQRIALARSIFKKSKLII 430
Cdd:TIGR02315 97 LENVLHGRLGYKPTWRSLLG--RFSEEDK-ERALSA-----LERVgladkaYQRADQLSGGQQQRVAIARALAQQPDLIL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 431 LDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASVK-MADRIIHLKDGQILEEGSHKEL 492
Cdd:TIGR02315 169 ADEPIASLDPKTSKQVMDYLKRINKEDgiTVIINLHQVDLAKkYADRIVGLKAGEIVFDGAPSEL 233
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
265-483 |
1.91e-32 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 124.40 E-value: 1.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlsNGYS-LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY-- 341
Cdd:COG3638 3 LELRNLSKRYP--GGTPaLDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLrr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 -VSVVFQDF--V-RyaLSVKENI---ALSDISQIDNL-----NEIKQTAFlsgadsfiEALpngydTTLGkvLPNSID-- 407
Cdd:COG3638 81 rIGMIFQQFnlVpR--LSVLTNVlagRLGRTSTWRSLlglfpPEDRERAL--------EAL-----ERVG--LADKAYqr 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 408 ---ISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL--TENKTAIFISHRLASVKM-ADRIIHLKDG 481
Cdd:COG3638 144 adqLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIarEDGITVVVNLHQVDLARRyADRIIGLRDG 223
|
..
gi 2105575177 482 QI 483
Cdd:COG3638 224 RV 225
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
280-491 |
2.23e-32 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 123.99 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 280 YSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENElsEYVSVVFQDFVRYA-LSVKE 358
Cdd:cd03299 13 FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK--RDISYVPQNYALFPhMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 359 NIA------LSDISQIDnlNEIKQTAFLSGadsfIEALPNGYDTTLgkvlpnsidiSGGQWQRIALARSIFKKSKLIILD 432
Cdd:cd03299 91 NIAyglkkrKVDKKEIE--RKVLEIAEMLG----IDHLLNRKPETL----------SGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2105575177 433 EPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASVK-MADRIIHLKDGQILEEGSHKE 491
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEFgvTVLHVTHDFEEAWaLADKVAIMLNGKLIQVGKPEE 216
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
265-483 |
2.72e-32 |
|
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: 121.38 E-value: 2.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlsNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE-LSEYVS 343
Cdd:cd03216 1 LELRGITKRFG--GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 344 VVFQdfvryalsvkenialsdisqidnlneikqtaflsgadsfiealpngydttlgkvlpnsidISGGQWQRIALARSIF 423
Cdd:cd03216 79 MVYQ------------------------------------------------------------LSVGERQMVEIARALA 98
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2105575177 424 KKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTA-IFISHRLASV-KMADRIIHLKDGQI 483
Cdd:cd03216 99 RNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAvIFISHRLDEVfEIADRVTVLRDGRV 160
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
266-483 |
2.77e-32 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 122.75 E-value: 2.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 266 SLKHVYFKYPlSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSvv 345
Cdd:cd03226 1 RIENISFSYK-KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSIGYVM-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 346 fQDfVRYAL---SVKENIALSDiSQIDNLNEIKQTAF-LSGADSFIEALPngydttlgkvlpnsIDISGGQWQRIALARS 421
Cdd:cd03226 78 -QD-VDYQLftdSVREELLLGL-KELDAGNEQAETVLkDLDLYALKERHP--------------LSLSGGQKQRLAIAAA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 422 IFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIF-ISH--RLASvKMADRIIHLKDGQI 483
Cdd:cd03226 141 LLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIvITHdyEFLA-KVCDRVLLLANGAI 204
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
282-492 |
4.33e-32 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 123.18 E-value: 4.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLC--QIDENELSEYVSVVFQDFVRYA-LSVKE 358
Cdd:COG1126 17 LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdsKKDINKLRRKVGMVFQQFNLFPhLTVLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 359 NIALSDIsQIDNLN--EIKQTAflsgadsfiEALpngydttLGKV-LPNSID-----ISGGQWQRIALARSIFKKSKLII 430
Cdd:COG1126 97 NVTLAPI-KVKKMSkaEAEERA---------MEL-------LERVgLADKADaypaqLSGGQQQRVAIARALAMEPKVML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 431 LDEPTAALDPKTEAYVFEKFREL-TENKTAIFISH--RLASvKMADRIIHLKDGQILEEGSHKEL 492
Cdd:COG1126 160 FDEPTSALDPELVGEVLDVMRDLaKEGMTMVVVTHemGFAR-EVADRVVFMDGGRIVEEGPPEEF 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
282-492 |
5.15e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 128.60 E-value: 5.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE-LSEYVSVVFQDF--VRYaLSVKE 358
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAIIHQELnlVPN-LSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 359 NIALSdisqidnlNEIKQTAFLSGADSFIEAL-----------PngyDTTLGkvlpnsiDISGGQWQRIALARSIFKKSK 427
Cdd:COG1129 99 NIFLG--------REPRRGGLIDWRAMRRRARellarlgldidP---DTPVG-------DLSVAQQQLVEIARALSRDAR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 428 LIILDEPTAALDPKTEAYVFEKFRELTENKTAI-FISHRLASVK-MADRIIHLKDGQILEEGSHKEL 492
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIiYISHRLDEVFeIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
265-483 |
5.20e-32 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 122.13 E-value: 5.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlsNGY-SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE---LSE 340
Cdd:cd03292 1 IEFINVTKTYP--NGTaALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 341 YVSVVFQDF-VRYALSVKENIALS----DISQIDNLNEIKQTAFLSGADSFIEALPNGydttlgkvlpnsidISGGQWQR 415
Cdd:cd03292 79 KIGVVFQDFrLLPDRNVYENVAFAlevtGVPPREIRKRVPAALELVGLSHKHRALPAE--------------LSGGEQQR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 416 IALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASV--KMADRIIHLKDGQI 483
Cdd:cd03292 145 VAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELvdTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
265-498 |
9.51e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 123.30 E-value: 9.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKY-PLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVS 343
Cdd:PRK13650 5 IEVKNLTFKYkEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 344 VVFQD----FVryALSVKENIAL----SDISQIDNLNEIKQTAFLSGADSFIEALPNgydttlgkvlpnsiDISGGQWQR 415
Cdd:PRK13650 85 MVFQNpdnqFV--GATVEDDVAFglenKGIPHEEMKERVNEALELVGMQDFKEREPA--------------RLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 416 IALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELM 493
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELF 228
|
....*
gi 2105575177 494 ALKGE 498
Cdd:PRK13650 229 SRGND 233
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
281-492 |
4.94e-31 |
|
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: 120.14 E-value: 4.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 281 SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSeyVSVVFQdfvRYAL----SV 356
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN--VGFVFQ---HYALfrhmTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 KENIA----LSDISQIDNLNEIKQTAF----LSGADSFIEALPNgydttlgkvlpnsiDISGGQWQRIALARSIFKKSKL 428
Cdd:cd03296 92 FDNVAfglrVKPRSERPPEAEIRAKVHellkLVQLDWLADRYPA--------------QLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 429 IILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLA-SVKMADRIIHLKDGQILEEGSHKEL 492
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
265-492 |
9.63e-31 |
|
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: 119.26 E-value: 9.63e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENElsEYVSV 344
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK--RPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDfvrYAL----SVKENIA----LSDISQIDNLNEIKQTAFLSGADSFIEALPNgydttlgkvlpnsiDISGGQWQRI 416
Cdd:cd03300 77 VFQN---YALfphlTVFENIAfglrLKKLPKAEIKERVAEALDLVQLEGYANRKPS--------------QLSGGQQQRV 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 417 ALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN--KTAIFISHRLA-SVKMADRIIHLKDGQILEEGSHKEL 492
Cdd:cd03300 140 AIARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKElgITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
282-496 |
1.23e-30 |
|
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: 119.91 E-value: 1.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY---VSVVFQD---FVRYALS 355
Cdd:TIGR02769 27 LTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFrrdVQLVFQDspsAVNPRMT 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 356 VKENIAlsdiSQIDNLNEIKQTAFLSGADSFIEALpnGYDTTLGKVLPNsiDISGGQWQRIALARSIFKKSKLIILDEPT 435
Cdd:TIGR02769 107 VRQIIG----EPLRHLTSLDESEQKARIAELLDMV--GLRSEDADKLPR--QLSGGQLQRINIARALAVKPKLIVLDEAV 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 436 AALDPKTEAYVFEKFREL-TENKTA-IFISHRLASV-KMADRIIHLKDGQILEEGSHKELMALK 496
Cdd:TIGR02769 179 SNLDMVLQAVILELLRKLqQAFGTAyLFITHDLRLVqSFCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
282-486 |
7.58e-30 |
|
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: 116.76 E-value: 7.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENEL----SEYVSVVFQDF-VRYALSV 356
Cdd:COG4181 28 LKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlrARHVGFVFQSFqLLPTLTA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 KENIALsdisqidnlneikqTAFLSG-ADSFIEALpngydTTLGKV--------LPNSidISGGQWQRIALARSIFKKSK 427
Cdd:COG4181 108 LENVML--------------PLELAGrRDARARAR-----ALLERVglghrldhYPAQ--LSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105575177 428 LIILDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASVKMADRIIHLKDGQILEE 486
Cdd:COG4181 167 ILFADEPTGNLDAATGEQIIDLLFELNRERgtTLVLVTHDPALAARCDRVLRLRAGRLVED 227
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
265-492 |
1.21e-29 |
|
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: 115.68 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQiDENELSEYVSV 344
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRY-ALSVKENIAL---------SDISQIDNlNEIKQTAFLSGADSFIEALpngydttlgkvlpnsidiSGGQWQ 414
Cdd:cd03263 80 CPQFDALFdELTVREHLRFyarlkglpkSEIKEEVE-LLLRVLGLTDKANKRARTL------------------SGGMKR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 415 RIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKM-ADRIIHLKDGQILEEGSHKEL 492
Cdd:cd03263 141 KLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
256-508 |
1.49e-29 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 123.60 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 256 IANKSDT-ANISLKHVYFKY-PLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYK---------------- 317
Cdd:PTZ00265 1156 IKNKNDIkGKIEIMDVNFRYiSRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtnd 1235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 318 --------------------------------------PTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKEN 359
Cdd:PTZ00265 1236 mtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYEN 1315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 360 IALSdiSQIDNLNEIKQTAFLSGADSFIEALPNGYDTTLGkvlPNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALD 439
Cdd:PTZ00265 1316 IKFG--KEDATREDVKRACKFAAIDEFIESLPNKYDTNVG---PYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2105575177 440 PKTEAYVFEKFRELTE--NKTAIFISHRLASVKMADRIIHL----KDGQILE-EGSHKELMALKGEYYNMYMTQAK 508
Cdd:PTZ00265 1391 SNSEKLIEKTIVDIKDkaDKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSVQDGVYKKYVKLAK 1466
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
265-488 |
1.96e-29 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 118.26 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNG--YSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY- 341
Cdd:COG1135 2 IELENLSKTFPTKGGpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 --VSVVFQDFvryAL----SVKENIALS-DISQIDNlNEIKQTAF-------LSG-ADSFIEALpngydttlgkvlpnsi 406
Cdd:COG1135 82 rkIGMIFQHF---NLlssrTVAENVALPlEIAGVPK-AEIRKRVAellelvgLSDkADAYPSQL---------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 407 diSGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELteNK----TAIFISHRLASVK-MADRIIHLKDG 481
Cdd:COG1135 142 --SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDI--NRelglTIVLITHEMDVVRrICDRVAVLENG 217
|
....*..
gi 2105575177 482 QILEEGS 488
Cdd:COG1135 218 RIVEQGP 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
282-492 |
2.81e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 118.33 E-value: 2.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcQIDenelseyVSV-------VFQDfvrYAL 354
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTN-------LPPrerrvgfVFQH---YAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 ----SVKENIA--LSDISQidNLNEIKQTAF-------LSGadsfiealpngydttLGKVLPNsiDISGGQWQRIALARS 421
Cdd:COG1118 87 fphmTVAENIAfgLRVRPP--SKAEIRARVEellelvqLEG---------------LADRYPS--QLSGGQRQRVALARA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 422 IFKKSKLIILDEPTAALDpkteAYVFEKFR-ELTE-----NKTAIFISH------RLasvkmADRIIHLKDGQILEEGSH 489
Cdd:COG1118 148 LAVEPEVLLLDEPFGALD----AKVRKELRrWLRRlhdelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTP 218
|
...
gi 2105575177 490 KEL 492
Cdd:COG1118 219 DEV 221
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
282-494 |
3.98e-29 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 120.56 E-value: 3.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYkPTAGNIFLEGKDLCQIDENELSEY---VSVVFQDfvRYA----- 353
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLrrrMQVVFQD--PFGslspr 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 354 LSVKENIA--LsDISQID-NLNEIKQTAflsgadsfIEALPN-GYDttlgkvlPNSID-----ISGGQWQRIALARSIFK 424
Cdd:COG4172 379 MTVGQIIAegL-RVHGPGlSAAERRARV--------AEALEEvGLD-------PAARHrypheFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 425 KSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASVK-MADRIIHLKDGQILEEGSHKELMA 494
Cdd:COG4172 443 EPKLLVLDEPTSALDVSVQAQILDLLRDLQRehGLAYLFISHDLAVVRaLAHRVMVMKDGKVVEQGPTEQVFD 515
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
282-488 |
1.06e-28 |
|
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: 112.89 E-value: 1.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENIa 361
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 362 lsdisqiDNLNEIKQtaflsgaDSFIEALpngydttlgKVLPNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPK 441
Cdd:cd03369 103 -------DPFDEYSD-------EEIYGAL---------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2105575177 442 TEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGS 488
Cdd:cd03369 160 TDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
282-485 |
1.30e-28 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 113.33 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKdlcQIDENELSEYVsvVFQDfvrYAL----SVK 357
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK---QITEPGPDRMV--VFQN---YSLlpwlTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENIALSDISQIDNLNEIKQTAFLsgaDSFIE--ALPNGYDTTLGKvlpnsidISGGQWQRIALARSIFKKSKLIILDEPT 435
Cdd:TIGR01184 73 ENIALAVDRVLPDLSKSERRAIV---EEHIAlvGLTEAADKRPGQ-------LSGGMKQRVAIARALSIRPKVLLLDEPF 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 436 AALDPKTEAYVFEKFRELTENK--TAIFISHRL-ASVKMADRIIHLKD------GQILE 485
Cdd:TIGR01184 143 GALDALTRGNLQEELMQIWEEHrvTVLMVTHDVdEALLLSDRVVMLTNgpaaniGQILE 201
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
282-480 |
3.04e-28 |
|
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: 111.42 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcQIDENELSEYVSVVF-QDFVRYALSVKENI 360
Cdd:COG4133 18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAYLGhADGLKPELTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 361 ALsdisqidnLNEIKQTAF-LSGADSFIEAL-PNGYDTTLGKVLpnsidiSGGQWQRIALARSIFKKSKLIILDEPTAAL 438
Cdd:COG4133 97 RF--------WAALYGLRAdREAIDEALEAVgLAGLADLPVRQL------SAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2105575177 439 DPKTEAYVFEKFRELTENKTAIFI-SHRLASVKmADRIIHLKD 480
Cdd:COG4133 163 DAAGVALLAELIAAHLARGGAVLLtTHQPLELA-AARVLDLGD 204
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
265-492 |
3.22e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 113.31 E-value: 3.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQD--------FVRYALSVK-ENIALSDISQIDNLNE-IKQTAFLSGADSfiealpngydttlgkvLPNSidISGGQWQ 414
Cdd:PRK13648 88 VFQNpdnqfvgsIVKYDVAFGlENHAVPYDEMHRRVSEaLKQVDMLERADY----------------EPNA--LSGGQKQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 415 RIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASVKMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK13648 150 RVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEI 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
265-492 |
3.79e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 113.26 E-value: 3.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKY----PLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCqiDENELSE 340
Cdd:PRK13633 5 IKCKNVSYKYesneESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS--DEENLWD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 341 YVS---VVFQ--DFVRYALSVKENIALSDisqiDNLNeIKQTAFLSGADSFIEALpNGYDTTlgKVLPNSIdiSGGQWQR 415
Cdd:PRK13633 83 IRNkagMVFQnpDNQIVATIVEEDVAFGP----ENLG-IPPEEIRERVDESLKKV-GMYEYR--RHAPHLL--SGGQKQR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 416 IALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASVKMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK13633 153 VAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYgiTIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEI 231
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
265-488 |
4.07e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.90 E-value: 4.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNG--YSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY- 341
Cdd:PRK11153 2 IELKNISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 --VSVVFQDFvrYALS---VKENIALSdiSQIDNL--NEIKQTAF----LSGadsfIEALPNGYDTTLgkvlpnsidiSG 410
Cdd:PRK11153 82 rqIGMIFQHF--NLLSsrtVFDNVALP--LELAGTpkAEIKARVTelleLVG----LSDKADRYPAQL----------SG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 411 GQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASVK-MADRIIHLKDGQILEEG 487
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKrICDRVAVIDAGRLVEQG 223
|
.
gi 2105575177 488 S 488
Cdd:PRK11153 224 T 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
282-494 |
5.95e-28 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 111.76 E-value: 5.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY-------VSVVFQDfvryaL 354
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgigrtfqIPRLFPE-----L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 SVKENIAL-----SDISQIDNLNEIKQTAFLSGADSFIEA--LPNGYDTTLGkvlpnsiDISGGQWQRIALARSIFKKSK 427
Cdd:cd03219 91 TVLENVMVaaqarTGSGLLLARARREEREARERAEELLERvgLADLADRPAG-------ELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 428 LIILDEPTAALDPKTEAYVFEKFRELTENKTAI-FISHRLASV-KMADRIIHLKDGQILEEGSHKELMA 494
Cdd:cd03219 164 LLLLDEPAAGLNPEETEELAELIRELRERGITVlLVEHDMDVVmSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
265-492 |
1.02e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 112.20 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGN---IFLEGKDLCQIDENELSEY 341
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 VSVVFQD----FVryALSVKENIALS----DISQIDNLNEIKQTAFLSGADSFIEALPNgydttlgkvlpnsiDISGGQW 413
Cdd:PRK13640 86 VGIVFQNpdnqFV--GATVGDDVAFGlenrAVPRPEMIKIVRDVLADVGMLDYIDSEPA--------------NLSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 414 QRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASVKMADRIIHLKDGQILEEGSHKE 491
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
|
.
