|
Name |
Accession |
Description |
Interval |
E-value |
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1-499 |
0e+00 |
|
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: 750.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 1 MRIVVVNKKKCTAGKgCDYVCMNFCPINRTGKDCIVEG-ADGKIVVEEELCIGCGICVNKCPFDAVKVVNLPDELESRMI 79
Cdd:COG1245 2 MRIAVVDRDRCQPKK-CNYECIKYCPVNRTGKEAIEIDeDDGKPVISEELCIGCGICVKKCPFDAISIVNLPEELEEDPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 80 HSYDKNGFKLFNLVIPQKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFGEVEGQKIIDFFKGTEAQNYFEKLYTTGL 159
Cdd:COG1245 81 HRYGENGFRLYGLPVPKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLKRFRGTELQDYFKKLANGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 160 ETSYKPQYVEQIPRIFKGSVKALLNKISE-GDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPS 238
Cdd:COG1245 161 KVAHKPQYVDLIPKVFKGTVRELLEKVDErGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 239 SYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIMLDYLADVEHIMYGRAGVYGIVSKSLSIRECINTYLEGYIREDNMRF 318
Cdd:COG1245 241 SYLDIYQRLNVARLIRELAEEGKYVLVVEHDLAILDYLADYVHILYGEPGVYGVVSKPKSVRVGINQYLDGYLPEENVRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 319 RSEEIKFEVKAPTKALNNIPIIEWSNIEKKLGDFKLKVKPGILMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTS 398
Cdd:COG1245 321 RDEPIEFEVHAPRREKEEETLVEYPDLTKSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 399 VKISYKPQYVQVENDDFVRSVLMKTPPSM----------IERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLD 468
Cdd:COG1245 401 LKISYKPQYISPDYDGTVEEFLRSANTDDfgssyykteiIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLD 480
|
490 500 510
....*....|....*....|....*....|.
gi 1278501429 469 EPSAHLDVEQRLNVAKILRDVIKKKEASAFV 499
Cdd:COG1245 481 EPSAHLDVEQRLAVAKAIRRFAENRGKTAMV 511
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1-499 |
0e+00 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 736.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 1 MRIVVVNKKKCTAGKgCDYVCMNFCPINRTGKDCIV-EGADGKIVVEEELCIGCGICVNKCPFDAVKVVNLPDELESRMI 79
Cdd:PRK13409 2 MRIAVVDYDRCQPKK-CNYECIKYCPVVRTGEETIEiDEDDGKPVISEELCIGCGICVKKCPFDAISIVNLPEELEEEPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 80 HSYDKNGFKLFNLVIPQKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFGEVEGQKIIDFFKGTEAQNYFEKLYTTGL 159
Cdd:PRK13409 81 HRYGVNGFKLYGLPIPKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPSWDEVLKRFRGTELQNYFKKLYNGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 160 ETSYKPQYVEQIPRIFKGSVKALLNKISE-GDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPS 238
Cdd:PRK13409 161 KVVHKPQYVDLIPKVFKGKVRELLKKVDErGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 239 SYLDIKQRLKVANLLRKHGSEKEcAVVVEHDLIMLDYLADVEHIMYGRAGVYGIVSKSLSIRECINTYLEGYIREDNMRF 318
Cdd:PRK13409 241 SYLDIRQRLNVARLIRELAEGKY-VLVVEHDLAVLDYLADNVHIAYGEPGAYGVVSKPKGVRVGINEYLKGYLPEENMRI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 319 RSEEIKFEVKAPTKALNNIPIIEWSNIEKKLGDFKLKVKPGILMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTS 398
Cdd:PRK13409 320 RPEPIEFEERPPRDESERETLVEYPDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 399 VKISYKPQYVQVENDDFVRSVLMKTPPSM---------IERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDE 469
Cdd:PRK13409 400 LKISYKPQYIKPDYDGTVEDLLRSITDDLgssyykseiIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 479
|
490 500 510
....*....|....*....|....*....|
gi 1278501429 470 PSAHLDVEQRLNVAKILRDVIKKKEASAFV 499
Cdd:PRK13409 480 PSAHLDVEQRLAVAKAIRRIAEEREATALV 509
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
73-326 |
7.92e-111 |
|
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: 328.94 E-value: 7.92e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 73 ELESRMIHSYDKNGFKLFNLVIPQKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFGEVEGQKIIDFFKGTEAQNYFE 152
Cdd:cd03236 1 ELEDEPVHRYGPNSFKLHRLPVPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEFRGSELQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 153 KLYTTGLETSYKPQYVEQIPRIFKGSVKALLNKISE-GDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDF 231
Cdd:cd03236 81 KLLEGDVKVIVKPQYVDLIPKAVKGKVGELLKKKDErGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 232 LFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIMLDYLADVEHIMYGRAGVYGIVSKSLSIRECINTYLEGYI 311
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGEPGAYGVVTLPKSVREGINEFLDGYL 240
|
250
....*....|....*
gi 1278501429 312 REDNMRFRSEEIKFE 326
Cdd:cd03236 241 PTENMRFREESIEFE 255
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
342-499 |
1.09e-63 |
|
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: 207.26 E-value: 1.09e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 342 WSNIEKKLGDFKLKVKPGILMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSV-KISYKPQYVQVENDDFVRSVL 420
Cdd:cd03237 3 YPTMKKTLGEFTLEVEGGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELdTVSYKPQYIKADYEGTVRDLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 421 MKTPPSM----------IERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVI 490
Cdd:cd03237 83 SSITKDFythpyfkteiAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
|
....*....
gi 1278501429 491 KKKEASAFV 499
Cdd:cd03237 163 ENNEKTAFV 171
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
81-308 |
1.92e-45 |
|
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: 159.11 E-value: 1.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 81 SYDKNGFKL------FNlvipqKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDfgEVEGQKIidffkgteaqnyfekl 154
Cdd:cd03237 7 KKTLGEFTLeveggsIS-----ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI--EIELDTV---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 155 yttgletSYKPQYVEqiPRiFKGSVKALLNKISEGDVNK------VCNELGIKHVLNRKVGDISGGELQRVAIAGALLKK 228
Cdd:cd03237 64 -------SYKPQYIK--AD-YEGTVRDLLSSITKDFYTHpyfkteIAKPLQIEQILDREVPELSGGELQRVAIAACLSKD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 229 SDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKE-CAVVVEHDLIMLDYLADVEHIMYGRAGVYGIVSKSLSIRECINTYL 307
Cdd:cd03237 134 ADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEkTAFVVEHDIIMIDYLADRLIVFEGEPSVNGVANPPQSLRSGMNRFL 213
|
.
gi 1278501429 308 E 308
Cdd:cd03237 214 K 214
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
76-307 |
2.80e-44 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 164.21 E-value: 2.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 76 SRMIHSYDknGFKLFnlVIP---QKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEgqkiidffkgteaqnyfe 152
Cdd:PRK13409 344 PDLTKKLG--DFSLE--VEGgeiYEGEVIGIVGPNGIGKTTFAKLLAGVLKP----DEGEVD------------------ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 153 klytTGLETSYKPQYVEqipRIFKGSVKALLNKISEgDVN------KVCNELGIKHVLNRKVGDISGGELQRVAIAGALL 226
Cdd:PRK13409 398 ----PELKISYKPQYIK---PDYDGTVEDLLRSITD-DLGssyyksEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLS 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 227 KKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAV-VVEHDLIMLDYLADVEHIMYGRAGVYGIVSKSLSIRECINT 305
Cdd:PRK13409 470 RDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATAlVVDHDIYMIDYISDRLMVFEGEPGKHGHASGPMDMREGMNR 549
|
..
gi 1278501429 306 YL 307
Cdd:PRK13409 550 FL 551
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
76-308 |
8.38e-44 |
|
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: 163.03 E-value: 8.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 76 SRMIHSYDknGFKLFnlVIP---QKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEGQKIIdffkgteaqnyfe 152
Cdd:COG1245 345 PDLTKSYG--GFSLE--VEGgeiREGEVLGIVGPNGIGKTTFAKILAGVLKP----DEGEVDEDLKI------------- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 153 klyttgletSYKPQYVEQIpriFKGSVKALLNKISEGDV------NKVCNELGIKHVLNRKVGDISGGELQRVAIAGALL 226
Cdd:COG1245 404 ---------SYKPQYISPD---YDGTVEEFLRSANTDDFgssyykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLS 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 227 KKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAV-VVEHDLIMLDYLADVEHIMYGRAGVYGIVSKSLSIRECINT 305
Cdd:COG1245 472 RDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAmVVDHDIYLIDYISDRLMVFEGEPGVHGHASGPMDMREGMNR 551
|
...
gi 1278501429 306 YLE 308
Cdd:COG1245 552 FLK 554
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
102-477 |
4.94e-42 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 156.76 E-value: 4.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 102 GLVGVNGIGKSTCLNILSGQLKPNLGN--------------DFGEVEGQKIIDF-FKG----TEAQNYFEKLYTTGLETS 162
Cdd:COG0488 28 GLVGRNGAGKSTLLKILAGELEPDSGEvsipkglrigylpqEPPLDDDLTVLDTvLDGdaelRALEAELEELEAKLAEPD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 163 ykpqyvEQIPRIFKgsvkaLLNKISEGD-------VNKVCNELGIKHV-LNRKVGDISGGELQRVAIAGALLKKSDFLFI 234
Cdd:COG0488 108 ------EDLERLAE-----LQEEFEALGgweaearAEEILSGLGFPEEdLDRPVSELSGGWRRRVALARALLSEPDLLLL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 235 DEPSSYLDIKQRLKVANLLRKHgseKECAVVVEHDLIMLDYLADveHIM---YGRAGVYG------IVSKSLSIRECINT 305
Cdd:COG0488 177 DEPTNHLDLESIEWLEEFLKNY---PGTVLVVSHDRYFLDRVAT--RILeldRGKLTLYPgnysayLEQRAERLEQEAAA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 306 Y---------LEGYIRednmRFRS---------------EEIKFEVKAPTKALNNI----------PIIEWSNIEKKLGD 351
Cdd:COG0488 252 YakqqkkiakEEEFIR----RFRAkarkakqaqsrikalEKLEREEPPRRDKTVEIrfppperlgkKVLELEGLSKSYGD 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 352 ------FKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKG--KTDTSVKISYKPQyvqvENDDF-----VRS 418
Cdd:COG0488 328 ktllddLSLRIDRG-----DRIGLIGPNGAGKSTLLKLLAGELEPDSGtvKLGETVKIGYFDQ----HQEELdpdktVLD 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278501429 419 VLMKTPPSMIERlDLSHLLKR----------KLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:COG0488 399 ELRDGAPGGTEQ-EVRGYLGRflfsgddafkPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIE 466
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
74-315 |
5.87e-41 |
|
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: 145.02 E-value: 5.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 74 LESRMIHSYDkNGFKLFNLVIPQKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDfgEVEGQKIidffkgteaqnyfek 153
Cdd:cd03222 2 LYPDCVKRYG-VFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDND--EWDGITP--------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 154 lyttgletSYKPQYVeqiprifkgsvkallnkisegdvnkvcnelgikhvlnrkvgDISGGELQRVAIAGALLKKSDFLF 233
Cdd:cd03222 64 --------VYKPQYI-----------------------------------------DLSGGELQRVAIAAALLRNATFYL 94
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 234 IDEPSSYLDIKQRLKVANLLRKHGSE-KECAVVVEHDLIMLDYLADVEHIMYGRAGVYGIVSKSLSIRECINTYLEGYIR 312
Cdd:cd03222 95 FDEPSAYLDIEQRLNAARAIRRLSEEgKKTALVVEHDLAVLDYLSDRIHVFEGEPGVYGIASQPKGTREGINRFLRGYLI 174
|
...
gi 1278501429 313 EDN 315
Cdd:cd03222 175 TFR 177
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
347-499 |
4.81e-40 |
|
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: 142.71 E-value: 4.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 347 KKLGDFKLKVKPGILMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGKTD-TSVKISYKPQYVqvenddfvrsvlmktpp 425
Cdd:cd03222 8 KRYGVFFLLVELGVVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEwDGITPVYKPQYI----------------- 70
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278501429 426 smierldlshllkrklsELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEASAFV 499
Cdd:cd03222 71 -----------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALV 127
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
99-488 |
2.63e-37 |
|
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: 143.51 E-value: 2.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPNlgndfGEVEGQKIIDffkGTEAQNYFEKLYTTGL-------ETSYKPQYV-EQ 170
Cdd:COG1123 33 ETVALVGESGSGKSTLALALMGLLPHG-----GRISGEVLLD---GRDLLELSEALRGRRIgmvfqdpMTQLNPVTVgDQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 I---PRIFKGSVKALLNKISEgdvnkVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRL 247
Cdd:COG1123 105 IaeaLENLGLSRAEARARVLE-----LLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDVTTQA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 248 KVANLLRKHGSEKECAVV-VEHDLIMLDYLADVEHIMYGragvyGIVSKSLSIRECINtylegyiREDNMRFRSEEIKFE 326
Cdd:COG1123 180 EILDLLRELQRERGTTVLlITHDLGVVAEIADRVVVMDD-----GRIVEDGPPEEILA-------APQALAAVPRLGAAR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 327 VKAPTKALNNIPIIEWSNIEKklgDFKLKVKPGI---------LMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGK--- 394
Cdd:COG1123 248 GRAAPAAAAAEPLLEVRNLSK---RYPVRGKGGVravddvsltLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSilf 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 395 ----TDTSVKISYKP-----QYVqvenddF------------VRSVLM-------KTPPS--------MIERLDLS-HLL 437
Cdd:COG1123 325 dgkdLTKLSRRSLRElrrrvQMV------FqdpysslnprmtVGDIIAeplrlhgLLSRAerrervaeLLERVGLPpDLA 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 438 KRKLSELSGGELQRVAIAECLSRDADVYLLDEP-SAhLDVEQRLNVAKILRD 488
Cdd:COG1123 399 DRYPHELSGGQRQRVAIARALALEPKLLILDEPtSA-LDVSVQAQILNLLRD 449
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
365-495 |
5.22e-34 |
|
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: 128.64 E-value: 5.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 365 EIIGVLGENGTGKTTFAKILAGMIKPDKGKTDT--------------------------SVKISYKPQYV-----QVEND 413
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDppdwdeildefrgselqnyftkllegDVKVIVKPQYVdlipkAVKGK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 414 dfVRSVLMKTPPS-----MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRD 488
Cdd:cd03236 107 --VGELLKKKDERgkldeLVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRE 184
|
....*..
gi 1278501429 489 VIKKKEA 495
Cdd:cd03236 185 LAEDDNY 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
349-493 |
1.07e-30 |
|
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: 117.15 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TDTSV--------KISYKPQyvqvenddf 415
Cdd:cd03214 15 LDDLSLSIEAG-----EIVGILGPNGAGKSTLLKTLAGLLKPSSGEilldgKDLASlspkelarKIAYVPQ--------- 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 416 vrsvlmktppsMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKK 493
Cdd:cd03214 81 -----------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLARER 147
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
349-492 |
1.68e-30 |
|
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: 117.63 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVKISYKPQYVQVEND------D 414
Cdd:cd03235 15 LEDVSFEVKPG-----EFLAIVGPNGAGKSTLLKAILGLLKPTSGSirvfgkplEKERKRIGYVPQRRSIDRDfpisvrD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 415 FVRSVLMKT-----PPS---------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRL 480
Cdd:cd03235 90 VVLMGLYGHkglfrRLSkadkakvdeALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQE 169
|
170
....*....|..
gi 1278501429 481 NVAKILRDVIKK 492
Cdd:cd03235 170 DIYELLRELRRE 181
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
354-488 |
2.73e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 118.27 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 354 LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVKISYKPQYVQVEND------DFVRSV 419
Cdd:COG1121 27 LTIPPG-----EFVAIVGPNGAGKSTLLKAILGLLPPTSGTvrlfgkppRRARRRIGYVPQRAEVDWDfpitvrDVVLMG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 420 LMKT-----PPS---------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKI 485
Cdd:COG1121 102 RYGRrglfrRPSradreavdeALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYEL 181
|
...
gi 1278501429 486 LRD 488
Cdd:COG1121 182 LRE 184
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
340-488 |
3.34e-28 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 112.08 E-value: 3.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKG----------KTDTSVK--I 401
Cdd:COG1131 1 IEVRGLTKRYGDKTaldgvsLTVEPG-----EIFGLLGPNGAGKTTTIRMLLGLLRPTSGevrvlgedvaRDPAEVRrrI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 402 SYKPQYVQV-------ENDDFV-------RSVLMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLL 467
Cdd:COG1131 76 GYVPQEPALypdltvrENLRFFarlyglpRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180
....*....|....*....|.
gi 1278501429 468 DEPSAHLDVEQRLNVAKILRD 488
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRE 176
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
349-488 |
3.39e-28 |
|
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: 112.44 E-value: 3.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVK-----ISYKPQYVQVeNDDF 415
Cdd:COG1120 17 LDDVSLSLPPG-----EVTALLGPNGSGKSTLLRALAGLLKPSSGEvlldgrdlASLSRRelarrIAYVPQEPPA-PFGL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 416 -VR-SVLM-KTP-------PS---------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDV 476
Cdd:COG1120 91 tVReLVALgRYPhlglfgrPSaedreaveeALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDL 170
|
170
....*....|..
gi 1278501429 477 EQRLNVAKILRD 488
Cdd:COG1120 171 AHQLEVLELLRR 182
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
340-493 |
7.17e-27 |
|
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: 108.79 E-value: 7.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKK------LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKT----DTSVKISYKPQ--- 406
Cdd:COG4555 2 IEVENLSKKygkvpaLKDVSFTAKDG-----EITGLLGPNGAGKTTLLRMLAGLLKPDSGSIlidgEDVRKEPREARrqi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 407 -YVQVEND--------DFVR--SVLMKTPPS--------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLL 467
Cdd:COG4555 77 gVLPDERGlydrltvrENIRyfAELYGLFDEelkkrieeLIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180
....*....|....*....|....*.
gi 1278501429 468 DEPSAHLDVEQRLNVAKILRDVIKKK 493
Cdd:COG4555 157 DEPTNGLDVMARRLLREILRALKKEG 182
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
349-472 |
2.39e-26 |
|
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: 104.27 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-------------TDTSVKISYKPQYVQV----- 410
Cdd:pfam00005 1 LKNVSLTLNPG-----EILALVGPNGAGKSTLLKLIAGLLSPTEGTilldgqdltdderKSLRKEIGYVFQDPQLfprlt 75
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278501429 411 --ENDDFVRSV--LMKTPPSM-----IERLDLSHLLKRKL----SELSGGELQRVAIAECLSRDADVYLLDEPSA 472
Cdd:pfam00005 76 vrENLRLGLLLkgLSKREKDAraeeaLEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
345-491 |
3.32e-26 |
|
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: 105.84 E-value: 3.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 345 IEKKLGDFKLKVKpgILMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGKT--------DTSVKISYKPQ-----YV-Q- 409
Cdd:cd03297 6 IEKRLPDFTLKID--FDLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIvlngtvlfDSRKKINLPPQqrkigLVfQq 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 410 ---------VENDDFV-----RSVLMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:cd03297 84 yalfphlnvRENLAFGlkrkrNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163
|
170
....*....|....*.
gi 1278501429 476 VEQRLNVAKILRDVIK 491
Cdd:cd03297 164 RALRLQLLPELKQIKK 179
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
349-492 |
1.27e-25 |
|
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: 104.09 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVK-------------------- 400
Cdd:cd03225 17 LDDISLTIKKG-----EFVLIVGPNGSGKSTLLRLLNGLLGPTSGEvlvdgkdlTKLSLKelrrkvglvfqnpddqffgp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 401 -----ISYKPQYVQVENDDFVRSVLmktppSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:cd03225 92 tveeeVAFGLENLGLPEEEIEERVE-----EALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170
....*....|....*..
gi 1278501429 476 VEQRLNVAKILRDVIKK 492
Cdd:cd03225 167 PAGRRELLELLKKLKAE 183
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
96-270 |
3.08e-25 |
|
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: 102.13 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVegqkiidFFKGTEAQNYfeklyttgletsykpqyveqiprif 175
Cdd:cd03214 23 EAGEIVGILGPNGAGKSTLLKTLAGLLKP----SSGEI-------LLDGKDLASL------------------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 176 kgSVKALLNKISEgdVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRK 255
Cdd:cd03214 67 --SPKELARKIAY--VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRR 142
|
170
....*....|....*.
gi 1278501429 256 HGSEKECAVV-VEHDL 270
Cdd:cd03214 143 LARERGKTVVmVLHDL 158
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
349-493 |
2.39e-24 |
|
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: 98.86 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsvkisykpqyVQVENDDFVRsvlmktppsmi 428
Cdd:cd00267 15 LDNVSLTLKAG-----EIVALVGPNGSGKSTLLRAIAGLLKPTSGE-------------ILIDGKDIAK----------- 65
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 429 erlDLSHLLKRKLS---ELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKK 493
Cdd:cd00267 66 ---LPLEELRRRIGyvpQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEG 130
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
80-278 |
6.05e-24 |
|
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: 99.46 E-value: 6.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 80 HSYDKNGFKLF---NLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVegqkiidFFKG--TEAQNYFEKL 154
Cdd:cd03225 7 FSYPDGARPALddiSLTIK-KGEFVLIVGPNGSGKSTLLRLLNGLLGP----TSGEV-------LVDGkdLTKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 155 YTTGletsykpqYVEQIPR--IFKGSVK-----ALLN-KISEGD----VNKVCNELGIKHVLNRKVGDISGGELQRVAIA 222
Cdd:cd03225 75 RKVG--------LVFQNPDdqFFGPTVEeevafGLENlGLPEEEieerVEEALELVGLEGLRDRSPFTLSGGQKQRVAIA 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 223 GALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIMLDYLAD 278
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELAD 202
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
340-498 |
6.81e-24 |
|
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: 99.52 E-value: 6.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLG------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSV---KIS 402
Cdd:cd03259 1 LELKGLSKTYGsvraldDLSLTVEPG-----EFLALLGPSGCGKTTLLRLIAGLERPDSGEilidgrdvTGVPPerrNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 403 YKPQ-Y-------VQvENDDF-VRSVLMKTPP------SMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLL 467
Cdd:cd03259 76 MVFQdYalfphltVA-ENIAFgLKLRGVPKAEirarvrELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190
....*....|....*....|....*....|.
gi 1278501429 468 DEPSAHLDVEQRLNVAKILRDVIKKKEASAF 498
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQRELGITTI 185
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
91-270 |
7.48e-24 |
|
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: 100.50 E-value: 7.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEV--EGQKIidffkgteaqnyfeklyttgleTSYKPQ-- 166
Cdd:COG1120 21 SLSLP-PGEVTALLGPNGSGKSTLLRALAGLLKP----SSGEVllDGRDL----------------------ASLSRRel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 167 -----YVEQIPRI-FKGSV-----------KALLNKISEGD---VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALL 226
Cdd:COG1120 74 arriaYVPQEPPApFGLTVrelvalgryphLGLFGRPSAEDreaVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1278501429 227 KKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDL 270
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVmVLHDL 198
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
349-493 |
1.45e-23 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 98.35 E-value: 1.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSV-----KISYKPQYVQV----- 410
Cdd:COG4619 16 LSPVSLTLEAG-----ECVAITGPSGSGKSTLLRALADLDPPTSGEiyldgkplSAMPPpewrrQVAYVPQEPALwggtv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 411 -ENDDFV-----RSVLMKTPPSMIERLDLSH-LLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVA 483
Cdd:COG4619 91 rDNLPFPfqlreRKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVE 170
|
170
....*....|
gi 1278501429 484 KILRDVIKKK 493
Cdd:COG4619 171 ELLREYLAEE 180
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
80-269 |
4.01e-23 |
|
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: 97.18 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 80 HSYDKNGFKLF-----NLVIpQKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEV--EGQKIIDFFKGTEA----- 147
Cdd:cd03255 8 KTYGGGGEKVQalkgvSLSI-EKGEFVAIVGPSGSGKSTLLNILGGLDRP----TSGEVrvDGTDISKLSEKELAafrrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 148 ------QNYfeKL--YTTGLETsykpqyVEqIPRIFKGSVKALLNKISEgdvnKVCNELGIKHVLNRKVGDISGGELQRV 219
Cdd:cd03255 83 higfvfQSF--NLlpDLTALEN------VE-LPLLLAGVPKKERRERAE----ELLERVGLGDRLNHYPSELSGGQQQRV 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 220 AIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRK-HGSEKECAVVVEHD 269
Cdd:cd03255 150 AIARALANDPKIILADEPTGNLDSETGKEVMELLRElNKEAGTTIVVVTHD 200
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
340-499 |
5.73e-23 |
|
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: 95.54 E-value: 5.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKISYKPqyVQVEND 413
Cdd:cd03230 1 IEVRNLSKRYGKKTalddisLTVEKG-----EIYGLLGPNGAGKTTLIKIILGLLKPDSG----EIKVLGKD--IKKEPE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 414 DFVRSV-LMKTPPSMIERLDLSHLLKrklseLSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDvIKK 492
Cdd:cd03230 70 EVKRRIgYLPEEPSLYENLTVRENLK-----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFWELLRE-LKK 143
|
....*..
gi 1278501429 493 KEASAFV 499
Cdd:cd03230 144 EGKTILL 150
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
99-239 |
1.01e-22 |
|
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: 94.25 E-value: 1.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPnlgndfgeVEGQKIIDffkGTEAQNYFEKLYTTGLetSYKPQYVEQIPR----- 173
Cdd:pfam00005 12 EILALVGPNGAGKSTLLKLIAGLLSP--------TEGTILLD---GQDLTDDERKSLRKEI--GYVFQDPQLFPRltvre 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 174 --IFKGSVKALLNKISEGDVNKVCNELGIKHVLNRKVGD----ISGGELQRVAIAGALLKKSDFLFIDEPSS 239
Cdd:pfam00005 79 nlRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
93-477 |
1.99e-22 |
|
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: 100.39 E-value: 1.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 93 VIPQKKQIM-------------GLVGVNGIGKSTCLNILSGQLKPNLGndfgevegqkiidffkgtEAQnyfeklyttgL 159
Cdd:TIGR03719 13 VVPPKKEILkdislsffpgakiGVLGLNGAGKSTLLRIMAGVDKDFNG------------------EAR----------P 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 160 ETSYKPQYVEQIPRI-----FKGSV-------KALLNKISE---------GDVNKVCNELG-----IKHV----LNRK-- 207
Cdd:TIGR03719 65 QPGIKVGYLPQEPQLdptktVRENVeegvaeiKDALDRFNEisakyaepdADFDKLAAEQAelqeiIDAAdawdLDSQle 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 208 --------------VGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQrlkVAnLLRKHGSEKECAVV-VEHDLIM 272
Cdd:TIGR03719 145 iamdalrcppwdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VA-WLERHLQEYPGTVVaVTHDRYF 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 273 LDYLAdvEHIM---YGRAGVY-GIVSKSLSIREcinTYLEGYIREDNMRFRSEEIKFE-VKAPTKA-------------- 333
Cdd:TIGR03719 221 LDNVA--GWILeldRGRGIPWeGNYSSWLEQKQ---KRLEQEEKEESARQKTLKRELEwVRQSPKGrqakskarlaryee 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 334 LNN-------------IP--------IIEWSNIEKKLGD--------FKLkvkPgilmRNEIIGVLGENGTGKTTFAKIL 384
Cdd:TIGR03719 296 LLSqefqkrnetaeiyIPpgprlgdkVIEAENLTKAFGDklliddlsFKL---P----PGGIVGVIGPNGAGKSTLFRMI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 385 AGMIKPDKG--KTDTSVKISYKPQYVQVENDDfvrsvlmKTPPSMI-ERLDLSHLLKR--------------------KL 441
Cdd:TIGR03719 369 TGQEQPDSGtiEIGETVKLAYVDQSRDALDPN-------KTVWEEIsGGLDIIKLGKReipsrayvgrfnfkgsdqqkKV 441
|
490 500 510
....*....|....*....|....*....|....*.
gi 1278501429 442 SELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:TIGR03719 442 GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVE 477
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
96-282 |
8.79e-22 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 93.97 E-value: 8.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVE--GQKIIDFFKGT--------EAQNYFEKLytTGLEtsykp 165
Cdd:COG1131 24 EPGEIFGLLGPNGAGKTTTIRMLLGLLRP----TSGEVRvlGEDVARDPAEVrrrigyvpQEPALYPDL--TVRE----- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 166 qYVEQIPRIFKGSVKALLNKISEgdvnkVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQ 245
Cdd:COG1131 93 -NLRFFARLYGLPRKEARERIDE-----LLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278501429 246 RLKVANLLRKHGSEKECAVVVEHdlimldYLADVEHI 282
Cdd:COG1131 167 RRELWELLRELAAEGKTVLLSTH------YLEEAERL 197
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
340-492 |
1.17e-21 |
|
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: 93.55 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLGDFKLKVKPGILMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TD-TSVK-----ISYKPQ-Y 407
Cdd:cd03299 1 LKVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKillngKDiTNLPpekrdISYVPQnY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 408 VQVENDDFVRSV-----LMKTPPSMIER--------LDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHL 474
Cdd:cd03299 81 ALFPHMTVYKNIayglkKRKVDKKEIERkvleiaemLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170
....*....|....*...
gi 1278501429 475 DVEQRLNVAKILRDVIKK 492
Cdd:cd03299 161 DVRTKEKLREELKKIRKE 178
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
340-487 |
1.64e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.60 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK---------TDTSV---KI 401
Cdd:COG1118 3 IEVRNISKRFGSFTllddvsLEIASG-----ELVALLGPSGSGKTTLLRIIAGLETPDSGRivlngrdlfTNLPPrerRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 402 SYKPQ-Y-------VQvENDDFVRSVLmktPPS----------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDAD 463
Cdd:COG1118 78 GFVFQhYalfphmtVA-ENIAFGLRVR---PPSkaeirarveeLLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
|
170 180
....*....|....*....|....
gi 1278501429 464 VYLLDEPSAHLDVeqrlNVAKILR 487
Cdd:COG1118 154 VLLLDEPFGALDA----KVRKELR 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
366-489 |
3.44e-21 |
|
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: 91.49 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 366 IIGVLGENGTGKTTFAKILAGMIKPDKGKT---DTSVK---------ISYKPQ----YVQVENDDFVR--SVLMKTPPS- 426
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPPSSGTIridGQDVLkqpqklrrrIGYLPQefgvYPNFTVREFLDyiAWLKGIPSKe 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 427 -------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDV 489
Cdd:cd03264 107 vkarvdeVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSEL 176
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
340-499 |
3.77e-21 |
|
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: 90.18 E-value: 3.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKISYKPqyvqvend 413
Cdd:cd03216 1 LELRGITKRFGGVKaldgvsLSVRRG-----EVHALLGENGAGKSTLMKILSGLYKPDSG----EILVDGKE-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 414 dfvrsvlmktppsmIERLDLSHLLKRKLS---ELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVI 490
Cdd:cd03216 64 --------------VSFASPRDARRAGIAmvyQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLR 129
|
....*....