gi 2105575177 492 L 492
Cdd:PRK13640 230 I 230
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
282-494 |
1.11e-27 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 110.60 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY-VSVVFQD---FVRyaLSVK 357
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEGrriFPE--LTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENIALSdisqidnlneikqtAFLSGADSFIEALPNGYD---------TTLGKVLpnsidiSGGQWQRIALARSIFKKSKL 428
Cdd:cd03224 94 ENLLLG--------------AYARRRAKRKARLERVYElfprlkerrKQLAGTL------SGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 429 IILDEPTAALDPKTEAYVFEKFRELTENKTAIFIS-HRLASV-KMADRIIHLKDGQILEEGSHKELMA 494
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVeQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
264-494 |
2.61e-27 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 109.84 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 264 NISLKHVYFKYplsNGYSLKdINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcqideNELSEY-- 341
Cdd:COG3840 1 MLRLDDLTYRY---GDFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-----TALPPAer 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 -VSVVFQD---FVRyaLSVKENIAL----------SDISQIDNLneIKQTaflsGADSFIEALPNgydttlgkvlpnsiD 407
Cdd:COG3840 72 pVSMLFQEnnlFPH--LTVAQNIGLglrpglkltaEQRAQVEQA--LERV----GLAGLLDRLPG--------------Q 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 408 ISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASVK-MADRIIHLKDGQIL 484
Cdd:COG3840 130 LSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERglTVLMVTHDPEDAArIADRVLLVADGRIA 209
|
250
....*....|
gi 2105575177 485 EEGSHKELMA 494
Cdd:COG3840 210 ADGPTAALLD 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
284-494 |
2.87e-27 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 112.13 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 284 DINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY---VSVVFQDfvRYA-----LS 355
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQD--PYAslnprMT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 356 VKENIA--LSdisqidnLNEIKQTAflsGADSFIEALpngydttLGKV--LPNSID-----ISGGQWQRIALARSIFKKS 426
Cdd:COG4608 114 VGDIIAepLR-------IHGLASKA---ERRERVAEL-------LELVglRPEHADrypheFSGGQRQRIGIARALALNP 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 427 KLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASVK-MADRII--HLkdGQILEEGSHKELMA 494
Cdd:COG4608 177 KLIVCDEPVSALDVSIQAQVLNLLEDLQDelGLTYLFISHDLSVVRhISDRVAvmYL--GKIVEIAPRDELYA 247
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
282-502 |
4.11e-27 |
|
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: 116.20 E-value: 4.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENia 361
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMN-- 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 362 LSDISQIDNlNEIKQTAFLSGADSFIEALPNGYDTTLGKVLPNsidISGGQWQRIALARSIFKKSKLIILDEPTAALDPK 441
Cdd:TIGR00957 1380 LDPFSQYSD-EEVWWALELAHLKTFVSALPDKLDHECAEGGEN---LSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105575177 442 TEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYNM 502
Cdd:TIGR00957 1456 TDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
265-494 |
4.75e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 110.49 E-value: 4.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKY----PLSnGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLeGKDLCQIDENE--- 337
Cdd:PRK13634 3 ITFQKVEHRYqyktPFE-RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNkkl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 338 --LSEYVSVVFQdFVRYAL---SVKENIALSDI----SQIDNLNEIKQTAFLSGADSfiealpngydttlgKVLPNS-ID 407
Cdd:PRK13634 81 kpLRKKVGIVFQ-FPEHQLfeeTVEKDICFGPMnfgvSEEDAKQKAREMIELVGLPE--------------ELLARSpFE 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 408 ISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASV-KMADRIIHLKDGQIL 484
Cdd:PRK13634 146 LSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKglTTVLVTHSMEDAaRYADQIVVMHKGTVF 225
|
250
....*....|
gi 2105575177 485 EEGSHKELMA 494
Cdd:PRK13634 226 LQGTPREIFA 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
282-482 |
6.03e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 113.97 E-value: 6.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcQI----DENELSeyVSVVFQDF--VRyALS 355
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIrsprDAIALG--IGMVHQHFmlVP-NLT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 356 VKENIALSdisqidnlNEIKQTAFLS--GADSFIEALPNGYdttlG-KVLPNSI--DISGGQWQRIALARSIFKKSKLII 430
Cdd:COG3845 97 VAENIVLG--------LEPTKGGRLDrkAARARIRELSERY----GlDVDPDAKveDLSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 431 LDEPTAALDPKtEA-YVFEKFRELTEN-KTAIFISHRLASVK-MADRIIHLKDGQ 482
Cdd:COG3845 165 LDEPTAVLTPQ-EAdELFEILRRLAAEgKSIIFITHKLREVMaIADRVTVLRRGK 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
265-487 |
6.57e-27 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 108.05 E-value: 6.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlsNGYSLKDINLEIkDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDlCQIDENELSEYVSV 344
Cdd:cd03264 1 LQLENLTKRYG--KKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYA-LSVKENIA----LSDISQidnlneikqtaflSGADSFIEALPNgyDTTLGKVLPNSI-DISGGQWQRIAL 418
Cdd:cd03264 77 LPQEFGVYPnFTVREFLDyiawLKGIPS-------------KEVKARVDEVLE--LVNLGDRAKKKIgSLSGGMRRRVGI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 419 ARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVK-MADRIIHLKDGQILEEG 487
Cdd:cd03264 142 AQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
265-494 |
1.47e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 108.92 E-value: 1.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDE-NELSEYVS 343
Cdd:PRK13644 2 IRLENVSYSYP-DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 344 VVFQD----FVryALSVKENIALSDisqiDNL----NEIKQTAFLSGADSFIEALPNGYDTTLgkvlpnsidiSGGQWQR 415
Cdd:PRK13644 81 IVFQNpetqFV--GRTVEEDLAFGP----ENLclppIEIRKRVDRALAEIGLEKYRHRSPKTL----------SGGQGQC 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 416 IALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN-KTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
282-491 |
2.01e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.42 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENElsEYVSVVFQDfvrYAL----SVK 357
Cdd:PRK09452 30 ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN--RHVNTVFQS---YALfphmTVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENIALSDISQIDNLNEIKQTAFlsgadsfiEALPNGYDTTLGKVLPNsiDISGGQWQRIALARSIFKKSKLIILDEPTAA 437
Cdd:PRK09452 105 ENVAFGLRMQKTPAAEITPRVM--------EALRMVQLEEFAQRKPH--QLSGGQQQRVAIARAVVNKPKVLLLDESLSA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 438 LDPKTEAYVFEKFREL--TENKTAIFISH-RLASVKMADRIIHLKDGQILEEGSHKE 491
Cdd:PRK09452 175 LDYKLRKQMQNELKALqrKLGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
284-494 |
2.98e-26 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 109.82 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 284 DINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQ----IDENELSEYVSVVFQDFVRYA-LSVKE 358
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPhLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 359 NIAL----SDISQiDNLNEIKQTAFLsGADSFIEALPNgydttlgkvlpnsiDISGGQWQRIALARSIFKKSKLIILDEP 434
Cdd:TIGR02142 95 NLRYgmkrARPSE-RRISFERVIELL-GIGHLLGRLPG--------------RLSGGEKQRVAIGRALLSSPRLLLMDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 435 TAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKELMA 494
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
282-493 |
4.05e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 106.72 E-value: 4.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLC--QIDENELSEYVSVVFQDFVRYA-LSVKE 358
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIRQEAGMVFQQFYLFPhLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 359 NIALSDIsqidnlneikQTAFLSGADSFIEALpngydTTLGKV--------LPNsiDISGGQWQRIALARSIFKKSKLII 430
Cdd:PRK09493 97 NVMFGPL----------RVRGASKEEAEKQAR-----ELLAKVglaerahhYPS--ELSGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 431 LDEPTAALDPKTEAYVFEKFREL-TENKTAIFISHRLA-SVKMADRIIHLKDGQILEEGSHKELM 493
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLaEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLI 224
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
297-494 |
4.83e-26 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 108.35 E-value: 4.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 297 IVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENElsEYVSVVFQDfvrYAL----SVKENIALSDISQIDNLN 372
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHL--RHINMVFQS---YALfphmTVEENVAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 373 EIKQTAflsgadsfIEALPNGYDTTLGKVLPnsIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRE 452
Cdd:TIGR01187 76 EIKPRV--------LEALRLVQLEEFADRKP--HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKT 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2105575177 453 LTEN--KTAIFISH-RLASVKMADRIIHLKDGQILEEGSHKELMA 494
Cdd:TIGR01187 146 IQEQlgITFVFVTHdQEEAMTMSDRIAIMRKGKIAQIGTPEEIYE 190
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
284-516 |
6.79e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 108.65 E-value: 6.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 284 DINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQ--IDENElseyVSVVFQDfvrYAL----SVK 357
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrsIQQRD----ICMVFQS---YALfphmSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENIALSDISQIDNLNEIKQ---TAF----LSG-ADSFIEalpngydttlgkvlpnsiDISGGQWQRIALARSIFKKSKLI 429
Cdd:PRK11432 97 ENVGYGLKMLGVPKEERKQrvkEALelvdLAGfEDRYVD------------------QISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 430 ILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISH-RLASVKMADRIIHLKDGQILEEGSHKEL-MALKGEYYNMYMT 505
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQELyRQPASRFMASFMG 238
|
250
....*....|.
gi 2105575177 506 QAKWFDGQREE 516
Cdd:PRK11432 239 DANIFPATLSG 249
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
265-493 |
1.43e-25 |
|
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: 105.17 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplsNG-YSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGN-IFLEGKDLCQIDENELSE-- 340
Cdd:COG1119 4 LELRNVTVRR---GGkTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKri 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 341 -YVSVVFQDFVRYALSVkENIALS----------DISQIDnLNEIKQTAFLSGADSFIealpngyDTTLGkvlpnsiDIS 409
Cdd:COG1119 81 gLVSPALQLRFPRDETV-LDVVLSgffdsiglyrEPTDEQ-RERARELLELLGLAHLA-------DRPFG-------TLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 410 GGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL--TENKTAIFISHRL----ASVkmaDRIIHLKDGQI 483
Cdd:COG1119 145 QGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaEGAPTLVLVTHHVeeipPGI---THVLLLKDGRV 221
|
250
....*....|
gi 2105575177 484 LEEGSHKELM 493
Cdd:COG1119 222 VAAGPKEEVL 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
282-494 |
1.50e-25 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 105.22 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLegKDLcQIDEN-----------ELSEYVSVVFQDFV 350
Cdd:PRK11264 19 LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV--GDI-TIDTArslsqqkglirQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 351 RYA-LSVKENIALSDISQidnLNEIKQTAFLSGADSFIEALPNGYDTTLGKVLpnsidiSGGQWQRIALARSIFKKSKLI 429
Cdd:PRK11264 96 LFPhRTVLENIIEGPVIV---KGEPKEEATARARELLAKVGLAGKETSYPRRL------SGGQQQRVAIARALAMRPEVI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 430 ILDEPTAALDPKTEAYVFEKFRELTENK-TAIFISHRLASVK-MADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK11264 167 LFDEPTSALDPELVGEVLNTIRQLAQEKrTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
286-494 |
1.87e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 104.66 E-value: 1.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 286 NLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSeyVSVVFQDFVRYA-LSVKENIALS- 363
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP--VSMLFQENNLFShLTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 364 ------DISQIDNLNEIKQTAFLsgaDSFIEALPNgydttlgkvlpnsiDISGGQWQRIALARSIFKKSKLIILDEPTAA 437
Cdd:PRK10771 97 npglklNAAQREKLHAIARQMGI---EDLLARLPG--------------QLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 438 LDPKTEAYVFEKFRELTENK--TAIFISHRLA-SVKMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK10771 160 LDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
265-487 |
1.99e-25 |
|
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: 103.73 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplsnGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSeyVSV 344
Cdd:cd03298 1 VRLDKIRFSY----GEQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYA-LSVKENIALSDISQIdNLNEIKQTAFLS-----GADSFIEALPNgydttlgkvlpnsiDISGGQWQRIAL 418
Cdd:cd03298 75 LFQENNLFAhLTVEQNVGLGLSPGL-KLTAEDRQAIEValarvGLAGLEKRLPG--------------ELSGGERQRVAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 419 ARSIFKKSKLIILDEPTAALDP----KTEAYVFEKFREltENKTAIFISHRLA-SVKMADRIIHLKDGQILEEG 487
Cdd:cd03298 140 ARVLVRDKPVLLLDEPFAALDPalraEMLDLVLDLHAE--TKMTVLMVTHQPEdAKRLAQRVVFLDNGRIAAQG 211
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
242-480 |
2.50e-25 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 110.89 E-value: 2.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 242 QNEDDAKKEKleknianksDTANISLKHVYFKYPLSNGYSL-KDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTA 320
Cdd:PTZ00265 369 ENNDDGKKLK---------DIKKIQFKNVRFHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTE 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 321 GNIFL-EGKDLCQIDENELSEYVSVVFQDFVRYALSVKENI-----------ALSDISQID------------------- 369
Cdd:PTZ00265 440 GDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIkyslyslkdleALSNYYNEDgndsqenknkrnscrakca 519
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 370 -NLNEIKQTAFLSG-----------ADS-------------FIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFK 424
Cdd:PTZ00265 520 gDLNDMSNTTDSNEliemrknyqtiKDSevvdvskkvlihdFVSALPDKYETLVGS---NASKLSGGQKQRISIARAIIR 596
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 425 KSKLIILDEPTAALDPKTEAYVFEKFREL--TENKTAIFISHRLASVKMADRIIHLKD 480
Cdd:PTZ00265 597 NPKILILDEATSSLDNKSEYLVQKTINNLkgNENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
281-503 |
4.09e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.86 E-value: 4.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 281 SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE----LSEYVSVVFQdFVRYAL-- 354
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyirpVRKRIGMVFQ-FPESQLfe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 -SVKENIALSDISQIDNLNEIKQTAFlsgaDSFIEAlpnGYDTTLGKVLPnsIDISGGQWQRIALARSIFKKSKLIILDE 433
Cdd:PRK13646 101 dTVEREIIFGPKNFKMNLDEVKNYAH----RLLMDL---GFSRDVMSQSP--FQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 434 PTAALDPKTEAYVFEKFRELT--ENKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKELMAlKGEYYNMY 503
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK-DKKKLADW 243
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
282-486 |
1.34e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 103.23 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY---VSVVFQD---FVRYALS 355
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFrrdIQMVFQDsisAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 356 VKENIAlSDISQIDNLNEIKQTAflsGADSFIEALpnGYDTTLGKVLPNSidISGGQWQRIALARSIFKKSKLIILDEPT 435
Cdd:PRK10419 108 VREIIR-EPLRHLLSLDKAERLA---RASEMLRAV--DLDDSVLDKRPPQ--LSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 436 AALDPKTEAYVFEKFRELTENK-TA-IFISHRLASV-KMADRIIHLKDGQILEE 486
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFgTAcLFITHDLRLVeRFCQRVMVMDNGQIVET 233
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
282-492 |
1.35e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 102.68 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQL---IIGLYKP--TAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYA-LS 355
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVfnrLIELYPEarVSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPIPnLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 356 VKENIALSdiSQIDNLNEIKQTAF------LSGADSFiEALPNGYDTTLGKvlpnsidISGGQWQRIALARSIFKKSKLI 429
Cdd:PRK14247 99 IFENVALG--LKLNRLVKSKKELQervrwaLEKAQLW-DEVKDRLDAPAGK-------LSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 430 ILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLA-SVKMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQqAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
282-487 |
1.70e-24 |
|
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: 101.20 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE---LSE----YVSVVFQDFVRYAL 354
Cdd:cd03269 16 LDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRigyLPEerglYPKMKVIDQLVYLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 SVKeNIALSDI-SQIDNLneIKQTAFLSGADSFIEALpngydttlgkvlpnsidiSGGQWQRIALARSIFKKSKLIILDE 433
Cdd:cd03269 96 QLK-GLKKEEArRRIDEW--LERLELSEYANKRVEEL------------------SKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2105575177 434 PTAALDPKTEAYVFEKFRELTEN-KTAIFISHRLASV-KMADRIIHLKDGQILEEG 487
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
265-494 |
1.84e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.85 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlsNGYS-LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcQIDENELSEY-- 341
Cdd:PRK13639 2 LETRDLKYSYP--DGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVrk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 -VSVVFQ--DFVRYALSVKENIALSDISQIDNLNEIKQTAflsgADSFIEALPNGYDTTLGKVLpnsidiSGGQWQRIAL 418
Cdd:PRK13639 79 tVGIVFQnpDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRV----KEALKAVGMEGFENKPPHHL------SGGQKKRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 419 ARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFIS-HRLASV-KMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK13639 149 AGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
286-483 |
2.30e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 101.09 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 286 NLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSeyVSVVFQDFVRYA-LSVKENIALSd 364
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP--VSMLFQENNLFAhLTVRQNIGLG- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 365 ISQIDNLN-----EIKQTAFLSGADSFIEALPNgydttlgkvlpnsiDISGGQWQRIALARSIFKKSKLIILDEPTAALD 439
Cdd:TIGR01277 95 LHPGLKLNaeqqeKVVDAAQQVGIADYLDRLPE--------------QLSGGQRQRVALARCLVRPNPILLLDEPFSALD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2105575177 440 PKTEAYVFEKFRELTENK--TAIFISHRLA-SVKMADRIIHLKDGQI 483
Cdd:TIGR01277 161 PLLREEMLALVKQLCSERqrTLLMVTHHLSdARAIASQIAVVSQGKI 207
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
276-483 |
2.59e-24 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 99.81 E-value: 2.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 276 LSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSE----YVS------VV 345
Cdd:cd03215 10 LSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRagiaYVPedrkreGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 346 FQDFvryalSVKENIALSdisqidnlneikqtAFLSGadsfiealpngydttlgkvlpnsidisGGQwQRIALARSIFKK 425
Cdd:cd03215 90 VLDL-----SVAENIALS--------------SLLSG---------------------------GNQ-QKVVLARWLARD 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 426 SKLIILDEPTAALDPKTEAYVFEKFRELTENKTAI-FISHRLASV-KMADRIIHLKDGQI 483
Cdd:cd03215 123 PRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVlLISSELDELlGLCDRILVMYEGRI 182
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
280-487 |
4.17e-24 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 100.06 E-value: 4.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 280 YSLKDINLEIK---DKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGK---DLCQ-IDENELSEYVSVVFQDfvrY 352
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkINLPPQQRKIGLVFQQ---Y 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 353 AL----SVKENIA-----LSDISQIDNLNEIKQtafLSGADSFIEALPNGydttlgkvlpnsidISGGQWQRIALARSIF 423
Cdd:cd03297 85 ALfphlNVRENLAfglkrKRNREDRISVDELLD---LLGLDHLLNRYPAQ--------------LSGGEKQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 424 KKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASV-KMADRIIHLKDGQILEEG 487
Cdd:cd03297 148 AQPELLLLDEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
265-496 |
9.07e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.08 E-value: 9.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGK--DLCQIDENELSEYV 342
Cdd:PRK13636 6 LKVEELNYNYS-DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 343 SVVFQ--DFVRYALSVKENIALSDISQIDNLNEIKQTAFLSGADSFIEALPNGYDTTLgkvlpnsidiSGGQWQRIALAR 420
Cdd:PRK13636 85 GMVFQdpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCL----------SFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 421 SIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASVKM-ADRIIHLKDGQILEEGSHKELMALK 496
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
265-487 |
1.69e-23 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 98.76 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYS--------------------LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIF 324
Cdd:cd03220 1 IELENVSKSYPTYKGGSsslkklgilgrkgevgefwaLKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 325 LEGKDLCQIDENelseyvsVVFQDfvryALSVKENIALS------DISQIDN-LNEIKQtaflsgadsFIEalpngydtt 397
Cdd:cd03220 81 VRGRVSSLLGLG-------GGFNP----ELTGRENIYLNgrllglSRKEIDEkIDEIIE---------FSE--------- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 398 lgkvLPNSIDI-----SGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN-KTAIFISHRLASVK- 470
Cdd:cd03220 132 ----LGDFIDLpvktySSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKr 207
|
250
....*....|....*..
gi 2105575177 471 MADRIIHLKDGQILEEG 487
Cdd:cd03220 208 LCDRALVLEKGKIRFDG 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
264-492 |
1.92e-23 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 101.32 E-value: 1.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 264 NISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY-- 341
Cdd:PRK15079 19 DIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 -VSVVFQDFVRyalSVKENIALSDIsqidnLNEIKQTAF--LSGADsfieaLPNGYDTTLGKV--LPNSI-----DISGG 411
Cdd:PRK15079 99 dIQMIFQDPLA---SLNPRMTIGEI-----IAEPLRTYHpkLSRQE-----VKDRVKAMMLKVglLPNLInryphEFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 412 QWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASVK-MADRIIHLKDGQILEEGS 488
Cdd:PRK15079 166 QCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKhISDRVLVMYLGHAVELGT 245
|
....
gi 2105575177 489 HKEL 492
Cdd:PRK15079 246 YDEV 249
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
247-516 |
2.22e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 104.67 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 247 AKKEKLEKNIANKSDTANISLKHVYFKYPL-SNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPtagnifl 325
Cdd:PLN03232 597 SEERILAQNPPLQPGAPAISIKNGYFSWDSkTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH------- 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 326 egkdlcqidenelSEYVSVVFQDFVRYA--------LSVKENIAL-SDISQIDNLNEIKQTAFLSGADSFiealpNGYDT 396
Cdd:PLN03232 670 -------------AETSSVVIRGSVAYVpqvswifnATVRENILFgSDFESERYWRAIDVTALQHDLDLL-----PGRDL 731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 397 TlgKVLPNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEK-FRELTENKTAIFISHRLASVKMADRI 475
Cdd:PLN03232 732 T--EIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRI 809
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2105575177 476 IHLKDGQILEEGSHKELMAlKGEYYNMYMTQAKWFDGQREE 516
Cdd:PLN03232 810 ILVSEGMIKEEGTFAELSK-SGSLFKKLMENAGKMDATQEV 849
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
265-494 |
2.53e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.42 E-value: 2.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNgYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:PRK13647 5 IEVEDLHFRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQ--DFVRYALSVKENIALSDISQ---IDNLNEIKQTAF-LSGADSFIEALPNgydttlgkvlpnsiDISGGQWQRIAL 418
Cdd:PRK13647 84 VFQdpDDQVFSSTVWDDVAFGPVNMgldKDEVERRVEEALkAVRMWDFRDKPPY--------------HLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 419 ARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN-KTAIFISHRL-ASVKMADRIIHLKDGQILEEGShKELMA 494
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVdLAAEWADQVIVLKEGRVLAEGD-KSLLT 226
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
282-497 |
2.75e-23 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 100.16 E-value: 2.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQiDENELSEYVSVVFQDFVRY-ALSVKENI 360
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR-EPRKVRRSIGIVPQYASVDeDLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 361 ALsdisqIDNLNEIKQTAFLSGADSFIEALPNGY--DTTLGKvlpnsidISGGQWQRIALARSIFKKSKLIILDEPTAAL 438
Cdd:TIGR01188 88 EM-----MGRLYGLPKDEAEERAEELLELFELGEaaDRPVGT-------YSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105575177 439 DPKTEAYVFEKFRELTENKTAIFI-SHRLASV-KMADRIIHLKDGQILEEGSHKELMALKG 497
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLtTHYMEEAdKLCDRIAIIDHGRIIAEGTPEELKRRLG 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
282-487 |
3.21e-23 |
|
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: 97.29 E-value: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcqideNELSEYVSVV-----FQDFVRYaLSV 356
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-----QKNIEALRRIgalieAPGFYPN-LTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 KENIALSDISQIDNLNEIKQTAFLSGADsfiealpngyDTTLGKVLpnsiDISGGQWQRIALARSIFKKSKLIILDEPTA 436
Cdd:cd03268 90 RENLRLLARLLGIRKKRIDEVLDVVGLK----------DSAKKKVK----GFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 437 ALDPKTEAYVFEKFRELTENKTAIFI-SHRLASV-KMADRIIHLKDGQILEEG 487
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLIsSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
282-492 |
3.67e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.54 E-value: 3.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENElsEYVSVVFQdfvRYAL----SVK 357
Cdd:PRK10851 18 LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVFQ---HYALfrhmTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENIA--LSDISQIDNLN--EIKQ--TAFLSGADsfIEALPNGYDTTLgkvlpnsidiSGGQWQRIALARSIFKKSKLIIL 431
Cdd:PRK10851 93 DNIAfgLTVLPRRERPNaaAIKAkvTQLLEMVQ--LAHLADRYPAQL----------SGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 432 DEPTAALDPKTEAYVFEKFRELTENK--TAIFISH-RLASVKMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELkfTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
272-487 |
4.84e-23 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 97.44 E-value: 4.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 272 FKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQiDENELSEYVSVVFQDFVR 351
Cdd:cd03266 11 FRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 352 YA-LSVKENIALsdisqIDNLNEIKQTAFLSGADSFIEALpnGYDTTLGKvlpNSIDISGGQWQRIALARSIFKKSKLII 430
Cdd:cd03266 90 YDrLTARENLEY-----FAGLYGLKGDELTARLEELADRL--GMEELLDR---RVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 431 LDEPTAALDPKTEAYVFEKFREL-TENKTAIFISHRLASV-KMADRIIHLKDGQILEEG 487
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLrALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
200-507 |
5.23e-23 |
|
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: 103.49 E-value: 5.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 200 SFVSTAqAIQGLQGTVNQTSHLLASLFESNLYIKDFFDFIEYQNEDdakKEKLEKNIANKSDTANISLKHVYFKYPLSNG 279
Cdd:TIGR00957 576 AFVSLA-LFNILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELE---PDSIERRTIKPGEGNSITVHNATFTWARDLP 651
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 280 YSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKdlcqidenelseyVSVVFQDFVRYALSVKEN 359
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWIQNDSLREN 718
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 360 IALSDISQIDNLNEIKQTAFLSgADsfIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALD 439
Cdd:TIGR00957 719 ILFGKALNEKYYQQVLEACALL-PD--LEILPSGDRTEIGE---KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105575177 440 PKTEAYVFEKF---RELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYNMYMTQA 507
Cdd:TIGR00957 793 AHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLRTYA 863
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
265-519 |
6.21e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 103.28 E-value: 6.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKY-PLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTA-GNIFLEGKdlcqidenelseyV 342
Cdd:PLN03130 615 ISIKNGYFSWdSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT-------------V 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 343 SVVFQDFVRYALSVKENIALSDISQIDNLNeikQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSI 422
Cdd:PLN03130 682 AYVPQVSWIFNATVRDNILFGSPFDPERYE---RAIDVTALQHDLDLLPGGDLTEIGE---RGVNISGGQKQRVSMARAV 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 423 FKKSKLIILDEPTAALDPKTEAYVFEK-FRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMAlKGEYYN 501
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN-NGPLFQ 834
|
250
....*....|....*...