gi 1278501429 491 KKKEASAFV 499
Cdd:cd03216 130 AQGVAVIFI 138
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
82-283 |
4.37e-21 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 89.61 E-value: 4.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 82 YDKNGFKLFNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEgqkiidfFKGTEaqnyfeklyttglet 161
Cdd:cd00267 10 GGRTALDNVSLTLK-AGEIVALVGPNGSGKSTLLRAIAGLLKP----TSGEIL-------IDGKD--------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 162 sykpqyveqiprIFKGSVKALLNKISEgdvnkvcnelgikhvlnrkVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYL 241
Cdd:cd00267 63 ------------IAKLPLEELRRRIGY-------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1278501429 242 DIKQRLKVANLLRKHGSEKECAVVVEHDLIMLDYLADVEHIM 283
Cdd:cd00267 112 DPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVL 153
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
354-488 |
6.21e-21 |
|
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: 91.24 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 354 LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TDTSVK----ISYKPQYV-QveN-DD--FVRSVL 420
Cdd:COG1122 22 LSIEKG-----EFVAIIGPNGSGKSTLLRLLNGLLKPTSGEvlvdgKDITKKnlreLRRKVGLVfQ--NpDDqlFAPTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 421 ---------MKTPPSMI--------ERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVA 483
Cdd:COG1122 95 edvafgpenLGLPREEIrerveealELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELL 174
|
....*
gi 1278501429 484 KILRD 488
Cdd:COG1122 175 ELLKR 179
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
340-492 |
7.00e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.98 E-value: 7.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVK---IS 402
Cdd:COG3839 4 LELENVSKSYGGVEalkdidLDIEDG-----EFLVLLGPSGCGKSTLLRMIAGLEDPTSGEiliggrdvTDLPPKdrnIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 403 YKPQyvqvendDFV----RSV---------LMKTPPSMIER--------LDLSHLLKRKLSELSGGELQRVAIAECLSRD 461
Cdd:COG3839 79 MVFQ-------SYAlyphMTVyeniafplkLRKVPKAEIDRrvreaaelLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151
|
170 180 190
....*....|....*....|....*....|.
gi 1278501429 462 ADVYLLDEPSAHLDVEQRLNvakiLRDVIKK 492
Cdd:COG3839 152 PKVFLLDEPLSNLDAKLRVE----MRAEIKR 178
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
340-479 |
7.65e-21 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 88.66 E-value: 7.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLG------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKG--KTDTSVKISYKPQyvqve 411
Cdd:cd03221 1 IELENLSKTYGgklllkDISLTINPG-----DRIGLVGRNGAGKSTLLKLIAGELEPDEGivTWGSTVKIGYFEQ----- 70
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 412 nddfvrsvlmktppsmierldlshllkrklseLSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQR 479
Cdd:cd03221 71 --------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI 106
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
363-488 |
1.81e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.22 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKG--KTDTSVKISYKPQyvQVENDD-----FVRSVLMKTPP---------- 425
Cdd:NF040873 17 AGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGtvRRAGGARVAYVPQ--RSEVPDslpltVRDLVAMGRWArrglwrrltr 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 426 -------SMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRD 488
Cdd:NF040873 95 ddraavdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAE 164
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
91-284 |
2.58e-20 |
|
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: 89.13 E-value: 2.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEgqkiIDFFKGTEAQNYFeklyttgletSYKPQYvEQ 170
Cdd:cd03235 19 SFEVK-PGEFLAIVGPNGAGKSTLLKAILGLLKP----TSGSIR----VFGKPLEKERKRI----------GYVPQR-RS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 IPRIFKGSVKAL-----------LNKISEGDVNKVCNEL---GIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDE 236
Cdd:cd03235 79 IDRDFPISVRDVvlmglyghkglFRRLSKADKAKVDEALervGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1278501429 237 PSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIMLDYLADveHIMY 284
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFD--RVLL 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
340-499 |
3.66e-20 |
|
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: 89.09 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEK--KLGDFK--------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TDTSvKISYK 404
Cdd:cd03255 1 IELKNLSKtyGGGGEKvqalkgvsLSIEKG-----EFVAIVGPSGSGKSTLLNILGGLDRPTSGEvrvdgTDIS-KLSEK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 405 pqyvqvENDDFVR----------------SVL---------MKTPP--------SMIERLDLSHLLKRKLSELSGGELQR 451
Cdd:cd03255 75 ------ELAAFRRrhigfvfqsfnllpdlTALenvelplllAGVPKkerreraeELLERVGLGDRLNHYPSELSGGQQQR 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1278501429 452 VAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEASAFV 499
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVV 196
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
338-488 |
5.08e-20 |
|
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: 88.30 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKKLGD---FK---LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK---TDTSVKISYKPQYV 408
Cdd:COG4133 1 MMLEAENLSCRRGErllFSglsFTLAAG-----EALALTGPNGSGKTTLLRILAGLLPPSAGEvlwNGEPIRDAREDYRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 409 QV----------------ENDDFVRSVL-----MKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLL 467
Cdd:COG4133 76 RLaylghadglkpeltvrENLRFWAALYglradREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180
....*....|....*....|.
gi 1278501429 468 DEPSAHLDVEQRLNVAKILRD 488
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAA 176
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
343-477 |
1.35e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 343 SNIEKKLGDFKL------KVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--TDTSVKISYKPQYVQVEND- 413
Cdd:COG0488 2 ENLSKSFGGRPLlddvslSINPG-----DRIGLVGRNGAGKSTLLKILAGELEPDSGEvsIPKGLRIGYLPQEPPLDDDl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 414 ---DFVRSVL----------------MKTPPSMIERLD---------------------LSHL------LKRKLSELSGG 447
Cdd:COG0488 77 tvlDTVLDGDaelraleaeleeleakLAEPDEDLERLAelqeefealggweaearaeeiLSGLgfpeedLDRPVSELSGG 156
|
170 180 190
....*....|....*....|....*....|
gi 1278501429 448 ELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLE 186
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
80-278 |
1.38e-19 |
|
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: 87.99 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 80 HSYDKN-GFKLFNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDFFKGTEAQNYFEKL--YT 156
Cdd:COG4555 9 KKYGKVpALKDVSFTAK-DGEITGLLGPNGAGKTTLLRMLAGLLKPD--------SGSILIDGEDVRKEPREARRQigVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 157 TGLETSYKPQYVEQIPRIFkgsvkALLNKISEGDVNKVCNEL----GIKHVLNRKVGDISGGELQRVAIAGALLKKSDFL 232
Cdd:COG4555 80 PDERGLYDRLTVRENIRYF-----AELYGLFDEELKKRIEELiellGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1278501429 233 FIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIMLDYLAD 278
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCD 200
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
96-283 |
2.41e-19 |
|
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: 86.79 E-value: 2.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgevegqkIIDFFKGTEAQNYFEKLyttgletSYKPQY-------- 167
Cdd:cd03263 26 YKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAY-------INGYSIRTDRKAARQSL-------GYCPQFdalfdelt 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 168 VEQIPRIFkGSVKALLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRL 247
Cdd:cd03263 92 VREHLRFY-ARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRR 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 1278501429 248 KVANLLRKHGSEKeCAVVVEHDLIMLDYLADVEHIM 283
Cdd:cd03263 171 AIWDLILEVRKGR-SIILTTHSMDEAEALCDRIAIM 205
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
93-477 |
2.67e-19 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 90.95 E-value: 2.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 93 VIPQKKQIM-------------GLVGVNGIGKSTCLNILSGQLKPNLGndfgevegqkiidffkgtEAQnyfeklyttgL 159
Cdd:PRK11819 15 VVPPKKQILkdislsffpgakiGVLGLNGAGKSTLLRIMAGVDKEFEG------------------EAR----------P 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 160 ETSYKPQYVEQIPRIFK------------GSVKALL---NKISE------GDVNKVCNELG-----IKHV----LNRK-- 207
Cdd:PRK11819 67 APGIKVGYLPQEPQLDPektvrenveegvAEVKAALdrfNEIYAayaepdADFDALAAEQGelqeiIDAAdawdLDSQle 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 208 --------------VGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQrlkVAnLLRKHGSEKECAVV-VEHDLIM 272
Cdd:PRK11819 147 iamdalrcppwdakVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES---VA-WLEQFLHDYPGTVVaVTHDRYF 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 273 LDYLAdvEHIM---YGRagvyGIVSKSlsireciN--TYL---------EGyiREDNMRFRSEEIKFE-VKAPTKA---- 333
Cdd:PRK11819 223 LDNVA--GWILeldRGR----GIPWEG-------NysSWLeqkakrlaqEE--KQEAARQKALKRELEwVRQSPKArqak 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 334 ----------LNN-------------IP--------IIEWSNIEKKLGD--------FKLkvkPgilmRNEIIGVLGENG 374
Cdd:PRK11819 288 skarlaryeeLLSeeyqkrnetneifIPpgprlgdkVIEAENLSKSFGDrlliddlsFSL---P----PGGIVGIIGPNG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 375 TGKTTFAKILAGMIKPDKG--KTDTSVKISYKPQYVQVENDDfvrsvlmKTPPSMI-ERLDLSHLLKR------------ 439
Cdd:PRK11819 361 AGKSTLFKMITGQEQPDSGtiKIGETVKLAYVDQSRDALDPN-------KTVWEEIsGGLDIIKVGNReipsrayvgrfn 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1278501429 440 --------KLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:PRK11819 434 fkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
349-493 |
2.70e-19 |
|
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: 85.13 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKISYKPqyVQVENDDFVRS----VLMKTp 424
Cdd:cd03228 18 LKDVSLTIKPG-----EKVAIVGPSGSGKSTLLKLLLRLYDPTSG----EILIDGVD--LRDLDLESLRKniayVPQDP- 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 425 psmierldlsHLLKRKLSE--LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKK 493
Cdd:cd03228 86 ----------FLFSGTIREniLSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRALAKGK 146
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
340-489 |
2.79e-19 |
|
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: 86.15 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLG------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVK----- 400
Cdd:cd03301 1 VELENVTKRFGnvtaldDLNLDIADG-----EFVVLLGPSGCGKTTTLRMIAGLEEPTSGRiyiggrdvTDLPPKdrdia 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 401 ---ISYK--PQYVQVENDDF---VRsvlmKTPPSMIER--------LDLSHLLKRKLSELSGGELQRVAIAECLSRDADV 464
Cdd:cd03301 76 mvfQNYAlyPHMTVYDNIAFglkLR----KVPKDEIDErvrevaelLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180
....*....|....*....|....*....
gi 1278501429 465 YLLDEP----SAHLDVEQRLNVAKILRDV 489
Cdd:cd03301 152 FLMDEPlsnlDAKLRVQMRAELKRLQQRL 180
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
91-278 |
3.46e-19 |
|
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: 86.23 E-value: 3.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVegqkIIDffkgteaqnyfeklyttGLETSYKP----- 165
Cdd:COG1122 21 SLSIE-KGEFVAIIGPNGSGKSTLLRLLNGLLKP----TSGEV----LVD-----------------GKDITKKNlrelr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 166 ---QYVEQIPR--IFKGSVK-----ALLN-KISEGD----VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSD 230
Cdd:COG1122 75 rkvGLVFQNPDdqLFAPTVEedvafGPENlGLPREEirerVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1278501429 231 FLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIMLDYLAD 278
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELAD 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
80-283 |
4.47e-19 |
|
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: 85.71 E-value: 4.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 80 HSYDKN-GFKLFNLVIPqkKQIMGLVGVNGIGKSTCLNILSGQLKPnlgndfgeVEGQKIIDffkGTEAQNYFEKLYTTg 158
Cdd:cd03264 8 KRYGKKrALDGVSLTLG--PGMYGLLGPNGAGKTTLMRILATLTPP--------SSGTIRID---GQDVLKQPQKLRRR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 159 leTSYKPQYVEQIPRIfkgSVK------ALLNKISEGDVNK----VCNELGIKHVLNRKVGDISGGELQRVAIAGALLKK 228
Cdd:cd03264 74 --IGYLPQEFGVYPNF---TVRefldyiAWLKGIPSKEVKArvdeVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGD 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1278501429 229 SDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKeCAVVVEHDLIMLDYLADVEHIM 283
Cdd:cd03264 149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDR-IVILSTHIVEDVESLCNQVAVL 202
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
344-489 |
6.13e-19 |
|
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: 88.25 E-value: 6.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 344 NIEKKLGDFKLKVK---PGilmrNEIIGVLGENGTGKTTFAKILAGMIKPDKGKT--------DTSVKISYKPQ-----Y 407
Cdd:TIGR02142 4 RFSKRLGDFSLDADftlPG----QGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtlfDSRKGIFLPPEkrrigY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 408 VQVENDDF----VRSVL---MK---------TPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPS 471
Cdd:TIGR02142 80 VFQEARLFphlsVRGNLrygMKrarpserriSFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170
....*....|....*...
gi 1278501429 472 AHLDVEQRLNVAKILRDV 489
Cdd:TIGR02142 160 AALDDPRKYEILPYLERL 177
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
354-491 |
8.58e-19 |
|
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: 85.11 E-value: 8.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 354 LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-TDTSVKISYKPQYVQ----VENDDF-------VRSVL- 420
Cdd:cd03266 26 FTVKPG-----EVTGLLGPNGAGKTTTLRMLAGLLEPDAGFaTVDGFDVVKEPAEARrrlgFVSDSTglydrltARENLe 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 421 -------MKTPP------SMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVeqrlNVAKILR 487
Cdd:cd03266 101 yfaglygLKGDEltarleELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV----MATRALR 176
|
....
gi 1278501429 488 DVIK 491
Cdd:cd03266 177 EFIR 180
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
91-284 |
9.26e-19 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 85.53 E-value: 9.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPQKkQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEgqkiidfFKGTEAQNYFEKLyttgletSYKPQYvEQ 170
Cdd:COG1121 26 SLTIPPG-EFVAIVGPNGAGKSTLLKAILGLLPP----TSGTVR-------LFGKPPRRARRRI-------GYVPQR-AE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 IPRIFKGSV-----------KALLNKISEGD---VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDE 236
Cdd:COG1121 86 VDWDFPITVrdvvlmgrygrRGLFRRPSRADreaVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDE 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 237 PSSYLDIKQRLKVANL---LRKHGsekeCAV-VVEHDLIMLDYLADveHIMY 284
Cdd:COG1121 166 PFAGVDAATEEALYELlreLRREG----KTIlVVTHDLGAVREYFD--RVLL 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
99-278 |
9.77e-19 |
|
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: 85.63 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEgqkiidfFKGTEAQNYFEKLYTTgletsyKPQYVEQIPRifkGS 178
Cdd:COG1124 32 ESFGLVGESGSGKSTLLRALAGLERP----WSGEVT-------FDGRPVTRRRRKAFRR------RVQMVFQDPY---AS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 179 V--------------KALLNKISEGDVNKVCNELGI-KHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDI 243
Cdd:COG1124 92 LhprhtvdrilaeplRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDV 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 1278501429 244 KQRLKVANLLRKHGSEKECAVV-VEHDLIMLDYLAD 278
Cdd:COG1124 172 SVQAEILNLLKDLREERGLTYLfVSHDLAVVAHLCD 207
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
338-492 |
1.18e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 84.71 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKKLGDFK----------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TDTSV--- 399
Cdd:COG1136 3 PLLELRNLTKSYGTGEgevtalrgvsLSIEAG-----EFVAIVGPSGSGKSTLLNILGGLDRPTSGEvlidgQDISSlse 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 400 ---------KISYKPQYVQ-------VENddfVR--SVLMKTPPS--------MIERLDLSHLLKRKLSELSGGELQRVA 453
Cdd:COG1136 78 relarlrrrHIGFVFQFFNllpeltaLEN---VAlpLLLAGVSRKerrerareLLERVGLGDRLDHRPSQLSGGQQQRVA 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 1278501429 454 IAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKK 492
Cdd:COG1136 155 IARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRE 193
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
96-285 |
1.26e-18 |
|
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: 84.86 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGndfgevegqKIIdfFKGTEAQNYFEKLYttgLETSYKPQYVEQ----- 170
Cdd:cd03257 29 KKGETLGLVGESGSGKSTLARAILGLLKPTSG---------SII--FDGKDLLKLSRRLR---KIRRKEIQMVFQdpmss 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 ------IPRIFKGSVKALLNKISEGDVNKVCNELGI-----KHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSS 239
Cdd:cd03257 95 lnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLLVgvglpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1278501429 240 YLDIKQRLKVANLLRKHGSEKECAVV-VEHDLIMLDYLADVEHIMYG 285
Cdd:cd03257 175 ALDVSVQAQILDLLKKLQEELGLTLLfITHDLGVVAKIADRVAVMYA 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
91-278 |
1.43e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 84.71 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIpQKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEV--EGQkiiDFFKGTEA--------------QNYFekL 154
Cdd:COG1136 28 SLSI-EAGEFVAIVGPSGSGKSTLLNILGGLDRP----TSGEVliDGQ---DISSLSERelarlrrrhigfvfQFFN--L 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 155 --YTTGLETsykpqyVEqIPRIFKGSVKallnKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFL 232
Cdd:COG1136 98 lpELTALEN------VA-LPLLLAGVSR----KERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLI 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1278501429 233 FIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDLIMLDYlAD 278
Cdd:COG1136 167 LADEPTGNLDSKTGEEVLELLRELNRELGTTIVmVTHDPELAAR-AD 212
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
338-492 |
1.48e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 87.08 E-value: 1.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSV---K 400
Cdd:COG3842 4 PALELENVSKRYGDVTalddvsLSIEPG-----EFVALLGPSGCGKTTLLRMIAGFETPDSGRilldgrdvTGLPPekrN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 401 ISYKPQ-Y-------VqVENddfvrsV-----LMKTPPS--------MIERLDLSHLLKRKLSELSGGELQRVAIAECLS 459
Cdd:COG3842 79 VGMVFQdYalfphltV-AEN------VafglrMRGVPKAeirarvaeLLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190
....*....|....*....|....*....|...
gi 1278501429 460 RDADVYLLDEPSAHLDVEQRLNVAKILRDVIKK 492
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRLQRE 184
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
363-495 |
2.80e-18 |
|
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: 83.08 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TDTSVKISYK-PQYVQVENDD--FVRSVL------MKTPPSMI 428
Cdd:cd03226 25 AGEIIALTGKNGAGKTTLAKILAGLIKESSGSillngKPIKAKERRKsIGYVMQDVDYqlFTDSVReelllgLKELDAGN 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278501429 429 ER-------LDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEA 495
Cdd:cd03226 105 EQaetvlkdLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKA 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
349-499 |
4.02e-18 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 83.99 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKISYKPqyVQVENDD--FV---------R 417
Cdd:COG1116 27 LDDVSLTVAAG-----EFVALVGPSGCGKSTLLRLIAGLEKPTSG----EVLVDGKP--VTGPGPDrgVVfqepallpwL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 418 SVL---------MKTPPS--------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRL 480
Cdd:COG1116 96 TVLdnvalglelRGVPKAerrerareLLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALDALTRE 175
|
170 180
....*....|....*....|
gi 1278501429 481 NVAKILRDVIKKKEASA-FV 499
Cdd:COG1116 176 RLQDELLRLWQETGKTVlFV 195
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
83-270 |
4.40e-18 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 82.66 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 83 DKNGFKLFNLVIpQKKQIMGLVGVNGIGKSTCLNIL-------SGQLKPNlGNDFGEVEGQKIIDFFKGTEA---QNYfe 152
Cdd:TIGR03608 10 DKVILDDLNLTI-EKGKMYAIIGESGSGKSTLLNIIgllekfdSGQVYLN-GQETPPLNSKKASKFRREKLGylfQNF-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 153 klyttGLETSYKPQYVEQIPRIF-KGSVKALLNKISEgdvnkVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDF 231
Cdd:TIGR03608 86 -----ALIENETVEENLDLGLKYkKLSKKEKREKKKE-----ALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPL 155
|
170 180 190
....*....|....*....|....*....|....*....
gi 1278501429 232 LFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDL 270
Cdd:TIGR03608 156 ILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDP 194
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
91-270 |
6.27e-18 |
|
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: 86.74 E-value: 6.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPQKKQImGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDffkGTEAQNYfeklyttgLETSYKPQ--YV 168
Cdd:COG4988 357 SLTIPPGERV-ALVGPSGAGKSTLLNLLLGFLPPY--------SGSILIN---GVDLSDL--------DPASWRRQiaWV 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 169 EQIPRIFKGSVKA--LLNK--ISEGDVNKVCNELGIKHVLNR-------KVGD----ISGGELQRVAIAGALLKKSDFLF 233
Cdd:COG4988 417 PQNPYLFAGTIREnlRLGRpdASDEELEAALEAAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRLALARALLRDAPLLL 496
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278501429 234 IDEPSSYLDIKQRLKVANLLRKHGSEKeCAVVVEHDL 270
Cdd:COG4988 497 LDEPTAHLDAETEAEILQALRRLAKGR-TVILITHRL 532
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
349-498 |
8.16e-18 |
|
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: 82.13 E-value: 8.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKISYKPqyVQVENDD--FV---------R 417
Cdd:cd03293 20 LEDISLSVEEG-----EFVALVGPSGCGKSTLLRIIAGLERPTSG----EVLVDGEP--VTGPGPDrgYVfqqdallpwL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 418 SVL--------MKTPP---------SMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRL 480
Cdd:cd03293 89 TVLdnvalgleLQGVPkaeareraeELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTRE 168
|
170
....*....|....*...
gi 1278501429 481 NVAKILRDVIKKKEASAF 498
Cdd:cd03293 169 QLQEELLDIWRETGKTVL 186
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
99-274 |
9.67e-18 |
|
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: 81.76 E-value: 9.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEV--EGQKIIDffkgtEAQNYFEKLYTTGLETSYKPQY--VEQIprI 174
Cdd:COG4133 29 EALALTGPNGSGKTTLLRILAGLLPP----SAGEVlwNGEPIRD-----AREDYRRRLAYLGHADGLKPELtvRENL--R 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 175 FKGSVKALlnKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLR 254
Cdd:COG4133 98 FWAALYGL--RADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIA 175
|
170 180
....*....|....*....|
gi 1278501429 255 KHGSEKECAVVVEHDLIMLD 274
Cdd:COG4133 176 AHLARGGAVLLTTHQPLELA 195
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
99-479 |
1.21e-17 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 85.99 E-value: 1.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgevegqkiidfFKGTEAQNYFEKlYTTGLETSyKPQYVEQIPRIFKGS 178
Cdd:PRK10636 28 QKVGLVGKNGCGKSTLLALLKNEISADGGSYT-----------FPGNWQLAWVNQ-ETPALPQP-ALEYVIDGDREYRQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 179 VKALLNKISEGDVNKVC----------------------NELGIKHV-LNRKVGDISGGELQRVAIAGALLKKSDFLFID 235
Cdd:PRK10636 95 EAQLHDANERNDGHAIAtihgkldaidawtirsraasllHGLGFSNEqLERPVSDFSGGWRMRLNLAQALICRSDLLLLD 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 236 EPSSYLDIKQRLKVANLLRkhgSEKECAVVVEHDLIMLDYLAD-VEHI----MYGRAGVYGIVSKSLSIR---------- 300
Cdd:PRK10636 175 EPTNHLDLDAVIWLEKWLK---SYQGTLILISHDRDFLDPIVDkIIHIeqqsLFEYTGNYSSFEVQRATRlaqqqamyes 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 301 --ECInTYLEGYIRednmRFRSEEIK---------------------------FEVKAPTKALNniPIIEWSNIEKKLGD 351
Cdd:PRK10636 252 qqERV-AHLQSYID----RFRAKATKakqaqsrikmlermeliapahvdnpfhFSFRAPESLPN--PLLKMEKVSAGYGD 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 352 ------FKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTS--VKISYKPQYvQVEnddFVRSvlMKT 423
Cdd:PRK10636 325 riildsIKLNLVPG-----SRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkgIKLGYFAQH-QLE---FLRA--DES 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 424 PPSMIERL---DLSHLLK----------RKLSE----LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQR 479
Cdd:PRK10636 394 PLQHLARLapqELEQKLRdylggfgfqgDKVTEetrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
96-278 |
1.32e-17 |
|
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: 81.65 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGndFGEVEGqkiIDFfkgteAQNYFEKLYTTGL----ETSYKPQYVEQI 171
Cdd:cd03266 29 KPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAG--FATVDG---FDV-----VKEPAEARRRLGFvsdsTGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 172 PRIFkGSVKALLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVAN 251
Cdd:cd03266 99 LEYF-AGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRE 177
|
170 180
....*....|....*....|....*..
gi 1278501429 252 LLRKHGSEKECAVVVEHDLIMLDYLAD 278
Cdd:cd03266 178 FIRQLRALGKCILFSTHIMQEVERLCD 204
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
91-270 |
2.17e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.98 E-value: 2.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPQKKqIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIIDFfkgtEAQNYFEKLyttgletSYKPQyveq 170
Cdd:PRK11231 22 SLSLPTGK-ITALIGPNGCGKSTLLKCFARLLTPQSGTVF--LGDKPISML----SSRQLARRL-------ALLPQ---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 IPRIFKG-SVKAL--------LN---KISEGD---VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFID 235
Cdd:PRK11231 84 HHLTPEGiTVRELvaygrspwLSlwgRLSAEDnarVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLD 163
|
170 180 190
....*....|....*....|....*....|....*
gi 1278501429 236 EPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDL 270
Cdd:PRK11231 164 EPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDL 198
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
349-489 |
2.20e-17 |
|
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: 84.82 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK---TDTSVK----------ISYKPQYVQV----- 410
Cdd:COG4987 351 LDGLSLTLPPG-----ERVAIVGPSGSGKSTLLALLLRFLDPQSGSitlGGVDLRdldeddlrrrIAVVPQRPHLfdttl 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 411 -EN---------DDFVRSVLmktppsmiERLDLSHLLKR-------KLSE----LSGGELQRVAIAECLSRDADVYLLDE 469
Cdd:COG4987 426 rENlrlarpdatDEELWAAL--------ERVGLGDWLAAlpdgldtWLGEggrrLSGGERRRLALARALLRDAPILLLDE 497
|
170 180
....*....|....*....|
gi 1278501429 470 PSAHLDVEqrlNVAKILRDV 489
Cdd:COG4987 498 PTEGLDAA---TEQALLADL 514
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
100-288 |
2.36e-17 |
|
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: 83.24 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 100 IMGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDffkGTEAQNYFEKLYTTglETSYKPQYVEQIPRIFKG-S 178
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPD--------EGEIVLN---GRTLFDSRKGIFLP--PEKRRIGYVFQEARLFPHlS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 179 VKALLN---KISEGDVNKVCNE-----LGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVA 250
Cdd:TIGR02142 92 VRGNLRygmKRARPSERRISFErvielLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 1278501429 251 NLLRK-HGSEKECAVVVEHDLIMLDYLADveHIMYGRAG 288
Cdd:TIGR02142 172 PYLERlHAEFGIPILYVSHSLQEVLRLAD--RVVVLEDG 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
340-492 |
2.44e-17 |
|
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: 80.88 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK------------TDTSVKI 401
Cdd:cd03265 1 IEVENLVKKYGDFEavrgvsFRVRRG-----EIFGLLGPNGAGKTTTIKMLTTLLKPTSGRatvaghdvvrepREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 402 SYKPQYVQVEND--------------DFVRSVLMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLL 467
Cdd:cd03265 76 GIVFQDLSVDDEltgwenlyiharlyGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180
....*....|....*....|....*
gi 1278501429 468 DEPSAHLDVEQRLNVAKILRDVIKK 492
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEE 180
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
340-489 |
2.97e-17 |
|
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: 79.54 E-value: 2.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLG------DFKLKVKpgilmRNEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsvkISYKPQYVQVEND 413
Cdd:cd03229 1 LELKNVSKRYGqktvlnDVSLNIE-----AGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS------ILIDGEDLTDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 414 ---DFVRSVLMktppsMIERLDL-SHL-LKRKLSE-LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILR 487
Cdd:cd03229 70 elpPLRRRIGM-----VFQDFALfPHLtVLENIALgLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLK 144
|
..
gi 1278501429 488 DV 489
Cdd:cd03229 145 SL 146
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
307-493 |
3.24e-17 |
|
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: 84.89 E-value: 3.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 307 LEGYIREDNMRFRSEEikfevkAPTKALNNIpiiewsniekklgdfKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAG 386
Cdd:COG2274 470 LKGDIELENVSFRYPG------DSPPVLDNI---------------SLTIKPG-----ERVAIVGRSGSGKSTLLKLLLG 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 387 MIKPDKGktdtSVKI------SYKPQ-------YVQVENDDFVRSV-----LMKTPPSM---IERLDLSHL--------- 436
Cdd:COG2274 524 LYEPTSG----RILIdgidlrQIDPAslrrqigVVLQDVFLFSGTIrenitLGDPDATDeeiIEAARLAGLhdfiealpm 599
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 437 -LKRKLSE----LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKK 493
Cdd:COG2274 600 gYDTVVGEggsnLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR 661
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
83-269 |
3.87e-17 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 79.86 E-value: 3.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 83 DKNGFKLFNLVIpQKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVegqkiidFFKGteaQNYfeklyttgleTS 162
Cdd:COG4619 12 GKPILSPVSLTL-EAGECVAITGPSGSGKSTLLRALADLDPP----TSGEI-------YLDG---KPL----------SA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 163 YKPQ-------YVEQIPRIFKGSVKALLN--------KISEGDVNKVCNELGI-KHVLNRKVGDISGGELQRVAIAGALL 226
Cdd:COG4619 67 MPPPewrrqvaYVPQEPALWGGTVRDNLPfpfqlrerKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1278501429 227 KKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHD 269
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLwVSHD 190
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
368-488 |
6.00e-17 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 80.63 E-value: 6.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 368 GVLGENGTGKTTFAKILAGMIKPDKGKTD-------------TSVKISYKPQYVQVENDDFVRSV--LMKTP-------- 424
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTVDlagvdlhglsrraRARRVALVEQDSDTAVPLTVRDVvaLGRIPhrslwagd 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 425 --------PSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRD 488
Cdd:TIGR03873 111 sphdaavvDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRE 182
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
343-488 |
6.87e-17 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 79.89 E-value: 6.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 343 SNIEKKLG------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TDTSVK---------IS 402
Cdd:cd03218 4 ENLSKRYGkrkvvnGVSLSVKQG-----EIVGLLGPNGAGKTTTFYMIVGLVKPDSGKilldgQDITKLpmhkrarlgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 403 YKPQYVQV-------ENddfVRSVLMKTPPS----------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVY 465
Cdd:cd03218 79 YLPQEASIfrkltveEN---ILAVLEIRGLSkkereekleeLLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180
....*....|....*....|....*.
gi 1278501429 466 LLDEPSAHLD---VEQRLNVAKILRD 488
Cdd:cd03218 156 LLDEPFAGVDpiaVQDIQKIIKILKD 181
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
340-489 |
7.43e-17 |
|
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: 80.08 E-value: 7.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKT-----DTSvkiSYKPQYV 408
Cdd:cd03296 3 IEVRNVSKRFGDFValddvsLDIPSG-----ELVALLGPSGSGKTTLLRLIAGLERPDSGTIlfggeDAT---DVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 409 QV----------------ENDDF---VRSVLMKTPPSMIER--------LDLSHLLKRKLSELSGGELQRVAIAECLSRD 461
Cdd:cd03296 75 NVgfvfqhyalfrhmtvfDNVAFglrVKPRSERPPEAEIRAkvhellklVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180
....*....|....*....|....*...
gi 1278501429 462 ADVYLLDEPSAHLDVEQRLNVAKILRDV 489
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRL 182
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
90-279 |
9.84e-17 |
|
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: 77.81 E-value: 9.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 90 FNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEgqkiIDffkGTEAQNYFEKlyttgletSYKPQ--Y 167
Cdd:cd03228 21 VSLTIK-PGEKVAIVGPSGSGKSTLLKLLLRLYDP----TSGEIL----ID---GVDLRDLDLE--------SLRKNiaY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 168 VEQIPRIFKGSVKA-LLnkisegdvnkvcnelgikhvlnrkvgdiSGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQR 246
Cdd:cd03228 81 VPQDPFLFSGTIREnIL----------------------------SGGQRQRIAIARALLRDPPILILDEATSALDPETE 132
|
170 180 190
....*....|....*....|....*....|...