gi 2105575177 502 MYMTQAkwfdGQREEVIS 519
Cdd:PLN03130 835 KLMENA----GKMEEYVE 848
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
282-487 |
1.14e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 98.23 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNI---FLEGKDLCQIDE---------------------NE 337
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEkekvleklviqktrfkkikkiKE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 338 LSEYVSVVFQdFVRYAL---SVKENIALSDISQIDNLNEIKQTaflsgADSFIE--ALPNGYdttlgkvLPNS-IDISGG 411
Cdd:PRK13651 103 IRRRVGVVFQ-FAEYQLfeqTIEKDIIFGPVSMGVSKEEAKKR-----AAKYIElvGLDESY-------LQRSpFELSGG 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 412 QWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN-KTAIFISHRLASV-KMADRIIHLKDGQILEEG 487
Cdd:PRK13651 170 QKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQgKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDG 247
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
262-494 |
1.22e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 98.16 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 262 TANISLKHVYFKYPLSNGYSLKDIN---LEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEG----KDLCQID 334
Cdd:PRK13645 4 SKDIILDNVSYTYAKKTPFEFKALNntsLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 335 E-NELSEYVSVVFQdFVRYAL---SVKENIALSDIsqidNLNEIKQTAFLSGADSF-IEALPNGYdttlgkVLPNSIDIS 409
Cdd:PRK13645 84 EvKRLRKEIGLVFQ-FPEYQLfqeTIEKDIAFGPV----NLGENKQEAYKKVPELLkLVQLPEDY------VKRSPFELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 410 GGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN--KTAIFISHRLASV-KMADRIIHLKDGQILEE 486
Cdd:PRK13645 153 GGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEykKRIIMVTHNMDQVlRIADEVIVMHEGKVISI 232
|
....*...
gi 2105575177 487 GSHKELMA 494
Cdd:PRK13645 233 GSPFEIFS 240
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
262-509 |
1.33e-22 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.72 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 262 TANISLKHVYFKYPLSNGYS--LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELS 339
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 340 ----EYVSVVFQdfvRYAL----SVKENIALSDISQIDNLNEIKQTAflsgadsfIEALpngydTTLGkvLPNSID---- 407
Cdd:PRK10535 82 qlrrEHFGFIFQ---RYHLlshlTAAQNVEVPAVYAGLERKQRLLRA--------QELL-----QRLG--LEDRVEyqps 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 408 -ISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN-KTAIFISHRLASVKMADRIIHLKDGQILE 485
Cdd:PRK10535 144 qLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRgHTVIIVTHDPQVAAQAERVIEIRDGEIVR 223
|
250 260
....*....|....*....|....
gi 2105575177 486 EGSHKELMALKGEYYNMYMTQAKW 509
Cdd:PRK10535 224 NPPAQEKVNVAGGTEPVVNTASGW 247
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
282-444 |
1.50e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 95.71 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSvvFQDFVRYALSVKENIA 361
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 362 LsdisqidnlneikQTAFLSGADSFIEA------------LPNGYdttlgkvlpnsidISGGQWQRIALARSIFKKSKLI 429
Cdd:PRK13539 96 F-------------WAAFLGGEELDIAAaleavglaplahLPFGY-------------LSAGQKRRVALARLLVSNRPIW 149
|
170
....*....|....*
gi 2105575177 430 ILDEPTAALDPKTEA 444
Cdd:PRK13539 150 ILDEPTAALDAAAVA 164
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
55-485 |
1.62e-22 |
|
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: 101.03 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 55 ISNSMHVL-----QLCITIVSYIgFLFFIHWGLVVLGILASIPAFIIQYkfgysnFNLNRLQSGLMREASYINSLFRNKQ 129
Cdd:COG4615 118 ISQAFVRLpellqSVALVLGCLA-YLAWLSPPLFLLTLVLLGLGVAGYR------LLVRRARRHLRRAREAEDRLFKHFR 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 130 SI----KEIKL-------FRSGNFL--INRWRKLTTSNNKKILKLFfkqNWANIgldsltaVLYSMSAVLMVWLLKLGKM 196
Cdd:COG4615 191 ALlegfKELKLnrrrrraFFDEDLQptAERYRDLRIRADTIFALAN---NWGNL-------LFFALIGLILFLLPALGWA 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 197 NIGSFVSTAQAIQGLQGTVNQTSHLLASLFESNLYIK--DFFDFIEYQNEDDAKKEKLEkniANKSDTANISLKHVYFKY 274
Cdd:COG4615 261 DPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRkiEELELALAAAEPAAADAAAP---PAPADFQTLELRGVTYRY 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 275 PLSNG---YSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKdlcQIDENELSEY---VSVVFQD 348
Cdd:COG4615 338 PGEDGdegFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNREAYrqlFSAVFSD 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 349 FV--RYALSVKENIALSDIS------QIDNLNEIKQTAFlsgadsfiealpngydTTLgkvlpnsiDISGGQWQRIALA- 419
Cdd:COG4615 415 FHlfDRLLGLDGEADPARARellerlELDHKVSVEDGRF----------------STT--------DLSQGQRKRLALLv 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 420 -----RSIfkksklIILDEPTAALDPkteayVF-EKF-REL-----TENKTAIFISH--RLASVkmADRIIHLKDGQILE 485
Cdd:COG4615 471 alledRPI------LVFDEWAADQDP-----EFrRVFyTELlpelkARGKTVIAISHddRYFDL--ADRVLKMDYGKLVE 537
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
282-493 |
1.95e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 96.29 E-value: 1.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGL--YKPTAGNIFLEGKDLCQIDENELSEY-VSVVFQ----------- 347
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAgIFLAFQypveipgvsvs 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 348 DFVRYALSvkeNIALSDISQIDNLNEIKQTA-FLSGADSFIE-ALPNGYdttlgkvlpnsidiSGGQWQRIALARSIFKK 425
Cdd:COG0396 96 NFLRTALN---ARRGEELSAREFLKLLKEKMkELGLDEDFLDrYVNEGF--------------SGGEKKRNEILQMLLLE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 426 SKLIILDEPTAALDP---KTEAYVFEKFREltENKTAIFISH--RLASVKMADRIIHLKDGQILEEGShKELM 493
Cdd:COG0396 159 PKLAILDETDSGLDIdalRIVAEGVNKLRS--PDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGG-KELA 228
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
276-495 |
2.54e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.09 E-value: 2.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 276 LSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcqidenELSE----------YVSV- 344
Cdd:COG1129 262 LSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV------RIRSprdairagiaYVPEd 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 -----VFQDfvryaLSVKENIALSDISQIDNLNEIKQTAFLSGADSFIEALpngydttlgKVLPNSIDI-----SGGQWQ 414
Cdd:COG1129 336 rkgegLVLD-----LSIRENITLASLDRLSRGGLLDRRRERALAEEYIKRL---------RIKTPSPEQpvgnlSGGNQQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 415 RIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAI-FIShrlaS-----VKMADRIIHLKDGQILEEGS 488
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAViVIS----SelpelLGLSDRILVMREGRIVGELD 477
|
250
....*....|..
gi 2105575177 489 HKE-----LMAL 495
Cdd:COG1129 478 REEateeaIMAA 489
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
249-504 |
3.10e-22 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 96.46 E-value: 3.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 249 KEKLEKNIAN-KSDTANISLKHvyfkYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEG 327
Cdd:cd03291 23 KAKQENNDRKhSSDDNNLFFSN----LCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 328 KdlcqidenelseyvsVVFQDFVRYAL--SVKENIALS-DISQIDNLNEIKQTAFlsgaDSFIEALPNGYDTTLGKvlpN 404
Cdd:cd03291 99 R---------------ISFSSQFSWIMpgTIKENIIFGvSYDEYRYKSVVKACQL----EEDITKFPEKDNTVLGE---G 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 405 SIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEK-FRELTENKTAIFISHRLASVKMADRIIHLKDGQI 483
Cdd:cd03291 157 GITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSS 236
|
250 260
....*....|....*....|.
gi 2105575177 484 LEEGSHKELMALKGEYYNMYM 504
Cdd:cd03291 237 YFYGTFSELQSLRPDFSSKLM 257
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
265-492 |
3.30e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 95.87 E-value: 3.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLI-------QLIIGLYkpTAGNIFLEGKDL--CQIDE 335
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLrclnrmnDLIPGAR--VEGEILLDGEDIydPDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 336 NELSEYVSVVFQDFVRYALSVKENIA----LSDISQIDNLNEIKQTAfLSGAdsfieALPNGYDTTLGKvlpNSIDISGG 411
Cdd:COG1117 88 VELRRRVGMVFQKPNPFPKSIYDNVAyglrLHGIKSKSELDEIVEES-LRKA-----ALWDEVKDRLKK---SALGLSGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 412 QWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRL--ASvKMADRIIHLKDGQILEEGSH 489
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMqqAA-RVSDYTAFFYLGELVEFGPT 237
|
...
gi 2105575177 490 KEL 492
Cdd:COG1117 238 EQI 240
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
282-493 |
3.38e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 95.95 E-value: 3.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQD----FvryALSVK 357
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHsslaF---PFTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENIAL----SDISQIDNLNEIKQTAFLSGADSFIEALpngYdTTLgkvlpnsidiSGGQWQRIALAR-------SIFKKS 426
Cdd:COG4559 94 EVVALgrapHGSSAAQDRQIVREALALVGLAHLAGRS---Y-QTL----------SGGEQQRVQLARvlaqlwePVDGGP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 427 KLIILDEPTAALDPKTEAYVFEKFRELTENKTAIF-ISH--RLASvKMADRIIHLKDGQILEEGSHKELM 493
Cdd:COG4559 160 RWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVaVLHdlNLAA-QYADRILLLHQGRLVAQGTPEEVL 228
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
282-496 |
3.66e-22 |
|
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: 95.75 E-value: 3.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENIA 361
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNLD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 362 LSDISQIDNLNEIKQTAFLSgadSFIEALPNGYDTTlgkVLPNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPK 441
Cdd:cd03288 117 PECKCTDDRLWEALEIAQLK---NMVKSLPGGLDAV---VTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 442 TEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALK 496
Cdd:cd03288 191 TENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQE 245
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
265-508 |
4.89e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.15 E-value: 4.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNG--------------------YSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIF 324
Cdd:COG1134 5 IEVENVSKSYRLYHEpsrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 325 LEGKDLCQIDenelseyVSVVFQDfvryALSVKENIALsdISQIDNLN--EIKQTAflsgadSFIEALpngydTTLGKVl 402
Cdd:COG1134 85 VNGRVSALLE-------LGAGFHP----ELTGRENIYL--NGRLLGLSrkEIDEKF------DEIVEF-----AELGDF- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 403 pnsID-----ISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN-KTAIFISHRLASVK-MADRI 475
Cdd:COG1134 140 ---IDqpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRrLCDRA 216
|
250 260 270
....*....|....*....|....*....|...
gi 2105575177 476 IHLKDGQILEEGSHKELMAlkgeYYNMYMTQAK 508
Cdd:COG1134 217 IWLEKGRLVMDGDPEEVIA----AYEALLAGRE 245
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
265-489 |
4.92e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 95.08 E-value: 4.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNgySLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGK--DLCQ-IDEN---EL 338
Cdd:PRK11124 3 IQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKtPSDKairEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 339 SEYVSVVFQDFVRYA-LSVKENI--------ALSDISQIDNLNEIKQTAFLSGadsFIEALPngydttlgkvlpnsIDIS 409
Cdd:PRK11124 81 RRNVGMVFQQYNLWPhLTVQQNLieapcrvlGLSKDQALARAEKLLERLRLKP---YADRFP--------------LHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 410 GGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK-TAIFISHRLA-SVKMADRIIHLKDGQILEEG 487
Cdd:PRK11124 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGiTQVIVTHEVEvARKTASRVVYMENGHIVEQG 223
|
..
gi 2105575177 488 SH 489
Cdd:PRK11124 224 DA 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
146-500 |
5.56e-22 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 100.44 E-value: 5.56e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 146 RWRKLTTSNNKkilklffkqnWANIGLDSLTAVLYSMSAVLMVwlLKLGKM-NIGSFVSTAQAIqgLQGTVNQTSHL--- 221
Cdd:PLN03232 1124 RFTLANTSSNR----------WLTIRLETLGGVMIWLTATFAV--LRNGNAeNQAGFASTMGLL--LSYTLNITTLLsgv 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 222 --LASLFESNL-YIKDFFDFIEYQNEDDAKKEKlEKNIANKSDTANISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIV 298
Cdd:PLN03232 1190 lrQASKAENSLnSVERVGNYIDLPSEATAIIEN-NRPVSGWPSRGSIKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVV 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 299 GHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENI-ALSDISQIDnLNEIKQT 377
Cdd:PLN03232 1269 GRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIdPFSEHNDAD-LWEALER 1347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 378 AFLSGAdsfIEALPNGYDttlGKVLPNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK 457
Cdd:PLN03232 1348 AHIKDV---IDRNPFGLD---AEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSC 1421
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2105575177 458 TAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYY 500
Cdd:PLN03232 1422 TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
264-489 |
8.46e-22 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 94.31 E-value: 8.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 264 NISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGK--DLCQ-IDEN---E 337
Cdd:COG4161 2 SIQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQkPSEKairL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 338 LSEYVSVVFQDFVRYA-LSVKENI--------ALSDISQIDNLNEIKQTAFLsgaDSFIEALPNgydttlgkvlpnsiDI 408
Cdd:COG4161 80 LRQKVGMVFQQYNLWPhLTVMENLieapckvlGLSKEQAREKAMKLLARLRL---TDKADRFPL--------------HL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 409 SGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK-TAIFISHRLA-SVKMADRIIHLKDGQILEE 486
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEfARKVASQVVYMEKGRIIEQ 222
|
...
gi 2105575177 487 GSH 489
Cdd:COG4161 223 GDA 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
282-494 |
1.58e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 94.51 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDEN----ELSEYVSVVFQdFVRYALSvk 357
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkKLRKKVSLVFQ-FPEAQLF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENIALSDIS-QIDNLNEIKQTAfLSGADSFIEALpnGYDTTLGKVLPnsIDISGGQWQRIALARSIFKKSKLIILDEPTA 436
Cdd:PRK13641 100 ENTVLKDVEfGPKNFGFSEDEA-KEKALKWLKKV--GLSEDLISKSP--FELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 437 ALDPKTEAYVFEKFREL-TENKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
265-492 |
1.63e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 94.43 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKY----PLSnGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE--- 337
Cdd:PRK13649 3 INLQNVSYTYqagtPFE-GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdik 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 338 -LSEYVSVVFQ--DFVRYALSVKENIALS----DISQIDNLNEIKQTAFLSG-ADSFIEAlpngydttlgkvlpNSIDIS 409
Cdd:PRK13649 82 qIRKKVGLVFQfpESQLFEETVLKDVAFGpqnfGVSQEEAEALAREKLALVGiSESLFEK--------------NPFELS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 410 GGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN-KTAIFISHRLASV-KMADRIIHLKDGQILEEG 487
Cdd:PRK13649 148 GGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSgMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSG 227
|
....*
gi 2105575177 488 SHKEL 492
Cdd:PRK13649 228 KPKDI 232
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
282-486 |
1.71e-21 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 93.30 E-value: 1.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSE----YVSVVFQDFVRY-ALSV 356
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlrakHVGFVFQSFMLIpTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 KENIALSDISQIDNLNEIKQtaflsGADSFIEALpngydtTLGKVLPN-SIDISGGQWQRIALARSIFKKSKLIILDEPT 435
Cdd:PRK10584 106 LENVELPALLRGESSRQSRN-----GAKALLEQL------GLGKRLDHlPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 436 AALDPKTEAYVFEKFRELTEN--KTAIFISHRLASVKMADRIIHLKDGQILEE 486
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREhgTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
282-488 |
2.06e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 93.68 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDF-VRYALSVKENI 360
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSsLSFPFTVEEVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 361 ALSDI---SQIDNLNEIKQTAfLSGADsfIEALPNGYDTTLgkvlpnsidiSGGQWQRIALAR------SIFKKSKLIIL 431
Cdd:PRK13548 98 AMGRAphgLSRAEDDALVAAA-LAQVD--LAHLAGRDYPQL----------SGGEQQRVQLARvlaqlwEPDGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105575177 432 DEPTAALDPKTEAYVFEKFRELT--ENKTAIFISH--RLASvKMADRIIHLKDGQILEEGS 488
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQLAheRGLAVIVVLHdlNLAA-RYADRIVLLHQGRLVADGT 224
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
263-492 |
2.26e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.87 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 263 ANISLKHVYFKY---PLSngyslKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELS 339
Cdd:PRK11000 2 ASVTLRNVTKAYgdvVIS-----KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 340 eyVSVVFQDFVRYA-LSVKENIAL---------SDISQ-IDNLNEIKQTAFLsgadsfIEALPNgydttlgkvlpnsiDI 408
Cdd:PRK11000 77 --VGMVFQSYALYPhLSVAENMSFglklagakkEEINQrVNQVAEVLQLAHL------LDRKPK--------------AL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 409 SGGQWQRIALARSIFKKSKLIILDEPTAALDpkteAYVFEKFR-ELTE-----NKTAIFISH-RLASVKMADRIIHLKDG 481
Cdd:PRK11000 135 SGGQRQRVAIGRTLVAEPSVFLLDEPLSNLD----AALRVQMRiEISRlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAG 210
|
250
....*....|.
gi 2105575177 482 QILEEGSHKEL 492
Cdd:PRK11000 211 RVAQVGKPLEL 221
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
265-494 |
2.42e-21 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 97.35 E-value: 2.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKdlcQIDENELSEY--- 341
Cdd:PRK10522 323 LELRNVTFAYQ-DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---PVTAEQPEDYrkl 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 VSVVFQDFVRYalsvkenialsdiSQIdnLNEIKQTAFLSGADSFIEALPNGYDTTL--GKVLpnSIDISGGQWQRIALA 419
Cdd:PRK10522 399 FSAVFTDFHLF-------------DQL--LGPEGKPANPALVEKWLERLKMAHKLELedGRIS--NLKLSKGQKKRLALL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 420 RSIFKKSKLIILDEPTAALDPkteayVFEKF--REL-----TENKTAIFISHRLASVKMADRIIHLKDGQILE-EGSHKE 491
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDP-----HFRREfyQVLlpllqEMGKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERD 536
|
...
gi 2105575177 492 LMA 494
Cdd:PRK10522 537 AAS 539
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
281-492 |
2.77e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.30 E-value: 2.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 281 SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLI--IGLYKP---TAGNIFLEGKDLC--QIDENELSEYVSVVFQDFVRYA 353
Cdd:PRK14239 20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYspRTDTVDLRKEIGMVFQQPNPFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 354 LSVKENIA----LSDISQIDNLNEIKQTAfLSGADSFIEALPNGYDTTLGkvlpnsidISGGQWQRIALARSIFKKSKLI 429
Cdd:PRK14239 100 MSIYENVVyglrLKGIKDKQVLDEAVEKS-LKGASIWDEVKDRLHDSALG--------LSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 430 ILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRL--ASvKMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqAS-RISDRTGFFLDGDLIEYNDTKQM 234
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
265-485 |
3.21e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.67 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKY---PLsngysLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIflegkdlcqidenELSEY 341
Cdd:COG0488 316 LELEGLSKSYgdkTL-----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-------------KLGET 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 VSVVF----QDFVRYALSVKENIalSDISqiDNLNEIKQTAFL-----SGADSF--IEALpngydttlgkvlpnsidiSG 410
Cdd:COG0488 378 VKIGYfdqhQEELDPDKTVLDEL--RDGA--PGGTEQEVRGYLgrflfSGDDAFkpVGVL------------------SG 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 411 GQWQRIALARSIFKKSKLIILDEPTAALDPKTeayvfekfRELTENK------TAIFISH-R--LASVkmADRIIHLKDG 481
Cdd:COG0488 436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIET--------LEALEEAlddfpgTVLLVSHdRyfLDRV--ATRILEFEDG 505
|
....
gi 2105575177 482 QILE 485
Cdd:COG0488 506 GVRE 509
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
282-494 |
3.21e-21 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 92.61 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSE----YV---SVVFQDfvryaL 354
Cdd:cd03218 16 VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARlgigYLpqeASIFRK-----L 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 SVKENIALsdISQIDNLNEIKQTAFLsgaDSFIEALpngydtTLGKVLPN-SIDISGGQWQRIALARSIFKKSKLIILDE 433
Cdd:cd03218 91 TVEENILA--VLEIRGLSKKEREEKL---EELLEEF------HITHLRKSkASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 434 PTAALDPKTEAYVFEKFRELTENKTAIFIS-HRL-ASVKMADRIIHLKDGQILEEGSHKELMA 494
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVrETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
282-483 |
4.69e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 96.29 E-value: 4.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKD----LCQidENELSEYVSV---VFQDFVRY-- 352
Cdd:COG0488 14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGLrigyLPQ--EPPLDDDLTVldtVLDGDAELra 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 353 ------ALSVKENIALSDISQIDNLneikQTAFLSG----ADSFIEALPNGydttLGkvLPNSI------DISGGQWQRI 416
Cdd:COG0488 92 leaeleELEAKLAEPDEDLERLAEL----QEEFEALggweAEARAEEILSG----LG--FPEEDldrpvsELSGGWRRRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 417 ALARSIFKKSKLIILDEPTAALDPKT----EAYVfekfreLTENKTAIFISH-R--LASVkmADRIIHLKDGQI 483
Cdd:COG0488 162 ALARALLSEPDLLLLDEPTNHLDLESiewlEEFL------KNYPGTVLVVSHdRyfLDRV--ATRILELDRGKL 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
265-493 |
6.48e-21 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 92.07 E-value: 6.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQD--------------FVRYALSvKENIALSDISQID------NLNEIkqtaflsgADSFIEALpngydttlgkvlpn 404
Cdd:COG4604 80 LRQEnhinsrltvrelvaFGRFPYS-KGRLTAEDREIIDeaiaylDLEDL--------ADRYLDEL-------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 405 sidiSGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRL--ASVkMADRIIHLKD 480
Cdd:COG4604 137 ----SGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADelGKTVVIVLHDInfASC-YADHIVAMKD 211
|
250
....*....|...
gi 2105575177 481 GQILEEGSHKELM 493
Cdd:COG4604 212 GRVVAQGTPEEII 224
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
280-492 |
8.79e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.13 E-value: 8.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 280 YSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSeyVSVVFQDFVRYA-LSVKE 358
Cdd:PRK11607 33 HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP--INMMFQSYALFPhMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 359 NIALSdisqidnlneIKQTAFLSG--ADSFIEALPNGYDTTLGKVLPNSIdiSGGQWQRIALARSIFKKSKLIILDEPTA 436
Cdd:PRK11607 111 NIAFG----------LKQDKLPKAeiASRVNEMLGLVHMQEFAKRKPHQL--SGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 437 ALDPKTEAYVFEKFRELTE--NKTAIFISH-RLASVKMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK11607 179 ALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
281-492 |
1.52e-20 |
|
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: 90.12 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 281 SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQiDENELSEYVSVVFQDF-VRYALSVKEN 359
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQDLsVDDELTGWEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 360 IALSdiSQIDNLNEIKQTAFLSGADSFIEaLPNGYDTTLGKvlpnsidISGGQWQRIALARSIFKKSKLIILDEPTAALD 439
Cdd:cd03265 94 LYIH--ARLYGVPGAERRERIDELLDFVG-LLEAADRLVKT-------YSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2105575177 440 PKTEAYVFEKFREL--TENKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKEL 492
Cdd:cd03265 164 PQTRAHVWEYIEKLkeEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
282-515 |
1.88e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 94.48 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGL--YKPTAGNIFLE----------------GKDlCQIDENELSEYV- 342
Cdd:TIGR03269 16 LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverpskvGEP-CPVCGGTLEPEEv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 343 ------SVVFQDFV-RYALSVKENIAL-SDISQIDNLNEIKQTAFLSGADSFIEALPNGYDTTLG-KVLPNSIDISGGQW 413
Cdd:TIGR03269 95 dfwnlsDKLRRRIRkRIAIMLQRTFALyGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLShRITHIARDLSGGEK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 414 QRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASV-KMADRIIHLKDGQILEEGSHK 490
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIeDLSDKAIWLENGEIKEEGTPD 254
|
250 260
....*....|....*....|....*
gi 2105575177 491 ELMAlkgeyynMYMTQAKWFDGQRE 515
Cdd:TIGR03269 255 EVVA-------VFMEGVSEVEKECE 272
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
282-504 |
2.08e-20 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 95.36 E-value: 2.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKdlcqidenelseyvsVVFQDFVRYAL--SVKEN 359
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR---------------ISFSPQTSWIMpgTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 360 IALSDisqidNLNEIKQTAFLSGA--DSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFKKSKLIILDEPTAA 437
Cdd:TIGR01271 507 IIFGL-----SYDEYRYTSVIKACqlEEDIALFPEKDKTVLGE---GGITLSGGQRARISLARAVYKDADLYLLDSPFTH 578
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 438 LDPKTEAYVFEK-FRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALKGEYYNMYM 504
Cdd:TIGR01271 579 LDVVTEKEIFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLL 646
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
282-486 |
2.22e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 90.26 E-value: 2.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY----VSVVFQ------DFVr 351
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELrnqkLGFIYQfhhllpDFT- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 352 yALsvkENIALSDISQIDNLNEIKQTAFLSGADSFIEALPNGYDTTLgkvlpnsidiSGGQWQRIALARSIFKKSKLIIL 431
Cdd:PRK11629 104 -AL---ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSEL----------SGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 432 DEPTAALDPKTEAYVFEKFRELTENKTAIF--ISHRLASVKMADRIIHLKDGQILEE 486
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQGTAFlvVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
282-487 |
2.68e-20 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 92.98 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDF-VRYALSVKENI 360
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTsLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 361 ALS---DISQIDNLNEIKQTAflsgADSFIEAlpngydTTLGKVLPNSID-ISGGQWQRIALARSIFKKSKLIILDEPTA 436
Cdd:PRK09536 99 EMGrtpHRSRFDTWTETDRAA----VERAMER------TGVAQFADRPVTsLSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 437 ALDPKTEAYVFEKFRELTEN-KTAIFISHRL-ASVKMADRIIHLKDGQILEEG 487
Cdd:PRK09536 169 SLDINHQVRTLELVRRLVDDgKTAVAAIHDLdLAARYCDELVLLADGRVRAAG 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
282-482 |
2.89e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 89.42 E-value: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFL----EGKDLCQIDENELSE-------YVSvvfQdFV 350
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASPREILAlrrrtigYVS---Q-FL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 351 R---------------YALSVKENIALSDISQI-DNLNeIKqtaflsgadsfiEALPNGYDTTLgkvlpnsidiSGGQWQ 414
Cdd:COG4778 103 RviprvsaldvvaeplLERGVDREEARARARELlARLN-LP------------ERLWDLPPATF----------SGGEQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 415 RIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIF-ISHRLASVK-MADRIIHLKDGQ 482
Cdd:COG4778 160 RVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREaVADRVVDVTPFS 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
282-494 |
3.72e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 90.03 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE-------------LSEYVSVVFQD 348
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrlLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 349 FVRYA-LSVKENIALSDIsqidnlneikQTAFLSGADSFIEAL----PNGYDTTLGKVLPnsIDISGGQWQRIALARSIF 423
Cdd:PRK10619 101 FNLWShMTVLENVMEAPI----------QVLGLSKQEARERAVkylaKVGIDERAQGKYP--VHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 424 KKSKLIILDEPTAALDPKTEAYVFEKFRELTEN-KTAIFISHRLASVK-MADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
282-492 |
5.08e-20 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 88.74 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSE----YVSVVFQDFVRyaLSVK 357
Cdd:TIGR03410 16 LRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARagiaYVPQGREIFPR--LTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENIalsdisqidnlneikqtafLSGAdsfiEALPNGydttlGKVLPNSI----------------DISGGQWQRIALARS 421
Cdd:TIGR03410 94 ENL-------------------LTGL----AALPRR-----SRKIPDEIyelfpvlkemlgrrggDLSGGQQQQLAIARA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 422 IFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKT-AIFISHRLASVKM--ADRIIHLKDGQILEEGSHKEL 492
Cdd:TIGR03410 146 LVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARelADRYYVMERGRVVASGAGDEL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
282-493 |
5.63e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 92.02 E-value: 5.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY----VSVVFQDFVRYA-LSV 356
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVrrkkIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 KENIALSDISQIDNLNEIKQTAFLSGADSFIEALPNGYdttlgkvlPNsiDISGGQWQRIALARSIFKKSKLIILDEPTA 436
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSY--------PD--ELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 437 ALDPKTEAYVFEKFREL--TENKTAIFISHRL-ASVKMADRIIHLKDGQILEEGSHKELM 493
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLqaKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
281-494 |
7.90e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 89.46 E-value: 7.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 281 SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDfVRYALSVKENi 360
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQD-PSTSLNPRQR- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 361 alsdISQIDNLNEIKQTAFLSgadsfiEALPNGYDTTLGKV--LPNSID-----ISGGQWQRIALARSIFKKSKLIILDE 433
Cdd:PRK15112 106 ----ISQILDFPLRLNTDLEP------EQREKQIIETLRQVglLPDHASyyphmLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 434 PTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASVK-MADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELQEKQgiSYIYVTQHLGMMKhISDQVLVMHQGEVVERGSTADVLA 239
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
277-492 |
1.10e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.09 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 277 SNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQ--DFVRYAL 354
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQnpDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 SVKENIALSDISQidNLNE------IKQTAFLSGADSFIEALPNgydttlgkvlpnsiDISGGQWQRIALARSIFKKSKL 428
Cdd:PRK13652 95 TVEQDIAFGPINL--GLDEetvahrVSSALHMLGLEELRDRVPH--------------HLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 429 IILDEPTAALDPKTEAYVFEKFRELTEN--KTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
263-476 |
1.22e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.77 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 263 ANISLKHVYFKYPLSNGY--SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENElse 340
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 341 yvSVVFQDfvrYAL----SVKENIAL---------SDISQI--DNLNEIKQTAFlsgADSFIEALpngydttlgkvlpns 405
Cdd:COG4525 79 --GVVFQK---DALlpwlNVLDNVAFglrlrgvpkAERRARaeELLALVGLADF---ARRRIWQL--------------- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 406 idiSGGQWQRIALARSIFKKSKLIILDEPTAALDpkteAYVFEKFREL------TENKTAIFISHrlaSVK----MADRI 475
Cdd:COG4525 136 ---SGGMRQRVGIARALAADPRFLLMDEPFGALD----ALTREQMQELlldvwqRTGKGVFLITH---SVEealfLATRL 205
|
.
gi 2105575177 476 I 476
Cdd:COG4525 206 V 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
265-481 |
1.32e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.77 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNgySLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY-VS 343
Cdd:PRK09700 6 ISMAGIGKSFGPVH--ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 344 VVFQDF-VRYALSVKENIALS--------DISQIDnLNEIKQTAFLSgadSFIEALPNGYDTTLGkvlpnsiDISGGQWQ 414
Cdd:PRK09700 84 IIYQELsVIDELTVLENLYIGrhltkkvcGVNIID-WREMRVRAAMM---LLRVGLKVDLDEKVA-------NLSISHKQ 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 415 RIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL-TENKTAIFISHRLASVK-MADRIIHLKDG 481
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLrKEGTAIVYISHKLAEIRrICDRYTVMKDG 221
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
272-500 |
1.80e-19 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 1.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 272 FKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTT----LIQLIiglykPTAGNIFLEGKDLCQIDENELSEY---VSV 344
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVrhrIQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDfvryalsvkENIALS---DISQI--DNLnEIKQTAfLSGA---DSFIEALPN-GYDTTLGKVLPNsiDISGGQWQR 415
Cdd:PRK15134 367 VFQD---------PNSSLNprlNVLQIieEGL-RVHQPT-LSAAqreQQVIAVMEEvGLDPETRHRYPA--EFSGGQRQR 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 416 IALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASVK-MADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK15134 434 IAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHqlAYLFISHDLHVVRaLCHQVIVLRQGEVVEQGDCERV 513
|
....*...
gi 2105575177 493 MALKGEYY 500
Cdd:PRK15134 514 FAAPQQEY 521
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
259-478 |
2.07e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 87.08 E-value: 2.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 259 KSDTANISLKHVYFKypLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENEL 338
Cdd:PRK10247 2 QENSPLLQLQNVGYL--AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 339 SEYVSVVFQDFVRYALSVKENIALSdiSQIDNlNEIKQTAFLSGADSFieALPngyDTTLGKvlpNSIDISGGQWQRIAL 418
Cdd:PRK10247 80 RQQVSYCAQTPTLFGDTVYDNLIFP--WQIRN-QQPDPAIFLDDLERF--ALP---DTILTK---NIAELSGGEKQRISL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2105575177 419 ARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASVKMADRIIHL 478
Cdd:PRK10247 149 IRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDEINHADKVITL 210
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
282-482 |
2.39e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 90.76 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYkPTA---GNIFLEGKDL--CQIDENELSEyVSVVFQDF--VRYaL 354
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELqaSNIRDTERAG-IAIIHQELalVKE-L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 SVKENIALSdisqidnlNEIKQTAFLSGADSFIEAlpngyDTTLGKVlpnSIDIS---------GGQWQRIALARSIFKK 425
Cdd:PRK13549 98 SVLENIFLG--------NEITPGGIMDYDAMYLRA-----QKLLAQL---KLDINpatpvgnlgLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 426 SKLIILDEPTAALDPKTEAYVFEKFRELTENKTA-IFISHRLASVK-MADRIIHLKDGQ 482
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIAcIYISHKLNEVKaISDTICVIRDGR 220
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
285-493 |
2.56e-19 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 87.30 E-value: 2.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 285 INLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYkPTAGNIFLEGKDLCQIDENELSEY-------VSVVFQ-DFVRY-ALS 355
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHraylsqqQTPPFAmPVFQYlTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 356 VKENIALSDISqiDNLNEIkqtaflsgadsfIEALpngydtTLGKVLPNSID-ISGGQWQRIALA-------RSIFKKSK 427
Cdd:PRK03695 94 QPDKTRTEAVA--SALNEV------------AEAL------GLDDKLGRSVNqLSGGEWQRVRLAavvlqvwPDINPAGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 428 LIILDEPTAALDPKTEAYVFEKFRELTENKTAIFIS-HRLA-SVKMADRIIHLKDGQILEEGSHKELM 493
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSELCQQGIAVVMSsHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
282-487 |
4.42e-19 |
|
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: 85.30 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGL--YKPTAGNIFLEGKdlcQIDENELSEYVSVVFQDFVRYA-LSVKE 358
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGR---PLDKRSFRKIIGYVPQDDILHPtLTVRE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 359 NIALSdisqidnlneikqtAFLSGadsfiealpngydttlgkvlpnsidISGGQWQRIALARSIFKKSKLIILDEPTAAL 438
Cdd:cd03213 102 TLMFA--------------AKLRG-------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2105575177 439 DPKTEAYVFEKFRELT-ENKTAIFISHRLAS--VKMADRIIHLKDGQILEEG 487
Cdd:cd03213 143 DSSSALQVMSLLRRLAdTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
284-494 |
4.88e-19 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 88.62 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 284 DINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcQIDENELSE-----YVSVVFQDfvryA----- 353
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVL-QDSARGIFLpphrrRIGYVFQE----Arlfph 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 354 LSVKENIALSdisqidnlneIKQTAFLSGADSF--------IEALPNGYDTTLgkvlpnsidiSGGQWQRIALARSIFKK 425
Cdd:COG4148 92 LSVRGNLLYG----------RKRAPRAERRISFdevvellgIGHLLDRRPATL----------SGGERQRVAIGRALLSS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 426 SKLIILDEPTAALDP--KTE--AYvFEKFREltenKTAI---FISHRLASV-KMADRIIHLKDGQILEEGSHKELMA 494
Cdd:COG4148 152 PRLLLMDEPLAALDLarKAEilPY-LERLRD----ELDIpilYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
282-494 |
6.05e-19 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 90.95 E-value: 6.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENI- 360
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLd 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 361 ALSDISQIDnLNEIKQTAFLSGAdsfIEALPNGYDttlGKVLPNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDP 440
Cdd:PLN03130 1335 PFNEHNDAD-LWESLERAHLKDV---IRRNSLGLD---AEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDV 1407
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 441 KTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PLN03130 1408 RTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLS 1461
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
276-493 |
8.64e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.84 E-value: 8.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 276 LSNGYS----LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQD-FV 350
Cdd:PRK11231 8 LTVGYGtkriLNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHhLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 351 RYALSVKENIA------LS---DISQIDNlnEIKQTAFlsgADSFIEALPNGYDTtlgkvlpnsiDISGGQWQRIALARS 421
Cdd:PRK11231 88 PEGITVRELVAygrspwLSlwgRLSAEDN--ARVNQAM---EQTRINHLADRRLT----------DLSGGQRQRAFLAMV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 422 IFKKSKLIILDEPTAALDPKTEAYVFEKFREL-TENKTAIFISHRL--ASvKMADRIIHLKDGQILEEGSHKELM 493
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLnqAS-RYCDHLVVLANGHVMAQGTPEEVM 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
282-493 |
9.80e-19 |
|
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: 84.50 E-value: 9.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGL--YKPTAGNIFLEGKDLCQIDENELS------------EYVSVVFQ 347
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERArlgiflafqyppEIPGVKNA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 348 DFVRYalsvkenialsdisqidnLNEikqtaflsgadSFiealpngydttlgkvlpnsidiSGGQWQRIALARSIFKKSK 427
Cdd:cd03217 96 DFLRY------------------VNE-----------GF----------------------SGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105575177 428 LIILDEPTAALDP---KTEAYVFEKFREltENKTAIFISH--RLASVKMADRIIHLKDGQILEEGShKELM 493
Cdd:cd03217 125 LAILDEPDSGLDIdalRLVAEVINKLRE--EGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELA 192
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
281-494 |
1.30e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.93 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 281 SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE-LSEYVSVVFQD---FVRyaLSV 356
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKiMREAVAIVPEGrrvFSR--MTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 KENIALSdisqidnlneikqtAFLSGADSFIEALPNGYD---TTLGKVLPNSIDISGGQWQRIALARSIFKKSKLIILDE 433
Cdd:PRK11614 98 EENLAMG--------------GFFAERDQFQERIKWVYElfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 434 PTAALDPKTEAYVFEKFRELTENKTAIFISHRLA--SVKMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnqALKLADRGYVLENGHVVLEDTGDALLA 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
285-495 |
1.32e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 88.71 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 285 INLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNI-FLEGKDLcqIDENEL--------SEYVSVVFQDFVRYA-L 354
Cdd:TIGR03269 303 VSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEW--VDMTKPgpdgrgraKRYIGILHQEYDLYPhR 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 SVKENIALS-DISQIDNLNEIKQTAFLSGAdsfiealpnGYDTTLGK-VLPNSID-ISGGQWQRIALARSIFKKSKLIIL 431
Cdd:TIGR03269 381 TVLDNLTEAiGLELPDELARMKAVITLKMV---------GFDEEKAEeILDKYPDeLSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 432 DEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASVKM-ADRIIHLKDGQILEEGSHKELMAL 495
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
265-491 |
1.99e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.16 E-value: 1.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYpLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE---LSEY 341
Cdd:PRK10908 2 IRFEHVSKAY-LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 VSVVFQD-FVRYALSVKENIALSDISQIDNLNEIKQTafLSGADSFIEALPNgydttlGKVLPnsIDISGGQWQRIALAR 420
Cdd:PRK10908 81 IGMIFQDhHLLMDRTVYDNVAIPLIIAGASGDDIRRR--VSAALDKVGLLDK------AKNFP--IQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 421 SIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE-NKTAIFISHRLASVKMAD-RIIHLKDGQiLEEGSHKE 491
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSyRMLTLSDGH-LHGGVGGE 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
282-494 |
2.30e-18 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 87.82 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKT----TLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY----VSVVFQdfvrya 353
Cdd:COG4172 26 VKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRIrgnrIAMIFQ------ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 354 lsvkE-----NIALSDISQIDNLNEIKQTafLSGADSFIEALpngydTTLGKV-LPNS---ID-----ISGGQWQRIALA 419
Cdd:COG4172 100 ----EpmtslNPLHTIGKQIAEVLRLHRG--LSGAAARARAL-----ELLERVgIPDPerrLDayphqLSGGQRQRVMIA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 420 RSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL-TENKTAI-FISHRLASV-KMADRIIHLKDGQILEEGSHKELMA 494
Cdd:COG4172 169 MALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALlLITHDLGVVrRFADRVAVMRQGEIVEQGPTAELFA 246
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
265-494 |
2.39e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 85.14 E-value: 2.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPL-SNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVS 343
Cdd:PRK13642 5 LEVENLVFKYEKeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 344 VVFQD----FVryALSVKENIALSDISQidnlnEIKQTAFLSGADSFIEALpngydTTLGKVLPNSIDISGGQWQRIALA 419
Cdd:PRK13642 85 MVFQNpdnqFV--GATVEDDVAFGMENQ-----GIPREEMIKRVDEALLAV-----NMLDFKTREPARLSGGQKQRVAVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 420 RSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
282-485 |
2.53e-18 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 87.54 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYkPTA---GNIFLEGKdLCQIDENELSEYVSVVF--QDF--VRYaL 354
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGE-VCRFKDIRDSEALGIVIihQELalIPY-L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 SVKENIALSdisqidnlNEIKQTAFLSGADSFIEAlpngyDTTLGKV----LPNSI--DISGGQWQRIALARSIFKKSKL 428
Cdd:NF040905 94 SIAENIFLG--------NERAKRGVIDWNETNRRA-----RELLAKVgldeSPDTLvtDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 429 IILDEPTAALDPKTEAYVFEKFRELTENK-TAIFISHRLASV-KMADRIIHLKDGQILE 485
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGiTSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
282-507 |
2.56e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 84.73 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENelseyVSVVFQDfVRYA--LSVKEN 359
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED-----TRLMFQD-ARLLpwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 360 IALSdisqidnlneikqtafLSGA--DSFIEAL--------PNGYDTTLgkvlpnsidiSGGQWQRIALARSIFKKSKLI 429
Cdd:PRK11247 102 VGLG----------------LKGQwrDAALQALaavgladrANEWPAAL----------SGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 430 ILDEPTAALDPKTEAyvfeKFRELTENK------TAIFISHRLA-SVKMADRIIHLKDGQI-LE----------EGSHKe 491
Cdd:PRK11247 156 LLDEPLGALDALTRI----EMQDLIESLwqqhgfTVLLVTHDVSeAVAMADRVLLIEEGKIgLDltvdlprprrRGSAR- 230
|
250
....*....|....*.
gi 2105575177 492 LMALKGEYYNMYMTQA 507
Cdd:PRK11247 231 LAELEAEVLQRVMSRG 246
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
282-463 |
3.62e-18 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 82.47 E-value: 3.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcQIDENELSEY---VSVVFQDFVR--YALSV 356
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLERrqrVGLVFQDPDDqlFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 KENIALSDISQidNLNEIKQTAFLSGADSFIEALpnGYDTTLGKVLpnsidiSGGQWQRIALARSIFKKSKLIILDEPTA 436
Cdd:TIGR01166 87 DQDVAFGPLNL--GLSEAEVERRVREALTAVGAS--GLRERPTHCL------SGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180
....*....|....*....|....*..
gi 2105575177 437 ALDPKTEAYVFEKFRELTENKTAIFIS 463
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAEGMTVVIS 183
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
293-451 |
5.17e-18 |
|
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: 82.54 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 293 EKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENI----ALSDISQI 368
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLrfwhADHSDEQV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 369 -DNLNEIKQTAFlsgadsfiEALPNGYdttlgkvlpnsidISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVF 447
Cdd:cd03231 107 eEALARVGLNGF--------EDRPVAQ-------------LSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFA 165
|
....