gi 1278501429 247 LKVANLLRKHGSEKECaVVVEHDLIMLDyLADV 279
Cdd:cd03228 133 ALILEALRALAKGKTV-IVIAHRLSTIR-DADR 163
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
81-278 |
1.02e-16 |
|
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: 82.96 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 81 SYDKNG---FKLFNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDffkGTEAQNYfeklytt 157
Cdd:COG2274 482 RYPGDSppvLDNISLTIK-PGERVAIVGRSGSGKSTLLKLLLGLYEPT--------SGRILID---GIDLRQI------- 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 158 gletsyKPQ-------YVEQIPRIFKGSVK---ALLNK-ISEGDVNKVCNELGIKHV-------LNRKVGD----ISGGE 215
Cdd:COG2274 543 ------DPAslrrqigVVLQDVFLFSGTIReniTLGDPdATDEEIIEAARLAGLHDFiealpmgYDTVVGEggsnLSGGQ 616
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 216 LQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECaVVVEHDLIMLDyLAD 278
Cdd:COG2274 617 RQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTV-IIIAHRLSTIR-LAD 677
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
103-283 |
1.02e-16 |
|
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: 79.30 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQLKPnlgnDFGEV--EGQKIIDFfkGTEAQNYfeklyttgletSYKPQYVEQIPR--IFK-- 176
Cdd:cd03299 30 ILGPTGSGKSVLLETIAGFIKP----DSGKIllNGKDITNL--PPEKRDI-----------SYVPQNYALFPHmtVYKni 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 177 --GSVKALLNKIS-EGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLL 253
Cdd:cd03299 93 ayGLKKRKVDKKEiERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREEL 172
|
170 180 190
....*....|....*....|....*....|.
gi 1278501429 254 RKHGSEKECAVV-VEHDLIMLDYLADVEHIM 283
Cdd:cd03299 173 KKIRKEFGVTVLhVTHDFEEAWALADKVAIM 203
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
347-493 |
1.23e-16 |
|
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: 79.09 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 347 KKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TDTSV-----------KISYKPQ---- 406
Cdd:cd03257 19 KALDDVSFSIKKG-----ETLGLVGESGSGKSTLARAILGLLKPTSGSiifdgKDLLKlsrrlrkirrkEIQMVFQdpms 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 407 -------------------YVQVENDDFVRSVLMKtppsMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLL 467
Cdd:cd03257 94 slnprmtigeqiaeplrihGKLSKKEARKEAVLLL----LVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIA 169
|
170 180
....*....|....*....|....*.
gi 1278501429 468 DEPSAHLDVEQRLNVAKILRDVIKKK 493
Cdd:cd03257 170 DEPTSALDVSVQAQILDLLKKLQEEL 195
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
349-487 |
1.49e-16 |
|
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: 79.08 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKISYKPQYvQVENDDFVRSVLM------- 421
Cdd:COG1124 21 LKDVSLEVAPG-----ESFGLVGESGSGKSTLLRALAGLERPWSG----EVTFDGRPVT-RRRRKAFRRRVQMvfqdpya 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 422 -------------------------KTPPSMIERLDL-SHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:COG1124 91 slhprhtvdrilaeplrihglpdreERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALD 170
|
170
....*....|..
gi 1278501429 476 VeqrLNVAKILR 487
Cdd:COG1124 171 V---SVQAEILN 179
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
338-475 |
2.12e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 78.53 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKKLG------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVK--- 400
Cdd:COG1137 2 MTLEAENLVKSYGkrtvvkDVSLEVNQG-----EIVGLLGPNGAGKTTTFYMIVGLVKPDSGRifldgediTHLPMHkra 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 401 ---ISYKPQYVQV-------ENddfVRSVLMKTPPS----------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSR 460
Cdd:COG1137 77 rlgIGYLPQEASIfrkltveDN---ILAVLELRKLSkkereerleeLLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170
....*....|....*
gi 1278501429 461 DADVYLLDEPSAHLD 475
Cdd:COG1137 154 NPKFILLDEPFAGVD 168
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
83-278 |
2.76e-16 |
|
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: 75.56 E-value: 2.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 83 DKNGFKLFNLVIpQKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGndfgevegqkIIDFFKGTeaqnyfeklyttglets 162
Cdd:cd03221 12 GKLLLKDISLTI-NPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG----------IVTWGSTV----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 163 yKPQYVEQIprifkgsvkallnkisegdvnkvcnelgikhvlnrkvgdiSGGELQRVAIAGALLKKSDFLFIDEPSSYLD 242
Cdd:cd03221 64 -KIGYFEQL----------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLD 102
|
170 180 190
....*....|....*....|....*....|....*.
gi 1278501429 243 IKQRLKVANLLRKHgseKECAVVVEHDLIMLDYLAD 278
Cdd:cd03221 103 LESIEALEEALKEY---PGTVILVSHDRYFLDQVAT 135
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
342-499 |
4.11e-16 |
|
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: 77.61 E-value: 4.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 342 WSNIEKKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKT---DTSV-------------KISY-- 403
Cdd:cd03256 10 YPNGKKALKDVSLSINPG-----EFVALIGPSGAGKSTLLRCLNGLVEPTSGSVlidGTDInklkgkalrqlrrQIGMif 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 404 ------KPQYVqVEN--------DDFVRSVLMKTPP-------SMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDA 462
Cdd:cd03256 85 qqfnliERLSV-LENvlsgrlgrRSTWRSLFGLFPKeekqralAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278501429 463 DVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEASAFV 499
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKRINREEGITVIV 200
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
349-477 |
5.06e-16 |
|
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: 80.57 E-value: 5.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-------------TDTSVKISYKPQYVQV----- 410
Cdd:COG4988 353 LDGLSLTIPPG-----ERVALVGPSGAGKSTLLNLLLGFLPPYSGSilingvdlsdldpASWRRQIAWVPQNPYLfagti 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 411 -EN---------DDFVRSVLmktppsmiERLDLSHLLKR-------KLSE----LSGGELQRVAIAECLSRDADVYLLDE 469
Cdd:COG4988 428 rENlrlgrpdasDEELEAAL--------EAAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRLALARALLRDAPLLLLDE 499
|
....*...
gi 1278501429 470 PSAHLDVE 477
Cdd:COG4988 500 PTAHLDAE 507
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
335-474 |
5.16e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.46 E-value: 5.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 335 NNIPIIEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKISYKPQYV 408
Cdd:COG3845 1 MMPPALELRGITKRFGGVVanddvsLTVRPG-----EIHALLGENGAGKSTLMKILYGLYQPDSG----EILIDGKPVRI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 409 ---------------Q----------VENddfvrsVLMKTPPSMIERLDLSHLLKR--KLSE--------------LSGG 447
Cdd:COG3845 72 rsprdaialgigmvhQhfmlvpnltvAEN------IVLGLEPTKGGRLDRKAARARirELSErygldvdpdakvedLSVG 145
|
170 180
....*....|....*....|....*..
gi 1278501429 448 ELQRVAIAECLSRDADVYLLDEPSAHL 474
Cdd:COG3845 146 EQQRVEILKALYRGARILILDEPTAVL 172
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
344-486 |
7.08e-16 |
|
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: 78.99 E-value: 7.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 344 NIEKKLGDFKLKVK---PGilmrNEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVKISYKPQ-----Y 407
Cdd:COG4148 6 DFRLRRGGFTLDVDftlPG----RGVTALFGPSGSGKTTLLRAIAGLERPDSGRirlggevlQDSARGIFLPPHrrrigY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 408 V-Q---------V-ENDDFV--RSVLMKTPPSM---IERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPS 471
Cdd:COG4148 82 VfQearlfphlsVrGNLLYGrkRAPRAERRISFdevVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPL 161
|
170
....*....|....*
gi 1278501429 472 AHLDVEQRlnvAKIL 486
Cdd:COG4148 162 AALDLARK---AEIL 173
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
338-496 |
7.17e-16 |
|
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: 79.95 E-value: 7.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKKLGDFKLKVKPGI---LMRNEIIGVLGENGTGKTTFAKILAGMIkPDKGKTDTSVK-------------- 400
Cdd:COG1123 3 PLLEVRDLSVRYPGGDVPAVDGVsltIAPGETVALVGESGSGKSTLALALMGLL-PHGGRISGEVLldgrdllelsealr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 401 ---ISYKPQ-------YVQVEND-DFVRSVLMKTPPSMIER-------LDLSHLLKRKLSELSGGELQRVAIAECLSRDA 462
Cdd:COG1123 82 grrIGMVFQdpmtqlnPVTVGDQiAEALENLGLSRAEARARvlelleaVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190
....*....|....*....|....*....|....
gi 1278501429 463 DVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEAS 496
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTT 195
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
342-499 |
7.33e-16 |
|
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: 76.95 E-value: 7.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 342 WSNIEKKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKG---KTDTSV-------------KISYKP 405
Cdd:TIGR02315 11 YPNGKQALKNINLNINPG-----EFVAIIGPSGAGKSTLLRCINRLVEPSSGsilLEGTDItklrgkklrklrrRIGMIF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 406 Q-YVQVENDDFVRSVLM------KTPPSM---------------IERLDLSHLLKRKLSELSGGELQRVAIAECLSRDAD 463
Cdd:TIGR02315 86 QhYNLIERLTVLENVLHgrlgykPTWRSLlgrfseedkeralsaLERVGLADKAYQRADQLSGGQQQRVAIARALAQQPD 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 1278501429 464 VYLLDEPSAHLDVEQRLNVAKILRDVIKKKEASAFV 499
Cdd:TIGR02315 166 LILADEPIASLDPKTSKQVMDYLKRINKEDGITVII 201
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
338-475 |
7.61e-16 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 77.02 E-value: 7.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKK-------LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKT---DTSV-KISYKP- 405
Cdd:COG3638 1 PMLELRNLSKRypggtpaLDDVSLEIERG-----EFVALIGPSGAGKSTLLRCLNGLVEPTSGEIlvdGQDVtALRGRAl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 406 ------------QYVQVENDD--------------FVRSVLMKTPPSMI-------ERLDLSHLLKRKLSELSGGELQRV 452
Cdd:COG3638 76 rrlrrrigmifqQFNLVPRLSvltnvlagrlgrtsTWRSLLGLFPPEDReralealERVGLADKAYQRADQLSGGQQQRV 155
|
170 180
....*....|....*....|...
gi 1278501429 453 AIAECLSRDADVYLLDEPSAHLD 475
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLD 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
96-286 |
8.65e-16 |
|
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: 76.71 E-value: 8.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVegqkiidFFKGTEaqnyfeklyTTGLetsyKP-QYVE----- 169
Cdd:cd03219 24 RPGEIHGLIGPNGAGKTTLFNLISGFLRP----TSGSV-------LFDGED---------ITGL----PPhEIARlgigr 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 170 --QIPRIF-----------------KGSVKALLNKISEGDVNKVCNEL----GIKHVLNRKVGDISGGELQRVAIAGALL 226
Cdd:cd03219 80 tfQIPRLFpeltvlenvmvaaqartGSGLLLARARREEREARERAEELlervGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 227 KKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIMLDYLADveHIM---YGR 286
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLAD--RVTvldQGR 220
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
91-256 |
8.86e-16 |
|
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: 76.10 E-value: 8.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEgqkiidfFKGTEAQNYFEKLYTTGLETSYKPQY--- 167
Cdd:cd03268 20 SLHVK-KGEIYGFLGPNGAGKTTTMKIILGLIKP----DSGEIT-------FDGKSYQKNIEALRRIGALIEAPGFYpnl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 168 --VEQIprifkgSVKALLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQ 245
Cdd:cd03268 88 taRENL------RLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG 161
|
170
....*....|.
gi 1278501429 246 RLKVANLLRKH 256
Cdd:cd03268 162 IKELRELILSL 172
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
344-476 |
1.17e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 78.38 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 344 NIEKKLGDFKLKVK---PGilmrNEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVKISYKPQ-----Y 407
Cdd:PRK11144 5 NFKQQLGDLCLTVNltlPA----QGITAIFGRSGAGKTSLINAISGLTRPQKGRivlngrvlFDAEKGICLPPEkrrigY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 408 VQVENDDF----VRSVL---MKtpPSM-------IERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAH 473
Cdd:PRK11144 81 VFQDARLFphykVRGNLrygMA--KSMvaqfdkiVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
...
gi 1278501429 474 LDV 476
Cdd:PRK11144 159 LDL 161
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
81-278 |
1.46e-15 |
|
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: 74.36 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 81 SYDKN-GFKLFNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVE--GQKIIDffKGTEAQNYFeklytt 157
Cdd:cd03230 9 RYGKKtALDDISLTVE-KGEIYGLLGPNGAGKTTLIKIILGLLKP----DSGEIKvlGKDIKK--EPEEVKRRI------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 158 gletSYKPQYVEQIPRIfkgSVKALLnkisegdvnkvcnelgikhvlnrkvgDISGGELQRVAIAGALLKKSDFLFIDEP 237
Cdd:cd03230 76 ----GYLPEEPSLYENL---TVRENL--------------------------KLSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1278501429 238 SSYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIMLDYLAD 278
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCD 163
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
86-278 |
1.49e-15 |
|
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: 75.41 E-value: 1.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 86 GFKL-FNLVIPQkkQIMGLVGVNGIGKSTCLNILSGQLKPNLG----NDFGEVEGQKIIDFFK-----GTEAQNYfeKLY 155
Cdd:cd03297 12 DFTLkIDFDLNE--EVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlNGTVLFDSRKKINLPPqqrkiGLVFQQY--ALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 156 T-----TGLETSYKPQYVEQIpRIFkgsvkallnkisegdVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSD 230
Cdd:cd03297 88 PhlnvrENLAFGLKRKRNRED-RIS---------------VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1278501429 231 FLFIDEPSSYLDIKQRLKVANLLRK-HGSEKECAVVVEHDLIMLDYLAD 278
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKQiKKNLNIPVIFVTHDLSEAEYLAD 200
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
90-270 |
2.33e-15 |
|
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: 74.86 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 90 FNLVIPQKkQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVE--GQKIID-----------FfkgteaQNYfeKLYT 156
Cdd:cd03259 19 LSLTVEPG-EFLALLGPSGCGKTTLLRLIAGLERP----DSGEILidGRDVTGvpperrnigmvF------QDY--ALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 157 T---------GLETSYKPQyvEQIPRifkgSVKALLNkisegdvnkvcnELGIKHVLNRKVGDISGGELQRVAIAGALLK 227
Cdd:cd03259 86 HltvaeniafGLKLRGVPK--AEIRA----RVRELLE------------LVGLEGLLNRYPHELSGGQQQRVALARALAR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1278501429 228 KSDFLFIDEPSSYLDIKQRL----KVANLLRKHGSekeCAVVVEHDL 270
Cdd:cd03259 148 EPSLLLLDEPLSALDAKLREelreELKELQRELGI---TTIYVTHDQ 191
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
210-484 |
2.81e-15 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 78.31 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 210 DISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVV-EHDLIMLDYLADVEHIMYGrag 288
Cdd:TIGR03269 168 DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLtSHWPEVIEDLSDKAIWLEN--- 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 289 vyGIVSKSLSIRECINTYLEGYirEDNMRFRseeiKFEVKAPTKALNNIPIIEWS---NIEKKLGDFKLKVKPGilmrnE 365
Cdd:TIGR03269 245 --GEIKEEGTPDEVVAVFMEGV--SEVEKEC----EVEVGEPIIKVRNVSKRYISvdrGVVKAVDNVSLEVKEG-----E 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 366 IIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVKISY----KP---------QYVQVENDDFV----RSVLMKTP---- 424
Cdd:TIGR03269 312 IFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWvdmtKPgpdgrgrakRYIGILHQEYDlyphRTVLDNLTeaig 391
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 425 ---PSMIERLDLSHLLK--------------RKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAK 484
Cdd:TIGR03269 392 lelPDELARMKAVITLKmvgfdeekaeeildKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTH 468
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
80-270 |
3.97e-15 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 74.22 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 80 HSYDKNGFKLFNLVIP-QKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIidffkgteaqNYFEKLYTTG 158
Cdd:cd03226 7 FSYKKGTEILDDLSLDlYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSIL--LNGKPI----------KAKERRKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 159 letsykpqYVEQIPR--IFKGSVKALL---NKI---SEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSD 230
Cdd:cd03226 75 --------YVMQDVDyqLFTDSVREELllgLKEldaGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1278501429 231 FLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDL 270
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDY 186
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
352-475 |
4.02e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.79 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 352 FKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsvkisykpqyVQVENDDfvrsvLMKTPP-----S 426
Cdd:COG3840 18 FDLTIAAG-----ERVAILGPSGAGKSTLLNLIAGFLPPDSGR-------------ILWNGQD-----LTALPPaerpvS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 427 MI--------------------------------------ERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLD 468
Cdd:COG3840 75 MLfqennlfphltvaqniglglrpglkltaeqraqveqalERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
....*..
gi 1278501429 469 EPSAHLD 475
Cdd:COG3840 155 EPFSALD 161
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
343-489 |
4.13e-15 |
|
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: 74.78 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 343 SNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TD-TSVK--------IS 402
Cdd:cd03219 4 RGLTKRFGGLValddvsFSVRPG-----EIHGLIGPNGAGKTTLFNLISGFLRPTSGSvlfdgEDiTGLPpheiarlgIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 403 YKPQYVQV-------ENddfVR-SVLMKTPPS-------------------MIERLDLSHLLKRKLSELSGGELQRVAIA 455
Cdd:cd03219 79 RTFQIPRLfpeltvlEN---VMvAAQARTGSGlllararreereareraeeLLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190
....*....|....*....|....*....|....
gi 1278501429 456 ECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDV 489
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIREL 189
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
340-479 |
4.18e-15 |
|
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: 74.58 E-value: 4.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVKI-----SYKPQYV 408
Cdd:cd03300 1 IELENVSKFYGGFValdgvsLDIKEG-----EFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 409 QV-------------ENDDF-VRsvLMKTPPSMIER--------LDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYL 466
Cdd:cd03300 76 TVfqnyalfphltvfENIAFgLR--LKKLPKAEIKErvaealdlVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170
....*....|...
gi 1278501429 467 LDEPSAHLDVEQR 479
Cdd:cd03300 154 LDEPLGALDLKLR 166
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
344-487 |
5.14e-15 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 74.62 E-value: 5.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 344 NIEKKLG------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TDTSVK---------ISY 403
Cdd:TIGR04406 6 NLIKSYKkrkvvnDVSLSVKSG-----EIVGLLGPNGAGKTTSFYMIVGLVRPDAGKilidgQDITHLpmherarlgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 404 KPQYVQV-------EN--------DDFVRSVLMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLD 468
Cdd:TIGR04406 81 LPQEASIfrkltveENimavleirKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170
....*....|....*....
gi 1278501429 469 EPSAHLDVEQRLNVAKILR 487
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIK 179
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
349-496 |
5.16e-15 |
|
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: 74.29 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVKISYKpqyvqvENDDFVR--SVLM--KT- 423
Cdd:cd03267 37 LKGISFTIEKG-----EIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWK------RRKKFLRriGVVFgqKTq 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 424 --------------------PPS--------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:cd03267 106 lwwdlpvidsfyllaaiydlPPArfkkrldeLSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180
....*....|....*....|.
gi 1278501429 476 VEQRLNVAKILRDVIKKKEAS 496
Cdd:cd03267 186 VVAQENIRNFLKEYNRERGTT 206
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
344-492 |
5.44e-15 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 73.80 E-value: 5.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 344 NIEKKLG------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsVKISYK--PQYVQVENDDF 415
Cdd:TIGR03608 3 NISKKFGdkvildDLNLTIEKG-----KMYAIIGESGSGKSTLLNIIGLLEKFDSGQ----VYLNGQetPPLNSKKASKF 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 416 VRSVL---------------------------------MKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDA 462
Cdd:TIGR03608 74 RREKLgylfqnfalienetveenldlglkykklskkekREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPP 153
|
170 180 190
....*....|....*....|....*....|
gi 1278501429 463 DVYLLDEPSAHLDVEQRLNVAKILRDVIKK 492
Cdd:TIGR03608 154 PLILADEPTGSLDPKNRDEVLDLLLELNDE 183
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
338-488 |
5.76e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.81 E-value: 5.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKKLG------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsVKI------SYK- 404
Cdd:PRK13548 1 AMLEARNLSVRLGgrtlldDVSLTLRPG-----EVVAILGPNGAGKSTLLRALSGELSPDSGE----VRLngrplaDWSp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 405 ----------PQYVQVENDDFVRSV--------------LMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECL-- 458
Cdd:PRK13548 72 aelarrravlPQHSSLSFPFTVEEVvamgraphglsraeDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaq 151
|
170 180 190
....*....|....*....|....*....|....
gi 1278501429 459 ----SRDADVYLLDEPSAHLDVEQRLNVAKILRD 488
Cdd:PRK13548 152 lwepDGPPRWLLLDEPTSALDLAHQHHVLRLARQ 185
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
103-270 |
6.13e-15 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 73.04 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEGqkiidffkgteaqnyfeklyTTGLETSYKPQYVEqIPRIFKGSV--- 179
Cdd:NF040873 23 VVGPNGSGKSTLLKVLAGVLRP----TSGTVRR--------------------AGGARVAYVPQRSE-VPDSLPLTVrdl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 180 --------KALLNKISEGD---VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLK 248
Cdd:NF040873 78 vamgrwarRGLWRRLTRDDraaVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180
....*....|....*....|..
gi 1278501429 249 VANLLRKHGSEKECAVVVEHDL 270
Cdd:NF040873 158 IIALLAEEHARGATVVVVTHDL 179
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
99-476 |
7.90e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 7.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKpnlgNDFGEVE--GQKIIdfFKGTEAQNyfeklyTTGL-----ETSYKPQY--VE 169
Cdd:PRK10762 31 RVMALVGENGAGKSTMMKVLTGIYT----RDAGSILylGKEVT--FNGPKSSQ------EAGIgiihqELNLIPQLtiAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 170 QI--PRIFKGSVKALLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYL---DIK 244
Cdd:PRK10762 99 NIflGREFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtdtETE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 245 QRLKVANLLRKHGsekecavvvehdlimldyladvehimygragvYGIVSKSLSIRECINtylegyIREDNMRFRseEIK 324
Cdd:PRK10762 179 SLFRVIRELKSQG--------------------------------RGIVYISHRLKEIFE------ICDDVTVFR--DGQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 325 FEVKAPTKALNNIPIIE----------WSNIEKKLGDFKLKVK----PGI------LMRNEIIGVLGENGTGKTTFAKIL 384
Cdd:PRK10762 219 FIAEREVADLTEDSLIEmmvgrkledqYPRLDKAPGEVRLKVDnlsgPGVndvsftLRKGEILGVSGLMGAGRTELMKVL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 385 AGMIKPDKG-----------------------------KTD-----TSVK---------------ISYKPQYVQVENDDF 415
Cdd:PRK10762 299 YGALPRTSGyvtldghevvtrspqdglangivyisedrKRDglvlgMSVKenmsltalryfsragGSLKHADEQQAVSDF 378
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 416 VRSVLMKTPpSMIERLDLshllkrklseLSGGELQRVAIAECLSRDADVYLLDEPSAHLDV 476
Cdd:PRK10762 379 IRLFNIKTP-SMEQAIGL----------LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDV 428
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
349-489 |
8.11e-15 |
|
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: 76.94 E-value: 8.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVK-----ISYKPQYVQVENDDF 415
Cdd:TIGR02857 338 LRPVSFTVPPG-----ERVALVGPSGAGKSTLLNLLLGFVDPTEGSiavngvplADADADswrdqIAWVPQHPFLFAGTI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 416 VRSVLMKTP---PSMIERL-----------DLSHLLKRKLSE----LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:TIGR02857 413 AENIRLARPdasDAEIREAleragldefvaALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170
....*....|..
gi 1278501429 478 QRLNVAKILRDV 489
Cdd:TIGR02857 493 TEAEVLEALRAL 504
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
338-490 |
8.42e-15 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 8.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKKLGDfkLKVKPGI---LMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGK-------------TDTSVKI 401
Cdd:PRK09536 2 PMIDVSDLSVEFGD--TTVLDGVdlsVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTvlvagddvealsaRAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 402 SYKPQYVQVENDDFVRSVL-M-KTP----------------PSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDAD 463
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVeMgRTPhrsrfdtwtetdraavERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180
....*....|....*....|....*..
gi 1278501429 464 VYLLDEPSAHLDVEQRLNVAKILRDVI 490
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLV 186
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
344-493 |
1.26e-14 |
|
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: 71.96 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 344 NIEKKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtsvkisykpqyvQVENDDFVRSVLMKT 423
Cdd:cd03247 13 QEQQVLKNLSLELKQG-----EKIALLGRSGSGKSTLLQLLTGDLKPQQG---------------EITLDGVPVSDLEKA 72
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 424 PPSMIERLDLS-HLLKRKLSE-----LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKK 493
Cdd:cd03247 73 LSSLISVLNQRpYLFDTTLRNnlgrrFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK 148
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
99-476 |
1.44e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 75.83 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGE--VEGQKIIdfFKGT-EAQNYfeklyttGLETSYkpQYVEQIPR-- 173
Cdd:COG1129 31 EVHALLGENGAGKSTLMKILSGVYQP----DSGEilLDGEPVR--FRSPrDAQAA-------GIAIIH--QELNLVPNls 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 174 ----IFKGSVKALLNKISEGDVNK----VCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIK- 244
Cdd:COG1129 96 vaenIFLGREPRRGGLIDWRAMRRrareLLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTERe 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 245 -QRL-KVANLLRKHGsekeCAVV-VEHDL--IMldYLAD---V----EHIMYGRAG-------VYGIVSKSLSirecint 305
Cdd:COG1129 176 vERLfRIIRRLKAQG----VAIIyISHRLdeVF--EIADrvtVlrdgRLVGTGPVAeltedelVRLMVGRELE------- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 306 ylEGYIREDNmrfRSEEIKFEVKaptkalnnipiiEWSNiEKKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILA 385
Cdd:COG1129 243 --DLFPKRAA---APGEVVLEVE------------GLSV-GGVVRDVSFSVRAG-----EILGIAGLVGAGRTELARALF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 386 GMIKPDKGK---TDTSVKISyKPQ--------YV------Q--------VEN------DDFVRSVLMKTP------PSMI 428
Cdd:COG1129 300 GADPADSGEirlDGKPVRIR-SPRdairagiaYVpedrkgEglvldlsiRENitlaslDRLSRGGLLDRRreralaEEYI 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1278501429 429 ERLDL-SHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDV 476
Cdd:COG1129 379 KRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDV 427
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
338-475 |
1.69e-14 |
|
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: 73.09 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsvkisykpqyVQVE 411
Cdd:COG1127 4 PMIEVRNLTKSFGDRVvldgvsLDVPRG-----EILAIIGGSGSGKSVLLKLIIGLLRPDSGE-------------ILVD 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 412 NDDFVR--------------------------SVL--------MKT--PPSMIERL--------DLSHLLKRKLSELSGG 447
Cdd:COG1127 66 GQDITGlsekelyelrrrigmlfqggalfdslTVFenvafplrEHTdlSEAEIRELvleklelvGLPGAADKMPSELSGG 145
|
170 180
....*....|....*....|....*...
gi 1278501429 448 ELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLD 173
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
363-475 |
1.79e-14 |
|
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: 72.14 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKGKTD------TSVKISYKP-----------QYVQVE-NDDFVRSVLMKTP 424
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLingvdvTAAPPADRPvsmlfqennlfAHLTVEqNVGLGLSPGLKLT 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 425 P-------SMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:cd03298 103 AedrqaieVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
349-489 |
2.35e-14 |
|
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: 75.47 E-value: 2.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKG-------------KTDTSVKISYKPQYVQVeNDDF 415
Cdd:TIGR02868 351 LDGVSLDLPPG-----ERVAILGPSGSGKSTLLATLAGLLDPLQGevtldgvpvssldQDEVRRRVSVCAQDAHL-FDTT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 416 VRSVLMKTPP--------SMIERLDLSHLLKR-------KLSE----LSGGELQRVAIAECLSRDADVYLLDEPSAHLDV 476
Cdd:TIGR02868 425 VRENLRLARPdatdeelwAALERVGLADWLRAlpdgldtVLGEggarLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170
....*....|...
gi 1278501429 477 EQRLNVAKILRDV 489
Cdd:TIGR02868 505 ETADELLEDLLAA 517
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
1-68 |
2.35e-14 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 68.15 E-value: 2.35e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 1 MRiVVVNKKKCTagkGCdYVCMNFCPinrtgKDCIVEGaDGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:COG4231 15 MR-YVIDEDKCT---GC-GACVKVCP-----ADAIEEG-DGKAVIDPDLCIGCGSCVQVCPVDAIKLE 71
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
349-495 |
3.21e-14 |
|
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: 72.13 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKT-------DTSVKISYKPQ--YVQVENDDFVRSV 419
Cdd:cd03252 18 LDNISLRIKPG-----EVVGIVGRSGSGKSTLTKLIQRFYVPENGRVlvdghdlALADPAWLRRQvgVVLQENVLFNRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 420 -----LMKTPPSM---IE--RLDLSHLLKRKLSE------------LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:cd03252 93 rdniaLADPGMSMervIEaaKLAGAHDFISELPEgydtivgeqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYE 172
|
170
....*....|....*...
gi 1278501429 478 QRLNVAKILRDVIKKKEA 495
Cdd:cd03252 173 SEHAIMRNMHDICAGRTV 190
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
364-476 |
3.72e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 3.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 364 NEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSV--KISY-------KPQYVQVENDDFVRSVLMKTPPS 426
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTikldggdiDDPDVaeACHYlghrnamKPALTVAENLEFWAAFLGGEELD 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 427 M---IERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDV 476
Cdd:PRK13539 108 IaaaLEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
349-494 |
3.83e-14 |
|
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: 72.46 E-value: 3.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TDTSV-----KISYK-------P--QYV- 408
Cdd:TIGR04520 18 LKNVSLSIEKG-----EFVAIIGHNGSGKSTLAKLLNGLLLPTSGKvtvdgLDTLDeenlwEIRKKvgmvfqnPdnQFVg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 409 -QVENDdfvrsV------LMKTPPSMIERLD-------LSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHL 474
Cdd:TIGR04520 93 aTVEDD-----VafglenLGVPREEMRKRVDealklvgMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSML 167
|
170 180
....*....|....*....|
gi 1278501429 475 DVEQRLNVAKILRDvIKKKE 494
Cdd:TIGR04520 168 DPKGRKEVLETIRK-LNKEE 186
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
91-286 |
5.59e-14 |
|
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: 71.59 E-value: 5.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVegqKIIDFFKGTEAQNYFEKLyttGLETSYKPQYVEQ 170
Cdd:cd03267 41 SFTIE-KGEIVGFIGPNGAGKTTTLKILSGLLQP----TSGEV---RVAGLVPWKRRKKFLRRI---GVVFGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 IPRIFKGSVKALLNKISEGD----VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQR 246
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARfkkrLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQ 189
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1278501429 247 LKVANLLRKHGSEKECAVVV-EHDLIMLDYLAD-VEHIMYGR 286
Cdd:cd03267 190 ENIRNFLKEYNRERGTTVLLtSHYMKDIEALARrVLVIDKGR 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
364-487 |
6.35e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.58 E-value: 6.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 364 NEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVK-----ISYKPQYVQVENDDFVRSVLM--KTP---- 424
Cdd:PRK11231 28 GKITALIGPNGCGKSTLLKCFARLLTPQSGTvflgdkpiSMLSSRqlarrLALLPQHHLTPEGITVRELVAygRSPwlsl 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278501429 425 ------------PSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILR 487
Cdd:PRK11231 108 wgrlsaednarvNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
80-278 |
6.43e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.95 E-value: 6.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 80 HSY-DKNGFKLFNLVIpQKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEgqkiidffkgteaqnyfeklYTTG 158
Cdd:COG0488 323 KSYgDKTLLDDLSLRI-DRGDRIGLIGPNGAGKSTLLKLLAGELEP----DSGTVK--------------------LGET 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 159 LETSYKPQYVEQipriFKGSvKALLNKISEGDVNKvcNELGIKHVLNR----------KVGDISGGELQRVAIAGALLKK 228
Cdd:COG0488 378 VKIGYFDQHQEE----LDPD-KTVLDELRDGAPGG--TEQEVRGYLGRflfsgddafkPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1278501429 229 SDFLFIDEPSSYLDIKQRLKVANLLRKHgseKECAVVVEHDLIMLDYLAD 278
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEALDDF---PGTVLLVSHDRYFLDRVAT 497
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
337-479 |
7.42e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 72.15 E-value: 7.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 337 IPIIEWSNIEKKLGD------FKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKTD------------TS 398
Cdd:PRK13537 5 VAPIDFRNVEKRYGDklvvdgLSFHVQRG-----ECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISlcgepvpsrarhAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 399 VKISYKPQYVQVENDDFVRSVLM--------------KTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADV 464
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVRENLLvfgryfglsaaaarALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170
....*....|....*
gi 1278501429 465 YLLDEPSAHLDVEQR 479
Cdd:PRK13537 160 LVLDEPTTGLDPQAR 174
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
349-488 |
8.70e-14 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 71.30 E-value: 8.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsvkISYK-------------------PQYVQ 409
Cdd:COG4559 17 LDDVSLTLRPG-----ELTAIIGPNGAGKSTLLKLLTGELTPSSGE------VRLNgrplaawspwelarrravlPQHSS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 410 V----------------------ENDDFVRSVLmktppsmiERLDLSHLLKRKLSELSGGELQRVAIAECL-----SRDA 462
Cdd:COG4559 86 LafpftveevvalgraphgssaaQDRQIVREAL--------ALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqlwePVDG 157
|
170 180
....*....|....*....|....*...
gi 1278501429 463 D--VYLLDEPSAHLDVEQRLNVAKILRD 488
Cdd:COG4559 158 GprWLFLDEPTSALDLAHQHAVLRLARQ 185
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
349-480 |
8.94e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 8.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKG--KTDTSVKISYKPQYVQVEND-DFVRSVLMKTPP 425
Cdd:PRK09544 20 LSDVSLELKPG-----KILTLLGPNGAGKSTLVRVVLGLVAPDEGviKRNGKLRIGYVPQKLYLDTTlPLTVNRFLRLRP 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 426 SM--------IERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRL 480
Cdd:PRK09544 95 GTkkedilpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV 157
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
340-489 |
9.89e-14 |
|
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: 70.13 E-value: 9.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKK-------LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TDTS----VKISY 403
Cdd:cd03292 1 IEFINVTKTypngtaaLDGINISISAG-----EFVFLVGPSGAGKSTLLKLIYKEELPTSGTirvngQDVSdlrgRAIPY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 404 KPQYVQV--------------ENDDFVRSVLMKTP-------PSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDA 462
Cdd:cd03292 76 LRRKIGVvfqdfrllpdrnvyENVAFALEVTGVPPreirkrvPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSP 155
|
170 180
....*....|....*....|....*..
gi 1278501429 463 DVYLLDEPSAHLDVEQRLNVAKILRDV 489
Cdd:cd03292 156 TILIADEPTGNLDPDTTWEIMNLLKKI 182
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
349-493 |
1.03e-13 |
|
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: 70.31 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKT---DTSVK----------ISYKPQYVQVENDDF 415
Cdd:cd03245 20 LDNVSLTIRAG-----EKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVlldGTDIRqldpadlrrnIGYVPQDVTLFYGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 416 VRSVLMKTPPSMIERL--------------DLSHLLKRKLSE----LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:cd03245 95 RDNITLGAPLADDERIlraaelagvtdfvnKHPNGLDLQIGErgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMN 174
|
170
....*....|....*.
gi 1278501429 478 QRLNVAKILRDVIKKK 493
Cdd:cd03245 175 SEERLKERLRQLLGDK 190
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
90-269 |
1.03e-13 |
|
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: 69.98 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 90 FNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPNLG------NDFGEVEGQK--IIDFFkgteaQNYfeKLY--TTGL 159
Cdd:cd03301 19 LNLDIA-DGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGriyiggRDVTDLPPKDrdIAMVF-----QNY--ALYphMTVY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 160 ETSYKPQYVEQIPRifkgsvkallNKISEGdVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSS 239
Cdd:cd03301 91 DNIAFGLKLRKVPK----------DEIDER-VREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190
....*....|....*....|....*....|.
gi 1278501429 240 YLDIKQRLKV-ANLLRKHGSEKECAVVVEHD 269
Cdd:cd03301 160 NLDAKLRVQMrAELKRLQQRLGTTTIYVTHD 190
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
363-490 |
1.60e-13 |
|
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: 69.62 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKGK---------TDTSVKISYKPQYVQVENDDFVRSVLM------------ 421
Cdd:cd03269 25 KGEIFGLLGPNGAGKTTTIRMILGIILPDSGEvlfdgkpldIAARNRIGYLPEERGLYPKMKVIDQLVylaqlkglkkee 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 422 --KTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVeqrLNVaKILRDVI 490
Cdd:cd03269 105 arRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP---VNV-ELLKDVI 171
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
103-270 |
1.95e-13 |
|
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: 70.11 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQLKPNLGND---FGEVEG--------QKIidffkG---TEAQNYFEKlYTTGLETsykpqyv 168
Cdd:COG1119 34 ILGPNGAGKSTLLSLITGDLPPTYGNDvrlFGERRGgedvwelrKRI-----GlvsPALQLRFPR-DETVLDV------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 169 eqiprI---FKGSVkALLNKISEGDVNKVC---NELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLD 242
Cdd:COG1119 101 -----VlsgFFDSI-GLYREPTDEQRERARellELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLD 174
|
170 180
....*....|....*....|....*....
gi 1278501429 243 IKQRLKVANLLRKHGSEKECAVV-VEHDL 270
Cdd:COG1119 175 LGARELLLALLDKLAAEGAPTLVlVTHHV 203
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
99-255 |
2.08e-13 |
|
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: 69.61 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLkPNLGNDFGEVegqkiidFFKGTEAqnyfeKLYTTGLETSYKPQY--------VEQ 170
Cdd:cd03234 34 QVMAILGSSGSGKTTLLDAISGRV-EGGGTTSGQI-------LFNGQPR-----KPDQFQKCVAYVRQDdillpgltVRE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 ---------IPRIFKGSVKallnkiSEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYL 241
Cdd:cd03234 101 tltytailrLPRKSSDAIR------KKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170
....*....|....
gi 1278501429 242 DIKQRLKVANLLRK 255
Cdd:cd03234 175 DSFTALNLVSTLSQ 188
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
80-288 |
2.64e-13 |
|
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: 69.04 E-value: 2.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 80 HSYDKNGFKL-----FNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEgqkiidfFKGTEAQnyfekl 154
Cdd:cd03293 8 KTYGGGGGAVtaledISLSVE-EGEFVALVGPSGCGKSTLLRIIAGLERP----TSGEVL-------VDGEPVT------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 155 yttglETSYKPQYVEQIPRIF---------------KGSVKALLNKISEGDVNKVcnelGIKHVLNRKVGDISGGELQRV 219
Cdd:cd03293 70 -----GPGPDRGYVFQQDALLpwltvldnvalglelQGVPKAEARERAEELLELV----GLSGFENAYPHQLSGGMRQRV 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 220 AIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDlimLD---YLADVEHIMYGRAG 288
Cdd:cd03293 141 ALARALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLlVTHD---IDeavFLADRVVVLSARPG 210
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
351-499 |
3.17e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 68.83 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 351 DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIK--PDKGKTDTSVKISYkpqyvqvENDDFVRSVLMKTPPSM- 427
Cdd:COG2401 48 DLNLEIEPG-----EIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFG-------REASLIDAIGRKGDFKDa 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 428 IERLD---LS--HLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEASAFV 499
Cdd:COG2401 116 VELLNavgLSdaVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVV 192
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
354-492 |
3.38e-13 |
|
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: 68.61 E-value: 3.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 354 LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK------------TDTSVK--ISYKPQYVQV-------EN 412
Cdd:cd03224 21 LTVPEG-----EIVALLGRNGAGKTTLLKTIMGLLPPRSGSirfdgrditglpPHERARagIGYVPEGRRIfpeltveEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 413 -----DDFVRSVLMKTPPSMIERL-DLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD---VEQrlnVA 483
Cdd:cd03224 96 lllgaYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLApkiVEE---IF 172
|
....*....
gi 1278501429 484 KILRDVIKK 492
Cdd:cd03224 173 EAIRELRDE 181
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
340-499 |
3.39e-13 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 70.88 E-value: 3.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLG------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMikpdkgKTDTSVKISYKPQYV----- 408
Cdd:PRK10851 3 IEIANIKKSFGrtqvlnDISLDIPSG-----QMVALLGPSGSGKTTLLRIIAGL------EHQTSGHIRFHGTDVsrlha 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 409 ---QV----------------ENDDFVRSVL-MKTPPS----------MIERLDLSHLLKRKLSELSGGELQRVAIAECL 458
Cdd:PRK10851 72 rdrKVgfvfqhyalfrhmtvfDNIAFGLTVLpRRERPNaaaikakvtqLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1278501429 459 SRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKK-KEASAFV 499
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFV 193
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
99-286 |
4.11e-13 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 71.47 E-value: 4.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVegqkiidFFKGTEaqnyfeklYTTGLETSYKP-----QYVEQ--- 170
Cdd:COG1123 292 ETLGLVGESGSGKSTLARLLLGLLRP----TSGSI-------LFDGKD--------LTKLSRRSLRElrrrvQMVFQdpy 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 ---IPRIfkgSVKA-------LLNKISEGDVNKVCNEL----GI-KHVLNRKVGDISGGELQRVAIAGALLKKSDFLFID 235
Cdd:COG1123 353 sslNPRM---TVGDiiaeplrLHGLLSRAERRERVAELlervGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILD 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 236 EPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDLIMLDYLADVEHIMY-GR 286
Cdd:COG1123 430 EPTSALDVSVQAQILNLLRDLQRELGLTYLfISHDLAVVRYIADRVAVMYdGR 482
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
352-489 |
4.69e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.46 E-value: 4.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 352 FKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsvkisykpqyVQVENDDFVRSVLMKTPPSMI--- 428
Cdd:PRK10771 18 FDLTVERG-----ERVAILGPSGAGKSTLLNLIAGFLTPASGS-------------LTLNGQDHTTTPPSRRPVSMLfqe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 429 -----------------------------------ERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAH 473
Cdd:PRK10771 80 nnlfshltvaqniglglnpglklnaaqreklhaiaRQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSA 159
|
170
....*....|....*.
gi 1278501429 474 LDVEQRLNVAKILRDV 489
Cdd:PRK10771 160 LDPALRQEMLTLVSQV 175
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
349-483 |
5.01e-13 |
|
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: 67.24 E-value: 5.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsVKISYKP--QYVQVENDDFVRSVlmktpPS 426
Cdd:cd03246 18 LRNVSFSIEPG-----ESLAIIGPSGSGKSTLARLILGLLRPTSGR----VRLDGADisQWDPNELGDHVGYL-----PQ 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 427 MIErldlshLLKRKLSE--LSGGELQRVAIAECLSRDADVYLLDEPSAHLDV--EQRLNVA 483
Cdd:cd03246 84 DDE------LFSGSIAEniLSGGQRQRLGLARALYGNPRILVLDEPNSHLDVegERALNQA 138
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
102-483 |
7.94e-13 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 70.69 E-value: 7.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 102 GLVGVNGIGKSTCLNILSGQLKPNLGNDFGEVeGQKIidffkGTEAQNYFeklyttgletSYKPQYVeqIPRIFKG---- 177
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSLDP-NERL-----GKLRQDQF----------AFEEFTV--LDTVIMGhtel 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 178 -SVKALLNKI------SEGDVNKVCN----------------------ELGI---KHvlNRKVGDISGGELQRVAIAGAL 225
Cdd:PRK15064 93 wEVKQERDRIyalpemSEEDGMKVADlevkfaemdgytaearagelllGVGIpeeQH--YGLMSEVAPGWKLRVLLAQAL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 226 LKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEkecAVVVEHDLIMLD----YLADVEhimYGRAGVY----------- 290
Cdd:PRK15064 171 FSNPDILLLDEPTNNLDINTIRWLEDVLNERNST---MIIISHDRHFLNsvctHMADLD---YGELRVYpgnydeymtaa 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 291 ---------GIVSKSLSIREcintyLEGYIRednmRF---------------RSEEIKF-EVKA-----------PTKAL 334
Cdd:PRK15064 245 tqarerllaDNAKKKAQIAE-----LQSFVS----RFsanaskakqatsrakQIDKIKLeEVKPssrqnpfirfeQDKKL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 335 -NNIPIIEwsNIEKKLG------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKG--KTDTSVKISYKP 405
Cdd:PRK15064 316 hRNALEVE--NLTKGFDngplfkNLNLLLEAG-----ERLAIIGENGVGKTTLLRTLVGELEPDSGtvKWSENANIGYYA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 406 Q------------------YVQVENDD-FVRSVLmktppsmiERLDLSH-LLKRKLSELSGGELQRVAIAECLSRDADVY 465
Cdd:PRK15064 389 QdhaydfendltlfdwmsqWRQEGDDEqAVRGTL--------GRLLFSQdDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
|
490 500
....*....|....*....|
gi 1278501429 466 LLDEPSAHLDVE--QRLNVA 483
Cdd:PRK15064 461 VMDEPTNHMDMEsiESLNMA 480
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
91-278 |
1.00e-12 |
|
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: 67.49 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIpQKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIIDffKGTEA----QNYFEKLYTTGLETSYKpq 166
Cdd:TIGR01184 5 NLTI-QQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVI--LEGKQITE--PGPDRmvvfQNYSLLPWLTVRENIAL-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 167 yveqiprifkgSVKALLNKISEGDVNKVCNE----LGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLD 242
Cdd:TIGR01184 78 -----------AVDRVLPDLSKSERRAIVEEhialVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALD 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278501429 243 IKQRLKVANLLRKHGSEKEC-AVVVEHDLIMLDYLAD 278
Cdd:TIGR01184 147 ALTRGNLQEELMQIWEEHRVtVLMVTHDVDEALLLSD 183
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
319-492 |
1.17e-12 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 69.09 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 319 RSEEIKFEVKAPTKALNNIPIIEWSNIEKKLGD------FKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDK 392
Cdd:PRK13536 21 RKHQGISEAKASIPGSMSTVAIDLAGVSKSYGDkavvngLSFTVASG-----ECFGLLGPNGAGKSTIARMILGMTSPDA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 393 GKTD------------TSVKISYKPQYVQVENDDFVRSVL--------MKTP------PSMIERLDLSHLLKRKLSELSG 446
Cdd:PRK13536 96 GKITvlgvpvpararlARARIGVVPQFDNLDLEFTVRENLlvfgryfgMSTReieaviPSLLEFARLESKADARVSDLSG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1278501429 447 GELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKK 492
Cdd:PRK13536 176 GMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLAR 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
334-499 |
1.17e-12 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.90 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 334 LNNIPIIEWSNIEKK--LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPdKGKTDTSV----------KI 401
Cdd:cd03233 6 WRNISFTTGKGRSKIpiLKDFSGVVKPG-----EMVLVLGRPGSGCSTLLKALANRTEG-NVSVEGDIhyngipykefAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 402 SYKPQYVQVENDDFVRSVLmktppSMIERLDLSHLLK--RKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQR 479
Cdd:cd03233 80 KYPGEIIYVSEEDVHFPTL-----TVRETLDFALRCKgnEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154
|
170 180
....*....|....*....|
gi 1278501429 480 LNVAKILRDVIKKKEASAFV 499
Cdd:cd03233 155 LEILKCIRTMADVLKTTTFV 174
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
91-282 |
1.22e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.26 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPQKKQImGLVGVNGIGKSTCLNILSGQLKpnlgndfgeVEGQKIIDffkGTEAQNyfeklyttgLE-TSYKPQ--Y 167
Cdd:PRK11174 370 NFTLPAGQRI-ALVGPSGAGKTSLLNALLGFLP---------YQGSLKIN---GIELRE---------LDpESWRKHlsW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 168 VEQIPRIFKGSVKA--LLNK--ISEGDVNKVCNELGIK-------HVLNRKVGD----ISGGELQRVAIAGALLKKSDFL 232
Cdd:PRK11174 428 VGQNPQLPHGTLRDnvLLGNpdASDEQLQQALENAWVSeflpllpQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLL 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1278501429 233 FIDEPSSYLDIKQRLKVANLLrKHGSEKECAVVVEHdliMLDYLADVEHI 282
Cdd:PRK11174 508 LLDEPTASLDAHSEQLVMQAL-NAASRRQTTLMVTH---QLEDLAQWDQI 553
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
91-243 |
1.27e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 69.13 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPQKKqIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEV--EGQKIIDFFKG----TEAQNyfeklytTGletsyk 164
Cdd:PRK11144 18 NLTLPAQG-ITAIFGRSGAGKTSLINAISGLTRP----QKGRIvlNGRVLFDAEKGiclpPEKRR-------IG------ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 165 pqYVEQIPRIF-----KGSVKALLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSS 239
Cdd:PRK11144 80 --YVFQDARLFphykvRGNLRYGMAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLA 157
|
....
gi 1278501429 240 YLDI 243
Cdd:PRK11144 158 SLDL 161
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
92-292 |
1.37e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.89 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 92 LVIPQKKqIMGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDffkGTEAQNYFEKLYTTglETSYKPQyveQI 171
Cdd:PRK10575 32 LTFPAGK-VTGLIGHNGSGKSTLLKMLGRHQPPS--------EGEILLD---AQPLESWSSKAFAR--KVAYLPQ---QL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 172 PRIFKGSVKAL-----------LNKISEGDVNKVCNEL---GIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEP 237
Cdd:PRK10575 95 PAAEGMTVRELvaigrypwhgaLGRFGAADREKVEEAIslvGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEP 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 238 SSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDLIM----LDYL-----------ADVEHIMYGRA--GVYGI 292
Cdd:PRK10575 175 TSALDIAHQVDVLALVHRLSQERGLTVIaVLHDINMaaryCDYLvalrggemiaqGTPAELMRGETleQIYGI 247
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
338-488 |
1.40e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.66 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKK------LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVK--- 400
Cdd:COG1129 3 PLLEMRGISKSfggvkaLDGVSLELRPG-----EVHALLGENGAGKSTLMKILSGVYQPDSGEilldgepvRFRSPRdaq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 401 ---ISYKPQYVQV-------ENddfvrsVLMKTPPS----------------MIERLDLSHLLKRKLSELSGGELQRVAI 454
Cdd:COG1129 78 aagIAIIHQELNLvpnlsvaEN------IFLGREPRrgglidwramrrrareLLARLGLDIDPDTPVGDLSVAQQQLVEI 151
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278501429 455 AECLSRDADVYLLDEPSAHL---DVEQRLNVAKILRD 488
Cdd:COG1129 152 ARALSRDARVLILDEPTASLterEVERLFRIIRRLKA 188
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
103-477 |
1.50e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.98 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQL-----KPNLGNDF----------GEVEGQkIIDFF-KGTEAQNYFEKLY---TTGLETSY 163
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEVllddgRIIYEQDLivarlqqdppRNVEGT-VYDFVaEGIEEQAEYLKRYhdiSHLVETDP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 164 KPQYVEQIPRifkgsVKALLNKIS----EGDVNKVCNELGIKHvlNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSS 239
Cdd:PRK11147 113 SEKNLNELAK-----LQEQLDHHNlwqlENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 240 YLDIKQRLKVANLLRkhgSEKECAVVVEHD----------LIMLD-------------YLADVEHIMYGRAGVYGIVSKS 296
Cdd:PRK11147 186 HLDIETIEWLEGFLK---TFQGSIIFISHDrsfirnmatrIVDLDrgklvsypgnydqYLLEKEEALRVEELQNAEFDRK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 297 LS-----IRECIN---TYLEGYIR-------EDNMRF--------------RSEEIKFEVKAptkaLN-NIPiiewsniE 346
Cdd:PRK11147 263 LAqeevwIRQGIKarrTRNEGRVRalkalrrERSERRevmgtakmqveeasRSGKIVFEMEN----VNyQID-------G 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 347 KKL-GDFKLKVkpgilMRNEIIGVLGENGTGKTTFAKILAGMIKPDKG--KTDTSVKISYKPQYvqVENDDFVRSVL--- 420
Cdd:PRK11147 332 KQLvKDFSAQV-----QRGDKIALIGPNGCGKTTLLKLMLGQLQADSGriHCGTKLEVAYFDQH--RAELDPEKTVMdnl 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 421 ---MKTppSMI---ERLDLSHLL------KRKLS---ELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:PRK11147 405 aegKQE--VMVngrPRHVLGYLQdflfhpKRAMTpvkALSGGERNRLLLARLFLKPSNLLILDEPTNDLDVE 474
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
100-272 |
1.51e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 69.10 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 100 IMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIidffKGTEAQNYFEKLYTTGLETSYKPQY-VEQIPRIFKGS 178
Cdd:PRK09536 31 LVGLVGPNGAGKTTLLRAINGTLTPTAGTVL--VAGDDV----EALSARAASRRVASVPQDTSLSFEFdVRQVVEMGRTP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 179 VKALLNKISEGD---VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRK 255
Cdd:PRK09536 105 HRSRFDTWTETDraaVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRR 184
|
170
....*....|....*..
gi 1278501429 256 HGSEKECAVVVEHDLIM 272
Cdd:PRK09536 185 LVDDGKTAVAAIHDLDL 201
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
340-475 |
1.54e-12 |
|
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: 67.14 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TDTSvKISYKPQY- 407
Cdd:cd03261 1 IELRGLTKSFGGRTvlkgvdLDVRRG-----EILAIIGPSGSGKSTLLRLIVGLLRPDSGEvlidgEDIS-GLSEAELYr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 408 -----------------------VQV---ENDDFVRS-----VLMKtppsmIERLDLSHLLKRKLSELSGGELQRVAIAE 456
Cdd:cd03261 75 lrrrmgmlfqsgalfdsltvfenVAFplrEHTRLSEEeireiVLEK-----LEAVGLRGAEDLYPAELSGGMKKRVALAR 149
|
170
....*....|....*....
gi 1278501429 457 CLSRDADVYLLDEPSAHLD 475
Cdd:cd03261 150 ALALDPELLLYDEPTAGLD 168
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
83-266 |
1.55e-12 |
|
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: 67.21 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 83 DKNGFKLFNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVegqkiidFFKGTEaqnyfeklyTTGLETS 162
Cdd:cd03256 13 GKKALKDVSLSIN-PGEFVALIGPSGAGKSTLLRCLNGLVEP----TSGSV-------LIDGTD---------INKLKGK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 163 YKPQYVEQIPRIF----------------------KGSVKALLNKISEGDVNKVC---NELGIKHVLNRKVGDISGGELQ 217
Cdd:cd03256 72 ALRQLRRQIGMIFqqfnlierlsvlenvlsgrlgrRSTWRSLFGLFPKEEKQRALaalERVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1278501429 218 RVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVV 266
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIV 200
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
90-278 |
1.71e-12 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 65.67 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 90 FNLVIpQKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNdfGEVEGQKIIDFFKGTEAQNYfeklyttgletsyKPQYVE 169
Cdd:cd03229 19 VSLNI-EAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGS--ILIDGEDLTDLEDELPPLRR-------------RIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 170 QIPRIFkgSVKALLNKISEGdvnkvcnelgikhvlnrkvgdISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKV 249
Cdd:cd03229 83 QDFALF--PHLTVLENIALG---------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREV 139
|
170 180 190
....*....|....*....|....*....|
gi 1278501429 250 ANLLRKHGSEKECAVV-VEHDLIMLDYLAD 278
Cdd:cd03229 140 RALLKSLQAQLGITVVlVTHDLDEAARLAD 169
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
363-477 |
1.74e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 69.59 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKGKT--DTSVKISY----KPQYVQVENDDFVR----------------SVL 420
Cdd:PRK11147 28 DNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIiyEQDLIVARlqqdPPRNVEGTVYDFVAegieeqaeylkryhdiSHL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 421 MKTPPS--MIERL-----DLSHL------------LKR-------KLSELSGGELQRVAIAECLSRDADVYLLDEPSAHL 474
Cdd:PRK11147 108 VETDPSekNLNELaklqeQLDHHnlwqlenrinevLAQlgldpdaALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHL 187
|
...
gi 1278501429 475 DVE 477
Cdd:PRK11147 188 DIE 190
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
363-493 |
1.83e-12 |
|
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: 66.76 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKG------------KTDTSVKISYKPQY-VQVEN---DDFVR-SVLMKTPP 425
Cdd:cd03263 27 KGEIFGLLGHNGAGKTTTLKMLTGELRPTSGtayingysirtdRKAARQSLGYCPQFdALFDEltvREHLRfYARLKGLP 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 426 S---------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKK 493
Cdd:cd03263 107 KseikeevelLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR 183
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
102-270 |
1.84e-12 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 67.15 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 102 GLVGVNGIGKSTCLNILSGQLKPNLGN-DFGeveGQKIIDFFKGTEAQNY--FEKLYTTGLETSYKPqyVEQIPRIFKGS 178
Cdd:TIGR03873 31 GLLGPNGSGKSTLLRLLAGALRPDAGTvDLA---GVDLHGLSRRARARRValVEQDSDTAVPLTVRD--VVALGRIPHRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 179 VKALLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGS 258
Cdd:TIGR03873 106 LWAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQEPKLLLLDEPTNHLDVRAQLETLALVRELAA 185
|
170
....*....|..
gi 1278501429 259 EKECAVVVEHDL 270
Cdd:TIGR03873 186 TGVTVVAALHDL 197
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
363-493 |
1.96e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.32 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDT-SVKISYK---------------P--QYV----------QVENDD 414
Cdd:PRK13632 34 EGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdGITISKEnlkeirkkigiifqnPdnQFIgatveddiafGLENKK 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278501429 415 FVRSVLMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKK 493
Cdd:PRK13632 114 VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTR 192
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
1-68 |
2.54e-12 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 62.05 E-value: 2.54e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 1 MRIVVVNKKKCTagkGCDyVCMNFCPinrtgKDCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:COG1149 3 RKIPVIDEEKCI---GCG-LCVEVCP-----EGAIKLDDGGAPVVDPDLCTGCGACVGVCPTGAITLE 61
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
345-488 |
2.66e-12 |
|
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: 65.15 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 345 IEKKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsvkisykpqyVQVENDDFVRsvlmKTP 424
Cdd:cd03215 12 VKGAVRDVSFEVRAG-----EIVGIAGLVGNGQTELAEALFGLRPPASGE-------------ITLDGKPVTR----RSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 425 PSMI---------ERLDLSHLLKRKLSE-------LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRD 488
Cdd:cd03215 70 RDAIragiayvpeDRKREGLVLDLSVAEnialsslLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRE 149
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
90-274 |
2.71e-12 |
|
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: 69.02 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 90 FNLVIPQKKQImGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDffkGTEAQNYFEK-LYTTgleTSYkpqyV 168
Cdd:COG4987 354 LSLTLPPGERV-AIVGPSGSGKSTLLALLLRFLDPQ--------SGSITLG---GVDLRDLDEDdLRRR---IAV----V 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 169 EQIPRIFKGSVKA-LL---NKISEGDVNKVCNELGIKHV-------LNRKVGD----ISGGELQRVAIAGALLKKSDFLF 233
Cdd:COG4987 415 PQRPHLFDTTLREnLRlarPDATDEELWAALERVGLGDWlaalpdgLDTWLGEggrrLSGGERRRLALARALLRDAPILL 494
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1278501429 234 IDEPSSYLDIKQRLKVANLLRKHGSEKeCAVVVEHDLIMLD 274
Cdd:COG4987 495 LDEPTEGLDAATEQALLADLLEALAGR-TVLLITHRLAGLE 534
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
90-243 |
3.10e-12 |
|
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: 68.85 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 90 FNLVIPQKKqIMGLVGVNGIGKSTCLNILSGQLKPNLGNdfGEVEGQKIIDFfkgteaqnyfeklyttgLETSYKPQ--Y 167
Cdd:TIGR02857 341 VSFTVPPGE-RVALVGPSGAGKSTLLNLLLGFVDPTEGS--IAVNGVPLADA-----------------DADSWRDQiaW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 168 VEQIPRIFKGSVK-------------ALLNKISEGDVNKVCNELGIKhvLNRKVGD----ISGGELQRVAIAGALLKKSD 230
Cdd:TIGR02857 401 VPQHPFLFAGTIAenirlarpdasdaEIREALERAGLDEFVAALPQG--LDTPIGEggagLSGGQAQRLALARAFLRDAP 478
|
170
....*....|...
gi 1278501429 231 FLFIDEPSSYLDI 243
Cdd:TIGR02857 479 LLLLDEPTAHLDA 491
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
86-242 |
3.37e-12 |
|
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: 67.82 E-value: 3.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 86 GFKL-FNLVIPQKKqIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEgqkiidfFKGteaqnyfEKLYTTGLETSYK 164
Cdd:COG4148 13 GFTLdVDFTLPGRG-VTALFGPSGSGKTTLLRAIAGLERP----DSGRIR-------LGG-------EVLQDSARGIFLP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 165 PQ-----YVEQIPRIFKG-SVKALLN--------KISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSD 230
Cdd:COG4148 74 PHrrrigYVFQEARLFPHlSVRGNLLygrkraprAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPR 153
|
170
....*....|..
gi 1278501429 231 FLFIDEPSSYLD 242
Cdd:COG4148 154 LLLMDEPLAALD 165
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
340-487 |
3.94e-12 |
|
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: 64.88 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKK------------LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAG--MIKPDKGktdtSVKISYKP 405
Cdd:cd03213 4 LSFRNLTVTvksspsksgkqlLKNVSGKAKPG-----ELTAIMGPSGAGKSTLLNALAGrrTGLGVSG----EVLINGRP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 406 QYVQ--------VENDDFVRSVLmktppSMIERLDLSHLLKRklseLSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:cd03213 75 LDKRsfrkiigyVPQDDILHPTL-----TVRETLMFAAKLRG----LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170
....*....|
gi 1278501429 478 QRLNVAKILR 487
Cdd:cd03213 146 SALQVMSLLR 155
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
3-73 |
5.01e-12 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 61.26 E-value: 5.01e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 3 IVVVNKKKCtagKGCDyVCMNFCPinrtgKDCIVEGADGK--IVVEEELCIGCGICVNKCPFDAVKVVNLPDE 73
Cdd:COG1146 2 MPVIDTDKC---IGCG-ACVEVCP-----VDVLELDEEGKkaLVINPEECIGCGACELVCPVGAITVEDDEPE 65
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
339-491 |
5.44e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 66.67 E-value: 5.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 339 IIEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK---------TDTSVKISY 403
Cdd:COG4152 1 MLELKGLTKRFGDKTavddvsFTVPKG-----EIFGLLGPNGAGKTTTIRIILGILAPDSGEvlwdgepldPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 404 KPQ----Y--VQVEndDFV----------RSVLMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLL 467
Cdd:COG4152 76 LPEerglYpkMKVG--EQLvylarlkglsKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLIL 153
|
170 180
....*....|....*....|....