gi 2105575177 448 EKFR 451
Cdd:cd03231 166 EAMA 169
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
282-493 |
7.66e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.97 E-value: 7.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYkPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFV-RYALSVKENI 360
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQQSpPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 361 ALSDISQIDNLNEIKQTAFLSgadsfiEALpngydtTLGKVLPNSID-ISGGQWQRIALARSIFK-------KSKLIILD 432
Cdd:COG4138 91 ALHQPAGASSEAVEQLLAQLA------EAL------GLEDKLSRPLTqLSGGEWQRVRLAAVLLQvwptinpEGQLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 433 EPTAALDPKTEAYVFEKFRELTENKTAIFIS-HRLA-SVKMADRIIHLKDGQILEEGSHKELM 493
Cdd:COG4138 159 EPMNSLDVAQQAALDRLLRELCQQGITVVMSsHDLNhTLRHADRVWLLKQGKLVASGETAEVM 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
265-482 |
7.96e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 80.19 E-value: 7.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIflegkdlcqidenelseyvsv 344
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 vfqdfvryalSVKENIALSDISQidnlneikqtaflsgadsfiealpngydttlgkvlpnsidISGGQWQRIALARSIFK 424
Cdd:cd03221 58 ----------TWGSTVKIGYFEQ----------------------------------------LSGGEKMRLALAKLLLE 87
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2105575177 425 KSKLIILDEPTAALDPKTEAYVFEKFRELteNKTAIFISH-R--LASVkmADRIIHLKDGQ 482
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIEALEEALKEY--PGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
281-488 |
1.01e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 281 SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNI----FLEGKDLCQIDENELSEYVSVVFQdFVRYALSv 356
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIKPVRKKVGVVFQ-FPESQLF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 kENIALSDIS-QIDNLNEIKQTAFLSGADSfIEALpnGYDTTLGKVLPnsIDISGGQWQRIALARSIFKKSKLIILDEPT 435
Cdd:PRK13643 99 -EETVLKDVAfGPQNFGIPKEKAEKIAAEK-LEMV--GLADEFWEKSP--FELSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 436 AALDPKTEAYVFEKFRELTEN-KTAIFISHRLASV-KMADRIIHLKDGQILEEGS 488
Cdd:PRK13643 173 AGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGT 227
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
293-441 |
1.16e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 81.25 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 293 EKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENialsdisqIDNLN 372
Cdd:TIGR01189 27 EALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN--------LHFWA 98
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 373 EIKQTAFLSGADSFIEALPNGYDTTLGKVLpnsidiSGGQWQRIALARSIFKKSKLIILDEPTAALDPK 441
Cdd:TIGR01189 99 AIHGGAQRTIEDALAAVGLTGFEDLPAAQL------SAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
282-492 |
1.38e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 83.23 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDenelseyvsvvfQDFVRY--------- 352
Cdd:COG4152 17 VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED------------RRRIGYlpeerglyp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 353 ALSVKENIA----LSDISQIDNLNEIKQ--TAF-LSG-ADSFIEALpngydttlgkvlpnsidiSGGQWQRIALARSIFK 424
Cdd:COG4152 85 KMKVGEQLVylarLKGLSKAEAKRRADEwlERLgLGDrANKKVEEL------------------SKGNQQKVQLIAALLH 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2105575177 425 KSKLIILDEPTAALDP------KTEayvfekFRELTEN-KTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKEL 492
Cdd:COG4152 147 DPELLILDEPFSGLDPvnvellKDV------IRELAAKgTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
282-492 |
1.49e-17 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 86.37 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENIa 361
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDGTVRQNV- 1404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 362 lsdisqidnlneikqtaflsgaDSFIEALP--------------------NGYDTtlgKVLPNSIDISGGQWQRIALARS 421
Cdd:PTZ00243 1405 ----------------------DPFLEASSaevwaalelvglrervasesEGIDS---RVLEGGSNYSVGQRQLMCMARA 1459
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2105575177 422 IFKK-SKLIILDEPTA----ALDPKTEAYVFEKFreltENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKEL 492
Cdd:PTZ00243 1460 LLKKgSGFILMDEATAnidpALDRQIQATVMSAF----SAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
285-492 |
1.70e-17 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 83.64 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 285 INLEIKDKEKVAIVGHNGSGKTTLIQLIIGLY----KPTAGNIFLEGKDLCQIDENE----LSEYVSVVFQDFVR----- 351
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKErrnlVGAEVAMIFQDPMTslnpc 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 352 YALSVKENIALSdISQIDNLNEIKQTAflsgadsfIEALpngydTTLGKVLPNS-IDI-----SGGQWQRIALARSIFKK 425
Cdd:PRK11022 106 YTVGFQIMEAIK-VHQGGNKKTRRQRA--------IDLL-----NQVGIPDPASrLDVyphqlSGGMSQRVMIAMAIACR 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 426 SKLIILDEPTAALDPKTEAYVFEKFRELT--ENKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAQIIELLLELQqkENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
262-466 |
1.81e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 82.14 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 262 TANISlkhVYFkyplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQ-------LIIGLYkpTAGNIFLEGKDL--CQ 332
Cdd:PRK14243 13 TENLN---VYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNLyaPD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 333 IDENELSEYVSVVFQDFVRYALSVKENIALSdiSQID----NLNEIKQTAFLSGADsfiealpngYDTTLGKVLPNSIDI 408
Cdd:PRK14243 84 VDPVEVRRRIGMVFQKPNPFPKSIYDNIAYG--ARINgykgDMDELVERSLRQAAL---------WDEVKDKLKQSGLSL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 409 SGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRL 466
Cdd:PRK14243 153 SGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
271-481 |
2.19e-17 |
|
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: 81.22 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 271 YFKYPlSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQ---IDENELSEYvSVVFQ 347
Cdd:cd03290 7 YFSWG-SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEpsfEATRSRNRY-SVAYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 348 DFVRYAL--SVKENIALSDISqidNLNEIKQTAFLSGADSFIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFKK 425
Cdd:cd03290 85 AQKPWLLnaTVEENITFGSPF---NKQRYKAVTDACSLQPDIDLLPFGDQTEIGE---RGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 426 SKLIILDEPTAALDPKTEAYVFEK--FRELTENK-TAIFISHRLASVKMADRIIHLKDG 481
Cdd:cd03290 159 TNIVFLDDPFSALDIHLSDHLMQEgiLKFLQDDKrTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
278-476 |
2.96e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 81.30 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 278 NGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcqideNELSEYVSVVFQDFVRYALSVK 357
Cdd:cd03237 11 GEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-----SYKPQYIKADYEGTVRDLLSSI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENIALSDiSQIDnlNEIKQtaflsgadsfiealPNGYDTTLGKVLPnsiDISGGQWQRIALARSIFKKSKLIILDEPTAA 437
Cdd:cd03237 86 TKDFYTH-PYFK--TEIAK--------------PLQIEQILDREVP---ELSGGELQRVAIAACLSKDADIYLLDEPSAY 145
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2105575177 438 LDPKTEAYVFEKFRELTEN--KTAIFISHRLASVKM-ADRII 476
Cdd:cd03237 146 LDVEQRLMASKVIRRFAENneKTAFVVEHDIIMIDYlADRLI 187
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
268-492 |
3.66e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 82.59 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 268 KHVYFKYPLSNGYSLKDINLEIKDKEKVA--------------------IVGHNGSGKTTLIQLIIGLYKPTAGNIFLE- 326
Cdd:PRK13631 8 KKLKVPNPLSDDIILRVKNLYCVFDEKQEnelvalnnisytfeknkiyfIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 327 ---GKDLCQIDEN------------ELSEYVSVVFQdFVRYAL---SVKENIALSDISQIDNLNEIKQTA--FLSG---A 383
Cdd:PRK13631 88 iyiGDKKNNHELItnpyskkiknfkELRRRVSMVFQ-FPEYQLfkdTIEKDIMFGPVALGVKKSEAKKLAkfYLNKmglD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 384 DSFIEALPNGydttlgkvlpnsidISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL-TENKTAIFI 462
Cdd:PRK13631 167 DSYLERSPFG--------------LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVI 232
|
250 260 270
....*....|....*....|....*....|.
gi 2105575177 463 SHRLASV-KMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK13631 233 THTMEHVlEVADEVIVMDKGKILKTGTPYEI 263
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
281-482 |
5.35e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 83.72 E-value: 5.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 281 SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYkPTA---GNIFLEGKDL--CQIDENElSEYVSVVFQDFVRYA-L 354
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLkaSNIRDTE-RAGIVIIHQELTLVPeL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 SVKENIALSdisqidnlNEIKQTAFLSGADSFIEALPNGYDTTLGKVLPNSI---DISGGQWQRIALARSIFKKSKLIIL 431
Cdd:TIGR02633 94 SVAENIFLG--------NEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRpvgDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 432 DEPTAALDPKTEAYVFEKFRELTENKTA-IFISHRLASVK-MADRIIHLKDGQ 482
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAHGVAcVYISHKLNEVKaVCDTICVIRDGQ 218
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
261-492 |
5.55e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.86 E-value: 5.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 261 DTANISLKHVYfkypLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLI---IGLYKP---TAGNIFLEGKDLCQID 334
Cdd:PRK14246 9 DVFNISRLYLY----INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLnrlIEIYDSkikVDGKVLYFGKDIFQID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 335 ENELSEYVSVVFQDFVRYA-LSVKENIALSDISQ-IDNLNEIKQtaFLSGADSFIEALPNGYDttlgKVLPNSIDISGGQ 412
Cdd:PRK14246 85 AIKLRKEVGMVFQQPNPFPhLSIYDNIAYPLKSHgIKEKREIKK--IVEECLRKVGLWKEVYD----RLNSPASQLSGGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 413 WQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKE 491
Cdd:PRK14246 159 QQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNE 238
|
.
gi 2105575177 492 L 492
Cdd:PRK14246 239 I 239
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
282-478 |
6.12e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.81 E-value: 6.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGkdlcqidenelSEYVSVVFQdfvRYA------LS 355
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQ---RSEvpdslpLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 356 VKENIALSDISQIDNLNEIKQTAFLSGADSfIEALpngydtTLGKVLPNSID-ISGGQWQRIALARSIFKKSKLIILDEP 434
Cdd:NF040873 74 VRDLVAMGRWARRGLWRRLTRDDRAAVDDA-LERV------GLADLAGRQLGeLSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2105575177 435 TAALDPKTEAYVFEKFRELTENKTAIF-ISHRLASVKMADRIIHL 478
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVvVTHDLELVRRADPCVLL 191
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
58-482 |
6.15e-17 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 83.70 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 58 SMHVLQLCITIVSYIGFLffihWGL------VVLGILASIPAFIIQYKFGYS-----------------NFNLNRlqsgl 114
Cdd:COG4178 145 SLGLLSSVVTLISFIGIL----WSLsgsltfTLGGYSITIPGYMVWAALIYAiigtllthligrplirlNFEQQR----- 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 115 mREASYINSLFRNKQSIKEIKLFRSGNflinRWRKLTTSNNKKILKLFFKQNWANIGLDSLTAVlYSMSAVLMVWLLKL- 193
Cdd:COG4178 216 -READFRFALVRVRENAESIALYRGEA----AERRRLRRRFDAVIANWRRLIRRQRNLTFFTTG-YGQLAVIFPILVAAp 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 194 ----GKMNIGSFVSTAQAIQGLQGTVnqtshllaSLFESNlyIKDFFDF---IE-----YQNEDDAKKEKLEKNIANKSD 261
Cdd:COG4178 290 ryfaGEITLGGLMQAASAFGQVQGAL--------SWFVDN--YQSLAEWratVDrlagfEEALEAADALPEAASRIETSE 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 262 TANISLKHVYFKypLSNGYSL-KDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFL-EGKDLCqidenels 339
Cdd:COG4178 360 DGALALEDLTLR--TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL-------- 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 340 eyvsvvfqdFV-----------RYALS---VKENIALSDISQIdnLNEIkqtaflsGADSFIEALpngyDTTL--GKVLp 403
Cdd:COG4178 430 ---------FLpqrpylplgtlREALLypaTAEAFSDAELREA--LEAV-------GLGHLAERL----DEEAdwDQVL- 486
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 404 nsidiSGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQ 482
Cdd:COG4178 487 -----SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
282-491 |
1.49e-16 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 78.59 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQideNELSEYVSVVFQDFVRYALSVKENIA 361
Cdd:TIGR03740 16 VNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR---KDLHKIGSLIESPPLYENLTARENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 362 LsdisqidnlneikQTAFLSGADSFIEALPNGYDTTLGKVLPNSiDISGGQWQRIALARSIFKKSKLIILDEPTAALDPk 441
Cdd:TIGR03740 93 V-------------HTTLLGLPDSRIDEVLNIVDLTNTGKKKAK-QFSLGMKQRLGIAIALLNHPKLLILDEPTNGLDP- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2105575177 442 teaYVFEKFREL-----TENKTAIFISHRLASVK-MADRIIHLKDGQILEEGSHKE 491
Cdd:TIGR03740 158 ---IGIQELRELirsfpEQGITVILSSHILSEVQqLADHIGIISEGVLGYQGKINK 210
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
257-494 |
1.58e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 79.75 E-value: 1.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 257 ANKSDTANISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLI------IGLYKpTAGNIFLEGKDL 330
Cdd:PRK14271 12 AADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYR-YSGDVLLGGRSI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 331 CQI-DENELSEYVSVVFQDFVRYALSVKENIalsdISQIDNLNEIKQTAFLSGADSFIEALpNGYDTTLGKVLPNSIDIS 409
Cdd:PRK14271 91 FNYrDVLEFRRRVGMLFQRPNPFPMSIMDNV----LAGVRAHKLVPRKEFRGVAQARLTEV-GLWDAVKDRLSDSPFRLS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 410 GGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLA-SVKMADRIIHLKDGQILEEGS 488
Cdd:PRK14271 166 GGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGP 245
|
....*.
gi 2105575177 489 HKELMA 494
Cdd:PRK14271 246 TEQLFS 251
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
284-487 |
1.61e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.20 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 284 DINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSE------------YVSVVFQDFVR 351
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEaerrrllrtewgFVHQHPRDGLR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 352 YALSVKENIA--LSDISQiDNLNEIKQTAflsgadsfiealpngyDTTLGKVL--PNSID-----ISGGQWQRIALARSI 422
Cdd:PRK11701 104 MQVSAGGNIGerLMAVGA-RHYGDIRATA----------------GDWLERVEidAARIDdlpttFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 423 FKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASVKM-ADRIIHLKDGQILEEG 487
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
282-494 |
1.81e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 82.00 E-value: 1.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY-VSVVFQDFVRYAL----SV 356
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLGRGLvpdmSV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 KENIALSDISQID-------NLNEIKQTaflsgADSFIEAlpngYDttlgkVLPNSIDI-----SGGQWQRIALARSIFK 424
Cdd:COG3845 354 AENLILGRYRRPPfsrggflDRKAIRAF-----AEELIEE----FD-----VRTPGPDTparslSGGNQQKVILARELSR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 425 KSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAI-FISHRLASV-KMADRIIHLKDGQILEEGSHKE--------LMA 494
Cdd:COG3845 420 DPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVlLISEDLDEIlALSDRIAVMYEGRIVGEVPAAEatreeiglLMA 499
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
283-493 |
1.82e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 79.26 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 283 KDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYA-LSVKENIA 361
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQELVA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 362 LSDISQidnlneikQTAFLSGADSFIEALPNGYDTT-LGKVLPNSID-ISGGQWQRIALARSIFKKSKLIILDEPTAALD 439
Cdd:PRK10253 104 RGRYPH--------QPLFTRWRKEDEEAVTKAMQATgITHLADQSVDtLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 440 PKTEAYVFEKFRELTENK--TAIFISHRL-ASVKMADRIIHLKDGQILEEGSHKELM 493
Cdd:PRK10253 176 ISHQIDLLELLSELNREKgyTLAAVLHDLnQACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
285-493 |
2.52e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 79.95 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 285 INLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKP----TAGNIFLEGKDLCQIDENE----LSEYVSVVFQDFVRYalsv 356
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRErrkiIGREIAMIFQEPSSC---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 keniaLSDISQIDnlneikqtaflsgaDSFIEALPNGYDT----------------TLGKV-----------LPNsiDIS 409
Cdd:COG4170 102 -----LDPSAKIG--------------DQLIEAIPSWTFKgkwwqrfkwrkkraieLLHRVgikdhkdimnsYPH--ELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 410 GGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK-TAI-FISHRLASV-KMADRIIHLKDGQILEE 486
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQgTSIlLISHDLESIsQWADTITVLYCGQTVES 240
|
....*..
gi 2105575177 487 GSHKELM 493
Cdd:COG4170 241 GPTEQIL 247
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
282-487 |
6.51e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 76.99 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQiDENELSEYVSVVF--QDFVRYALSVKEN 359
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK-RRKKFLRRIGVVFgqKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 360 IAL-SDISQIDnlneikQTAFLSGADSFIEALpngydtTLGKVLPNSI-DISGGQWQRIALARSIFKKSKLIILDEPTAA 437
Cdd:cd03267 116 FYLlAAIYDLP------PARFKKRLDELSELL------DLEELLDTPVrQLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 438 LDPKTEAYVFEKFRELTENK--TAIFISHRLASV-KMADRIIHLKDGQILEEG 487
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
263-483 |
6.89e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.12 E-value: 6.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 263 ANISLKHVYFKYPlsNGYS-LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDlcqIDENELSEY 341
Cdd:PRK11650 2 AGLKLQAVRKSYD--GKTQvIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV---VNELEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 -VSVVFQDfvrYAL----SVKENIAL---------SDISQidnlnEIKQTAFLSGADSFIEALPNgydttlgkvlpnsiD 407
Cdd:PRK11650 77 dIAMVFQN---YALyphmSVRENMAYglkirgmpkAEIEE-----RVAEAARILELEPLLDRKPR--------------E 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 408 ISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISH-RLASVKMADRIIHLKDGQI 483
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRrlKTTSLYVTHdQVEAMTLADRVVVMNGGVA 213
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
284-486 |
6.94e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.15 E-value: 6.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 284 DINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE-LSEY---VSVVFQD---FVRYalSV 356
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIcLPPEkrrIGYVFQDarlFPHY--KV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 KEN----IALSDISQIDNLneikqTAFLSgadsfIEALPNGYDTTLgkvlpnsidiSGGQWQRIALARSIFKKSKLIILD 432
Cdd:PRK11144 94 RGNlrygMAKSMVAQFDKI-----VALLG-----IEPLLDRYPGSL----------SGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 433 EPTAALD-P-KTE--AYVFEKFRELteNKTAIFISHRLASV-KMADRIIHLKDGQI-----LEE 486
Cdd:PRK11144 154 EPLASLDlPrKREllPYLERLAREI--NIPILYVSHSLDEIlRLADRVVVLEQGKVkafgpLEE 215
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
265-480 |
8.68e-16 |
|
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: 74.88 E-value: 8.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNI-FLEGKDlcqidenelseyvs 343
Cdd:cd03223 1 IELENLSLATP-DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIgMPEGED-------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 344 VVFqdfvryalsvkenialsdisqidnlneIKQTAFLsgadsfiealPNGydtTLGKVL--PNSIDISGGQWQRIALARS 421
Cdd:cd03223 66 LLF---------------------------LPQRPYL----------PLG---TLREQLiyPWDDVLSGGEQQRLAFARL 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 422 IFKKSKLIILDEPTAALDPKTEAYVFEKFRE-LTenkTAIFISHRLASVKMADRIIHLKD 480
Cdd:cd03223 106 LLHKPKFVFLDEATSALDEESEDRLYQLLKElGI---TVISVGHRPSLWKFHDRVLDLDG 162
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
282-494 |
9.58e-16 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 77.15 E-value: 9.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGK---------------DLCQIDEneLSEYVSVVF 346
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdrdgelvpaDRRQLQR--IRTRLGMVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 347 QDFVRYA-LSVKENIALSDIsQIDNLN--EIKQTAflsgadsfiEALpngydttLGKV-LPNSID-----ISGGQWQRIA 417
Cdd:COG4598 102 QSFNLWShMTVLENVIEAPV-HVLGRPkaEAIERA---------EAL-------LAKVgLADKRDaypahLSGGQQQRAA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 418 LARSIFKKSKLIILDEPTAALDPKTEAYVFEKFREL-TENKTAIFISHRLASVK-MADRIIHLKDGQILEEGSHKELMA 494
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLaEEGRTMLVVTHEMGFARdVSSHVVFLHQGRIEEQGPPAEVFG 243
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
274-494 |
1.44e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 77.70 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 274 YPLSNGY--------SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE---LSEYV 342
Cdd:PRK11308 15 YPVKRGLfkperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 343 SVVFQDfvRYAlsvkenialsdisqidNLNEIKQTaflsgadSFIEALPNGYDTTLG------KVL---------PNSID 407
Cdd:PRK11308 95 QIVFQN--PYG----------------SLNPRKKV-------GQILEEPLLINTSLSaaerreKALammakvglrPEHYD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 408 -----ISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN-KTA-IFISHRLASVK-MADRIIHLK 479
Cdd:PRK11308 150 ryphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSyVFISHDLSVVEhIADEVMVMY 229
|
250
....*....|....*
gi 2105575177 480 DGQILEEGSHKELMA 494
Cdd:PRK11308 230 LGRCVEKGTKEQIFN 244
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
265-496 |
1.67e-15 |
|
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: 76.82 E-value: 1.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKpTAGNIFLEGKDLCQIDENELSEYVSV 344
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYALSVKENIalsDISQIDNLNEIKQTAFLSGADSFIEALPNGYDTTL---GKVLpnsidiSGGQWQRIALARS 421
Cdd:cd03289 82 IPQKVFIFSGTFRKNL---DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLvdgGCVL------SHGHKQLMCLARS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 422 IFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMALK 496
Cdd:cd03289 153 VLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEK 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
284-482 |
2.31e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.84 E-value: 2.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 284 DINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDEnelsEYvsvvFQD--FVRYALSVKenia 361
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD----EY----HQDllYLGHQPGIK---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 362 lSDISQIDNLNEIKQTAFLSGADSFIEALPN----GYDTTLGKVLpnsidiSGGQWQRIALARSIFKKSKLIILDEPTAA 437
Cdd:PRK13538 87 -TELTALENLRFYQRLHGPGDDEALWEALAQvglaGFEDVPVRQL------SAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2105575177 438 LDPKTEAYVFEKFRELTENK-TAIFISHRLASVKmADRIIHLKDGQ 482
Cdd:PRK13538 160 IDKQGVARLEALLAQHAEQGgMVILTTHQDLPVA-SDKVRKLRLGQ 204
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
281-492 |
2.64e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.82 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 281 SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLY---KPTAGNIFLEGKDLCQI-----DENELSEYVSVVFQDF-VR 351
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREgrlarDIRKSRANTGYIFQQFnLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 352 YALSVKENIALSDISQIDNLN--------EIKQTAFLSGADSFIEALPNGYDTTLgkvlpnsidiSGGQWQRIALARSIF 423
Cdd:PRK09984 99 NRLSVLENVLIGALGSTPFWRtcfswftrEQKQRALQALTRVGMVHFAHQRVSTL----------SGGQQQRVAIARALM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2105575177 424 KKSKLIILDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRL-ASVKMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK09984 169 QQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVdYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
282-478 |
2.73e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 74.83 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKP---TAGNIFLEGKDLCQIDENElsEYVSVVFQDFVRYA-LSVK 357
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ--RRIGILFQDDLLFPhLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENIALSDISQIdNLNEIKQTAflsgadsfIEALPNGYDTTLGKVLPNSIdiSGGQWQRIALARSIFKKSKLIILDEPTAA 437
Cdd:COG4136 95 ENLAFALPPTI-GRAQRRARV--------EQALEEAGLAGFADRDPATL--SGGQRARVALLRALLAEPRALLLDEPFSK 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2105575177 438 LDP----KTEAYVFEKFRELteNKTAIFISHRLASVKMADRIIHL 478
Cdd:COG4136 164 LDAalraQFREFVFEQIRQR--GIPALLVTHDEEDAPAAGRVLDL 206
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
282-488 |
3.40e-15 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 75.45 E-value: 3.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIG--LYKPTAGNIFLEGKDLCQIDENELS------------EYVSVVFQ 347
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAhlgiflafqypiEIPGVSNA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 348 DFVRYAL-SVKENIALSDISQIDNLNEIKQTAFLSGAD-SFIEALPN-GYdttlgkvlpnsidiSGGQWQRIALARSIFK 424
Cdd:CHL00131 103 DFLRLAYnSKRKFQGLPELDPLEFLEIINEKLKLVGMDpSFLSRNVNeGF--------------SGGEKKRNEILQMALL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 425 KSKLIILDEPTAALDP---KTEAYVFEKFRelTENKTAIFISH--RLASVKMADRIIHLKDGQILEEGS 488
Cdd:CHL00131 169 DSELAILDETDSGLDIdalKIIAEGINKLM--TSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD 235
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
282-492 |
3.77e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY-VSVVFQDFVRYA-LSVKEN 359
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYLVPQEPLLFPnLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 360 IALSDISQIDNLNEIKQtaflsgadsFIEALPNGYDTtlgKVLPNSIDISGGQWQRIAlaRSIFKKSKLIILDEPTAALD 439
Cdd:PRK15439 107 ILFGLPKRQASMQKMKQ---------LLAALGCQLDL---DSSAGSLEVADRQIVEIL--RGLMRDSRILILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2105575177 440 P-KTEAyVFEKFRELTENKTAI-FISHRLASV-KMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK15439 173 PaETER-LFSRIRELLAQGVGIvFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
284-494 |
4.31e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.57 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 284 DINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY---VSVVFQDFVRYA-LSVKEN 359
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVrkrMSMLFQSGALFTdMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 360 IALSdISQIDNLNE--IKQTAFLSgadsfIEALpnGYDTTlGKVLPNsiDISGGQWQRIALARSIFKKSKLIILDEPTAA 437
Cdd:PRK11831 105 VAYP-LREHTQLPAplLHSTVMMK-----LEAV--GLRGA-AKLMPS--ELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 438 LDPKTEAYVFEKFRELTE--NKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK11831 174 QDPITMGVLVKLISELNSalGVTCVVVSHDVPEVlSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
285-488 |
4.99e-15 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 78.52 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 285 INLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcqidENELseyvsvvfqDFVRYALSV--KENIAL 362
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNL---------DAVRQSLGMcpQHNILF 1015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 363 SDISQIDNLNEIKQTAFLSGADSFIEALPNGYDTTL-GKVLPNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPK 441
Cdd:TIGR01257 1016 HHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLhHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPY 1095
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2105575177 442 TEAYVFEKFRELTENKTAIFISHRLASVK-MADRIIHLKDGQILEEGS 488
Cdd:TIGR01257 1096 SRRSIWDLLLKYRSGRTIIMSTHHMDEADlLGDRIAIISQGRLYCSGT 1143
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
269-492 |
5.10e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 74.88 E-value: 5.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 269 HVYFkyplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYK--PTA---GNIFLEGKDL--CQIDENELSEY 341
Cdd:PRK14267 11 RVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIysPDVDPIEVRRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 VSVVFQDFVRYA-LSVKENIALSD-----ISQIDNLNEIKQTAFLSGA--DSFIEALpNGYDTTLgkvlpnsidiSGGQW 413
Cdd:PRK14267 87 VGMVFQYPNPFPhLTIYDNVAIGVklnglVKSKKELDERVEWALKKAAlwDEVKDRL-NDYPSNL----------SGGQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 414 QRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRLA-SVKMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAqAARVSDYVAFLYLGKLIEVGPTRKV 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
279-494 |
5.71e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.35 E-value: 5.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 279 GYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE-LSEYVSVVFQDFVRYAL--- 354
Cdd:PRK10762 265 GPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLANGIVYISEDRKRDGLvlg 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 -SVKENIALSDISQIDNLN-EIKQTAFLSGADSFIEAL----PNgYDTTLGKvlpnsidISGGQWQRIALARSIFKKSKL 428
Cdd:PRK10762 345 mSVKENMSLTALRYFSRAGgSLKHADEQQAVSDFIRLFniktPS-MEQAIGL-------LSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 429 IILDEPTAALD--PKTEAY-VFEKFREltENKTAIFISHRLASV-KMADRIIHLKDGQI-----LEEGSHKELMA 494
Cdd:PRK10762 417 LILDEPTRGVDvgAKKEIYqLINQFKA--EGLSIILVSSEMPEVlGMSDRILVMHEGRIsgeftREQATQEKLMA 489
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
265-485 |
9.20e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.35 E-value: 9.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlsNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcqidENELSEYvSV 344
Cdd:PRK11248 2 LQISHLYADYG--GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV----EGPGAER-GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDfvrYAL----SVKENIAL-------SDISQIDNLNEIKQTAFLSGADS-FIEALpngydttlgkvlpnsidiSGGQ 412
Cdd:PRK11248 75 VFQN---EGLlpwrNVQDNVAFglqlagvEKMQRLEIAHQMLKKVGLEGAEKrYIWQL------------------SGGQ 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 413 WQRIALARSIFKKSKLIILDEPTAALDpkteAYVFEKFREL------TENKTAIFISHRL-ASVKMADRIIHLK--DGQI 483
Cdd:PRK11248 134 RQRVGIARALAANPQLLLLDEPFGALD----AFTREQMQTLllklwqETGKQVLLITHDIeEAVFMATELVLLSpgPGRV 209
|
..
gi 2105575177 484 LE 485
Cdd:PRK11248 210 VE 211
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
282-487 |
1.33e-14 |
|
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: 73.07 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGL---YKPTAGNIFLEGkdlCQIDENELSEYVSVVFQD--FVRYaLSV 356
Cdd:cd03234 23 LNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNG---QPRKPDQFQKCVAYVRQDdiLLPG-LTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 KENIALSDISQIDNLNEIKQTAFLSgADSFIEALPngyDTTLGKVLPNSidISGGQWQRIALARSIFKKSKLIILDEPTA 436
Cdd:cd03234 99 RETLTYTAILRLPRKSSDAIRKKRV-EDVLLRDLA---LTRIGGNLVKG--ISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 437 ALDPKTEAYVFEKFREL-TENKTAIFISHRLAS--VKMADRIIHLKDGQILEEG 487
Cdd:cd03234 173 GLDSFTALNLVSTLSQLaRRNRIVILTIHQPRSdlFRLFDRILLLSSGEIVYSG 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
296-492 |
1.34e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 296 AIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY-VSVVFQDF-VRYALSVKENIALSdiSQIDN-LN 372
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQELnLIPQLTIAENIFLG--REFVNrFG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 373 EIKQTAFLSGADSFIEAL--PNGYDTTLGkvlpnsiDISGGQWQRIALARSIFKKSKLIILDEPTAAL-DPKTEAyVFEK 449
Cdd:PRK10762 112 RIDWKKMYAEADKLLARLnlRFSSDKLVG-------ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTETES-LFRV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2105575177 450 FRELTENKTAI-FISHRLASV-KMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK10762 184 IRELKSQGRGIvYISHRLKEIfEICDDVTVFRDGQFIAEREVADL 228
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
282-493 |
1.51e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 73.71 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIG-LYKPTA-------GNIFLEGKDLCQIDENELSEYVSVVFQDFVR-Y 352
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPaF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 353 ALSVKENIAL--------SDISQIDNLNEIKQTAFLSGADSFIealpnGYDTTlgkvlpnsiDISGGQWQRIALARSIFK 424
Cdd:PRK13547 97 AFSAREIVLLgrypharrAGALTHRDGEIAWQALALAGATALV-----GRDVT---------TLSGGELARVQFARVLAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 425 ---------KSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISH--RLASvKMADRIIHLKDGQILEEGSHKE 491
Cdd:PRK13547 163 lwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHdpNLAA-RHADRIAMLADGAIVAHGAPAD 241
|
..
gi 2105575177 492 LM 493
Cdd:PRK13547 242 VL 243
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
167-466 |
1.63e-14 |
|
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: 76.87 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 167 WANIGLDSLTAVLYSMSAVLMVWLLKLGKMNIGSFVSTAQAIQG-LQGTVNqTSHLLASLFESnlyIKDFFDFIEYQNED 245
Cdd:TIGR01271 1110 WFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILStLQWAVN-SSIDVDGLMRS---VSRVFKFIDLPQEE 1185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 246 DAKKEKLEKNiaNKSDTANISLKHVYFKYP---------LSNGYS------LKDINLEIKDKEKVAIVGHNGSGKTTLIQ 310
Cdd:TIGR01271 1186 PRPSGGGGKY--QLSTVLVIENPHAQKCWPsggqmdvqgLTAKYTeagravLQDLSFSVEGGQRVGLLGRTGSGKSTLLS 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 311 LIIGLYKpTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSVKENiaLSDISQIDNlNEIKQTAFLSGADSFIEAL 390
Cdd:TIGR01271 1264 ALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKN--LDPYEQWSD-EEIWKVAEEVGLKSVIEQF 1339
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 391 PNGYDTTL---GKVLPNsidisgGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRL 466
Cdd:TIGR01271 1340 PDKLDFVLvdgGYVLSN------GHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV 1412
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
282-482 |
1.79e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE-LSEYVSVVFQDfVRYA--LSVKE 358
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQE-LHLVpeMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 359 NIALSDISQidNLNEIKQTAFLSGADSFIEAL-----PngyDTTLGKVlpnSIdisgGQWQRIALARSIFKKSKLIILDE 433
Cdd:PRK11288 99 NLYLGQLPH--KGGIVNRRLLNYEAREQLEHLgvdidP---DTPLKYL---SI----GQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2105575177 434 PTAALDPKTEAYVFEKFREL-TENKTAIFISHRLASV-KMADRIIHLKDGQ 482
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELrAEGRVILYVSHRMEEIfALCDAITVFKDGR 217
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
270-494 |
2.17e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 73.50 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 270 VYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDEN--ELSEYVSVVFQ 347
Cdd:PRK13638 7 LWFRY--QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 348 DFVR--YALSVKENIALSdisqIDNLN--EIKQTAFLSGADSFIEAlpNGYDTTLGKVLpnsidiSGGQWQRIALARSIF 423
Cdd:PRK13638 85 DPEQqiFYTDIDSDIAFS----LRNLGvpEAEITRRVDEALTLVDA--QHFRHQPIQCL------SHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 424 KKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFI-SHRLASV-KMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIIsSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
282-494 |
2.88e-14 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.97 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEgkdlcqidenelSEYVSVVFQDFVRYAlSVKENIA 361
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RSIAYVPQQAWIMNA-TVRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 362 LSDISQIDNLNEIKQTAFLSgADsfIEALPNGYDTTLGKvlpNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPK 441
Cdd:PTZ00243 743 FFDEEDAARLADAVRVSQLE-AD--LAQLGGGLETEIGE---KGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAH 816
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 442 T-EAYVFEKFRELTENKTAIFISHRLASVKMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PTZ00243 817 VgERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
262-494 |
6.07e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.53 E-value: 6.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 262 TANISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQiDENELSEY 341
Cdd:PRK13537 5 VAPIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 VSVVFQ-DFVRYALSVKENIALsdISQIDNLNEIKQTAFLSGADSFIEaLPNGYDTTLGkvlpnsiDISGGQWQRIALAR 420
Cdd:PRK13537 82 VGVVPQfDNLDPDFTVRENLLV--FGRYFGLSAAAARALVPPLLEFAK-LENKADAKVG-------ELSGGMKRRLTLAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2105575177 421 SIFKKSKLIILDEPTAALDPKTEAYVFEKFREL-TENKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK13537 152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
280-465 |
6.90e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 70.76 E-value: 6.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 280 YSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEgkdlcqIDENELSEYVSVVfqDFVRYALSVKEN 359
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------VPDNQFGREASLI--DAIGRKGDFKDA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 360 IALsdisqidnLNeikqTAFLSGADSFIeALPNGYdttlgkvlpnsidiSGGQWQRIALARSIFKKSKLIILDEPTAALD 439
Cdd:COG2401 116 VEL--------LN----AVGLSDAVLWL-RRFKEL--------------STGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180
....*....|....*....|....*...
gi 2105575177 440 PKTEAYVFEKFRELTE--NKTAIFISHR 465
Cdd:COG2401 169 RQTAKRVARNLQKLARraGITLVVATHH 196
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
285-492 |
6.92e-14 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 71.56 E-value: 6.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 285 INLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSV-VFQDfVRY--ALSVKENIA 361
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVrTFQH-VRLfrEMTVIENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 362 lsdISQIDNLNeikqTAFLSG---ADSFIEALPNGYD---TTLGKV----LPN--SIDISGGQWQRIALARSIFKKSKLI 429
Cdd:PRK11300 103 ---VAQHQQLK----TGLFSGllkTPAFRRAESEALDraaTWLERVglleHANrqAGNLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2105575177 430 ILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVmGISDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
278-487 |
8.38e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.84 E-value: 8.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 278 NGYS-LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDFVRYALSV 356
Cdd:PRK15056 18 NGHTaLRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 KENIALSDISQIDNLNEIKQ--TAFLSGADSFIEALPNGYdTTLGkvlpnsiDISGGQWQRIALARSIFKKSKLIILDEP 434
Cdd:PRK15056 98 EDVVMMGRYGHMGWLRRAKKrdRQIVTAALARVDMVEFRH-RQIG-------ELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 435 TAALDPKTEAYVFEKFREL-TENKTAIFISHRLASV-KMADRIIHLKdGQILEEG 487
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVtEFCDYTVMVK-GTVLASG 223
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
269-492 |
1.00e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.06 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 269 HVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKP---TAGNIFLEGKDLCQIDENEL----SEY 341
Cdd:PRK09473 19 RVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELnklrAEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 VSVVFQDFVryalsvkenIALSDISQI-DNLNEI-KQTAFLSGADSFIEA--------LPNGYDTTlgKVLPNsiDISGG 411
Cdd:PRK09473 99 ISMIFQDPM---------TSLNPYMRVgEQLMEVlMLHKGMSKAEAFEESvrmldavkMPEARKRM--KMYPH--EFSGG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 412 QWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASVK-MADRIIHLKDGQILEEGS 488
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAgICDKVLVMYAGRTMEYGN 245
|
....
gi 2105575177 489 HKEL 492
Cdd:PRK09473 246 ARDV 249
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
284-493 |
1.29e-13 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.17 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 284 DINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcqIDENELSEY-VSVVFQ-DFVRYALSVKENIA 361
Cdd:PRK13536 59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV--PARARLARArIGVVPQfDNLDLEFTVRENLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 362 LsdISQIDNLNEIKQTAFLSGADSFIEaLPNGYDTTLGkvlpnsiDISGGQWQRIALARSIFKKSKLIILDEPTAALDPK 441
Cdd:PRK13536 137 V--FGRYFGMSTREIEAVIPSLLEFAR-LESKADARVS-------DLSGGMKRRLTLARALINDPQLLILDEPTTGLDPH 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 442 TEAYVFEKFRE-LTENKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKELM 493
Cdd:PRK13536 207 ARHLIWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
284-508 |
3.03e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 284 DINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYK-PTAGNIFLEGKDL----CQideNELSEYVSVVFQDFVRY----AL 354
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVkirnPQ---QAIAQGIAMVPEDRKRDgivpVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 SVKENIALSDISQIDNLNEIKQTAFLSGADSFIEALpngydttlgKVLPNSID-----ISGGQWQRIALARSIFKKSKLI 429
Cdd:PRK13549 357 GVGKNITLAALDRFTGGSRIDDAAELKTILESIQRL---------KVKTASPElaiarLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 430 ILDEPTAALD--PKTEAYVFekFRELTENKTA-IFISHRLASV-KMADRIIHLKDGQIleegshkelmalKGEYYNMYMT 505
Cdd:PRK13549 428 ILDEPTRGIDvgAKYEIYKL--INQLVQQGVAiIVISSELPEVlGLSDRVLVMHEGKL------------KGDLINHNLT 493
|
...
gi 2105575177 506 QAK 508
Cdd:PRK13549 494 QEQ 496
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
299-473 |
5.52e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 67.67 E-value: 5.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 299 GHNGSGKTTLIQLIIGLYKPTAGNIFLEG----KDLCQIDEnelsEYVSVVFQDFVRYALSVKENiALSDISQIDNLNEI 374
Cdd:PRK13540 34 GSNGAGKTTLLKLIAGLLNPEKGEILFERqsikKDLCTYQK----QLCFVGHRSGINPYLTLREN-CLYDIHFSPGAVGI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 375 KQTAFLSGADSFIEaLPNGYdttlgkvlpnsidISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELT 454
Cdd:PRK13540 109 TELCRLFSLEHLID-YPCGL-------------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHR 174
|
170 180
....*....|....*....|
gi 2105575177 455 ENKTAIFI-SHRLASVKMAD 473
Cdd:PRK13540 175 AKGGAVLLtSHQDLPLNKAD 194
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
282-464 |
8.26e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.75 E-value: 8.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDK-------------EKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKdlcqidenelseyVSVVFQD 348
Cdd:PRK11147 322 MENVNYQIDGKqlvkdfsaqvqrgDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK-------------LEVAYFD 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 349 FVRYALSVKENIalsdisqIDNLNEIKQTAFLSGADSFIEalpnGY--D--------TTLGKVLpnsidiSGGQWQRIAL 418
Cdd:PRK11147 389 QHRAELDPEKTV-------MDNLAEGKQEVMVNGRPRHVL----GYlqDflfhpkraMTPVKAL------SGGERNRLLL 451
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2105575177 419 ARSIFKKSKLIILDEPTAALDPKTeayvFEKFRELTEN--KTAIFISH 464
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLDVET----LELLEELLDSyqGTVLLVSH 495
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
282-492 |
1.05e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.96 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQiDENELSEYVSVVF----QdfVRYALSVK 357
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK-RRKEFARRIGVVFgqrsQ--LWWDLPAI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENIAL-SDISQIDNlNEIKQTaflsgADSFIEALpngydtTLGKVLpnsiDI-----SGGQWQRIALARSIFKKSKLIIL 431
Cdd:COG4586 115 DSFRLlKAIYRIPD-AEYKKR-----LDELVELL------DLGELL----DTpvrqlSLGQRMRCELAAALLHRPKILFL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 432 DEPTAALDPKTEAYVFEKFREL-TENKTAIFI-SHRLASV-KMADRIIHLKDGQILEEGSHKEL 492
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYnRERGTTILLtSHDMDDIeALCDRVIVIDHGRIIYDGSLEEL 242
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
296-493 |
1.22e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 296 AIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVVFQDF-VRYALSVKENI---------ALSDI 365
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLpAAEGMTVRELVaigrypwhgALGRF 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 366 SQIDNlNEIKQTAFLSGADSFIEALPNgydttlgkvlpnsiDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAY 445
Cdd:PRK10575 121 GAADR-EKVEEAISLVGLKPLAHRLVD--------------SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 446 VFEKFRELTENK--TAIFISHrlaSVKMA----DRIIHLKDGQILEEGSHKELM 493
Cdd:PRK10575 186 VLALVHRLSQERglTVIAVLH---DINMAarycDYLVALRGGEMIAQGTPAELM 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
265-492 |
1.66e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 67.75 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPLSNgySLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKpTAGNIFLEGKDLC--------QIDEN 336
Cdd:PRK14258 8 IKVNNLSFYYDTQK--ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRVEFfnqniyerRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 337 ELSEYVSVVFQDFVRYALSVKENIALSdISQID-----NLNEIKQTAfLSGADSfiealpngYDTTLGKVLPNSIDISGG 411
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNVAYG-VKIVGwrpklEIDDIVESA-LKDADL--------WDEIKHKIHKSALDLSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 412 QWQRIALARSIFKKSKLIILDEPTAALDP----KTEAYVfeKFRELTENKTAIFISHRLASV-KMADRIIHLKD-----G 481
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPiasmKVESLI--QSLRLRSELTMVIVSHNLHQVsRLSDFTAFFKGnenriG 232
|
250
....*....|.