gi 1278501429 468 DEPSAHLDVeqrLNVaKILRDVIK 491
Cdd:COG4152 154 DEPFSGLDP---VNV-ELLKDVIR 173
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
81-281 |
5.53e-12 |
|
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: 64.26 E-value: 5.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 81 SYDKNG---FKLFNLVIPQKKQImGLVGVNGIGKSTCLNILSGQLKPNLGndfgEVegqkiidFFKGTEAQNYFEKLytt 157
Cdd:cd03247 9 SYPEQEqqvLKNLSLELKQGEKI-ALLGRSGSGKSTLLQLLTGDLKPQQG----EI-------TLDGVPVSDLEKAL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 158 gletSYKPQYVEQIPRIFKGSVKallnkisegdvnkvcNELGIKhvlnrkvgdISGGELQRVAIAGALLKKSDFLFIDEP 237
Cdd:cd03247 74 ----SSLISVLNQRPYLFDTTLR---------------NNLGRR---------FSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1278501429 238 SSYLDIKQRLKVANLLRKHGSEKECAVVVEHdlimldyLADVEH 281
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKDKTLIWITHH-------LTGIEH 162
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
361-493 |
5.96e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 66.19 E-value: 5.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 361 LMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKISYKP----------------------QYV--QVEnDDFV 416
Cdd:PRK13635 30 VYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAG----TITVGGMVlseetvwdvrrqvgmvfqnpdnQFVgaTVQ-DDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 417 RSVLMKTPP--SMIERLD-------LSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILR 487
Cdd:PRK13635 105 FGLENIGVPreEMVERVDqalrqvgMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVR 184
|
....*.
gi 1278501429 488 DVIKKK 493
Cdd:PRK13635 185 QLKEQK 190
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
339-492 |
5.98e-12 |
|
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: 65.30 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 339 IIEWSNIEKKLGDFK----------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVK 400
Cdd:cd03258 1 MIELKNVSKVFGDTGgkvtalkdvsLSVPKG-----EIFGIIGRSGAGKSTLIRCINGLERPTSGSvlvdgtdlTLLSGK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 401 --------ISYKPQYVQVENDdfvRSV---------LMKTPPSMIER--------LDLSHLLKRKLSELSGGELQRVAIA 455
Cdd:cd03258 76 elrkarrrIGMIFQHFNLLSS---RTVfenvalpleIAGVPKAEIEErvlellelVGLEDKADAYPAQLSGGQKQRVGIA 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278501429 456 ECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKK 492
Cdd:cd03258 153 RALANNPKVLLCDEATSALDPETTQSILALLRDINRE 189
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
206-477 |
6.15e-12 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 67.96 E-value: 6.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 206 RKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRK---------HGSEKECAVVVE----HDLIM 272
Cdd:PLN03073 340 KATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKwpktfivvsHAREFLNTVVTDilhlHGQKL 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 273 LDYLADVEHIMYGRAGVYGIVSKSLSIRECINTYLEGYIreDNMRFRSEEIKFeVKAPTKALNNI--------------- 337
Cdd:PLN03073 420 VTYKGDYDTFERTREEQLKNQQKAFESNERSRSHMQAFI--DKFRYNAKRASL-VQSRIKALDRLghvdavvndpdykfe 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 ----------PIIEWSNiekklGDFKLKVKPgILMRN--------EIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTS- 398
Cdd:PLN03073 497 fptpddrpgpPIISFSD-----ASFGYPGGP-LLFKNlnfgidldSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSa 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 399 -VKISYKPQYvQVENDDFVRSVL---MKTPPSMIERLDLSHLLKRKLS---------ELSGGELQRVAIAECLSRDADVY 465
Cdd:PLN03073 571 kVRMAVFSQH-HVDGLDLSSNPLlymMRCFPGVPEQKLRAHLGSFGVTgnlalqpmyTLSGGQKSRVAFAKITFKKPHIL 649
|
330
....*....|..
gi 1278501429 466 LLDEPSAHLDVE 477
Cdd:PLN03073 650 LLDEPSNHLDLD 661
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
351-477 |
6.21e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 67.88 E-value: 6.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 351 DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----------TDTSV--KISYKPQYVQV------E 411
Cdd:COG1132 358 DISLTIPPG-----ETVALVGPSGSGKSTLVNLLLRFYDPTSGRilidgvdirdlTLESLrrQIGVVPQDTFLfsgtirE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 412 N----------------------DDFvrsvlmktppsmIERLD--LSHLLKRKLSELSGGELQRVAIAECLSRDADVYLL 467
Cdd:COG1132 433 NirygrpdatdeeveeaakaaqaHEF------------IEALPdgYDTVVGERGVNLSGGQRQRIAIARALLKDPPILIL 500
|
170
....*....|
gi 1278501429 468 DEPSAHLDVE 477
Cdd:COG1132 501 DEATSALDTE 510
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
354-488 |
6.39e-12 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 65.07 E-value: 6.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 354 LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TDTSvKISYK--PQY------V-Q---------V 410
Cdd:COG2884 23 LEIEKG-----EFVFLTGPSGAGKSTLLKLLYGEERPTSGQvlvngQDLS-RLKRReiPYLrrrigvVfQdfrllpdrtV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 411 -ENDDFV-------RSVLMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNV 482
Cdd:COG2884 97 yENVALPlrvtgksRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEI 176
|
....*.
gi 1278501429 483 AKILRD 488
Cdd:COG2884 177 MELLEE 182
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
97-269 |
7.06e-12 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 66.78 E-value: 7.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 97 KKQIMGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDffkgteaqnyfeklyttGLETSYKPQYVEQIPRIFK 176
Cdd:PRK11607 44 KGEIFALLGASGCGKSTLLRMLAGFEQPT--------AGQIMLD-----------------GVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 177 GSvkALL---------------NKISEGDVNKVCNE-LGIKHVL---NRKVGDISGGELQRVAIAGALLKKSDFLFIDEP 237
Cdd:PRK11607 99 SY--ALFphmtveqniafglkqDKLPKAEIASRVNEmLGLVHMQefaKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176
|
170 180 190
....*....|....*....|....*....|....*.
gi 1278501429 238 SSYLDIKQR----LKVANLLRKHGSekECaVVVEHD 269
Cdd:PRK11607 177 MGALDKKLRdrmqLEVVDILERVGV--TC-VMVTHD 209
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
361-499 |
7.64e-12 |
|
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: 64.86 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 361 LMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVKISY--------KPQYVQVENDDFVRSVLMKTPPSMIERLD 432
Cdd:cd03220 45 VPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSllglgggfNPELTGRENIYLNGRLLGLSRKEIDEKID 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278501429 433 ----LSHL---LKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEASAFV 499
Cdd:cd03220 125 eiieFSELgdfIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILV 198
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
99-270 |
8.14e-12 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 65.08 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEgqkiidfFKGTEAQnyfeKLYTTGLeTSYKPQ--YVEQ----IP 172
Cdd:COG3638 30 EFVALIGPSGAGKSTLLRCLNGLVEP----TSGEIL-------VDGQDVT----ALRGRAL-RRLRRRigMIFQqfnlVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 173 RI------------FKGSVKALLNKISEGDVNKVCN---ELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEP 237
Cdd:COG3638 94 RLsvltnvlagrlgRTSTWRSLLGLFPPEDRERALEaleRVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEP 173
|
170 180 190
....*....|....*....|....*....|....
gi 1278501429 238 SSYLDIKQRLKVANLLRKHGSEKECAVVVE-HDL 270
Cdd:COG3638 174 VASLDPKTARQVMDLLRRIAREDGITVVVNlHQV 207
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
5-68 |
9.52e-12 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 60.84 E-value: 9.52e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278501429 5 VVNKKKCTagkGCDyVCMNFCPinrtgKDCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:COG1144 26 VVDEDKCI---GCG-LCWIVCP-----DGAIRVDDGKYYGIDYDYCKGCGICAEVCPVKAIEMV 80
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
90-268 |
9.93e-12 |
|
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: 64.44 E-value: 9.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 90 FNLVIPQKkQIMGLVGVNGIGKSTCLNILSGQLKPNLGN--------DFGEVEGQKIIDFFkgtEAQNYFEKLYttglet 161
Cdd:cd03298 17 FDLTFAQG-EITAIVGPSGSGKSTLLNLIAGFETPQSGRvlingvdvTAAPPADRPVSMLF---QENNLFAHLT------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 162 sykpqyVEQipRIFKGSVKAL-LNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSY 240
Cdd:cd03298 87 ------VEQ--NVGLGLSPGLkLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180
....*....|....*....|....*....
gi 1278501429 241 LDIKQRLKVANLLRK-HGSEKECAVVVEH 268
Cdd:cd03298 159 LDPALRAEMLDLVLDlHAETKMTVLMVTH 187
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
4-78 |
1.01e-11 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 60.51 E-value: 1.01e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 4 VVVNKKKCTagkGCDyVCMNFCPinrtgKDCIVEGaDGKIVVEEELCIGCGICVNKCPFDAVKVV-NLPDELESRM 78
Cdd:COG2768 6 PYVDEEKCI---GCG-ACVKVCP-----VGAISIE-DGKAVIDPEKCIGCGACIEVCPVGAIKIEwEEDEEFQEKM 71
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
90-270 |
1.05e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.39 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 90 FNLVIPQKkQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIIDFFK-------GTEAQNYFEKLYTTGLETS 162
Cdd:PRK10253 26 LTVEIPDG-HFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVW--LDGEHIQHYASkevarriGLLAQNATTPGDITVQELV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 163 YKPQYVEQiPRIFKgsvkalLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLD 242
Cdd:PRK10253 103 ARGRYPHQ-PLFTR------WRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180
....*....|....*....|....*....
gi 1278501429 243 IKQRLKVANLLRKHGSEKECAV-VVEHDL 270
Cdd:PRK10253 176 ISHQIDLLELLSELNREKGYTLaAVLHDL 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
347-488 |
1.62e-11 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 64.14 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 347 KKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKT-----DTSV---------KISYKPQYVQV-- 410
Cdd:PRK10895 17 RVVEDVSLTVNSG-----EIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddeDISLlplhararrGIGYLPQEASIfr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 411 -----EN--------DDFVRSVLMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:PRK10895 92 rlsvyDNlmavlqirDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170
....*....|....
gi 1278501429 478 QRLNVAKI---LRD 488
Cdd:PRK10895 172 SVIDIKRIiehLRD 185
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
328-479 |
1.65e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 65.74 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 328 KAPTKALNNIPIIEWSNIEKK------LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK------- 394
Cdd:PRK09452 3 KLNKQPSSLSPLVELRGISKSfdgkevISNLDLTINNG-----EFLTLLGPSGCGKTTVLRLIAGFETPDSGRimldgqd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 395 -TDT--------SVKISYK--PQYVQVENDDF-VRsvLMKTPPSMIER--------LDLSHLLKRKLSELSGGELQRVAI 454
Cdd:PRK09452 78 iTHVpaenrhvnTVFQSYAlfPHMTVFENVAFgLR--MQKTPAAEITPrvmealrmVQLEEFAQRKPHQLSGGQQQRVAI 155
|
170 180
....*....|....*....|....*
gi 1278501429 455 AECLSRDADVYLLDEPSAHLDVEQR 479
Cdd:PRK09452 156 ARAVVNKPKVLLLDESLSALDYKLR 180
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
329-489 |
1.83e-11 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 65.63 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 329 APTKALNniPIIEWSNIEKK------LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKTD-TSVKI 401
Cdd:PRK11607 11 KTRKALT--PLLEIRNLTKSfdgqhaVDDVSLTIYKG-----EIFALLGASGCGKSTLLRMLAGFEQPTAGQIMlDGVDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 402 SYKPQYVQVENDDFVRSVLM----------------KTPPSMI-----ERLDLSHLL---KRKLSELSGGELQRVAIAEC 457
Cdd:PRK11607 84 SHVPPYQRPINMMFQSYALFphmtveqniafglkqdKLPKAEIasrvnEMLGLVHMQefaKRKPHQLSGGQRQRVALARS 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 1278501429 458 LSRDADVYLLDEPSAHLDVEQR----LNVAKILRDV 489
Cdd:PRK11607 164 LAKRPKLLLLDEPMGALDKKLRdrmqLEVVDILERV 199
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
340-488 |
2.30e-11 |
|
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: 63.32 E-value: 2.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVKIS--- 402
Cdd:cd03262 1 IEIKNLHKSFGDFHvlkgidLTVKKG-----EVVVIIGPSGSGKSTLLRCINLLEEPDSGTiiidglklTDDKKNINelr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 403 -----------------------YKPQYVQVENDDFVRSVLMKtppsMIERLDLSHLLKRKLSELSGGELQRVAIAECLS 459
Cdd:cd03262 76 qkvgmvfqqfnlfphltvlenitLAPIKVKGMSKAEAEERALE----LLEKVGLADKADAYPAQLSGGQQQRVAIARALA 151
|
170 180
....*....|....*....|....*....
gi 1278501429 460 RDADVYLLDEPSAHLDVEQRLNVAKILRD 488
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKD 180
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
341-493 |
2.65e-11 |
|
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: 63.44 E-value: 2.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 341 EWSNIEKKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKT------------DTSVK-ISYKPQY 407
Cdd:cd03234 15 NWNKYARILNDVSLHVESG-----QVMAILGSSGSGKTTLLDAISGRVEGGGTTSgqilfngqprkpDQFQKcVAYVRQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 408 --------------------VQVENDDFVRSvlMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLL 467
Cdd:cd03234 90 dillpgltvretltytailrLPRKSSDAIRK--KRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180
....*....|....*....|....*.
gi 1278501429 468 DEPSAHLDVEQRLNVAKILRDVIKKK 493
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLSQLARRN 193
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
321-476 |
3.15e-11 |
|
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: 64.11 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 321 EEIKFEVKApTKALNNIPIIEWSNIEKK----LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKTD 396
Cdd:cd03291 22 EKAKQENND-RKHSSDDNNLFFSNLCLVgapvLKNINLKIEKG-----EMLAITGSTGSGKTSLLMLILGELEPSEGKIK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 397 TSVKISYKPQYVQV------ENDDFVRSVLMKTPPSMIERLDLSHLLKrKLSE------------LSGGELQRVAIAECL 458
Cdd:cd03291 96 HSGRISFSSQFSWImpgtikENIIFGVSYDEYRYKSVVKACQLEEDIT-KFPEkdntvlgeggitLSGGQRARISLARAV 174
|
170
....*....|....*...
gi 1278501429 459 SRDADVYLLDEPSAHLDV 476
Cdd:cd03291 175 YKDADLYLLDSPFGYLDV 192
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
363-475 |
3.18e-11 |
|
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: 62.97 E-value: 3.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSvKISYKPQYVQVENDDFV---RSVLM---KTPP----------- 425
Cdd:cd03260 25 KGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEG-EVLLDGKDIYDLDVDVLelrRRVGMvfqKPNPfpgsiydnvay 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 426 ------------------SMIERLDLSHLLKRKLS--ELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:cd03260 104 glrlhgiklkeelderveEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANEPEVLLLDEPTSALD 173
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
83-270 |
3.42e-11 |
|
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: 63.47 E-value: 3.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 83 DKNGFKLFNLVIpQKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIidffkgTEAQNyfEKLYTTGLETS 162
Cdd:TIGR02315 14 GKQALKNINLNI-NPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSIL--LEGTDI------TKLRG--KKLRKLRRRIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 163 YKPQYVEQIPRI------------FKGSVKALLNKISEGDVNKVCN---ELGIKHVLNRKVGDISGGELQRVAIAGALLK 227
Cdd:TIGR02315 83 MIFQHYNLIERLtvlenvlhgrlgYKPTWRSLLGRFSEEDKERALSaleRVGLADKAYQRADQLSGGQQQRVAIARALAQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1278501429 228 KSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVE-HDL 270
Cdd:TIGR02315 163 QPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINlHQV 206
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
365-477 |
3.43e-11 |
|
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: 62.38 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 365 EIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVK------------ISY-------KPQYVQVENDDFVRSVL---MK 422
Cdd:TIGR01189 27 EALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTplaeqrdephenILYlghlpglKPELSALENLHFWAAIHggaQR 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1278501429 423 TPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:TIGR01189 107 TIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
102-278 |
3.53e-11 |
|
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: 62.99 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 102 GLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDffkGTEAQnyfeklyttgletSYKPQ-------YVEQIPRI 174
Cdd:cd03245 34 AIIGRVGSGKSTLLKLLAGLYKPT--------SGSVLLD---GTDIR-------------QLDPAdlrrnigYVPQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 175 FKGSVKALLN----KISEGDVNKVCNELGI-------KHVLNRKVGD----ISGGELQRVAIAGALLKKSDFLFIDEPSS 239
Cdd:cd03245 90 FYGTLRDNITlgapLADDERILRAAELAGVtdfvnkhPNGLDLQIGErgrgLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 1278501429 240 YLDIKQRLKVANLLRKHGSEKeCAVVVEHDLIMLDyLAD 278
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGDK-TLIIITHRPSLLD-LVD 206
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
91-278 |
3.62e-11 |
|
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: 62.90 E-value: 3.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQkiiDFFKGTEAQnyfekLYTTGLETSYkpqyveq 170
Cdd:cd03261 20 DLDVR-RGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVL--IDGE---DISGLSEAE-----LYRLRRRMGM------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 iprIFKGSvkALLNKISEGD--------------------VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSD 230
Cdd:cd03261 82 ---LFQSG--ALFDSLTVFEnvafplrehtrlseeeireiVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1278501429 231 FLFIDEPSSYLDIKQRLKVANLLRK-HGSEKECAVVVEHDLIMLDYLAD 278
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAIAD 205
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
100-283 |
3.83e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 63.49 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 100 IMGLVGVNGIGKSTCLNILSGQLKPNLGndfgEVEGQ-KIIDFFK-GTEAqnyFEKLYTTGLETSYKPQYVEQIPRIFKG 177
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKG----AVLWQgKPLDYSKrGLLA---LRQQVATVFQDPEQQIFYTDIDSDIAF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 178 SVKALlnKISEGDVNKVCNE----LGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLL 253
Cdd:PRK13638 102 SLRNL--GVPEAEITRRVDEaltlVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAII 179
|
170 180 190
....*....|....*....|....*....|
gi 1278501429 254 RKHGSEKECAVVVEHDLIMLDYLADVEHIM 283
Cdd:PRK13638 180 RRIVAQGNHVIISSHDIDLIYEISDAVYVL 209
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
339-492 |
3.89e-11 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 63.09 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 339 IIEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsvkISYKPQYVQVEN 412
Cdd:COG1126 1 MIEIENLHKSFGDLEvlkgisLDVEKG-----EVVVIIGPSGSGKSTLLRCINLLEEPDSGT------ITVDGEDLTDSK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 413 DD---------FV---------RSVL----------MKTPPS--------MIERLDLSHLLKRKLSELSGGELQRVAIAE 456
Cdd:COG1126 70 KDinklrrkvgMVfqqfnlfphLTVLenvtlapikvKKMSKAeaeerameLLERVGLADKADAYPAQLSGGQQQRVAIAR 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278501429 457 CLSRDADVYLLDEP-SAhLDVEqrlNVAKILrDVIKK 492
Cdd:COG1126 150 ALAMEPKVMLFDEPtSA-LDPE---LVGEVL-DVMRD 181
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
349-475 |
4.04e-11 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 63.34 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKISYKPqyvqVENDDFVRSV--------- 419
Cdd:COG4525 23 LQDVSLTIESG-----EFVVALGASGCGKTTLLNLIAGFLAPSSG----EITLDGVP----VTGPGADRGVvfqkdallp 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 420 -------------LMKTPPS--------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:COG4525 90 wlnvldnvafglrLRGVPKAerraraeeLLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
338-494 |
4.22e-11 |
|
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: 63.18 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNI-----EKK-LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKT---------DTSV--- 399
Cdd:COG1119 2 PLLELRNVtvrrgGKTiLDDISWTVKPG-----EHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgerrgGEDVwel 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 400 --KISYkpqyV------QVENDDFVRSVLM-----------KTPPSMIER-------LDLSHLLKRKLSELSGGELQRVA 453
Cdd:COG1119 77 rkRIGL----VspalqlRFPRDETVLDVVLsgffdsiglyrEPTDEQRERarellelLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1278501429 454 IAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKE 494
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGA 193
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
74-295 |
4.41e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 63.67 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 74 LESR-MIHSY--DKNGFKLFNLVIPQKKQImGLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKI-------IDFFK 143
Cdd:PRK13652 4 IETRdLCYSYsgSKEALNNINFIAPRNSRI-AVIGPNGAGKSTLFRHFNGILKPTSGSVL--IRGEPItkenireVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 144 GTEAQNYFEKLYTTGletsykpqyVEQipRIFKGSVKALLNKIS-EGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIA 222
Cdd:PRK13652 81 GLVFQNPDDQIFSPT---------VEQ--DIAFGPINLGLDEETvAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278501429 223 GALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVE-HDLIMLDYLADVEHIM-YGRAGVYGIVSK 295
Cdd:PRK13652 150 GVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFStHQLDLVPEMADYIYVMdKGRIVAYGTVEE 224
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
96-245 |
5.22e-11 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 62.68 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIIDFFKGTEAQnyfeklyttgLETSYKPQYveqiPRIF 175
Cdd:TIGR04406 25 KSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKIL--IDGQDITHLPMHERAR----------LGIGYLPQE----ASIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 176 KG-----SVKALLNKISEGD-------VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDE------P 237
Cdd:TIGR04406 89 RKltveeNIMAVLEIRKDLDraereerLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEpfagvdP 168
|
....*...
gi 1278501429 238 SSYLDIKQ 245
Cdd:TIGR04406 169 IAVGDIKK 176
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
351-476 |
5.24e-11 |
|
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: 65.32 E-value: 5.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 351 DFKLKVKPGI------LMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVKISYKPQYVQV------EN------ 412
Cdd:TIGR01271 433 NFSLYVTPVLknisfkLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWImpgtikDNiifgls 512
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 413 -DDF-VRSVL----MKTPPSMIERLDLSHLLKRKLSeLSGGELQRVAIAECLSRDADVYLLDEPSAHLDV 476
Cdd:TIGR01271 513 yDEYrYTSVIkacqLEEDIALFPEKDKTVLGEGGIT-LSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
340-475 |
5.91e-11 |
|
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: 62.70 E-value: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLG-------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKT-----DTS----VKISY 403
Cdd:cd03295 1 IEFENVTKRYGggkkavnNLNLEIAKG-----EFLVLIGPSGSGKTTTMKMINRLIEPTSGEIfidgeDIReqdpVELRR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 404 KPQYV--QV---------ENDDFVRSVLMKTPPSMIER---------LDLSHLLKRKLSELSGGELQRVAIAECLSRDAD 463
Cdd:cd03295 76 KIGYViqQIglfphmtveENIALVPKLLKWPKEKIRERadellalvgLDPAEFADRYPHELSGGQQQRVGVARALAADPP 155
|
170
....*....|..
gi 1278501429 464 VYLLDEPSAHLD 475
Cdd:cd03295 156 LLLMDEPFGALD 167
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
340-489 |
5.94e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.98 E-value: 5.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-------TDTSVK---ISYKPQYVQ 409
Cdd:PRK15056 14 VTWRNGHTALRDASFTVPGG-----SIAALVGVNGSGKSTLFKALMGFVRLASGKisilgqpTRQALQknlVAYVPQSEE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 410 VEND--DFVRSVLM----------KTPPS--------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDE 469
Cdd:PRK15056 89 VDWSfpVLVEDVVMmgryghmgwlRRAKKrdrqivtaALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180
....*....|....*....|
gi 1278501429 470 PSAHLDVEQRLNVAKILRDV 489
Cdd:PRK15056 169 PFTGVDVKTEARIISLLREL 188
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
429-485 |
7.21e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.90 E-value: 7.21e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 429 ERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD----VEQRLNVAKI 485
Cdd:PRK11000 119 EVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRL 179
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
91-270 |
8.03e-11 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 62.03 E-value: 8.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIpQKKQIMGLVGVNGIGKST---CLNIL----SGQLKpnlgndfgeVEGQKIIDFFKGT-----EAQNYFEKLY--- 155
Cdd:PRK09493 21 DLNI-DQGEVVVIIGPSGSGKSTllrCINKLeeitSGDLI---------VDGLKVNDPKVDErlirqEAGMVFQQFYlfp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 156 -TTGLETsykpqyVEQIPRIFKGSVKALLNKISEGDVNKVcnelGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFI 234
Cdd:PRK09493 91 hLTALEN------VMFGPLRVRGASKEEAEKQARELLAKV----GLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 1278501429 235 DEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDL 270
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEI 196
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
97-285 |
8.88e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 62.36 E-value: 8.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 97 KKQIMGLVGVNGIGKST---CLNILSgQLKpnlgndfGEVEGQKIIDFFkgteAQNYFEKLYTTGlETSYKPQYVEQIPR 173
Cdd:PRK14258 32 QSKVTAIIGPSGCGKSTflkCLNRMN-ELE-------SEVRVEGRVEFF----NQNIYERRVNLN-RLRRQVSMVHPKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 174 IFKGSV---------------KALLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPS 238
Cdd:PRK14258 99 LFPMSVydnvaygvkivgwrpKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPC 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1278501429 239 SYLDIKQRLKVANLLRKHGSEKECA-VVVEHDLIMLDYLADVEHIMYG 285
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSELTmVIVSHNLHQVSRLSDFTAFFKG 226
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
363-496 |
9.15e-11 |
|
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: 60.08 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsvkisykpqyvqvenddfvrsVLMKTPPSMIERLDLS---HLLKR 439
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGG------------------------VIYIDGEDILEEVLDQlllIIVGG 56
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 440 KLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEAS 496
Cdd:smart00382 57 KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLLLLLKS 113
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
99-237 |
9.28e-11 |
|
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: 61.79 E-value: 9.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPNLGndfgevegqKIidFFKGTEAQNY--FEKlytTGLETSYKPQYveqiPRIFK 176
Cdd:cd03218 27 EIVGLLGPNGAGKTTTFYMIVGLVKPDSG---------KI--LLDGQDITKLpmHKR---ARLGIGYLPQE----ASIFR 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 177 G-SVK----------ALLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEP 237
Cdd:cd03218 89 KlTVEenilavleirGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
100-283 |
9.42e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 64.19 E-value: 9.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 100 IMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEgqkiidffkgteaqnyfeklyttgLETSYKPQYVEQIPRIFKGSv 179
Cdd:TIGR03719 350 IVGVIGPNGAGKSTLFRMITGQEQP----DSGTIE------------------------IGETVKLAYVDQSRDALDPN- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 180 KALLNKISEG-DVNKVCN-ELGIKHVLNR----------KVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIK--Q 245
Cdd:TIGR03719 401 KTVWEEISGGlDIIKLGKrEIPSRAYVGRfnfkgsdqqkKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVEtlR 480
|
170 180 190
....*....|....*....|....*....|....*...
gi 1278501429 246 RLKVAnLLRKHGsekeCAVVVEHDLIMLDYLAdvEHIM 283
Cdd:TIGR03719 481 ALEEA-LLNFAG----CAVVISHDRWFLDRIA--THIL 511
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
345-487 |
1.00e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.17 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 345 IEKKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIkPDKGK-------------TDTSVKISYKPQ----- 406
Cdd:COG4138 8 VAGRLGPISAQVNAG-----ELIHLIGPNGAGKSTLLARMAGLL-PGQGEillngrplsdwsaAELARHRAYLSQqqspp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 407 -------YVQ-----VENDDFVRSVLMKtppsMIERLDLSHLLKRKLSELSGGELQRVAIAECL-------SRDADVYLL 467
Cdd:COG4138 82 fampvfqYLAlhqpaGASSEAVEQLLAQ----LAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptiNPEGQLLLL 157
|
170 180
....*....|....*....|
gi 1278501429 468 DEPSAHLDVEQRLNVAKILR 487
Cdd:COG4138 158 DEPMNSLDVAQQAALDRLLR 177
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
99-270 |
1.08e-10 |
|
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: 61.72 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDffkGTEAQNYFEKLYTTgletsyKPQYVEQIPRIFKGS 178
Cdd:cd03248 41 EVTALVGPSGSGKSTVVALLENFYQPQ--------GGQVLLD---GKPISQYEHKYLHS------KVSLVGQEPVLFARS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 179 VKallNKISEG--DVNKVC----------------NELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSY 240
Cdd:cd03248 104 LQ---DNIAYGlqSCSFECvkeaaqkahahsfiseLASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190
....*....|....*....|....*....|
gi 1278501429 241 LDIKQRLKVANLLRKhGSEKECAVVVEHDL 270
Cdd:cd03248 181 LDAESEQQVQQALYD-WPERRTVLVIAHRL 209
|
|
| DsrA |
COG2221 |
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ... |
1-69 |
1.14e-10 |
|
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];
Pssm-ID: 441823 [Multi-domain] Cd Length: 69 Bit Score: 57.37 E-value: 1.14e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278501429 1 MRIVVVNKKKCTagkGCDyVCMNFCPinrtgKDCIVEgADGKIVVEEELCIGCGICVNKCPFDAVKVVN 69
Cdd:COG2221 7 TWPPKIDEEKCI---GCG-LCVAVCP-----TGAISL-DDGKLVIDEEKCIGCGACIRVCPTGAIKGEK 65
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
191-278 |
1.43e-10 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 62.78 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 191 VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSD-FLFiDEPSSYLDIKQRLKV----ANLLRKHGSekeCAVV 265
Cdd:COG3839 114 VREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKvFLL-DEPLSNLDAKLRVEMraeiKRLHRRLGT---TTIY 189
|
90
....*....|....*
gi 1278501429 266 VEHDLI--MLdyLAD 278
Cdd:COG3839 190 VTHDQVeaMT--LAD 202
|
|
| PorD_KorD |
TIGR02179 |
2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family; A number ... |
5-68 |
1.50e-10 |
|
2-oxoacid:acceptor oxidoreductase, delta subunit, pyruvate/2-ketoisovalerate family; A number of anaerobic and microaerophilic species lack pyruvate dehydrogenase and have instead a four subunit, oxygen-sensitive pyruvate oxidoreductase, with either ferredoxins or flavodoxins used as the acceptor. Several related four-subunit enzymes may exist in the same species. This model describes a subfamily of delta subunits, representing mostly pyruvate, 2-ketoisovalerate, and 2-oxoglutarate specific enzymes. The delta subunit is the smallest and resembles ferredoxins.