gi 2105575177 482 QILEEGSHKEL 492
Cdd:PRK14258 233 QLVEFGLTKKI 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
284-506 |
1.77e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.47 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 284 DINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPT-AGNIFLEGKdlcQID----ENELSEYVSVVFQDFVRYA----L 354
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGK---PVDirnpAQAIRAGIAMVPEDRKRHGivpiL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 SVKENIALSDISQIDNLNEIKQTAFLSGADSFIEALpngYDTTLGKVLPNSiDISGGQWQRIALARSIFKKSKLIILDEP 434
Cdd:TIGR02633 355 GVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRL---KVKTASPFLPIG-RLSGGNQQKAVLAKMLLTNPRVLILDEP 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 435 TAALDPKTEAYVFEKFRELTENKTA-IFISHRLASV-KMADRIIHLKDGQileegshkelmaLKGEYYNMYMTQ 506
Cdd:TIGR02633 431 TRGVDVGAKYEIYKLINQLAQEGVAiIVVSSELAEVlGLSDRVLVIGEGK------------LKGDFVNHALTQ 492
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
281-482 |
3.29e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.60 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 281 SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE-LSEYVSVVFQDF--VRYAlSVK 357
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELnlVLQR-SVM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENIALSDISQ----IDNLNEIKQT-AFLSGADsfIEALPNGYDTTLgkvlpnsidiSGGQWQRIALARSIFKKSKLIILD 432
Cdd:PRK10982 92 DNMWLGRYPTkgmfVDQDKMYRDTkAIFDELD--IDIDPRAKVATL----------SVSQMQMIEIAKAFSYNAKIVIMD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2105575177 433 EPTAALDPKTEAYVFEKFRELTENKTAI-FISHRLASV-KMADRIIHLKDGQ 482
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKERGCGIvYISHKMEEIfQLCDEITILRDGQ 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
284-494 |
5.06e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 5.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 284 DINLEIKDKEKVAIVGHNGSGKT-TLIQLIIGLYKP----TAGNIFLEGKDLCQIDENEL----SEYVSVVFQDFVrYAL 354
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLrgvrGNKIAMIFQEPM-VSL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 SVKENIAlSDISQIDNLN-----EIKQTAFLSGADSFiealpnGYDTTLGKVLPNSIDISGGQWQRIALARSIFKKSKLI 429
Cdd:PRK15134 106 NPLHTLE-KQLYEVLSLHrgmrrEAARGEILNCLDRV------GIRQAAKRLTDYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 430 ILDEPTAALDPKTEAYVFEKFRELTE--NKTAIFISHRLASV-KMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFS 246
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
282-494 |
5.27e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 65.69 E-value: 5.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSE----YVSVVFQDFVRyaLSVK 357
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARrgigYLPQEASIFRR--LSVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENI-ALSDISQIDNLNEIKQTAFLSGADSFIEALPNgydtTLGKVLpnsidiSGGQWQRIALARSIFKKSKLIILDEPTA 436
Cdd:PRK10895 97 DNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRD----SMGQSL------SGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 437 ALDPKTEAYVFEKFRELTENKTAIFIS-HRL-ASVKMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK10895 167 GVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
288-476 |
6.78e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.91 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 288 EIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKdlcqideneLS---EYVSVVFQDFVRYAL-SVKENIALS 363
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK---------ISykpQYIKPDYDGTVEDLLrSITDDLGSS 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 364 ----DISQIDNLNEIkqtaflsgadsfiealpngYDTTLGkvlpnsiDISGGQWQRIALARSIFKKSKLIILDEPTAALD 439
Cdd:PRK13409 432 yyksEIIKPLQLERL-------------------LDKNVK-------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2105575177 440 PKTEAYVFEKFRELTEN--KTAIFISHRLASVKM-ADRII 476
Cdd:PRK13409 486 VEQRLAVAKAIRRIAEEreATALVVDHDIYMIDYiSDRLM 525
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
288-482 |
7.69e-12 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 63.75 E-value: 7.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 288 EIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGkdlcqidenelseyVSVVFQdfvryalsvkenialsdisq 367
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG--------------ITPVYK-------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 368 idnlneikqtaflsgadsfiealpngydttlgkvlPNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVF 447
Cdd:cd03222 67 -----------------------------------PQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAA 111
|
170 180 190
....*....|....*....|....*....|....*..
gi 2105575177 448 EKFRELTEN--KTAIFISHRLASVKMADRIIHLKDGQ 482
Cdd:cd03222 112 RAIRRLSEEgkKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
279-483 |
4.34e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 279 GYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQID-ENELSEYVSVVFQDFVRYALSVK 357
Cdd:PRK15439 276 GEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALStAQRLARGLVYLPEDRQSSGLYLD 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENIALSDISQIDN-----LNEIKQTAFLsgadsfiealpNGYDTTLGKVLpNSID-----ISGGQWQRIALARSIFKKSK 427
Cdd:PRK15439 356 APLAWNVCALTHNrrgfwIKPARENAVL-----------ERYRRALNIKF-NHAEqaartLSGGNQQKVLIAKCLEASPQ 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 428 LIILDEPTAALDPKTEAYVFEKFRELTENKTAI-FISHRLASV-KMADRIIHLKDGQI 483
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVlFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
285-491 |
4.46e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 285 INLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKD---------------LCQIDENelseyvsvvfQDF 349
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPidirsprdairagimLCPEDRK----------AEG 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 350 VRYALSVKENIALSDISQ-------IDNLNEIKQtaflsgADSFIEAL----PNGyDTTLGKvlpnsidISGGQWQRIAL 418
Cdd:PRK11288 342 IIPVHSVADNINISARRHhlragclINNRWEAEN------ADRFIRSLniktPSR-EQLIMN-------LSGGNQQKAIL 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 419 ARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAI-FISHRLASV-KMADRIIHLKDGQILEEGSHKE 491
Cdd:PRK11288 408 GRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVlFVSSDLPEVlGVADRIVVMREGRIAGELAREQ 482
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
290-477 |
5.27e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 63.15 E-value: 5.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 290 KDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDE---NELSEYVSVVFQDFVRYAL----------SV 356
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEfrgSELQNYFTKLLEGDVKVIVkpqyvdlipkAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 KENIalsdisqIDNLNEIKQTAFLsgaDSFIEALpngydtTLGKVLPNSID-ISGGQWQRIALARSIFKKSKLIILDEPT 435
Cdd:cd03236 104 KGKV-------GELLKKKDERGKL---DELVDQL------ELRHVLDRNIDqLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2105575177 436 AALDPKTEAYVFEKFRELTENKTAIF-ISHRLASVKMADRIIH 477
Cdd:cd03236 168 SYLDIKQRLNAARLIRELAEDDNYVLvVEHDLAVLDYLSDYIH 210
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
288-476 |
1.07e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.04 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 288 EIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKdlcqideneLS---EYVSVVFQDFVRYALS--VKENIAL 362
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK---------ISykpQYISPDYDGTVEEFLRsaNTDDFGS 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 363 SDISqidnlNEIkqtaflsgadsfIEALpngydtTLGKVLPNSI-DISGGQWQRIALARSIFKKSKLIILDEPTAALDPK 441
Cdd:COG1245 433 SYYK-----TEI------------IKPL------GLEKLLDKNVkDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489
|
170 180 190
....*....|....*....|....*....|....*....
gi 2105575177 442 tEAYVFEKF-RELTEN--KTAIFISHRLASVKM-ADRII 476
Cdd:COG1245 490 -QRLAVAKAiRRFAENrgKTAMVVDHDIYLIDYiSDRLM 527
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
276-483 |
1.12e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.20 E-value: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 276 LSNGYS--LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIiglykptAGNIFL-EGKdlcQIDENELSeyVSVVFQD---- 348
Cdd:PRK11147 11 LSFSDAplLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLdDGR---IIYEQDLI--VARLQQDpprn 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 349 -------FVRYALS-----VKENIALSDISQID----NLNEikqtafLSGADSFIEALpNGY--DTTLGKVL------PN 404
Cdd:PRK11147 79 vegtvydFVAEGIEeqaeyLKRYHDISHLVETDpsekNLNE------LAKLQEQLDHH-NLWqlENRINEVLaqlgldPD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 405 SI--DISGGqWQR-IALARSIFKKSKLIILDEPTAALDPKTEAYVfEKFReLTENKTAIFISHRLASV-KMADRIIHLKD 480
Cdd:PRK11147 152 AAlsSLSGG-WLRkAALGRALVSNPDVLLLDEPTNHLDIETIEWL-EGFL-KTFQGSIIFISHDRSFIrNMATRIVDLDR 228
|
...
gi 2105575177 481 GQI 483
Cdd:PRK11147 229 GKL 231
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
277-488 |
1.20e-10 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 61.86 E-value: 1.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 277 SNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIigLYKPTAGNIFLEGKDLCQIDENELSEYVS---VVFQD----- 348
Cdd:cd03271 6 ARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDT--LYPALARRLHLKKEQPGNHDRIEGLEHIDkviVIDQSpigrt 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 349 ---------------------------FVRYALSVK---ENIAlsDISQIDnLNEikqtaflsgADSFIEALPN------ 392
Cdd:cd03271 84 prsnpatytgvfdeirelfcevckgkrYNRETLEVRykgKSIA--DVLDMT-VEE---------ALEFFENIPKiarklq 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 393 -------GYdTTLGKvlpNSIDISGGQWQRIALARSIFKKSK---LIILDEPTAALDPKTEAYVFEKFRELTEN-KTAIF 461
Cdd:cd03271 152 tlcdvglGY-IKLGQ---PATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKgNTVVV 227
|
250 260 270
....*....|....*....|....*....|...
gi 2105575177 462 ISHRLASVKMADRIIHL------KDGQILEEGS 488
Cdd:cd03271 228 IEHNLDVIKCADWIIDLgpeggdGGGQVVASGT 260
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
282-482 |
3.48e-10 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 59.26 E-value: 3.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQliiglykptagNIFLEGKDLCQIDENELSEYVSVVFqdfvryalsvkenia 361
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-----------EGLYASGKARLISFLPKFSRNKLIF--------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 362 lsdisqIDNLneikqtaflsgadSFIEALPNGYdTTLGKVLPNsidISGGQWQRIALARSIFKKSK--LIILDEPTAALD 439
Cdd:cd03238 65 ------IDQL-------------QFLIDVGLGY-LTLGQKLST---LSGGELQRVKLASELFSEPPgtLFILDEPSTGLH 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2105575177 440 PKTEAYVFEKFRELTENK-TAIFISHRLASVKMADRIIHLKDGQ 482
Cdd:cd03238 122 QQDINQLLEVIKGLIDLGnTVILIEHNLDVLSSADWIIDFGPGS 165
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
265-439 |
4.94e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 62.18 E-value: 4.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYPlsNGYSL-KDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKdlcqidenelseyvs 343
Cdd:PLN03073 509 ISFSDASFGYP--GGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAK--------------- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 344 vvfqdfVRYALSVKENIALSDISQIDNLNEIKqtAFLSGADSFIEALPNGYDTTLGKVLPNSIDISGGQWQRIALARSIF 423
Cdd:PLN03073 572 ------VRMAVFSQHHVDGLDLSSNPLLYMMR--CFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITF 643
|
170
....*....|....*.
gi 2105575177 424 KKSKLIILDEPTAALD 439
Cdd:PLN03073 644 KKPHILLLDEPSNHLD 659
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
281-492 |
8.95e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 8.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 281 SLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNI-----FLEGKDLCQIDENELSEY---------VSVVF 346
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmLLRRRSRQVIELSEQSAAqmrhvrgadMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 347 QD---FVRYALSVKENIALSdisqidnlneIKQTAFLSGADSFIEA--------LPNGyDTTLGKvLPNSIdiSGGQWQR 415
Cdd:PRK10261 111 QEpmtSLNPVFTVGEQIAES----------IRLHQGASREEAMVEAkrmldqvrIPEA-QTILSR-YPHQL--SGGMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 416 IALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKT--AIFISHRLASV-KMADRIIHLKDGQILEEGSHKEL 492
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVaEIADRVLVMYQGEAVETGSVEQI 256
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
284-465 |
2.39e-09 |
|
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: 59.76 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 284 DINLEIKDKEKVAIVGHNGSGKTTLIQLIIGL--------YKPTAGNIFLegkdLCQidenelSEYVSV-VFQDFVRYAL 354
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFY----VPQ------RPYMTLgTLRDQIIYPD 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 355 SVKENI--ALSDISQIDNLNEIKQTAFLSGADSFiEALPNGYDTtlgkvlpnsidISGGQWQRIALARSIFKKSKLIILD 432
Cdd:TIGR00954 540 SSEDMKrrGLSDKDLEQILDNVQLTHILEREGGW-SAVQDWMDV-----------LSGGEKQRIAMARLFYHKPQFAILD 607
|
170 180 190
....*....|....*....|....*....|...
gi 2105575177 433 EPTAALDPKTEAYVFEKFRELteNKTAIFISHR 465
Cdd:TIGR00954 608 ECTSAVSVDVEGYMYRLCREF--GITLFSVSHR 638
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
276-497 |
2.88e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 276 LSNGYS----LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIflegkdlcqidenELSEYVSVVFqdfvr 351
Cdd:PRK15064 325 LTKGFDngplFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-------------KWSENANIGY----- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 352 YALSVKENIAlSDISQIDNLNEIKQTaflSGADSFIEAlpngydtTLGKVLPNSIDI-------SGGQWQRIALARSIFK 424
Cdd:PRK15064 387 YAQDHAYDFE-NDLTLFDWMSQWRQE---GDDEQAVRG-------TLGRLLFSQDDIkksvkvlSGGEKGRMLFGKLMMQ 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 425 KSKLIILDEPTAALDPKT-EAY--VFEKFReltenKTAIFISHRLASVK-MADRIIHLKDGQILE-EGSHKELMALKG 497
Cdd:PRK15064 456 KPNVLVMDEPTNHMDMESiESLnmALEKYE-----GTLIFVSHDREFVSsLATRIIEITPDGVVDfSGTYEEYLRSQG 528
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
407-507 |
3.52e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 58.28 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 407 DISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASV-KMADRIIHLKDGQI 483
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLsQWADKINVLYCGQT 237
|
90 100
....*....|....*....|....
gi 2105575177 484 LEEGSHKELMALKGEYYnmymTQA 507
Cdd:PRK15093 238 VETAPSKELVTTPHHPY----TQA 257
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
282-464 |
5.63e-09 |
|
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: 58.41 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFL-EGKD---LCQidENELSEyvsvvfqdfvryALSVK 357
Cdd:TIGR03719 21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGIKvgyLPQ--EPQLDP------------TKTVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENI--ALSDISQI-DNLNEIkqTAFLSGADSFIEAL-------PNGYDTTLGKVLPNSIDI-----------------SG 410
Cdd:TIGR03719 87 ENVeeGVAEIKDAlDRFNEI--SAKYAEPDADFDKLaaeqaelQEIIDAADAWDLDSQLEIamdalrcppwdadvtklSG 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 411 GQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVfEKFreLTENK-TAIFISH 464
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWL-ERH--LQEYPgTVVAVTH 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
282-495 |
6.10e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 58.26 E-value: 6.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIG-LY-KPTAGNIFLEGKdlcQIDENELSE-------YVSvvfQDFVRY 352
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrSYgRNISGTVFKDGK---EVDVSTVSDaidaglaYVT---EDRKGY 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 353 AL----SVKENIALSDISQIDN---LNEIKQTAFlsgADSFIEAL----PNGYDTTlGKvlpnsidISGGQWQRIALARS 421
Cdd:NF040905 350 GLnlidDIKRNITLANLGKVSRrgvIDENEEIKV---AEEYRKKMniktPSVFQKV-GN-------LSGGNQQKVVLSKW 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 422 IFKKSKLIILDEPTAALD--PKTEAYVFekFRELT-ENKTAIFISHRLASV-KMADRIIHLKDGQIL-----EEGSHKEL 492
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDvgAKYEIYTI--INELAaEGKGVIVISSELPELlGMCDRIYVMNEGRITgelprEEASQERI 496
|
...
gi 2105575177 493 MAL 495
Cdd:NF040905 497 MRL 499
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
295-478 |
7.07e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.28 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 295 VAIVGHNGSGKTTLIQLIIGLYKPTAGNifLEGKDlcQIDE-------NELSEYvsvvFQDfvryaLSVKENIALSDISQ 367
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGELIPNLGD--YEEEP--SWDEvlkrfrgTELQNY----FKK-----LYNGEIKVVHKPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 368 ID--------NLNEI-KQTAFLSGADSFIEALpngydtTLGKVLPNSID-ISGGQWQRIALARSIFKKSKLIILDEPTAA 437
Cdd:PRK13409 169 VDlipkvfkgKVRELlKKVDERGKLDEVVERL------GLENILDRDISeLSGGELQRVAIAAALLRDADFYFFDEPTSY 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2105575177 438 LDpkteayVFEKF------RELTENKTAIFISHRLASVKM-ADrIIHL 478
Cdd:PRK13409 243 LD------IRQRLnvarliRELAEGKYVLVVEHDLAVLDYlAD-NVHI 283
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
292-481 |
7.08e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.69 E-value: 7.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 292 KEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLegkdlcqIDENELSEYVSVVFQDFVRYalsvkenialsdisqidnl 371
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLDQLLLIIVG------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 372 neikqtaflsgadsfiealpngydttlgkvlPNSIDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEA------- 444
Cdd:smart00382 56 -------------------------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEAlllllee 104
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2105575177 445 YVFEKFRELTENKTAIFISHRLASVK------MADRIIHLKDG 481
Cdd:smart00382 105 LRLLLLLKSEKNLTVILTTNDEKDLGpallrrRFDRRIVLLLI 147
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
293-440 |
1.20e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 55.24 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 293 EKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSvvfqdfvrYALSVKEnialsDISQIDNLN 372
Cdd:PRK13543 38 EALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLG--------HLPGLKA-----DLSTLENLH 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 373 eikqtaFLSGADSF-IEALPN---------GYDTTLGKVLpnsidiSGGQWQRIALARSIFKKSKLIILDEPTAALDP 440
Cdd:PRK13543 105 ------FLCGLHGRrAKQMPGsalaivglaGYEDTLVRQL------SAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
267-519 |
1.28e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 267 LKHVYFKYplSNG---YSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKdlcqidenelseyVS 343
Cdd:PRK13545 24 LKDLFFRS--KDGeyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-------------AA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 344 VVfqdfvryALSVKENIALSDISQIdnlnEIKQTAFLSGADSFIEALPNGYD-TTLGKVLPNSIDI-SGGQWQRIALARS 421
Cdd:PRK13545 89 LI-------AISSGLNGQLTGIENI----ELKGLMMGLTKEKIKEIIPEIIEfADIGKFIYQPVKTySSGMKSRLGFAIS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 422 IFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN-KTAIFISHRLASVK-MADRIIHLKDGQILEEGSHKELMALKG-- 497
Cdd:PRK13545 158 VHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFISHSLSQVKsFCTKALWLHYGQVKEYGDIKEVVDHYDef 237
|
250 260
....*....|....*....|....
gi 2105575177 498 --EYYNMYMTQAKWFdgqREEVIS 519
Cdd:PRK13545 238 lkKYNQMSVEERKDF---REEQIS 258
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
383-492 |
1.36e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 57.72 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 383 ADSFIEALPN-------------GYdTTLGKvlpNSIDISGGQWQRIALARSIFKKSK---LIILDEPTAAL---DPKTE 443
Cdd:TIGR00630 796 AYEFFEAVPSisrklqtlcdvglGY-IRLGQ---PATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLhfdDIKKL 871
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 444 AYVFEKFRELteNKTAIFISHRLASVKMADRIIHL------KDGQILEEGSHKEL 492
Cdd:TIGR00630 872 LEVLQRLVDK--GNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
293-494 |
1.50e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.20 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 293 EKVAIVGHNGSGKTTLIQLIIGLYKPT--AGNIFLEGKDLCQidenELSEYVSVVFQDFVRYA-LSVKENIALSDISQID 369
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTK----QILKRTGFVTQDDILYPhLTVRETLVFCSLLRLP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 370 NlnEIKQTAFLSGADSFIEALpnGYDTTLGKVLPNSI--DISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVF 447
Cdd:PLN03211 171 K--SLTKQEKILVAESVISEL--GLTKCENTIIGNSFirGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLV 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2105575177 448 EKFRELTEN-KTAIFISHRLAS--VKMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PLN03211 247 LTLGSLAQKgKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
283-494 |
2.90e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 56.33 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 283 KDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLcqideNELSEYVSV---------------VFQ 347
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDI-----SPRSPLDAVkkgmayitesrrdngFFP 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 348 DFvryalSVKENIALSdisqidnlNEIKQTAFLSGADSFIEALPNGYDTTLGKVLP--------NSIDISGGQWQRIALA 419
Cdd:PRK09700 355 NF-----SIAQNMAIS--------RSLKDGGYKGAMGLFHEVDEQRTAENQRELLAlkchsvnqNITELSGGNQQKVLIS 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 420 RSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTEN-KTAIFISHRLASV-KMADRIIHLKDGQI------LEEGSHKE 491
Cdd:PRK09700 422 KWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIiTVCDRIAVFCEGRLtqiltnRDDMSEEE 501
|
...