Pssm-ID: 131234 [Multi-domain] Cd Length: 78 Bit Score: 57.34 E-value: 1.50e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278501429 5 VVNKKKCTagkGCdYVCMNFCPINrtgkdCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:TIGR02179 21 VVDKEKCI---KC-KNCWLYCPEG-----AIQEDEGGFVGIDYDYCKGCGICANVCPVKAIEMV 75
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
99-257 |
1.90e-10 |
|
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: 59.36 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVegqkiidFFKGTEAQnyfeklyttgletsykpqyveqipriFKGS 178
Cdd:cd03216 27 EVHALLGENGAGKSTLMKILSGLYKP----DSGEI-------LVDGKEVS--------------------------FASP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 179 VKALlnkisegdvnkvcnELGIkhvlnRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQR---LKVANLLRK 255
Cdd:cd03216 70 RDAR--------------RAGI-----AMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVerlFKVIRRLRA 130
|
..
gi 1278501429 256 HG 257
Cdd:cd03216 131 QG 132
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
347-489 |
1.96e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 61.67 E-value: 1.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 347 KKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVKISYKPQYVQV-------E 411
Cdd:PRK13643 20 RALFDIDLEVKKG-----SYTALIGHTGSGKSTLLQHLNGLLQPTEGKvtvgdivvSSTSKQKEIKPVRKKVgvvfqfpE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 412 NDDFVRSVLM-----------------KTPPSMIERLDLS-HLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAH 473
Cdd:PRK13643 95 SQLFEETVLKdvafgpqnfgipkekaeKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAG 174
|
170
....*....|....*.
gi 1278501429 474 LDVEQRLNVAKILRDV 489
Cdd:PRK13643 175 LDPKARIEMMQLFESI 190
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
349-479 |
2.33e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.87 E-value: 2.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKISYKP-------QYVQVENDDFV--RSV 419
Cdd:PRK11248 17 LEDINLTLESG-----ELLVVLGPSGCGKTTLLNLIAGFVPYQHG----SITLDGKPvegpgaeRGVVFQNEGLLpwRNV 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 420 L-----------------MKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQR 479
Cdd:PRK11248 88 QdnvafglqlagvekmqrLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTR 164
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
349-488 |
2.98e-10 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 59.92 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsvkISYKPQYVQVENDDFVR-SVLMKTP--- 424
Cdd:cd03268 16 LDDISLHVKKG-----EIYGFLGPNGAGKTTTMKIILGLIKPDSGE------ITFDGKSYQKNIEALRRiGALIEAPgfy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 425 PSM-----------------------IERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLN 481
Cdd:cd03268 85 PNLtarenlrllarllgirkkridevLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGIKE 164
|
....*..
gi 1278501429 482 VAKILRD 488
Cdd:cd03268 165 LRELILS 171
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
349-492 |
3.09e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 60.87 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKT-----DTSV-----KISYKPQYV-QVENDDFVR 417
Cdd:PRK13633 26 LDDVNLEVKKG-----EFLVILGRNGSGKSTIAKHMNALLIPSEGKVyvdglDTSDeenlwDIRNKAGMVfQNPDNQIVA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 418 SVL----------MKTPPSMI-ERLDLShLLKRKLSE--------LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQ 478
Cdd:PRK13633 101 TIVeedvafgpenLGIPPEEIrERVDES-LKKVGMYEyrrhaphlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSG 179
|
170
....*....|....
gi 1278501429 479 RLNVAKILRDVIKK 492
Cdd:PRK13633 180 RREVVNTIKELNKK 193
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
344-477 |
3.15e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.86 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 344 NIEKKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVK----------ISY-------KPQ 406
Cdd:PRK13543 22 NEEPVFGPLDFHVDAG-----EALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgdrsrfMAYlghlpglKAD 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278501429 407 YVQVENDDFVRSV----LMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:PRK13543 97 LSTLENLHFLCGLhgrrAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
331-494 |
3.18e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 61.22 E-value: 3.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 331 TKALNNIpiiewsNIEKKLGDFklkvkpgilmrneiIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVK-- 400
Cdd:PRK13637 20 KKALDNV------NIEIEDGEF--------------VGLIGHTGSGKSTLIQHLNGLLKPTSGKiiidgvdiTDKKVKls 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 401 -------------------------ISYKPQYVQVENDDfvrsVLMKTPPSM-IERLDLSHLLKRKLSELSGGELQRVAI 454
Cdd:PRK13637 80 dirkkvglvfqypeyqlfeetiekdIAFGPINLGLSEEE----IENRVKRAMnIVGLDYEDYKDKSPFELSGGQKRRVAI 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1278501429 455 AECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKE 494
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYN 195
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
99-476 |
3.74e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 61.97 E-value: 3.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGE--VEGQKI----------------------IDFFkgTEAQNYfekl 154
Cdd:COG3845 32 EIHALLGENGAGKSTLMKILYGLYQP----DSGEilIDGKPVrirsprdaialgigmvhqhfmlVPNL--TVAENI---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 155 yTTGLETSykpqyveqipRIFKGSVKALLNKISEgdvnkVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFI 234
Cdd:COG3845 102 -VLGLEPT----------KGGRLDRKAARARIRE-----LSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 235 DEPSSYL---DIKQRLKVANLLRKHGsekeCAVV-VEHDL--IMLdyLADVEHIMygRAG--VYGIVSKSLSIREcinty 306
Cdd:COG3845 166 DEPTAVLtpqEADELFEILRRLAAEG----KSIIfITHKLreVMA--IADRVTVL--RRGkvVGTVDTAETSEEE----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 307 legyIREdnMRFRsEEIKFEVKAPTKALNNiPIIEWSNIE-------KKLGDFKLKVKPGilmrnEIIGVLGENGTGKTT 379
Cdd:COG3845 233 ----LAE--LMVG-REVLLRVEKAPAEPGE-VVLEVENLSvrddrgvPALKDVSLEVRAG-----EILGIAGVAGNGQSE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 380 FAKILAGMIKPDKGK--------TDTSVK------ISYKPQ----------YVQVEN--------DDFVRSVLMKTPP-- 425
Cdd:COG3845 300 LAEALAGLRPPASGSirldgediTGLSPRerrrlgVAYIPEdrlgrglvpdMSVAENlilgryrrPPFSRGGFLDRKAir 379
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 426 ----SMIERLDL-SHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDV 476
Cdd:COG3845 380 afaeELIEEFDVrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDV 435
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
363-492 |
3.94e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 60.59 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVKISYKPQYVQVEN-DDFVRSVLMKTP--------- 424
Cdd:PRK13652 29 RNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSvlirgepiTKENIREVRKFVGLVFQNpDDQIFSPTVEQDiafgpinlg 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 425 ----------PSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKK 492
Cdd:PRK13652 109 ldeetvahrvSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPET 186
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
365-476 |
4.24e-10 |
|
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: 59.43 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 365 EIIGVLGENGTGKTTFAKILAGMIKPDKGktdtsvKISYKPQYVQVENDDFVRSVL-------MKTPPSMIERL------ 431
Cdd:cd03231 27 EALQVTGPNGSGKTTLLRILAGLSPPLAG------RVLLNGGPLDFQRDSIARGLLylghapgIKTTLSVLENLrfwhad 100
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 432 -------------DLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDV 476
Cdd:cd03231 101 hsdeqveealarvGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
365-489 |
4.56e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 60.41 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 365 EIIGVLGENGTGKTTFAKILAGMIKPDK----------------GKTDTSVKISYK------PQYVQVENDDFVRSVLM- 421
Cdd:PRK09984 31 EMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellgrtvqreGRLARDIRKSRAntgyifQQFNLVNRLSVLENVLIg 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 422 ---KTP-----------------PSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLN 481
Cdd:PRK09984 111 algSTPfwrtcfswftreqkqraLQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARI 190
|
....*...
gi 1278501429 482 VAKILRDV 489
Cdd:PRK09984 191 VMDTLRDI 198
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
4-68 |
4.95e-10 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 57.41 E-value: 4.95e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278501429 4 VVVNKKKCtagKGCDyVCMNFCPInrtgkDCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:cd10549 73 AEIDEEKC---IGCG-LCVKVCPV-----DAITLEDELEIVIDKEKCIGCGICAEVCPVNAIKLV 128
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
339-488 |
5.53e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 59.72 E-value: 5.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 339 IIEWSNIEKKLG------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVKI--- 401
Cdd:PRK09493 1 MIEFKNVSKHFGptqvlhNIDLNIDQG-----EVVVIIGPSGSGKSTLLRCINKLEEITSGDlivdglkvNDPKVDErli 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 402 -----------SYKPQYVQVENDDF----VRsvlmKTPPSMIERLDLSHLLKRKL--------SELSGGELQRVAIAECL 458
Cdd:PRK09493 76 rqeagmvfqqfYLFPHLTALENVMFgplrVR----GASKEEAEKQARELLAKVGLaerahhypSELSGGQQQRVAIARAL 151
|
170 180 190
....*....|....*....|....*....|
gi 1278501429 459 SRDADVYLLDEPSAHLDVEQRLNVAKILRD 488
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQD 181
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
97-487 |
5.62e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 61.34 E-value: 5.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 97 KKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNdfgevegqkIIdfFKGTEAQNYFEKL-YTTGLETSYkpqyvEQIPRIF 175
Cdd:PRK09700 30 PGEIHALLGENGAGKSTLMKVLSGIHEPTKGT---------IT--INNINYNKLDHKLaAQLGIGIIY-----QELSVID 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 176 KGSVKALLnKISEGDVNKVCN------------------ELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEP 237
Cdd:PRK09700 94 ELTVLENL-YIGRHLTKKVCGvniidwremrvraammllRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 238 SSYL---DIKQRLKVANLLRKHGSekeCAVVVEHDLIMLDYLADVEHIMYGRAGVYGIVSKSLSIRECInTYLEGyiRED 314
Cdd:PRK09700 173 TSSLtnkEVDYLFLIMNQLRKEGT---AIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIV-RLMVG--REL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 315 NMRFRSeeikfeVKAPTKALNNIPIIEWSNI----EKKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKP 390
Cdd:PRK09700 247 QNRFNA------MKENVSNLAHETVFEVRNVtsrdRKKVRDISFSVCRG-----EILGFAGLVGSGRTELMNCLFGVDKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 391 DKGK------------------------TDTSVKISYKPQYVQVENDDFVRSVLM----------------KTPPSMIER 430
Cdd:PRK09700 316 AGGEirlngkdisprspldavkkgmayiTESRRDNGFFPNFSIAQNMAISRSLKDggykgamglfhevdeqRTAENQREL 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 431 LDLS-HLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILR 487
Cdd:PRK09700 396 LALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMR 453
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
99-270 |
5.77e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.79 E-value: 5.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVE-GQKIIDFFKGTEAQNYFEKLyttgletsykPQY--------VE 169
Cdd:PRK13548 29 EVVAILGPNGAGKSTLLRALSGELSP----DSGEVRlNGRPLADWSPAELARRRAVL----------PQHsslsfpftVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 170 QIPRIfKGSVKALLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGAL--LKKSD----FLFIDEPSSYLDI 243
Cdd:PRK13548 95 EVVAM-GRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALDL 173
|
170 180
....*....|....*....|....*...
gi 1278501429 244 KQRLKVANLLRKHGSEKECAV-VVEHDL 270
Cdd:PRK13548 174 AHQHHVLRLARQLAHERGLAViVVLHDL 201
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
100-270 |
6.43e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 59.56 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 100 IMGLVGVNGIGKSTCLNILSGQLKPNlgndfGEVegqkiidFFKGTEAQNYfeKLYTTGLETSYKPQyveQIPRIFKGSV 179
Cdd:PRK03695 24 ILHLVGPNGAGKSTLLARMAGLLPGS-----GSI-------QFAGQPLEAW--SAAELARHRAYLSQ---QQTPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 180 KALL---------NKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLK-------KSDFLFIDEPSSYLDI 243
Cdd:PRK03695 87 FQYLtlhqpdktrTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDV 166
|
170 180
....*....|....*....|....*..
gi 1278501429 244 KQRLKVANLLRKHGSEKECAVVVEHDL 270
Cdd:PRK03695 167 AQQAALDRLLSELCQQGIAVVMSSHDL 193
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
369-498 |
6.54e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.20 E-value: 6.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 369 VLGENGTGKTTFAKILAGMIKPDK---------GKTDTS---------VKISYKP---QYVQ----------VENDDFVR 417
Cdd:PRK13640 38 LIGHNGSGKSTISKLINGLLLPDDnpnskitvdGITLTAktvwdirekVGIVFQNpdnQFVGatvgddvafgLENRAVPR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 418 SVLMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEASA 497
Cdd:PRK13640 118 PEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTV 197
|
.
gi 1278501429 498 F 498
Cdd:PRK13640 198 I 198
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
2-69 |
7.08e-10 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 57.02 E-value: 7.08e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 2 RIVVVNKKKCTagkGCdYVCMNFCPIN---RTGKDCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVVN 69
Cdd:cd10549 33 RGPEIDEDKCV---FC-GACVEVCPTGaieLTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCPVDAITLED 99
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
1-61 |
7.20e-10 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 57.65 E-value: 7.20e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278501429 1 MRIVVVNKKKCTA---GKGCDyVCMNFCPINrtGKDCIVEGADGKIVVEEELCIGCGICVNKCP 61
Cdd:cd16373 83 MGVAVIDKDRCLAwqgGTDCG-VCVEACPTE--AIAIVLEDDVLRPVVDEDKCVGCGLCEYVCP 143
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
199-475 |
7.42e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 61.26 E-value: 7.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 199 GIKHVLNRkVGD----ISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDLIML 273
Cdd:PRK15134 142 GIRQAAKR-LTDyphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLfITHNLSIV 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 274 DYLADVEHIM-YGRAgvygiVSKSlSIRECINTYLEGYIREdnmRFRSEEIKFEVKAPTKAlnnIPIIEWSNIE----KK 348
Cdd:PRK15134 221 RKLADRVAVMqNGRC-----VEQN-RAATLFSAPTHPYTQK---LLNSEPSGDPVPLPEPA---SPLLDVEQLQvafpIR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGI--------LMRNEIIGVLGENGTGKTTFAKILAGMIkPDKGktdtsvKISYKPQYVQVENDDF---VR 417
Cdd:PRK15134 289 KGILKRTVDHNVvvknisftLRPGETLGLVGESGSGKSTTGLALLRLI-NSQG------EIWFDGQPLHNLNRRQllpVR 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 418 S---VLMKTPPSMIE-RLDLSHLLKRKL----------------------------------SELSGGELQRVAIAECLS 459
Cdd:PRK15134 362 HriqVVFQDPNSSLNpRLNVLQIIEEGLrvhqptlsaaqreqqviavmeevgldpetrhrypAEFSGGQRQRIAIARALI 441
|
330
....*....|....*.
gi 1278501429 460 RDADVYLLDEPSAHLD 475
Cdd:PRK15134 442 LKPSLIILDEPTSSLD 457
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
99-270 |
7.55e-10 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 59.36 E-value: 7.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEV--EGQKIIDFfKGTE--------AQNyfeklytTGLETSYKPQYV 168
Cdd:COG4559 28 ELTAIIGPNGAGKSTLLKLLTGELTP----SSGEVrlNGRPLAAW-SPWElarrravlPQH-------SSLAFPFTVEEV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 169 EQIPRIFKGSVKALLNKIsegdVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGAL--LKKSD-----FLFIDEPSSYL 241
Cdd:COG4559 96 VALGRAPHGSSAAQDRQI----VREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLaqLWEPVdggprWLFLDEPTSAL 171
|
170 180 190
....*....|....*....|....*....|
gi 1278501429 242 DIKQRLKVANLLRKHGSEKeCAVV-VEHDL 270
Cdd:COG4559 172 DLAHQHAVLRLARQLARRG-GGVVaVLHDL 200
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
81-255 |
7.74e-10 |
|
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: 59.16 E-value: 7.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 81 SYDKN--GFKLFNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDffkGTEAQNYFEKLYTTG 158
Cdd:cd03254 11 SYDEKkpVLKDINFSIK-PGETVAIVGPTGAGKTTLINLLMRFYDPQ--------KGQILID---GIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 159 LetsykpQYVEQIPRIFKGSVKALL----NKISEGDVNKVCNELGI-----------KHVLNRKVGDISGGELQRVAIAG 223
Cdd:cd03254 79 I------GVVLQDTFLFSGTIMENIrlgrPNATDEEVIEAAKEAGAhdfimklpngyDTVLGENGGNLSQGERQLLAIAR 152
|
170 180 190
....*....|....*....|....*....|..
gi 1278501429 224 ALLKKSDFLFIDEPSSYLDIKQRLKVANLLRK 255
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEK 184
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
349-496 |
8.01e-10 |
|
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: 59.43 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKG----------KTDTSVKISYKpQYVQVENDDFVRS 418
Cdd:TIGR02769 27 LTNVSLSIEEG-----ETVGLLGRSGCGKSTLARLLLGLEKPAQGtvsfrgqdlyQLDRKQRRAFR-RDVQLVFQDSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 419 V--------LMKTPPSMIERLD-------LSHLLK---------RKL-SELSGGELQRVAIAECLSRDADVYLLDEPSAH 473
Cdd:TIGR02769 101 VnprmtvrqIIGEPLRHLTSLDeseqkarIAELLDmvglrsedaDKLpRQLSGGQLQRINIARALAVKPKLIVLDEAVSN 180
|
170 180
....*....|....*....|...
gi 1278501429 474 LDveqRLNVAKILRDVIKKKEAS 496
Cdd:TIGR02769 181 LD---MVLQAVILELLRKLQQAF 200
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
339-475 |
8.20e-10 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 58.80 E-value: 8.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 339 IIEWSNIEKK-------LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKI---------- 401
Cdd:TIGR02673 1 MIEFHNVSKAypggvaaLHDVSLHIRKG-----EFLFLTGPSGAGKTTLLKLLYGALTPSRG----QVRIagedvnrlrg 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 402 SYKP---QYVQVENDDFvRSVLMKT--------------PPSMIER--------LDLSHLLKRKLSELSGGELQRVAIAE 456
Cdd:TIGR02673 72 RQLPllrRRIGVVFQDF-RLLPDRTvyenvalplevrgkKEREIQRrvgaalrqVGLEHKADAFPEQLSGGEQQRVAIAR 150
|
170
....*....|....*....
gi 1278501429 457 CLSRDADVYLLDEPSAHLD 475
Cdd:TIGR02673 151 AIVNSPPLLLADEPTGNLD 169
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
99-499 |
9.22e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 60.83 E-value: 9.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPNLGNDfgEVEGQKiidFFKGTEAQNYFEKLYttgletsykpqYVEQIPRIFKG- 177
Cdd:PRK15439 38 EVHALLGGNGAGKSTLMKIIAGIVPPDSGTL--EIGGNP---CARLTPAKAHQLGIY-----------LVPQEPLLFPNl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 178 SVKA----LLNKiSEGDVNKVCN---ELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVA 250
Cdd:PRK15439 102 SVKEnilfGLPK-RQASMQKMKQllaALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLF 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 251 NLLRKHGSEKECAVVVEHDLIMLDYLADveHIMYGRAGVYGIVSKSLSI-RECINTYLEGYIREDNMrfrSEEIKFEVKA 329
Cdd:PRK15439 181 SRIRELLAQGVGIVFISHKLPEIRQLAD--RISVMRDGTIALSGKTADLsTDDIIQAITPAAREKSL---SASQKLWLEL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 330 P----TKAlNNIPIIEWSNIEKK-LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TD 396
Cdd:PRK15439 256 PgnrrQQA-AGAPVLTVEDLTGEgFRNISLEVRAG-----EILGLAGVVGAGRTELAETLYGLRPARGGRimlngkeiNA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 397 TSVK------ISYKPQYVQVE----------NddfVRSVLMKTPPSMIERLDLSHLLKR-------KLSE-------LSG 446
Cdd:PRK15439 330 LSTAqrlargLVYLPEDRQSSglyldaplawN---VCALTHNRRGFWIKPARENAVLERyrralniKFNHaeqaartLSG 406
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 447 GELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEASAFV 499
Cdd:PRK15439 407 GNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFI 459
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
96-238 |
1.11e-09 |
|
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: 58.60 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGndfgevegqKIIdfFKGTEAqnyfeklytTGLETSYKPQ----YVEQI 171
Cdd:cd03224 24 PEGEIVALLGRNGAGKTTLLKTIMGLLPPRSG---------SIR--FDGRDI---------TGLPPHERARagigYVPEG 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 172 PRIFKG-SVK--------ALLNKISEGDVNKVCNELGI-KHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPS 238
Cdd:cd03224 84 RRIFPElTVEenlllgayARRRAKRKARLERVYELFPRlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
96-242 |
1.28e-09 |
|
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: 58.06 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEV--EGQKIidffkGTEAQNYFEKL-YTTGLetsYKPQYV-EQI 171
Cdd:cd03269 24 EKGEIFGLLGPNGAGKTTTIRMILGIILP----DSGEVlfDGKPL-----DIAARNRIGYLpEERGL---YPKMKViDQL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 172 prIFKGSVKALLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLD 242
Cdd:cd03269 92 --VYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
349-497 |
1.33e-09 |
|
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: 58.25 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVKISYKP---QYVQVENDDF---------- 415
Cdd:TIGR01184 1 LKGVNLTIQQG-----EFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgpdRMVVFQNYSLlpwltvreni 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 416 ---VRSVLMKTPPS--------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAK 484
Cdd:TIGR01184 76 alaVDRVLPDLSKSerraiveeHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170
....*....|...
gi 1278501429 485 ILRDVIKKKEASA 497
Cdd:TIGR01184 156 ELMQIWEEHRVTV 168
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
191-270 |
1.44e-09 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 58.70 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 191 VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLK-------KSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECA 263
Cdd:COG4138 107 LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQGITV 186
|
....*..
gi 1278501429 264 VVVEHDL 270
Cdd:COG4138 187 VMSSHDL 193
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
311-493 |
1.66e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.19 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 311 IREDNMRFRSEEIKFEVKApTKALNNIpiiewsNIEKKLGDFKLkvkpgilmrneiigVLGENGTGKTTFAKILAGMIKP 390
Cdd:PRK10247 1 MQENSPLLQLQNVGYLAGD-AKILNNI------SFSLRAGEFKL--------------ITGPSGCGKSTLLKIVASLISP 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 391 DKGK-----TDTSV--------KISYKPQYVQV------ENDDFVRSVLMKTPPSMIERLDLS------HLLKRKLSELS 445
Cdd:PRK10247 60 TSGTllfegEDISTlkpeiyrqQVSYCAQTPTLfgdtvyDNLIFPWQIRNQQPDPAIFLDDLErfalpdTILTKNIAELS 139
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1278501429 446 GGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKK 493
Cdd:PRK10247 140 GGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQ 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
96-270 |
1.96e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.20 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDfgEVEGQKIIDFFKgteaqnyfEKLYttgLETSYkPQYVEQIPRIF 175
Cdd:PRK09544 28 KPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--KRNGKLRIGYVP--------QKLY---LDTTL-PLTVNRFLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 176 KGSVKAllnkisegDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRK 255
Cdd:PRK09544 94 PGTKKE--------DILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQ 165
|
170
....*....|....*.
gi 1278501429 256 HGSEKECAVV-VEHDL 270
Cdd:PRK09544 166 LRRELDCAVLmVSHDL 181
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
74-303 |
2.00e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 58.71 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 74 LESRMIHSYDKNG---FKLFNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgevEGQKIIDFfkgtEAQNY 150
Cdd:PRK13636 6 LKVEELNYNYSDGthaLKGININIK-KGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIL---FDGKPIDY----SRKGL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 151 FEKLYTTGLetsykpqyVEQIP--RIFKGSVkalLNKISEGDVN----------KVCNEL---GIKHVLNRKVGDISGGE 215
Cdd:PRK13636 78 MKLRESVGM--------VFQDPdnQLFSASV---YQDVSFGAVNlklpedevrkRVDNALkrtGIEHLKDKPTHCLSFGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 216 LQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVV-EHDLIMLDYLADVEHIM-YGRAGVYGIV 293
Cdd:PRK13636 147 KKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIaTHDIDIVPLYCDNVFVMkEGRVILQGNP 226
|
250
....*....|
gi 1278501429 294 SKSLSIRECI 303
Cdd:PRK13636 227 KEVFAEKEML 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
349-477 |
2.18e-09 |
|
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: 59.73 E-value: 2.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-------------TDTSVKISYKPQYVQVEND-- 413
Cdd:TIGR02203 348 LDSISLVIEPG-----ETVALVGRSGSGKSTLVNLIPRFYEPDSGQilldghdladytlASLRRQVALVSQDVVLFNDti 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 414 ---------------DFVRSVLMKTPPSMIERLD--LSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDV 476
Cdd:TIGR02203 423 anniaygrteqadraEIERALAAAYAQDFVDKLPlgLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDN 502
|
.
gi 1278501429 477 E 477
Cdd:TIGR02203 503 E 503
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
89-284 |
2.19e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 58.59 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 89 LFNLVIPQKK-QIMGLVGVNGIGKSTCLNILSGQLKPNLGN-DFGEV-----EGQKIID--------FFKGTEAQNYFEk 153
Cdd:PRK13643 22 LFDIDLEVKKgSYTALIGHTGSGKSTLLQHLNGLLQPTEGKvTVGDIvvsstSKQKEIKpvrkkvgvVFQFPESQLFEE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 154 lyTTGLETSYKPQYVeqiprifkgsvkallnKISEGDVNKVCNE----LGI-KHVLNRKVGDISGGELQRVAIAGALLKK 228
Cdd:PRK13643 101 --TVLKDVAFGPQNF----------------GIPKEKAEKIAAEklemVGLaDEFWEKSPFELSGGQMRRVAIAGILAME 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 229 SDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHdliMLDYLADVEHIMY 284
Cdd:PRK13643 163 PEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH---LMDDVADYADYVY 215
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
99-283 |
2.28e-09 |
|
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: 57.38 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPNLGNdfGEVEGQKIIdffkgTEAQNYFEKLYTTGLETSYKP-----QYVEQIPR 173
Cdd:cd03265 27 EIFGLLGPNGAGKTTTIKMLTTLLKPTSGR--ATVAGHDVV-----REPREVRRRIGIVFQDLSVDDeltgwENLYIHAR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 174 IFKGSVKALLNKISEgdvnkVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLL 253
Cdd:cd03265 100 LYGVPGAERRERIDE-----LLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI 174
|
170 180 190
....*....|....*....|....*....|...
gi 1278501429 254 RKhgSEKECAVVV---EHDLIMLDYLADVEHIM 283
Cdd:cd03265 175 EK--LKEEFGMTIlltTHYMEEAEQLCDRVAII 205
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
349-488 |
2.93e-09 |
|
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: 57.48 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKT--DTSVKISYKPQY-------VQVENDDFVRSV 419
Cdd:cd03248 30 LQDVSFTLHPG-----EVTALVGPSGSGKSTVVALLENFYQPQGGQVllDGKPISQYEHKYlhskvslVGQEPVLFARSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 420 -------LMKTPPSMI-ERLDLSHL--------------LKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:cd03248 105 qdniaygLQSCSFECVkEAAQKAHAhsfiselasgydteVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170
....*....|.
gi 1278501429 478 QRLNVAKILRD 488
Cdd:cd03248 185 SEQQVQQALYD 195
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
340-496 |
3.03e-09 |
|
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: 59.05 E-value: 3.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLGDFK-LKVKPGILMRNEIIGVLGENGTGKTTFAKILAGM--IKPDKGKTDTSVKISYKPQYVQV------ 410
Cdd:TIGR03269 1 IEVKNLTKKFDGKEvLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHVALCEKCGYVERpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 411 ------------------------------------------ENDDFVRSVL-------------MKTPPSMIERLDLSH 435
Cdd:TIGR03269 81 pcpvcggtlepeevdfwnlsdklrrrirkriaimlqrtfalyGDDTVLDNVLealeeigyegkeaVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 436 LLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEAS 496
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGIS 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
157-291 |
3.29e-09 |
|
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: 56.18 E-value: 3.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 157 TGLETSYKPQYVEQIPR------IFKGSVKALLNkisegdvnkvcneLGIKHV-LNRKVGDISGGELQRVAIA---GALL 226
Cdd:cd03238 40 EGLYASGKARLISFLPKfsrnklIFIDQLQFLID-------------VGLGYLtLGQKLSTLSGGELQRVKLAselFSEP 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 227 KKSDFLFiDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIML---DYLADVEHimygRAGVYG 291
Cdd:cd03238 107 PGTLFIL-DEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDVLssaDWIIDFGP----GSGKSG 169
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
103-269 |
3.80e-09 |
|
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: 56.65 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQLKPNLGNDfgEVEGQKIIDFFK----------GTEAQNyFEKLYTT--------GLETSYK 164
Cdd:cd03292 32 LVGPSGAGKSTLLKLIYKEELPTSGTI--RVNGQDVSDLRGraipylrrkiGVVFQD-FRLLPDRnvyenvafALEVTGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 165 PqyveqiPRIFKGSVKALLNKisegdvnkvcneLGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIK 244
Cdd:cd03292 109 P------PREIRKRVPAALEL------------VGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
170 180
....*....|....*....|....*
gi 1278501429 245 QRLKVANLLRKHGSEKECAVVVEHD 269
Cdd:cd03292 171 TTWEIMNLLKKINKAGTTVVVATHA 195
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
346-493 |
3.89e-09 |
|
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: 56.32 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 346 EKKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVKISYKPQYVQVEND------------ 413
Cdd:cd03250 18 SFTLKDINLEVPKG-----ELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEPWIQNGtirenilfgkpf 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 414 --DFVRSVlmktppsmIE----RLDLSHLLKRKLSE-------LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVeqrl 480
Cdd:cd03250 93 deERYEKV--------IKacalEPDLEILPDGDLTEigekginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA---- 160
|
170
....*....|....
gi 1278501429 481 NVAK-ILRDVIKKK 493
Cdd:cd03250 161 HVGRhIFENCILGL 174
|
|
| NuoI |
COG1143 |
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ... |
8-77 |
4.17e-09 |
|
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase
Pssm-ID: 440758 [Multi-domain] Cd Length: 66 Bit Score: 52.83 E-value: 4.17e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 8 KKKCTagkGCDyVCMNFCPinrtgKDCIV---EGADGKIVVEEELCIGCGICVNKCPFDAVKVVNLPDELESR 77
Cdd:COG1143 1 EDKCI---GCG-LCVRVCP-----VDAITiedGEPGKVYVIDPDKCIGCGLCVEVCPTGAISMTPFELAVEDR 64
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
340-488 |
4.34e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 56.95 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLG------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKG-------KTDTSVKISYK-- 404
Cdd:COG4161 3 IQLKNINCFYGshqalfDINLECPSG-----ETLVLLGPSGAGKSSLLRVLNLLETPDSGqlniaghQFDFSQKPSEKai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 405 -----------------PQYVQVEN--------DDFVRSVLMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLS 459
Cdd:COG4161 78 rllrqkvgmvfqqynlwPHLTVMENlieapckvLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180
....*....|....*....|....*....
gi 1278501429 460 RDADVYLLDEPSAHLDVEQRLNVAKILRD 488
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRE 186
|
|
| HycB |
COG1142 |
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion]; |
21-68 |
4.54e-09 |
|
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
Pssm-ID: 440757 [Multi-domain] Cd Length: 138 Bit Score: 54.66 E-value: 4.54e-09
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1278501429 21 CMNFCPinrtgKDCIVEGaDGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:COG1142 60 CAEVCP-----VGAITRD-DGAVVVDEEKCIGCGLCVLACPFGAITMV 101
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
335-499 |
4.72e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 58.64 E-value: 4.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 335 NNIPIIEWSNIEKKLG------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-------------- 394
Cdd:PRK09700 1 MATPYISMAGIGKSFGpvhalkSVNLTVYPG-----EIHALLGENGAGKSTLMKVLSGIHEPTKGTitinninynkldhk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 395 --TDTSVKISYKPQYV----QVENDDFV-----RSVL---------MKTPPSMI-ERLDLSHLLKRKLSELSGGELQRVA 453
Cdd:PRK09700 76 laAQLGIGIIYQELSVidelTVLENLYIgrhltKKVCgvniidwreMRVRAAMMlLRVGLKVDLDEKVANLSISHKQMLE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1278501429 454 IAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVikKKEASAFV 499
Cdd:PRK09700 156 IAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQL--RKEGTAIV 199
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
369-475 |
5.05e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 57.34 E-value: 5.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 369 VLGENGTGKTTFAKILAGMIKPDKG------------KTDTSVK-------------------------ISYKPQYVQVE 411
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQPTSGtvtigervitagKKNKKLKplrkkvgivfqfpehqlfeetvekdICFGPMNFGVS 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278501429 412 NDDfvrsvLMKTPPSMIERLDLSH-LLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:PRK13634 118 EED-----AKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
90-242 |
5.20e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 58.64 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 90 FNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDffkGTEAQNYfeklyttGLEtSYKPQ--Y 167
Cdd:COG1132 359 ISLTIP-PGETVALVGPSGSGKSTLVNLLLRFYDPT--------SGRILID---GVDIRDL-------TLE-SLRRQigV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 168 VEQIPRIFKGSVKAllN------KISEGDVNKVCNELGIKHVLNR-------KVGD----ISGGELQRVAIAGALLKKSD 230
Cdd:COG1132 419 VPQDTFLFSGTIRE--NirygrpDATDEEVEEAAKAAQAHEFIEAlpdgydtVVGErgvnLSGGQRQRIAIARALLKDPP 496
|
170
....*....|..