gi 2105575177 492 LMA 494
Cdd:PRK09700 502 IMA 504
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
265-472 |
4.56e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.35 E-value: 4.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 265 ISLKHVYFKYplSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKdlCQIDENELSEYVSV 344
Cdd:PRK09544 5 VSLENVSVSF--GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK--LRIGYVPQKLYLDT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 345 VFQDFVRYALSVKENIALSDIsqidnLNEIKQTAflsgADSFIEAlpngydtTLGKvlpnsidISGGQWQRIALARSIFK 424
Cdd:PRK09544 81 TLPLTVNRFLRLRPGTKKEDI-----LPALKRVQ----AGHLIDA-------PMQK-------LSGGETQRVLLARALLN 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2105575177 425 KSKLIILDEPTAALDPKTEAYVFEKFREL-TENKTAIF-ISHRLASVkMA 472
Cdd:PRK09544 138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLrRELDCAVLmVSHDLHLV-MA 186
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
282-492 |
6.30e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 55.44 E-value: 6.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQlIIGLYKPT----AGNIFLEGKdlcQIDENELSEYVSVVFQD--FVRyALS 355
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMN-ALAFRSPKgvkgSGSVLLNGM---PIDAKEMRAISAYVQQDdlFIP-TLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 356 VKENIALSDISQIDNLNEIKQTafLSGADSFIEA--LPNGYDTTLGkvLPNSID-ISGGQWQRIALARSIFKKSKLIILD 432
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKKEK--RERVDEVLQAlgLRKCANTRIG--VPGRVKgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 433 EPTAALDPKTEAYVFEKFRELTEN-KTAIFISHRLAS--VKMADRIIHLKDGQILEEGSHKEL 492
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQA 254
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
296-479 |
7.27e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 52.99 E-value: 7.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 296 AIVGHNGSGKTTLIQLI-IGLY--KPTAGNIFLEGKDLCQidENELSEYVSVVFQDFVRyalsvKENIALSDISQIDNln 372
Cdd:cd03240 26 LIVGQNGAGKTTIIEALkYALTgeLPPNSKGGAHDPKLIR--EGEVRAQVKLAFENANG-----KKYTITRSLAILEN-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 373 eikqTAFLSGADSFiealpngydttlgKVLPNSID-ISGGQWQ------RIALARSIFKKSKLIILDEPTAALDpktEAY 445
Cdd:cd03240 97 ----VIFCHQGESN-------------WPLLDMRGrCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD---EEN 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2105575177 446 VFEKFRELTE------NKTAIFISHRLASVKMADRIIHLK 479
Cdd:cd03240 157 IEESLAEIIEerksqkNFQLIVITHDEELVDAADHIYRVE 196
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
273-487 |
9.81e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.48 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 273 KYPLSNG---------YSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENELSEY-- 341
Cdd:PRK10261 322 RFPLRSGllnrvtrevHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALrr 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 342 -VSVVFQDfvRYA-LSVKENIALSDISqidnlnEIKQTAFLSGadsfiEALPNGYDTTLGKV--LPNSI-----DISGGQ 412
Cdd:PRK10261 402 dIQFIFQD--PYAsLDPRQTVGDSIME------PLRVHGLLPG-----KAAAARVAWLLERVglLPEHAwryphEFSGGQ 468
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 413 WQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENK--TAIFISHRLASV-KMADRIIHLKDGQILEEG 487
Cdd:PRK10261 469 RQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFgiAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
408-479 |
1.24e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.21 E-value: 1.24e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 408 ISGGQWQRIALArSIFKKSK-----LIILDEPTAALDPKTEAYVFEKFRELTENK-TAIFISHRLASVKMADRIIHLK 479
Cdd:cd03227 78 LSGGEKELSALA-LILALASlkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGaQVIVITHLPELAELADKLIHIK 154
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
295-464 |
2.23e-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: 53.40 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 295 VAIVGHNGSGKTTLIQLIIGLYKPTAGNIflegkdlcqidenELSEYVSVVFQDFVRYAL----SVKENIAL-SDISQID 369
Cdd:TIGR03719 351 VGVIGPNGAGKSTLFRMITGQEQPDSGTI-------------EIGETVKLAYVDQSRDALdpnkTVWEEISGgLDIIKLG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 370 NLnEIKQTAFLS-----GADSfiealpngyDTTLGkvlpnsiDISGGQWQRIALARSIFKKSKLIILDEPTAALDPKTea 444
Cdd:TIGR03719 418 KR-EIPSRAYVGrfnfkGSDQ---------QKKVG-------QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVET-- 478
|
170 180
....*....|....*....|....*
gi 2105575177 445 yvfekFRELTEN-----KTAIFISH 464
Cdd:TIGR03719 479 -----LRALEEAllnfaGCAVVISH 498
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
282-500 |
3.21e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 51.72 E-value: 3.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGL--YKPTAGNIFLEGKDLCQID-ENELSEYVSVVFQDFV-------R 351
Cdd:PRK09580 17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSpEDRAGEGIFMAFQYPVeipgvsnQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 352 YALsvkeNIALSDISQIDNLNEIKQTAFLSGADSFIEALPNGYDttlgkVLPNSIDI--SGGQWQRIALARSIFKKSKLI 429
Cdd:PRK09580 97 FFL----QTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPED-----LLTRSVNVgfSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 430 ILDEPTAALDPKTEAYVFEKFRELTENKTA-IFISH--RLASVKMADRIIHLKDGQILEEGSHKELMALKGEYY 500
Cdd:PRK09580 168 ILDESDSGLDIDALKIVADGVNSLRDGKRSfIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQGY 241
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
269-483 |
4.57e-07 |
|
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: 50.34 E-value: 4.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 269 HVYFKYPLSNGYSLKDINLEIKDKEKVAIVGHNGSGKTTL---IQLIIGLYKPTAGNIFLEGKDLCQIDENELSEYVSVV 345
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLlkaLANRTEGNVSVEGDIHYNGIPYKEFAEKYPGEIIYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 346 FQDFVRYALSVKENI--ALSdisqidnlneIKQTAFLSGadsfiealpngydttlgkvlpnsidISGGQWQRIALARSIF 423
Cdd:cd03233 90 EEDVHFPTLTVRETLdfALR----------CKGNEFVRG-------------------------ISGGERKRVSIAEALV 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2105575177 424 KKSKLIILDEPTAALDPKTEAYVFEKFRELT-ENKTAIFISHRLAS---VKMADRIIHLKDGQI 483
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRTMAdVLKTTTFVSLYQASdeiYDLFDKVLVLYEGRQ 198
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
278-499 |
8.56e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 278 NGYSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKDLCQIDENE-LSEYVSVVFQDfvRYALSV 356
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEaINHGFALVTEE--RRSTGI 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 357 KENIALSDISQIDNLNEIK-QTAFLSGA----------DSFIEALPnGYDTTLGKvlpnsidISGGQWQRIALARSIFKK 425
Cdd:PRK10982 338 YAYLDIGFNSLISNIRNYKnKVGLLDNSrmksdtqwviDSMRVKTP-GHRTQIGS-------LSGGNQQKVIIGRWLLTQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 426 SKLIILDEPTAALDPKTEAYVFEKFRELT-ENKTAIFISHRLAS-VKMADRIIHLKDGQI-----LEEGSHKELMALKGE 498
Cdd:PRK10982 410 PEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPElLGITDRILVMSNGLVagivdTKTTTQNEILRLASL 489
|
.
gi 2105575177 499 Y 499
Cdd:PRK10982 490 H 490
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
295-467 |
1.15e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.32 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 295 VAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKdlcqIDE-------NELSEYVSVVFQDFVRyaLSVKenialsdISQ 367
Cdd:COG1245 102 TGILGPNGIGKSTALKILSGELKPNLGDYDEEPS----WDEvlkrfrgTELQDYFKKLANGEIK--VAHK-------PQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 368 IDNLNE-IKQTA--FLSGAD------SFIEALpngydtTLGKVLPNSID-ISGGQWQRIALARSIFKKSKLIILDEPTAA 437
Cdd:COG1245 169 VDLIPKvFKGTVreLLEKVDergkldELAEKL------GLENILDRDISeLSGGELQRVAIAAALLRDADFYFFDEPSSY 242
|
170 180 190
....*....|....*....|....*....|....*..
gi 2105575177 438 LDpkteayVFEKF------RELTE-NKTAIFISHRLA 467
Cdd:COG1245 243 LD------IYQRLnvarliRELAEeGKYVLVVEHDLA 273
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
59-215 |
1.85e-06 |
|
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: 49.56 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 59 MHVLQLCITIVSYIGFLFFIHWGLVVLGILASIPAFIIQYKFGYSNFNLNRLQSGLMREA-SYINSLFRNkqsIKEIKLF 137
Cdd:pfam00664 120 GLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKAsSVAEESLSG---IRTVKAF 196
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 138 RSGNFLINRWRKLTTSNNKKILKLFFKQNWANIGLDSLTAVLYSMSAVLMVWLLKLGKMNIGSFVSTAQAIQGLQGTV 215
Cdd:pfam00664 197 GREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
281-463 |
5.92e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 48.46 E-value: 5.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 281 SLKDINLEIKDKeKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFlEGKDLCQIDENELSE-----YVSVVFQDFVRYALS 355
Cdd:COG3593 13 SIKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSRKF-DEEDFYLGDDPDLPEieielTFGSLLSRLLRLLLK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 356 VKENIALSDisQIDNLN-EIKQ--TAFLSGADSFIEALPNGYDTTLGKVLPNSIDI--------------------SGGQ 412
Cdd:COG3593 91 EEDKEELEE--ALEELNeELKEalKALNELLSEYLKELLDGLDLELELSLDELEDLlkslslriedgkelpldrlgSGFQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2105575177 413 W-QRIALARSIF-----KKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFIS 463
Cdd:COG3593 169 RlILLALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIIT 225
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
396-499 |
7.88e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.92 E-value: 7.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 396 TTLgkvlpnsidiSGGQWQRIALARSIFKKSK---LIILDEPTAALDpkteayvFEKFRELTE---------NkTAIFIS 463
Cdd:PRK00349 829 TTL----------SGGEAQRVKLAKELSKRSTgktLYILDEPTTGLH-------FEDIRKLLEvlhrlvdkgN-TVVVIE 890
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2105575177 464 HRLASVKMADRIIHL------KDGQILEEGSHKELMALKGEY 499
Cdd:PRK00349 891 HNLDVIKTADWIIDLgpeggdGGGEIVATGTPEEVAKVEASY 932
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
276-439 |
9.29e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 48.24 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 276 LSNGYS----LKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFL-EGKDLCQIDENELseyvsvvfqDFV 350
Cdd:PRK10636 318 VSAGYGdriiLDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQHQL---------EFL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 351 RyalsvkenialSDISQIDNLNEIkqtaflsgADSFIEALPNGYDTTLG----KVLPNSIDISGGQWQRIALARSIFKKS 426
Cdd:PRK10636 389 R-----------ADESPLQHLARL--------APQELEQKLRDYLGGFGfqgdKVTEETRRFSGGEKARLVLALIVWQRP 449
|
170
....*....|...
gi 2105575177 427 KLIILDEPTAALD 439
Cdd:PRK10636 450 NLLLLDEPTNHLD 462
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
409-492 |
1.05e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.81 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 409 SGGQWQRIALARSIFKKSKLIILDEPTAALDPKTEAYVFEKFRELTENKTAIFISHRL--ASVKMADRIIHLKDGQILEE 486
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYmeEAEQLAHELTVIDRGRVIAD 225
|
....*.
gi 2105575177 487 GSHKEL 492
Cdd:NF000106 226 GKVDEL 231
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
56-225 |
1.13e-05 |
|
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: 47.16 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 56 SNSMHVLQLCITIVSYIGFLFFIHWGLvVLGILASIPAFIIqykfgysnfnLNRLQSGLMREASY--------INSLFRN 127
Cdd:cd07346 115 SGLLQLLSDVLTLIGALVILFYLNWKL-TLVALLLLPLYVL----------ILRYFRRRIRKASRevreslaeLSAFLQE 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 128 K-QSIKEIKLFRSGNFLINRWRKLTTSNNKKILKLFFKQNWANIGLDSLTAVlySMSAVLMV--WLLKLGKMNIGSFVST 204
Cdd:cd07346 184 SlSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTAL--GTALVLLYggYLVLQGSLTIGELVAF 261
|
170 180
....*....|....*....|.
gi 2105575177 205 AQAIQGLQGTVNQTSHLLASL 225
Cdd:cd07346 262 LAYLGMLFGPIQRLANLYNQL 282
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
295-442 |
2.08e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 2.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 295 VAIVGHNGSGKTTLIQLIIGLYKPTAGNIflegkdlcqidenELSEYVSVVFQDFVRYAL----SVKENIAL-SDISQID 369
Cdd:PRK11819 353 VGIIGPNGAGKSTLFKMITGQEQPDSGTI-------------KIGETVKLAYVDQSRDALdpnkTVWEEISGgLDIIKVG 419
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2105575177 370 NlNEIKQTAFLS-----GADSfiealpngydTTLGKVLpnsidiSGGQWQRIALARSIFKKSKLIILDEPTAALDPKT 442
Cdd:PRK11819 420 N-REIPSRAYVGrfnfkGGDQ----------QKKVGVL------SGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVET 480
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
408-495 |
3.65e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 408 ISGGQWQRIALARSIF---KKSKLIILDEPTAALDPKTEAYVFEKFRELT-ENKTAIFISHRLASVKMADRIIHL----- 478
Cdd:PRK00635 810 LSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYVLELgpegg 889
|
90
....*....|....*...
gi 2105575177 479 -KDGQILEEGSHKELMAL 495
Cdd:PRK00635 890 nLGGYLLASCSPEELIHL 907
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
289-485 |
4.07e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 289 IKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEG--------KDLCQIDENELsEYVSVVFQDFVRYALSVKENI 360
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPAL-EYVIDGDREYRQLEAQLHDAN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 361 ALSDISQI----DNLNEIKQTAFLSGADSFIEALpnGYDTTLgkvLPNSI-DISGGQWQRIALARSIFKKSKLIILDEPT 435
Cdd:PRK10636 103 ERNDGHAIatihGKLDAIDAWTIRSRAASLLHGL--GFSNEQ---LERPVsDFSGGWRMRLNLAQALICRSDLLLLDEPT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2105575177 436 AALDpkTEAYVF-EKFRElTENKTAIFISH-RLASVKMADRIIHLKDGQILE 485
Cdd:PRK10636 178 NHLD--LDAVIWlEKWLK-SYQGTLILISHdRDFLDPIVDKIIHIEQQSLFE 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
260-464 |
4.36e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 260 SDTANISLKHVYFKY---PLsngysLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIG-----------LYKPTAGNifl 325
Cdd:PRK10938 256 ANEPRIVLNNGVVSYndrPI-----LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndltLFGRRRGS--- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 326 eGKDLCQIDENelSEYVSVVFQDFVRYALSVKENI------------ALSDISQIDnlneikqtaflsgADSFIEALpnG 393
Cdd:PRK10938 328 -GETIWDIKKH--IGYVSSSLHLDYRVSTSVRNVIlsgffdsigiyqAVSDRQQKL-------------AQQWLDIL--G 389
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2105575177 394 YDTTLGKVLPNSidISGGQwQRIAL-ARSIFKKSKLIILDEPTAALDPKTEAYVfEKFRE--LTENKTA-IFISH 464
Cdd:PRK10938 390 IDKRTADAPFHS--LSWGQ-QRLALiVRALVKHPTLLILDEPLQGLDPLNRQLV-RRFVDvlISEGETQlLFVSH 460
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
283-494 |
5.84e-05 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 44.69 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 283 KDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKP----TAGNIFLEGKdlcQIDENEL-SEYVSVVFQDfVRYALSVK 357
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGK---PVAPCALrGRKIATIMQN-PRSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 358 ENIAlsdisqiDNLNE-IKQTAFLSGADSFIEALPN-GYDTTlGKVLP-NSIDISGGQWQRIALARSIFKKSKLIILDEP 434
Cdd:PRK10418 96 HTMH-------THAREtCLALGKPADDATLTAALEAvGLENA-ARVLKlYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 435 TAALDPKTEAYVFEKFRELTENKT--AIFISHRLASV-KMADRIIHLKDGQILEEGSHKELMA 494
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
396-499 |
8.49e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 396 TTLgkvlpnsidiSGGQWQRIALARSIFKKSK---LIILDEPTAAL---DPKTEAYVFEKFRELteNKTAIFISHRLASV 469
Cdd:COG0178 825 TTL----------SGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhDIRKLLEVLHRLVDK--GNTVVVIEHNLDVI 892
|
90 100 110
....*....|....*....|....*....|....*.
gi 2105575177 470 KMADRIIHL------KDGQILEEGSHKELMALKGEY 499
Cdd:COG0178 893 KTADWIIDLgpeggdGGGEIVAEGTPEEVAKVKASY 928
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
409-515 |
8.51e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 409 SGGQWQRIALARSIFKKSKLIILDEPTAALDPKT----EAYVfekfreLTENKTAIFISHR---LASVkMADrIIHLKdG 481
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAvlwlETYL------LKWPKTFIVVSHArefLNTV-VTD-ILHLH-G 416
|
90 100 110
....*....|....*....|....*....|....
gi 2105575177 482 QileegshkELMALKGEYYNMYMTQAKWFDGQRE 515
Cdd:PLN03073 417 Q--------KLVTYKGDYDTFERTREEQLKNQQK 442
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
408-508 |
1.09e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 408 ISGGQWQRIALARSIfkKSKLI----ILDEPTAALDPKTEAYVFEKFRELTE-NKTAIFISHRLASVKMADRIIHL---- 478
Cdd:TIGR00630 489 LSGGEAQRIRLATQI--GSGLTgvlyVLDEPSIGLHQRDNRRLINTLKRLRDlGNTLIVVEHDEDTIRAADYVIDIgpga 566
|
90 100 110
....*....|....*....|....*....|..
gi 2105575177 479 --KDGQILEEGSHKELMALKGEYYNMYMTQAK 508
Cdd:TIGR00630 567 geHGGEVVASGTPEEILANPDSLTGQYLSGRK 598
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
282-487 |
1.38e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.40 E-value: 1.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 282 LKDINLEIKDKEKVAIVGHNGSGKTTLI----------QLIIGLykPTAGNIFLEGKDLCQIDENE-LSEYVSVVFQDFV 350
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESL--SAYARQFLGQMDKPDVDSIEgLSPAIAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 351 RYALSvkeniALSDISQI-DNLNEIKQTAFLSGADSFIEALPNGYdTTLGKVLPNsidISGGQWQRIALARSIfkKSKLI 429
Cdd:cd03270 89 RNPRS-----TVGTVTEIyDYLRLLFARVGIRERLGFLVDVGLGY-LTLSRSAPT---LSGGEAQRIRLATQI--GSGLT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2105575177 430 ----ILDEPTAALDPKTEAYVFEKFRELTE-NKTAIFISHRLASVKMADRIIHL------KDGQILEEG 487
Cdd:cd03270 158 gvlyVLDEPSIGLHPRDNDRLIETLKRLRDlGNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
416-504 |
1.64e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 416 IALARSIF---KKSKLIILDEPTAALDPKTEAYVFEKFREL-TENKTAIFISHRLASVKMADRIIHL------KDGQILE 485
Cdd:PRK00635 1708 IKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLvSLGHSVIYIDHDPALLKQADYLIEMgpgsgkTGGKILF 1787
|
90
....*....|....*....
gi 2105575177 486 EGSHKELMALKGEYYNMYM 504
Cdd:PRK00635 1788 SGPPKDISASKDSLLKTYM 1806
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
66-203 |
3.93e-04 |
|
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: 42.41 E-value: 3.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 66 ITIVSYIGFLFFIHWGLVVLGILASIPAFIIQYKFGYSnfnLNRLQSGLMREASYINSLFR-NKQSIKEIKLFRSGNFLI 144
Cdd:cd18552 125 LTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIGKR---LRKISRRSQESMGDLTSVLQeTLSGIRVVKAFGAEDYEI 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 145 NRWRKLttsnNKKILKLFFKQNWANIGLDSLTAVLYSMSAVLMVW----LLKLGKMNIGSFVS 203
Cdd:cd18552 202 KRFRKA----NERLRRLSMKIARARALSSPLMELLGAIAIALVLWyggyQVISGELTPGEFIS 260
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
280-508 |
5.32e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.73 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 280 YSLKDINLEIKDKEKVAIVGHNGSGKTTLIQLIIGLYKPTAGNIFLEGKdlcqidenelseyVSVVfqdfvryALSVKEN 359
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-------------VSVI-------AISAGLS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 360 IALSDISQIdnlnEIKQTAFLSGADSFIEALPNGYD-TTLGKVLPNSI-DISGGQWQRIALARSIFKKSKLIILDEPTAA 437
Cdd:PRK13546 98 GQLTGIENI----EFKMLCMGFKRKEIKAMTPKIIEfSELGEFIYQPVkKYSSGMRAKLGFSINITVNPDILVIDEALSV 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2105575177 438 LDPKTEAYVFEKFRELTE-NKTAIFISHRLASVK-MADRIIHLKDGQILEEGSHKELMALKGEYYNMYMTQAK 508
Cdd:PRK13546 174 GDQTFAQKCLDKIYEFKEqNKTIFFVSHNLGQVRqFCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFKKKSK 246
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
295-464 |
6.00e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 295 VAIVGHNGSGKTTLIQLI-IGLYKPTAG------NIFLEGKDLCQID---ENELSEYVSVVFQ-DFVRYALSVKENI--A 361
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIrYALYGKARSrsklrsDLINVGSEEASVElefEHGGKRYRIERRQgEFAEFLEAKPSERkeA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 362 LSDISQIDNLNEIKQ-----TAFLSGADSFIEALPNGYDTTLGKV--LPNSIDISGGQWQRIALARSIfkkskLIILDep 434
Cdd:COG0419 106 LKRLLGLEIYEELKErlkelEEALESALEELAELQKLKQEILAQLsgLDPIETLSGGERLRLALADLL-----SLILD-- 178
|
170 180 190
....*....|....*....|....*....|
gi 2105575177 435 TAALDPKTEAYVFEKFRELTenktaiFISH 464
Cdd:COG0419 179 FGSLDEERLERLLDALEELA------IITH 202
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
416-476 |
3.28e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 40.43 E-value: 3.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2105575177 416 IALARSIF--KKSKLIILDEPTAALDpktEAYVF---EKFRELTENKTAIFISHRLASVKMADRII 476
Cdd:TIGR02168 1100 LALLFAIFkvKPAPFCILDEVDAPLD---DANVErfaNLLKEFSKNTQFIVITHNKGTMEVADQLY 1162
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
408-494 |
3.35e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 408 ISGGQWQRIALARSIfkKSKLI----ILDEPTAALDPK-TEAY--VFEKFREltENKTAIFISHRLASVKMADRIIHLK- 479
Cdd:PRK00635 477 LSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQdTHKLinVIKKLRD--QGNTVLLVEHDEQMISLADRIIDIGp 552
|
90 100
....*....|....*....|
gi 2105575177 480 -----DGQILEEGSHKELMA 494
Cdd:PRK00635 553 gagifGGEVLFNGSPREFLA 572
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
8-203 |
4.20e-03 |
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Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 39.42 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 8 MELKLNLKLGNMIIEKSLNSPFFYFDMPEFYNHQFRINNygHSFLRPI-SNSMHVLQL-CITIVSYIGFLFFIHWGLVVL 85
Cdd:cd18555 69 LQTKLDKSLMSDFFEHLLKLPYSFFENRSSGDLLFRANS--NVYIRQIlSNQVISLIIdLLLLVIYLIYMLYYSPLLTLI 146
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2105575177 86 GILASIPAFIIQYKFGYSNFNLNRLQsgLMREA---SYINSLFRNkqsIKEIKLFRSGNFLINRWRKlttsNNKKILKLF 162
Cdd:cd18555 147 VLLLGLLIVLLLLLTRKKIKKLNQEE--IVAQTkvqSYLTETLYG---IETIKSLGSEKNIYKKWEN----LFKKQLKAF 217
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170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2105575177 163 FK-QNWANIgLDSLTAVLYSMSAVLMVWL-LKL---GKMNIGSFVS 203
Cdd:cd18555 218 KKkERLSNI-LNSISSSIQFIAPLLILWIgAYLvinGELTLGELIA 262
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