gi 1278501429 231 FLFIDEPSSYLD 242
Cdd:COG1132 497 ILILDEATSALD 508
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
91-270 |
5.33e-09 |
|
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: 56.42 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPqKKQIMGLVGVNGIGKSTCLNILsgqlkpNLGNDFGE---VEGQKIIDffkgteAQNYFEKLYTTgLETSYKPQY 167
Cdd:cd03260 20 SLDIP-KGEITALIGPSGCGKSTLLRLL------NRLNDLIPgapDEGEVLLD------GKDIYDLDVDV-LELRRRVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 168 VEQIPRIFKGSVKA-----------LLNKISEGDVNKVCNELGI-KHVLNR-KVGDISGGELQRVAIAGALLKKSDFLFI 234
Cdd:cd03260 86 VFQKPNPFPGSIYDnvayglrlhgiKLKEELDERVEEALRKAALwDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278501429 235 DEPSSYLDIKQRLKVANLLRKHGseKECAVV-VEHDL 270
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAELK--KEYTIViVTHNM 200
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
338-488 |
5.46e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKK------LGDFKLKVKPGILMrneiiGVLGENGTGKTTFAKILAGMIKPDKG--------------KTDT 397
Cdd:PRK10762 3 ALLQLKGIDKAfpgvkaLSGAALNVYPGRVM-----ALVGENGAGKSTMMKVLTGIYTRDAGsilylgkevtfngpKSSQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 398 SVKIS-------YKPQYVQVEN----DDFVRSV-------LMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLS 459
Cdd:PRK10762 78 EAGIGiihqelnLIPQLTIAENiflgREFVNRFgridwkkMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS 157
|
170 180 190
....*....|....*....|....*....|..
gi 1278501429 460 RDADVYLLDEPSAHL---DVEQRLNVAKILRD 488
Cdd:PRK10762 158 FESKVIIMDEPTDALtdtETESLFRVIRELKS 189
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
103-274 |
5.46e-09 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 56.10 E-value: 5.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQLKPNLGNdfGEVEGQKIIDF------------------FKGTEAQNYFEKLYTTgLETSYK 164
Cdd:TIGR02673 33 LTGPSGAGKTTLLKLLYGALTPSRGQ--VRIAGEDVNRLrgrqlpllrrrigvvfqdFRLLPDRTVYENVALP-LEVRGK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 165 PQyvEQIPRifkgSVKALLNKIsegdvnkvcnelGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIK 244
Cdd:TIGR02673 110 KE--REIQR----RVGAALRQV------------GLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPD 171
|
170 180 190
....*....|....*....|....*....|
gi 1278501429 245 QRLKVANLLRKHGSEKECAVVVEHDLIMLD 274
Cdd:TIGR02673 172 LSERILDLLKRLNKRGTTVIVATHDLSLVD 201
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
96-270 |
5.66e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 56.75 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGndfgEV--EGQKIIDFFKGTEAQNYFEKL---YT--------TGLETS 162
Cdd:PRK11629 33 GEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSG----DVifNGQPMSKLSSAAKAELRNQKLgfiYQfhhllpdfTALENV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 163 YKPqyveqiprifkgsvkALLNKISEGDVNKVCNEL----GIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPS 238
Cdd:PRK11629 109 AMP---------------LLIGKKKPAEINSRALEMlaavGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 1278501429 239 SYLDIKQRLKVANLL----RKHGSekeCAVVVEHDL 270
Cdd:PRK11629 174 GNLDARNADSIFQLLgelnRLQGT---AFLVVTHDL 206
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
335-475 |
5.93e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 56.36 E-value: 5.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 335 NNIPIIEWSNIEKKLGDFKLKVKpgiLMRN--------EIIGVLGENGTGKTTFAKILAGMIKPD------KGKTDTSVK 400
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTD---VLHNvsfsigegEMMAIVGSSGSGKSTLLHLLGGLDTPTsgdvifNGQPMSKLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 401 ISYK------------------PQYVQVENddfvrsVLM-----KTPPS--------MIERLDLSHLLKRKLSELSGGEL 449
Cdd:PRK11629 78 SAAKaelrnqklgfiyqfhhllPDFTALEN------VAMplligKKKPAeinsraleMLAAVGLEHRANHRPSELSGGER 151
|
170 180
....*....|....*....|....*.
gi 1278501429 450 QRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
354-474 |
6.26e-09 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 56.53 E-value: 6.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 354 LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKG------------KTDTSVK--ISYKPQYVQV-------EN 412
Cdd:COG0410 24 LEVEEG-----EIVALLGRNGAGKTTLLKAISGLLPPRSGsirfdgeditglPPHRIARlgIGYVPEGRRIfpsltveEN 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 413 ddfvrsvLM------KTPPSMIERLD--------LSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHL 474
Cdd:COG0410 99 -------LLlgayarRDRAEVRADLErvyelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
339-489 |
8.50e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 56.66 E-value: 8.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 339 IIEWSNIEKK---------LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSV-- 399
Cdd:PRK13650 4 IIEVKNLTFKykedqekytLNDVSFHVKQG-----EWLSIIGHNGSGKSTTVRLIDGLLEAESGQiiidgdllTEENVwd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 400 ---KISY---KP--QYV--QVEnDDFVRSVLMKTPP--SMIERLD-------LSHLLKRKLSELSGGELQRVAIAECLSR 460
Cdd:PRK13650 79 irhKIGMvfqNPdnQFVgaTVE-DDVAFGLENKGIPheEMKERVNealelvgMQDFKEREPARLSGGQKQRVAIAGAVAM 157
|
170 180
....*....|....*....|....*....
gi 1278501429 461 DADVYLLDEPSAHLDVEQRLNVAKILRDV 489
Cdd:PRK13650 158 RPKIIILDEATSMLDPEGRLELIKTIKGI 186
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
363-492 |
9.21e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 56.55 E-value: 9.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----------------------------------TDTSVKISYKPQY 407
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAvlwqgkpldyskrgllalrqqvatvfqdpeqqifyTDIDSDIAFSLRN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 408 VQVENDDFVRSVlmktpPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILR 487
Cdd:PRK13638 106 LGVPEAEITRRV-----DEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIR 180
|
....*
gi 1278501429 488 DVIKK 492
Cdd:PRK13638 181 RIVAQ 185
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
351-492 |
9.47e-09 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 57.02 E-value: 9.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 351 DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVKISYKpqyvqvENDDFVR--SVLM--KT--- 423
Cdd:COG4586 40 DISFTIEPG-----EIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK------RRKEFARriGVVFgqRSqlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 424 ---PPS-----------------------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVe 477
Cdd:COG4586 109 wdlPAIdsfrllkaiyripdaeykkrldeLVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV- 187
|
170
....*....|....*.
gi 1278501429 478 qrlnVAKI-LRDVIKK 492
Cdd:COG4586 188 ----VSKEaIREFLKE 199
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
103-277 |
1.11e-08 |
|
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: 55.71 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIIDF--FK---GTEAQNY--FEKLYTT-----GLETSYKPQyveq 170
Cdd:cd03300 31 LLGPSGCGKTTLLRLIAGFETPTSGEIL--LDGKDITNLppHKrpvNTVFQNYalFPHLTVFeniafGLRLKKLPK---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 ipRIFKGSVKALLNKIsegdvnkvcnelGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQR---- 246
Cdd:cd03300 105 --AEIKERVAEALDLV------------QLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRkdmq 170
|
170 180 190
....*....|....*....|....*....|....*
gi 1278501429 247 LKVANLLRKHGSekeCAVVVEHD----LIMLDYLA 277
Cdd:cd03300 171 LELKRLQKELGI---TFVFVTHDqeeaLTMSDRIA 202
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
347-488 |
1.12e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.23 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 347 KKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK----------TDTS------VKISYK-----P 405
Cdd:PRK11288 18 KALDDISFDCRAG-----QVHALMGENGAGKSTLLKILSGNYQPDAGSilidgqemrfASTTaalaagVAIIYQelhlvP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 406 QYVQVEN---------DDFV-RSVLMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHL- 474
Cdd:PRK11288 93 EMTVAENlylgqlphkGGIVnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLs 172
|
170
....*....|....*.
gi 1278501429 475 --DVEQRLNVAKILRD 488
Cdd:PRK11288 173 arEIEQLFRVIRELRA 188
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
338-489 |
1.39e-08 |
|
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: 55.52 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKKLG----------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKIS----- 402
Cdd:COG4181 7 PIIELRGLTKTVGtgageltilkGISLEVEAG-----ESVAIVGASGSGKSTLLGLLAGLDRPTSG----TVRLAgqdlf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 403 ---------YKPQYV----Q----------VEN-----------DDFVRSVlmktppSMIERLDLSHLLKRKLSELSGGE 448
Cdd:COG4181 78 aldedararLRARHVgfvfQsfqllptltaLENvmlplelagrrDARARAR------ALLERVGLGHRLDHYPAQLSGGE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1278501429 449 LQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDV 489
Cdd:COG4181 152 QQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFEL 192
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
90-278 |
1.42e-08 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 55.37 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 90 FNLVIPQKKqIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVE--GQkiiDFFKGTEAQNYfeklyttgletsykpqy 167
Cdd:COG1127 24 VSLDVPRGE-ILAIIGGSGSGKSVLLKLIIGLLRP----DSGEILvdGQ---DITGLSEKELY----------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 168 veQIPR----IFKGSvkALLN----------------KISEGDVNKVCNE----LGIKHVLNRKVGDISGGELQRVAIAG 223
Cdd:COG1127 79 --ELRRrigmLFQGG--ALFDsltvfenvafplrehtDLSEAEIRELVLEklelVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 224 ALLKKSDFLFIDEPSSYLDIKQRLKVANLLRK-HGSEKECAVVVEHDLIMLDYLAD 278
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRElRDELGLTSVVVTHDLDSAFAIAD 210
|
|
| FDH_b_like |
cd10562 |
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes ... |
18-67 |
1.45e-08 |
|
uncharacterized subfamily of beta subunit of formate dehydrogenase; This subfamily includes the beta-subunit of formate dehydrogenases that are as yet uncharacterized. Members of the DMSO reductase family include formate dehydrogenase N and O (FDH-N, FDH-O) and tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N, a major component of nitrate respiration of Escherichia coli, is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. It forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. W-FDH contains a tungsten instead of molybdenum at the catalytic center. This enzyme seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It is a heterodimer of a large and a small subunit; the large subunit harbors the W site and one [4Fe-4S] center and the small subunit, containing three [4Fe-4S] clusters, functions to transfer electrons.
Pssm-ID: 319884 [Multi-domain] Cd Length: 161 Bit Score: 53.85 E-value: 1.45e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1278501429 18 DYVCMNFCPinrtgKDCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKV 67
Cdd:cd10562 75 DAACVKVCP-----TGALYKTENGAVVVDEDKCIGCGYCVAACPFDVPRY 119
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
96-476 |
1.62e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGqLKPnlgndFGEVEGQKIID-------FFKGTEA-------QNYFEKLYTTGLET 161
Cdd:PRK13549 29 RAGEIVSLCGENGAGKSTLMKVLSG-VYP-----HGTYEGEIIFEgeelqasNIRDTERagiaiihQELALVKELSVLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 162 sykpqyveqiprIFKGsvkallNKISEGDV----------NKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDF 231
Cdd:PRK13549 103 ------------IFLG------NEITPGGImdydamylraQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 232 LFIDEPSSYL---DIKQRLKVANLLRKHG------SEKECAVVVEHDLIMLdyLADVEHIMYGRAgvygivsKSLSIREC 302
Cdd:PRK13549 165 LILDEPTASLtesETAVLLDIIRDLKAHGiaciyiSHKLNEVKAISDTICV--IRDGRHIGTRPA-------AGMTEDDI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 303 InTYLEGyiREDNMRFRSE-----EIKFEVKaptkalnNIPIIEWSNIEKKLGD---FKLKvkpgilmRNEIIGVLGENG 374
Cdd:PRK13549 236 I-TMMVG--RELTALYPREphtigEVILEVR-------NLTAWDPVNPHIKRVDdvsFSLR-------RGEILGIAGLVG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 375 TGKTTFAKILAGMIkpdKGKTDTSVKISYKPqyVQVEN------------------------------------DDFV-R 417
Cdd:PRK13549 299 AGRTELVQCLFGAY---PGRWEGEIFIDGKP--VKIRNpqqaiaqgiamvpedrkrdgivpvmgvgknitlaalDRFTgG 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 418 SVL-----MKTPPSMIERLDL--SHLLKRkLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDV 476
Cdd:PRK13549 374 SRIddaaeLKTILESIQRLKVktASPELA-IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| HycB_like |
cd10554 |
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ... |
21-68 |
1.72e-08 |
|
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.
Pssm-ID: 319876 [Multi-domain] Cd Length: 149 Bit Score: 53.42 E-value: 1.72e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1278501429 21 CMNFCPINrtgkdCIVEGaDGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:cd10554 64 CANVCPVG-----AISQE-DGVVQVDEERCIGCKLCVLACPFGAIEMA 105
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
340-477 |
1.82e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 55.14 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKK------LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKT-------DTSVKISYKPQ 406
Cdd:PRK11264 4 IEVKNLVKKfhgqtvLHGIDLEVKPG-----EVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditiDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 407 YVQV--ENDDFV---------RSVL----------MKTPPSMIERLDLSHLLKRKLS--------ELSGGELQRVAIAEC 457
Cdd:PRK11264 79 LIRQlrQHVGFVfqnfnlfphRTVLeniiegpvivKGEPKEEATARARELLAKVGLAgketsyprRLSGGQQQRVAIARA 158
|
170 180
....*....|....*....|
gi 1278501429 458 LSRDADVYLLDEPSAHLDVE 477
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPE 178
|
|
| FDH_beta_like |
cd16366 |
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family ... |
21-68 |
1.93e-08 |
|
beta FeS subunits of formate dehydrogenase N (FDH-N) and similar proteins; This family contains beta FeS subunits of several dehydrogenases in the DMSO reductase superfamily, including formate dehydrogenase N (FDH-N), tungsten-containing formate dehydrogenase (W-FDH) and other similar proteins. FDH-N is a major component of nitrate respiration of Escherichia coli; it catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate to a cytochrome. W-FDH contains a tungsten instead of molybdenum at the catalytic center and seems to be exclusively found in organisms such as hyperthermophilic archaea that live in extreme environments. It catalyzes the oxidation of formate to carbon dioxide, donating the electrons to a second substrate.
Pssm-ID: 319888 [Multi-domain] Cd Length: 156 Bit Score: 53.56 E-value: 1.93e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1278501429 21 CMNFCPinrTGkdCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:cd16366 78 CLAACP---TG--AIIRTETGTVVVDPETCIGCGYCVNACPFDIPRFD 120
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
78-282 |
2.12e-08 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 54.76 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 78 MIH----SYDKNGFKL-FNLVIPQKkQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVegqkiidFFKGteaQNYfe 152
Cdd:COG3840 1 MLRlddlTYRYGDFPLrFDLTIAAG-ERVAILGPSGAGKSTLLNLIAGFLPP----DSGRI-------LWNG---QDL-- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 153 klytTGLETSYKPqyveqIPRIFKG-------SVK---AL-LN---KISEGDVNKV---CNELGIKHVLNRKVGDISGGE 215
Cdd:COG3840 64 ----TALPPAERP-----VSMLFQEnnlfphlTVAqniGLgLRpglKLTAEQRAQVeqaLERVGLAGLLDRLPGQLSGGQ 134
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 216 LQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDlimldyLADVEHI 282
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLmVTHD------PEDAARI 196
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
92-269 |
2.23e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.79 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 92 LVIpQKKQIMGLVGVNGIGKSTCLNILSGQlkpNLGNDfGEVE--GQKIIDFFKGTEAQ----------NYFEKLYT-TG 158
Cdd:PRK10584 31 LVV-KRGETIALIGESGSGKSTLLAILAGL---DDGSS-GEVSlvGQPLHQMDEEARAKlrakhvgfvfQSFMLIPTlNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 159 LETSykpqyveQIPRIFKGSVkallNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPS 238
Cdd:PRK10584 106 LENV-------ELPALLRGES----SRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190
....*....|....*....|....*....|....*
gi 1278501429 239 SYLDIKQRLKVANLL----RKHGSekeCAVVVEHD 269
Cdd:PRK10584 175 GNLDRQTGDKIADLLfslnREHGT---TLILVTHD 206
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
101-270 |
2.43e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 55.12 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 101 MGLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIidffkgTEaQNYFEKLYTTGLetsykpqyVEQIP-RIFKGSV 179
Cdd:PRK13650 36 LSIIGHNGSGKSTTVRLIDGLLEAESGQII--IDGDLL------TE-ENVWDIRHKIGM--------VFQNPdNQFVGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 180 -----------KALLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLK 248
Cdd:PRK13650 99 veddvafglenKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLE 178
|
170 180
....*....|....*....|...
gi 1278501429 249 VANLLRKHGSEKECAVV-VEHDL 270
Cdd:PRK13650 179 LIKTIKGIRDDYQMTVIsITHDL 201
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
338-488 |
2.49e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.09 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMI-------------KPDKGKT--D 396
Cdd:PRK13549 4 YLLEMKNITKTFGGVKaldnvsLKVRAG-----EIVSLCGENGAGKSTLMKVLSGVYphgtyegeiifegEELQASNirD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 397 TSVK---ISYK-----PQYVQVEN----DDFVRSVLMKTpPSMIERLDlsHLLKR---------KLSELSGGELQRVAIA 455
Cdd:PRK13549 79 TERAgiaIIHQelalvKELSVLENiflgNEITPGGIMDY-DAMYLRAQ--KLLAQlkldinpatPVGNLGLGQQQLVEIA 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 1278501429 456 ECLSRDADVYLLDEPSAHL---DVEQRLNVAKILRD 488
Cdd:PRK13549 156 KALNKQARLLILDEPTASLtesETAVLLDIIRDLKA 191
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
96-242 |
2.68e-08 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 55.11 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVE--GQKIidffkGTEAQNYF-----EKlyttGLetsYKPQYV 168
Cdd:COG4152 25 PKGEIFGLLGPNGAGKTTTIRIILGILAP----DSGEVLwdGEPL-----DPEDRRRIgylpeER----GL---YPKMKV 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278501429 169 -EQIprIFKGSVKALLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLD 242
Cdd:COG4152 89 gEQL--VYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD 161
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
340-487 |
2.73e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 54.70 E-value: 2.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKK------LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsvkisykpqyVQVEND 413
Cdd:COG4604 2 IEIKNVSKRyggkvvLDDVSLTIPKG-----GITALIGPNGAGKSTLLSMISRLLPPDSGE-------------VLVDGL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 414 DFVR----------SVLMKTP-----------------P---------------SMIERLDLSHLLKRKLSELSGGELQR 451
Cdd:COG4604 64 DVATtpsrelakrlAILRQENhinsrltvrelvafgrfPyskgrltaedreiidEAIAYLDLEDLADRYLDELSGGQRQR 143
|
170 180 190
....*....|....*....|....*....|....*.
gi 1278501429 452 VAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILR 487
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLR 179
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
335-494 |
2.75e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 55.14 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 335 NNIPIIEWSNIEKKL-GD--FKLKVKPGILMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsvkISYKPQYVQVE 411
Cdd:PRK13648 3 DKNSIIVFKNVSFQYqSDasFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGE------IFYNNQAITDD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 412 N----------------DDFVRSV------------------LMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAEC 457
Cdd:PRK13648 77 NfeklrkhigivfqnpdNQFVGSIvkydvafglenhavpydeMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGV 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278501429 458 LSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKE 494
Cdd:PRK13648 157 LALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHN 193
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
340-493 |
2.86e-08 |
|
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: 54.54 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNI-----EKK--LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----------TDTSV-- 399
Cdd:cd03254 3 IEFENVnfsydEKKpvLKDINFSIKPG-----ETVAIVGPTGAGKTTLINLLMRFYDPQKGQilidgidirdiSRKSLrs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 400 KISYKPQYVQVENDDFVRSVLMKTPPS----------------MIERL--DLSHLLKRKLSELSGGELQRVAIAECLSRD 461
Cdd:cd03254 78 MIGVVLQDTFLFSGTIMENIRLGRPNAtdeevieaakeagahdFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRD 157
|
170 180 190
....*....|....*....|....*....|..
gi 1278501429 462 ADVYLLDEPSAHLDVEQRLNVAKILRDVIKKK 493
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKLMKGR 189
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
191-270 |
3.08e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 54.81 E-value: 3.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 191 VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHD 269
Cdd:PRK13640 124 VRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVIsITHD 203
|
.
gi 1278501429 270 L 270
Cdd:PRK13640 204 I 204
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
90-278 |
3.37e-08 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 54.71 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 90 FNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVE--GQKIidffKGTEA------QNYfeKLY---TT- 157
Cdd:COG1116 30 VSLTVA-AGEFVALVGPSGCGKSTLLRLIAGLEKP----TSGEVLvdGKPV----TGPGPdrgvvfQEP--ALLpwlTVl 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 158 -----GLETSYKPQyvEQIPRIfkgsVKALLNKIsegdvnkvcnelGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFL 232
Cdd:COG1116 99 dnvalGLELRGVPK--AERRER----ARELLELV------------GLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1278501429 233 FIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDlimLD---YLAD 278
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLWQETGKTVLfVTHD---VDeavFLAD 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
98-279 |
3.44e-08 |
|
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: 55.96 E-value: 3.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 98 KQIMGLVGVNGIGKSTCLNILSGQLKPNLGndfgEVE---GQKIIDFFK-------------GTEAQNYfeKLYT--TGL 159
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGVLEPTSG----EVNvrvGDEWVDMTKpgpdgrgrakryiGILHQEY--DLYPhrTVL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 160 ETSYKPQYVEqIPRIFkGSVKALLNKISEGdvnkvCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSS 239
Cdd:TIGR03269 384 DNLTEAIGLE-LPDEL-ARMKAVITLKMVG-----FDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTG 456
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1278501429 240 YLDIKQRLKVANLLRKHGSE-KECAVVVEHDlimLDYLADV 279
Cdd:TIGR03269 457 TMDPITKVDVTHSILKAREEmEQTFIIVSHD---MDFVLDV 494
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
203-287 |
3.83e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.10 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 203 VLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDLIMLDYLADVEH 281
Cdd:PRK15079 154 LINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIfIAHDLAVVKHISDRVL 233
|
....*..
gi 1278501429 282 IMY-GRA 287
Cdd:PRK15079 234 VMYlGHA 240
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
369-493 |
4.23e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.41 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 369 VLGENGTGKTTFAKILAGMIKPDKGKTDTS----VKISYKPQYVQVEN--------------DDFVRSVL------MKTP 424
Cdd:PRK10938 34 FVGANGSGKSALARALAGELPLLSGERQSQfshiTRLSFEQLQKLVSDewqrnntdmlspgeDDTGRTTAeiiqdeVKDP 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 425 P---SMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKK 493
Cdd:PRK10938 114 ArceQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSG 185
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
348-478 |
4.37e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 54.17 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 348 KLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIkPDKGK-------------TDTSVKISY-----KP---- 405
Cdd:PRK03695 11 RLGPLSAEVRAG-----EILHLVGPNGAGKSTLLARMAGLL-PGSGSiqfagqpleawsaAELARHRAYlsqqqTPpfam 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 406 ---QYVQVE-----NDDFVRSVLmktpPSMIERLDLSHLLKRKLSELSGGELQRVAIAE-CL--SRDADVY----LLDEP 470
Cdd:PRK03695 85 pvfQYLTLHqpdktRTEAVASAL----NEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAvVLqvWPDINPAgqllLLDEP 160
|
....*...
gi 1278501429 471 SAHLDVEQ 478
Cdd:PRK03695 161 MNSLDVAQ 168
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
349-493 |
4.47e-08 |
|
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: 53.77 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----------TDTSV--KISYKPQYVQVENDDF 415
Cdd:cd03253 17 LKDVSFTIPAG-----KKVAIVGPSGSGKSTILRLLFRFYDVSSGSilidgqdirevTLDSLrrAIGVVPQDTVLFNDTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 416 VRSV----LMKTPPSMIERLDLSHLLKR----------KLSE----LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:cd03253 92 GYNIrygrPDATDEEVIEAAKAAQIHDKimrfpdgydtIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTH 171
|
170
....*....|....*.
gi 1278501429 478 QRLNVAKILRDVIKKK 493
Cdd:cd03253 172 TEREIQAALRDVSKGR 187
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
339-475 |
4.66e-08 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 54.70 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 339 IIEWSNIEK----KLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsvkisykpqyV 408
Cdd:COG1135 1 MIELENLSKtfptKGGPVTalddvsLTIEKG-----EIFGIIGYSGAGKSTLIRCINLLERPTSGS-------------V 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 409 QVENDDFV--------------------------RSV---------LMKTPPS--------MIERLDLSHLLKRKLSELS 445
Cdd:COG1135 63 LVDGVDLTalserelraarrkigmifqhfnllssRTVaenvalpleIAGVPKAeirkrvaeLLELVGLSDKADAYPSQLS 142
|
170 180 190
....*....|....*....|....*....|
gi 1278501429 446 GGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:COG1135 143 GGQKQRVGIARALANNPKVLLCDEATSALD 172
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
353-475 |
4.74e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 53.63 E-value: 4.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 353 KLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMikpDKGkTDTSVKISYKPQY---------VQVENDDFVRSVLMKT 423
Cdd:PRK10584 30 ELVVKRG-----ETIALIGESGSGKSTLLAILAGL---DDG-SSGEVSLVGQPLHqmdeearakLRAKHVGFVFQSFMLI 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 424 PP--------------------------SMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:PRK10584 101 PTlnalenvelpallrgessrqsrngakALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
91-270 |
4.86e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 54.22 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIpQKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIIDFFKGTEAQNYFEKLYTTGlETSYKPQYVEQ 170
Cdd:PRK13644 22 NLVI-KKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVL--VSGIDTGDFSKLQGIRKLVGIVFQNP-ETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 ipRIFKGSVKALLNKIS-EGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKV 249
Cdd:PRK13644 98 --DLAFGPENLCLPPIEiRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180
....*....|....*....|.
gi 1278501429 250 ANLLRKHGSEKECAVVVEHDL 270
Cdd:PRK13644 176 LERIKKLHEKGKTIVYITHNL 196
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
212-287 |
5.27e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.59 E-value: 5.27e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 212 SGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECA-VVVEHDLIMLDYLADVEHIMY-GRA 287
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSyVFISHDLSVVEHIADEVMVMYlGRC 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
100-270 |
5.39e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 54.12 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 100 IMGLVGVNGIGKSTCLNILSGQLKPN------LGNDFGEVEGQKIIDFFKGTEAQNYfeklyttgletSYkPQYVEQIPR 173
Cdd:PRK15056 35 IAALVGVNGSGKSTLFKALMGFVRLAsgkisiLGQPTRQALQKNLVAYVPQSEEVDW-----------SF-PVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 174 IFKGSVKALLNKISEGD---VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVA 250
Cdd:PRK15056 103 MGRYGHMGWLRRAKKRDrqiVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARII 182
|
170 180
....*....|....*....|
gi 1278501429 251 NLLRKHGSEKECAVVVEHDL 270
Cdd:PRK15056 183 SLLRELRDEGKTMLVSTHNL 202
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
427-488 |
5.52e-08 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 53.86 E-value: 5.52e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 427 MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRD 488
Cdd:PRK11124 125 LLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRE 186
|
|
| DMSOR_beta-like |
cd04410 |
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ... |
21-67 |
5.90e-08 |
|
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319870 [Multi-domain] Cd Length: 136 Bit Score: 51.62 E-value: 5.90e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1278501429 21 CMNFCPinrtgKDCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKV 67
Cdd:cd04410 58 CVKACP-----TGAIYKDEDGIVLIDEDKCIGCGSCVEACPYGAIVF 99
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
101-285 |
5.99e-08 |
|
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: 54.04 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 101 MGLVGVNGIGKSTCLNILSGQLKPNLGN------DFGEVEGQKIIDFFKgtEAQNYFEKLYTtgletSYKPQY-VEQIPR 173
Cdd:TIGR02769 40 VGLLGRSGCGKSTLARLLLGLEKPAQGTvsfrgqDLYQLDRKQRRAFRR--DVQLVFQDSPS-----AVNPRMtVRQIIG 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 174 -----IFKGSVKALLNKISEgdvnkVCNELGIK-HVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRL 247
Cdd:TIGR02769 113 eplrhLTSLDESEQKARIAE-----LLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQA 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 1278501429 248 KVANLLRKHGSEKECA-VVVEHDLIMLDYLADVEHIMYG 285
Cdd:TIGR02769 188 VILELLRKLQQAFGTAyLFITHDLRLVQSFCQRVAVMDK 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
96-283 |
6.60e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 54.09 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGN----DFgeVEGQKIiDFFKGTEAQNY-----FEKLYTTGLETSYKPQ 166
Cdd:PRK13631 50 EKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTiqvgDI--YIGDKK-NNHELITNPYSkkiknFKELRRRVSMVFQFPE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 167 YveqipRIFKGSVKallNKISEGDVN-------------KVCNELGIKH-VLNRKVGDISGGELQRVAIAGALLKKSDFL 232
Cdd:PRK13631 127 Y-----QLFKDTIE---KDIMFGPVAlgvkkseakklakFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 233 FIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIMLDYLADVEHIM 283
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVM 249
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
354-483 |
6.94e-08 |
|
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: 55.14 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 354 LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsVK-----------------ISYKPQYVQ------V 410
Cdd:COG4618 353 FSLEPG-----EVLGVIGPSGSGKSTLARLLVGVWPPTAGS----VRldgadlsqwdreelgrhIGYLPQDVElfdgtiA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 411 ENddFVRsvlMKTPPS--------------MIERL----DLshllkrKLSE----LSGGELQRVAIAECLSRDADVYLLD 468
Cdd:COG4618 424 EN--IAR---FGDADPekvvaaaklagvheMILRLpdgyDT------RIGEggarLSGGQRQRIGLARALYGDPRLVVLD 492
|
170
....*....|....*..
gi 1278501429 469 EPSAHLDV--EQRLNVA 483
Cdd:COG4618 493 EPNSNLDDegEAALAAA 509
|
|
| DMSOR_beta_like |
cd16371 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
20-66 |
7.14e-08 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319893 [Multi-domain] Cd Length: 140 Bit Score: 51.41 E-value: 7.14e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1278501429 20 VCMNFCPINRTGKDcivegADGKIVVEEELCIGCGICVNKCPFDAVK 66
Cdd:cd16371 61 ACVKVCPTGAITKR-----EDGIVVVDQDKCIGCGYCVWACPYGAPQ 102
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
212-257 |
7.21e-08 |
|
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: 52.16 E-value: 7.21e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1278501429 212 SGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHG 257
Cdd:cd03223 93 SGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG 138
|
|
| vorD |
PRK09623 |
3-methyl-2-oxobutanoate dehydrogenase subunit delta; |
3-68 |
7.29e-08 |
|
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
Pssm-ID: 170016 [Multi-domain] Cd Length: 105 Bit Score: 50.33 E-value: 7.29e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 3 IVVVNKKKCTAgkgCdYVCMNFCPinrtgKDCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:PRK09623 45 MPVVDESKCVK---C-YICWKFCP-----EPAIYIKEDGYVAIDYDYCKGCGICANECPTKAITMV 101
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
61-270 |
7.47e-08 |
|
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: 54.67 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 61 PFDAVKVVNLPDELESRMIHSYDKNG--FKLFNLVIPQKKQImGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKI 138
Cdd:TIGR02868 323 PAAGAVGLGKPTLELRDLSAGYPGAPpvLDGVSLDLPPGERV-AILGPSGSGKSTLLATLAGLLDPL--------QGEVT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 139 IDffkGTEAQNYFEKlyttglETSYKPQYVEQIPRIFKGSVKALL----NKISEGDVNKVCNELGI-------KHVLNRK 207
Cdd:TIGR02868 394 LD---GVPVSSLDQD------EVRRRVSVCAQDAHLFDTTVRENLrlarPDATDEELWAALERVGLadwlralPDGLDTV 464
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 208 VGD----ISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKeCAVVVEHDL 270
Cdd:TIGR02868 465 LGEggarLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGR-TVVLITHHL 530
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
353-491 |
8.12e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.94 E-value: 8.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 353 KLKVKPGILMR---NEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVK--------------------- 400
Cdd:PRK15079 33 TLKAVDGVTLRlyeGETLGVVGESGCGKSTFARAIIGLVKATDGEvawlgkdlLGMKDDewravrsdiqmifqdplasln 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 401 -------------ISYKPQYVQVENDDFVRSVLMKTP--PSMIERLdlSHllkrklsELSGGELQRVAIAECLSRDADVY 465
Cdd:PRK15079 113 prmtigeiiaeplRTYHPKLSRQEVKDRVKAMMLKVGllPNLINRY--PH-------EFSGGQCQRIGIARALILEPKLI 183
|
170 180
....*....|....*....|....*.
gi 1278501429 466 LLDEPSAHLDVEQRLNVAKILRDVIK 491
Cdd:PRK15079 184 ICDEPVSALDVSIQAQVVNLLQQLQR 209
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
18-67 |
8.12e-08 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 51.04 E-value: 8.12e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1278501429 18 DYVCMNFCPINRTGKDciveGADGKIVVEEELCIGCGICVNKCPFDAVKV 67
Cdd:cd10550 54 DAPCVEACPVGAISRD----EETGAVVVDEDKCIGCGMCVEACPFGAIRV 99
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
102-268 |
8.56e-08 |
|
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: 51.83 E-value: 8.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 102 GLVGVNGIGKSTCLNILSGQLKPnlgndfgeVEGQKIIDffkGTEAQNYFEKLYttGLETSYKPQYVEqiprIFKGSvka 181
Cdd:cd03246 32 AIIGPSGSGKSTLARLILGLLRP--------TSGRVRLD---GADISQWDPNEL--GDHVGYLPQDDE----LFSGS--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 182 llnkISEgdvnkvcNELgikhvlnrkvgdiSGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKE 261
Cdd:cd03246 92 ----IAE-------NIL-------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGA 147
|
....*..
gi 1278501429 262 CAVVVEH 268
Cdd:cd03246 148 TRIVIAH 154
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
99-278 |
8.60e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 53.39 E-value: 8.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPNLGN-DFGEVEGQkIIDFFKGTEAQNYFekLYTT--GletsykpqYVEQIPRif 175
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSARLAPDAGEvHYRMRDGQ-LRDLYALSEAERRR--LLRTewG--------FVHQHPR-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 176 kgsvKALLNKISEG-DVNKVCNELGIKHVlnrkvGDI-------------------------SGGELQRVAIAGALLKKS 229
Cdd:PRK11701 100 ----DGLRMQVSAGgNIGERLMAVGARHY-----GDIratagdwlerveidaariddlpttfSGGMQQRLQIARNLVTHP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1278501429 230 DFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDLIMLDYLAD 278
Cdd:PRK11701 171 RLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVViVTHDLAVARLLAH 220
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
366-490 |
8.74e-08 |
|
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: 54.95 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 366 IIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVKISYKPQYVQVENDDFVRSVLMKTP------PSMIERL----DLSH 435
Cdd:TIGR00957 666 LVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKAlnekyyQQVLEACallpDLEI 745
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 436 L-------LKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVeqrlNVAK-ILRDVI 490
Cdd:TIGR00957 746 LpsgdrteIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA----HVGKhIFEHVI 804
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
99-237 |
8.98e-08 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 53.11 E-value: 8.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPNLGndfgevegqKIidFFKGTE---------AQNyfeklyttGLetSYKPQyvE 169
Cdd:COG1137 30 EIVGLLGPNGAGKTTTFYMIVGLVKPDSG---------RI--FLDGEDithlpmhkrARL--------GI--GYLPQ--E 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278501429 170 qiPRIFKG-SV----KALL--NKISEGDVNKVCNEL----GIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEP 237
Cdd:COG1137 87 --ASIFRKlTVedniLAVLelRKLSKKEREERLEELleefGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEP 163
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
272-480 |
9.06e-08 |
|
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: 54.75 E-value: 9.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 272 MLDYLADVEHIMYGRAGVYGIVSKSLSIRECINTYLEGYI-REDNMrfrseeIKFEvkaptkalnNIPIIEWSNiEKKLG 350
Cdd:TIGR00954 406 LLQVLDDVKSGNFKRPRVEEIESGREGGRNSNLVPGRGIVeYQDNG------IKFE---------NIPLVTPNG-DVLIE 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 351 DFKLKVKPGilmRNEIIgvLGENGTGKTTFAKILAGM--------IKPDKGKtdtsvkISYKPQ--------------YV 408
Cdd:TIGR00954 470 SLSFEVPSG---NNLLI--CGPNGCGKSSLFRILGELwpvyggrlTKPAKGK------LFYVPQrpymtlgtlrdqiiYP 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 409 QVENDDFVRSVLMKTPPSMIERLDLSHLLKRKLS---------ELSGGELQRVAIAECLSRDADVYLLDE-PSA-HLDVE 477
Cdd:TIGR00954 539 DSSEDMKRRGLSDKDLEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDEcTSAvSVDVE 618
|
...
gi 1278501429 478 QRL 480
Cdd:TIGR00954 619 GYM 621
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
349-488 |
9.70e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.15 E-value: 9.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKG----------KTDTSVKISYKPQYVQVENDDF--- 415
Cdd:PRK10419 28 LNNVSLSLKSG-----ETVALLGRSGCGKSTLARLLVGLESPSQGnvswrgeplaKLNRAQRKAFRRDIQMVFQDSIsav 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 416 -----VRSVL---MKTPPSMIER--------------LDLSHLLKRKlSELSGGELQRVAIAECLSRDADVYLLDEPSAH 473
Cdd:PRK10419 103 nprktVREIIrepLRHLLSLDKAerlarasemlravdLDDSVLDKRP-PQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170
....*....|....*
gi 1278501429 474 LDVEQRLNVAKILRD 488
Cdd:PRK10419 182 LDLVLQAGVIRLLKK 196
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
97-270 |
1.05e-07 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 52.55 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 97 KKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDfgEVEGQKIidfFKGTEAQNYFEKLYttglETSYK-PQYVEQIPRIF 175
Cdd:TIGR03771 5 KGELLGLLGPNGAGKTTLLRAILGLIPPAKGTV--KVAGASP---GKGWRHIGYVPQRH----EFAWDfPISVAHTVMSG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 176 KGSVKALLNKISEGDVNKVCNEL---GIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANL 252
Cdd:TIGR03771 76 RTGHIGWLRRPCVADFAAVRDALrrvGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTEL 155
|
170
....*....|....*...
gi 1278501429 253 LRKHGSEKECAVVVEHDL 270
Cdd:TIGR03771 156 FIELAGAGTAILMTTHDL 173
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
99-486 |
1.07e-07 |
|
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: 54.45 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGqLKPNlGNDFGEV--EGQKII-DFFKGTE-------------------AQNYF--EKL 154
Cdd:TIGR02633 28 ECVGLCGENGAGKSTLMKILSG-VYPH-GTWDGEIywSGSPLKaSNIRDTEragiviihqeltlvpelsvAENIFlgNEI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 155 YTTGLETSYKPQYVEqiprifkgsVKALLNKISEGDVNkvcnelgikhvLNRKVGDISGGELQRVAIAGALLKKSDFLFI 234
Cdd:TIGR02633 106 TLPGGRMAYNAMYLR---------AKNLLRELQLDADN-----------VTRPVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 235 DEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIMLDYLADVEHIMYGRAGVYGIVSKSLSIRECInTYLEGyiRED 314
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDII-TMMVG--REI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 315 NMRFRSE--EIKFEVkaptkaLNNIPIIEWSNIE---KKLGDFKLKVKpgilmRNEIIGVLGENGTGKTTFAKILAGMIk 389
Cdd:TIGR02633 243 TSLYPHEphEIGDVI------LEARNLTCWDVINphrKRVDDVSFSLR-----RGEILGVAGLVGAGRTELVQALFGAY- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 390 pdKGKTDTSVKISYKPqyVQVEN-DDFVRSVLMKTP---------PSM----------------IERLDLSHLLKRKLSE 443
Cdd:TIGR02633 311 --PGKFEGNVFINGKP--VDIRNpAQAIRAGIAMVPedrkrhgivPILgvgknitlsvlksfcfKMRIDAAAELQIIGSA 386
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 444 -----------------LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKIL 486
Cdd:TIGR02633 387 iqrlkvktaspflpigrLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLI 446
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
340-491 |
1.07e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 53.96 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLG------DFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVK----- 400
Cdd:PRK11432 7 VVLKNITKRFGsntvidNLNLTIKQG-----TMVTLLGPSGCGKTTVLRLVAGLEKPTEGQifidgedvTHRSIQqrdic 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 401 ---ISYK--PQYVQVENDDFVRSVLMKTPPSMIERL-------DLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLD 468
Cdd:PRK11432 82 mvfQSYAlfPHMSLGENVGYGLKMLGVPKEERKQRVkealelvDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180
....*....|....*....|...
gi 1278501429 469 EPSAHLDVeqrlNVAKILRDVIK 491
Cdd:PRK11432 162 EPLSNLDA----NLRRSMREKIR 180
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
319-499 |
1.10e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.07 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 319 RSEEIKFEVKAPTKALNNIpiiewsNIEKKLGDFklkvkpgilmrneiIGVLGENGTGKTTFAKILAGMIKPDKGKT--- 395
Cdd:PRK13644 3 RLENVSYSYPDGTPALENI------NLVIKKGEY--------------IGIIGKNGSGKSTLALHLNGLLRPQKGKVlvs 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 396 --DTS-----------VKISYK---PQYV--QVENDDFVRSVLMKTPPSMIERLDLSHLLKRKLSE--------LSGGEL 449
Cdd:PRK13644 63 giDTGdfsklqgirklVGIVFQnpeTQFVgrTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKyrhrspktLSGGQG 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1278501429 450 QRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEASAFV 499
Cdd:PRK13644 143 QCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYI 192
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
191-318 |
1.19e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 53.88 E-value: 1.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 191 VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLD----IKQRLKVANLLRKHGSekeCAVVV 266
Cdd:PRK11000 114 VNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDaalrVQMRIEISRLHKRLGR---TMIYV 190
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 267 EHDLIMLDYLADveHIMYGRAGVYGIVSKSLSIREC-INTYLEGYIREDNMRF 318
Cdd:PRK11000 191 THDQVEAMTLAD--KIVVLDAGRVAQVGKPLELYHYpANRFVAGFIGSPKMNF 241
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
361-488 |
1.20e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 53.29 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 361 LMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGKTD---------TSVKiSYKPQYVQV-------ENDDFVRSVL---M 421
Cdd:PRK13641 30 LEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITiagyhitpeTGNK-NLKKLRKKVslvfqfpEAQLFENTVLkdvE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 422 KTPPSM--------------IERLDLSH-LLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKIL 486
Cdd:PRK13641 109 FGPKNFgfsedeakekalkwLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLF 188
|
..
gi 1278501429 487 RD 488
Cdd:PRK13641 189 KD 190
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
99-269 |
1.22e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 53.55 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNIL-------SGQLKPNlGNDFGEVEGQkiiDFFKGTEAQNY--------FEKLyTTGLETsy 163
Cdd:PRK10851 29 QMVALLGPSGSGKTTLLRIIaglehqtSGHIRFH-GTDVSRLHAR---DRKVGFVFQHYalfrhmtvFDNI-AFGLTV-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 164 kpqyveqIPRIFKGSVKALLNKisegdVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDI 243
Cdd:PRK10851 102 -------LPRRERPNAAAIKAK-----VTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
170 180
....*....|....*....|....*..
gi 1278501429 244 KQRLKVANLLRK-HGSEKECAVVVEHD 269
Cdd:PRK10851 170 QVRKELRRWLRQlHEELKFTSVFVTHD 196
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
212-488 |
1.31e-07 |
|
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: 53.92 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 212 SGGELQRVAIAGALLKKSDFLFIDEPSSYLDI---KQRLK-VANLLRKHGSekecAVV-VEHDLIMLDYLADVEHIMYgr 286
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVtvqAQILDlLKDLQRELGM----ALLlITHDLGVVRRFADRVAVMR-- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 287 agvygivskslsirecintylEGYIREDNmrfRSEEIkFEvkAP----TKAL--------------NNIPIIEWSNIE-- 346
Cdd:COG4172 232 ---------------------QGEIVEQG---PTAEL-FA--APqhpyTRKLlaaeprgdprpvppDAPPLLEARDLKvw 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 347 ---------KKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIkpdkgktDTSVKISY-------- 403
Cdd:COG4172 285 fpikrglfrRTVGHVKavdgvsLTLRRG-----ETLGLVGESGSGKSTLGLALLRLI-------PSEGEIRFdgqdldgl 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 404 -----KP--QYVQV---------------------------------ENDDFVRSVLMKT--PPSMIERLdlSHllkrkl 441
Cdd:COG4172 353 srralRPlrRRMQVvfqdpfgslsprmtvgqiiaeglrvhgpglsaaERRARVAEALEEVglDPAARHRY--PH------ 424
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1278501429 442 sELSGGELQRVAIAECLSRDADVYLLDEP-SAhLDVEQRLNVAKILRD 488
Cdd:COG4172 425 -EFSGGQRQRIAIARALILEPKLLVLDEPtSA-LDVSVQAQILDLLRD 470
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
94-270 |
1.35e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 52.83 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 94 IPqKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFGE---VEGQKIIDFFK--GTEAQNYFEKLYTT--------GLE 160
Cdd:PRK13648 32 IP-KGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNnqaITDDNFEKLRKhiGIVFQNPDNQFVGSivkydvafGLE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 161 TSYKPQyvEQIPRIfkgsvkallnkisegdVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSY 240
Cdd:PRK13648 111 NHAVPY--DEMHRR----------------VSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190
....*....|....*....|....*....|.
gi 1278501429 241 LDIKQRLKVANLLRKHGSEKECAVV-VEHDL 270
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIIsITHDL 203
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
2-69 |
1.36e-07 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 53.88 E-value: 1.36e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 2 RIVVVNKKKCtagKGCdYVCMNFCPINRTGKDcivegaDGKIVVEEELCIGCGICVNKCPFDAVKVVN 69
Cdd:COG4624 84 PSIIRDKEKC---KNC-YPCVRACPVKAIKVD------DGKAEIDEEKCISCGQCVAVCPFGAITEKS 141
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
87-242 |
1.49e-07 |
|
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: 52.54 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 87 FKLFNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDffkGTEAQNYFEKLYTTgletsyKPQ 166
Cdd:cd03249 19 LKGLSLTIP-PGKTVALVGSSGCGKSTVVSLLERFYDPT--------SGEILLD---GVDIRDLNLRWLRS------QIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 167 YVEQIPRIFKGSVK---AL-LNKISEGDVNKVCNELGIK-------HVLNRKVGD----ISGGELQRVAIAGALLKKSDF 231
Cdd:cd03249 81 LVSQEPVLFDGTIAeniRYgKPDATDEEVEEAAKKANIHdfimslpDGYDTLVGErgsqLSGGQKQRIAIARALLRNPKI 160
|
170
....*....|.
gi 1278501429 232 LFIDEPSSYLD 242
Cdd:cd03249 161 LLLDEATSALD 171
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
85-269 |
1.56e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.02 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 85 NGFKLfNLViPQKKqiMGLVGVNGIGKSTCLNILSGQLKPNLGnDFGEVEGQKIidffkGTEAQNYFEKLYT--TGLE-- 160
Cdd:PRK10636 329 DSIKL-NLV-PGSR--IGLLGRNGAGKSTLIKLLAGELAPVSG-EIGLAKGIKL-----GYFAQHQLEFLRAdeSPLQhl 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 161 TSYKPQYVEQIPRIFKGSVKALLNKISEgdvnkvcnelgikhvlnrKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSY 240
Cdd:PRK10636 399 ARLAPQELEQKLRDYLGGFGFQGDKVTE------------------ETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170 180 190
....*....|....*....|....*....|
gi 1278501429 241 LDIKQRLKVANLLrkhgSEKECA-VVVEHD 269
Cdd:PRK10636 461 LDLDMRQALTEAL----IDFEGAlVVVSHD 486
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
349-493 |
1.57e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 54.36 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGILmrneiIGVLGENGTGKTTFAKILAGMIKPdkgKTDTSV----KISYKPQYVQVENDDFVRSVLMKTP 424
Cdd:PLN03130 633 LSNINLDVPVGSL-----VAIVGSTGEGKTSLISAMLGELPP---RSDASVvirgTVAYVPQVSWIFNATVRDNILFGSP 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 425 --PSMIERL--------DLSHLLKRKLSE-------LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNV-AKIL 486
Cdd:PLN03130 705 fdPERYERAidvtalqhDLDLLPGGDLTEigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCI 784
|
....*..
gi 1278501429 487 RDVIKKK 493
Cdd:PLN03130 785 KDELRGK 791
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
10-65 |
1.66e-07 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 47.93 E-value: 1.66e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 10 KCTagkGCDYvCMNFCPINRTGKDCIVEGADGKIvvEEELCIGCGICVNKCPFDAV 65
Cdd:pfam13187 1 KCT---GCGA-CVAACPAGAIVPDLVGQTIRGDI--AGLACIGCGACVDACPRGAI 50
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
339-499 |
1.90e-07 |
|
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: 53.29 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 339 IIEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGmIKPdKGKTDTSVKISYKPQYVQVEN 412
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKaldgidLEVRPG-----ECVGLCGENGAGKSTLMKILSG-VYP-HGTWDGEIYWSGSPLKASNIR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 413 DD------FVRSVLMKTPP-SMIERLDLSH--------------------LLK----------RKLSELSGGELQRVAIA 455
Cdd:TIGR02633 74 DTeragivIIHQELTLVPElSVAENIFLGNeitlpggrmaynamylraknLLRelqldadnvtRPVGDYGGGQQQLVEIA 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1278501429 456 ECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEASAFV 499
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYI 197
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
354-469 |
1.99e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 52.01 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 354 LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVKIS--------YKPQYVQVENDDFVRSVLMKTPP 425
Cdd:COG1134 47 FEVERG-----ESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSallelgagFHPELTGRENIYLNGRLLGLSRK 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 426 SMIERLD-------LSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDE 469
Cdd:COG1134 122 EIDEKFDeivefaeLGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDE 172
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
363-491 |
2.21e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 52.54 E-value: 2.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKGKT-------DTSVK----------------------------ISYKPQY 407
Cdd:PRK13636 31 KGEVTAILGGNGAGKSTLFQNLNGILKPSSGRIlfdgkpiDYSRKglmklresvgmvfqdpdnqlfsasvyqdVSFGAVN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 408 VQVENDDFVRSVlmktpPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILR 487
Cdd:PRK13636 111 LKLPEDEVRKRV-----DNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLV 185
|
....
gi 1278501429 488 DVIK 491
Cdd:PRK13636 186 EMQK 189
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
212-256 |
2.31e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 53.27 E-value: 2.31e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1278501429 212 SGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKH 256
Cdd:COG4178 487 SLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE 531
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
97-305 |
2.66e-07 |
|
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: 53.48 E-value: 2.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 97 KKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKI---IDFFKGTEAQNYFEKLYTTGLETSykpqyvEQIpr 173
Cdd:TIGR01257 955 ENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVL--VGGKDIetnLDAVRQSLGMCPQHNILFHHLTVA------EHI-- 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 174 IFKGSVKALLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLL 253
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 254 RKHGSEKECaVVVEHDLIMLDYLAD-VEHIMYGRAGVYGivsKSLSIRECINT 305
Cdd:TIGR01257 1105 LKYRSGRTI-IMSTHHMDEADLLGDrIAIISQGRLYCSG---TPLFLKNCFGT 1153
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
87-243 |
2.85e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 53.33 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 87 FKLFNLVIPQKKQImGLVGVNGIGKSTCLNILSGQLKPNLGNDFGEVEGQKIIdffkgteaqnyFEKLYTTGLETSYKPq 166
Cdd:PLN03073 525 FKNLNFGIDLDSRI-AMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAV-----------FSQHHVDGLDLSSNP- 591
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 167 yVEQIPRIFKGsvkallnkISEGDVNKVCNELGIKHVLN-RKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDI 243
Cdd:PLN03073 592 -LLYMMRCFPG--------VPEQKLRAHLGSFGVTGNLAlQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
349-469 |
3.13e-07 |
|
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: 52.88 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK--------TDTSVkisykPQYVQ----------- 409
Cdd:COG4615 348 LGPIDLTIRRG-----ELVFIVGGNGSGKSTLAKLLTGLYRPESGEilldgqpvTADNR-----EAYRQlfsavfsdfhl 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 410 ---------VENDDFVRsvlmktppSMIERLDLSHLLK---RKLS--ELSGGelQR------VAIAEclsrDADVYLLDE 469
Cdd:COG4615 418 fdrllgldgEADPARAR--------ELLERLELDHKVSvedGRFSttDLSQG--QRkrlallVALLE----DRPILVFDE 483
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
363-488 |
3.37e-07 |
|
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: 50.40 E-value: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAkiLAGMIKPDKGKTDTSVKISYKPQYVqvenddFVRSVlmktppSMIERLDLSHL-LKRKL 441
Cdd:cd03238 20 LNVLVVVTGVSGSGKSTLV--NEGLYASGKARLISFLPKFSRNKLI------FIDQL------QFLIDVGLGYLtLGQKL 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 442 SELSGGELQRVAIAECL--SRDADVYLLDEPSAHL---DVEQRLNVAKILRD 488
Cdd:cd03238 86 STLSGGELQRVKLASELfsEPPGTLFILDEPSTGLhqqDINQLLEVIKGLID 137
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
103-255 |
3.41e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 50.70 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQlkpnlgNDFGEVEGQKIIDFFKGTEaqnYFEKlyTTGletsykpqYVEQIPrIFKGSVK-- 180
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGR------KTAGVITGEILINGRPLDK---NFQR--STG--------YVEQQD-VHSPNLTvr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 181 ------ALLNKISegdvnkvcnelgikhVLNRKvgdisggelqRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLR 254
Cdd:cd03232 98 ealrfsALLRGLS---------------VEQRK----------RLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
.
gi 1278501429 255 K 255
Cdd:cd03232 153 K 153
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
316-492 |
3.41e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 52.01 E-value: 3.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 316 MRFRSEEIK--FEVKAPT--KALNNIpiiewsNIEKKLGDFklkvkpgilmrneiIGVLGENGTGKTTFAKILAGMIKPD 391
Cdd:PRK13651 1 MQIKVKNIVkiFNKKLPTelKALDNV------SVEINQGEF--------------IAIIGQTGSGKTTFIEHLNALLLPD 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 392 KGKTD---TSVKISYKPQYVQVENDDFV----------------RSV-------------------LMKTPPSM------ 427
Cdd:PRK13651 61 TGTIEwifKDEKNKKKTKEKEKVLEKLViqktrfkkikkikeirRRVgvvfqfaeyqlfeqtiekdIIFGPVSMgvskee 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278501429 428 --------IERLDLS-HLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKK 492
Cdd:PRK13651 141 akkraakyIELVGLDeSYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ 214
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
354-477 |
3.44e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 50.96 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 354 LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtsvKISYKPQYVQVENDDFVRSVL-------MKTPPS 426
Cdd:PRK13538 22 FTLNAG-----ELVQIEGPNGAGKTSLLRILAGLARPDAG------EVLWQGEPIRRQRDEYHQDLLylghqpgIKTELT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 427 MIERLDLSHLLKRKLSE----------------------LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:PRK13538 91 ALENLRFYQRLHGPGDDealwealaqvglagfedvpvrqLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
422-475 |
3.45e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 52.15 E-value: 3.45e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 422 KTPPSMIER--------LDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:PRK11650 105 GMPKAEIEErvaeaariLELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
198-269 |
3.45e-07 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 52.02 E-value: 3.45e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 198 LGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKEC-AVVVEHD 269
Cdd:COG3842 123 VGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGItFIYVTHD 195
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
212-270 |
4.24e-07 |
|
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: 50.90 E-value: 4.24e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 212 SGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLL----RKHGSekeCAVVVEHDL 270
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfelnRERGT---TLVLVTHDP 207
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
362-475 |
4.28e-07 |
|
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: 51.49 E-value: 4.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 362 MRNEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TDTSvKISYK--------------------PQYVQVENDDF- 415
Cdd:cd03294 48 REGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKvlidgQDIA-AMSRKelrelrrkkismvfqsfallPHRTVLENVAFg 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 416 --VRSVLMKTPPSM----IERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:cd03294 127 leVQGVPRAEREERaaeaLELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
100-283 |
4.33e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 100 IMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVE-GQkiidffkgteaqnyfeklyttgletSYKPQYVEQiprifkgS 178
Cdd:PRK11819 352 IVGIIGPNGAGKSTLFKMITGQEQP----DSGTIKiGE-------------------------TVKLAYVDQ-------S 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 179 VKALLNK------ISEG-DVNKVcnelGIKHVLNR---------------KVGDISGGELQRVAIAGALLKKSDFLFIDE 236
Cdd:PRK11819 396 RDALDPNktvweeISGGlDIIKV----GNREIPSRayvgrfnfkggdqqkKVGVLSGGERNRLHLAKTLKQGGNVLLLDE 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1278501429 237 PSSYLDIK--QRLKVAnLLRKHGsekeCAVVVEHDLIMLDYLAdvEHIM 283
Cdd:PRK11819 472 PTNDLDVEtlRALEEA-LLEFPG----CAVVISHDRWFLDRIA--THIL 513
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
91-269 |
4.34e-07 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 51.19 E-value: 4.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPQKKQImGLVGVNGIGKSTCLNILSGQLKPNLGNDF--GE-VEGQKIIDFFKGTEAQNY--------FEKLyTTGL 159
Cdd:cd03296 22 SLDIPSGELV-ALLGPSGSGKTTLLRLIAGLERPDSGTILfgGEdATDVPVQERNVGFVFQHYalfrhmtvFDNV-AFGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 160 ETsyKPQYVEQIPRIFKGSVKALLNKIS-EGDVNKVCNELgikhvlnrkvgdiSGGELQRVAIAGALLKKSDFLFIDEPS 238
Cdd:cd03296 100 RV--KPRSERPPEAEIRAKVHELLKLVQlDWLADRYPAQL-------------SGGQRQRVALARALAVEPKVLLLDEPF 164
|
170 180 190
....*....|....*....|....*....|..
gi 1278501429 239 SYLDIKQRLKVANLLRK-HGSEKECAVVVEHD 269
Cdd:cd03296 165 GALDAKVRKELRRWLRRlHDELHVTTVFVTHD 196
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
91-254 |
4.78e-07 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 51.64 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPQKKQIMgLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIIDffkgTEAQNyfeklyttgletsykpqyvEQ 170
Cdd:PRK11432 26 NLTIKQGTMVT-LLGPSGCGKTTVLRLVAGLEKPTEGQIF--IDGEDVTH----RSIQQ-------------------RD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 IPRIFKGSvkALLNKISEGD----------VNKVCNELGIKHVL---------NRKVGDISGGELQRVAIAGALLKKSDF 231
Cdd:PRK11432 80 ICMVFQSY--ALFPHMSLGEnvgyglkmlgVPKEERKQRVKEALelvdlagfeDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180
....*....|....*....|...
gi 1278501429 232 LFIDEPSSYLDikqrlkvANLLR 254
Cdd:PRK11432 158 LLFDEPLSNLD-------ANLRR 173
|
|
| NapF |
COG1145 |
Ferredoxin [Energy production and conversion]; |
3-73 |
4.94e-07 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440760 [Multi-domain] Cd Length: 238 Bit Score: 50.88 E-value: 4.94e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 3 IVVVNKKKCTagkGCDyVCMNFCPINrtgkdcIVEGADGK--IVVEEELCIGCGICVNKCPFDAVKVVNLPDE 73
Cdd:COG1145 176 KAVIDAEKCI---GCG-LCVKVCPTG------AIRLKDGKpqIVVDPDKCIGCGACVKVCPVGAISLEPKEIE 238
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
90-283 |
5.09e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 52.13 E-value: 5.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 90 FNLVIPQKKQImGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDffkGTEAQNYFEKLYTTGLETsykpqyVE 169
Cdd:PRK11160 359 LSLQIKAGEKV-ALLGRTGCGKSTLLQLLTRAWDPQ--------QGEILLN---GQPIADYSEAALRQAISV------VS 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 170 QIPRIFKGSVKA--LLNKISEGD------VNKVcnELGiKHV-----LNRKVGD----ISGGELQRVAIAGALLKKSDFL 232
Cdd:PRK11160 421 QRVHLFSATLRDnlLLAAPNASDealievLQQV--GLE-KLLeddkgLNAWLGEggrqLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 233 FIDEPSSYLDIKQRLKVANLLRKHGSEKEcAVVVEHDLIMLDYLaDVEHIM 283
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELLAEHAQNKT-VLMITHRLTGLEQF-DRICVM 546
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
349-493 |
5.55e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 52.13 E-value: 5.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK---TDTSVK----------ISYKPQYVQVENDDF 415
Cdd:PRK11160 356 LKGLSLQIKAG-----EKVALLGRTGCGKSTLLQLLTRAWDPQQGEillNGQPIAdyseaalrqaISVVSQRVHLFSATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 416 VRSVLMKTPPS-------MIERLDLSHLLKRK------LSE----LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQ 478
Cdd:PRK11160 431 RDNLLLAAPNAsdealieVLQQVGLEKLLEDDkglnawLGEggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET 510
|
170
....*....|....*
gi 1278501429 479 RLNVAKILRDVIKKK 493
Cdd:PRK11160 511 ERQILELLAEHAQNK 525
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
211-270 |
5.66e-07 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 50.90 E-value: 5.66e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 211 ISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDL 270
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEM 204
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
207-270 |
6.05e-07 |
|
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: 50.69 E-value: 6.05e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 207 KVGD----ISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKEcAVVVEHDL 270
Cdd:cd03253 130 IVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRT-TIVIAHRL 196
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
74-285 |
6.45e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 50.85 E-value: 6.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 74 LESRMIH-SYDKNGFKLFNLVIPQKK-QIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVegqkiidFFKGtEAQNYF 151
Cdd:PRK13639 2 LETRDLKySYPDGTEALKGINFKAEKgEMVALLGPNGAGKSTLFLHFNGILKP----TSGEV-------LIKG-EPIKYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 152 EKlytTGLETSYKPQYVEQIP--RIFKGSVK-----ALLN-KISEGDVNKVCNE----LGIKHVLNRKVGDISGGELQRV 219
Cdd:PRK13639 70 KK---SLLEVRKTVGIVFQNPddQLFAPTVEedvafGPLNlGLSKEEVEKRVKEalkaVGMEGFENKPPHHLSGGQKKRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 220 AIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIMLDYLADVEHIMYG 285
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSD 212
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
103-270 |
6.55e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.78 E-value: 6.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQLKPNLGNDfgEVEGQKIID-------------F------FKGTEAQN--YFeklyttGLET 161
Cdd:PRK13635 38 IVGHNGSGKSTLAKLLNGLLLPEAGTI--TVGGMVLSEetvwdvrrqvgmvFqnpdnqFVGATVQDdvAF------GLEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 162 SYKPQyVEQIPRifkgsvkallnkisegdVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYL 241
Cdd:PRK13635 110 IGVPR-EEMVER-----------------VDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSML 171
|
170 180 190
....*....|....*....|....*....|
gi 1278501429 242 DIKQRLKVANLLRKHGSEKECAVV-VEHDL 270
Cdd:PRK13635 172 DPRGRREVLETVRQLKEQKGITVLsITHDL 201
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
102-268 |
6.61e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 50.82 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 102 GLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIIDffKGTEAQNYFEKLyttGLETSYkPQYVEQIPRIFKGSVKA 181
Cdd:PRK13637 37 GLIGHTGSGKSTLIQHLNGLLKPTSGKII--IDGVDITD--KKVKLSDIRKKV---GLVFQY-PEYQLFEETIEKDIAFG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 182 LLN-KISEGDVN----KVCNELGIKH--VLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLR 254
Cdd:PRK13637 109 PINlGLSEEEIEnrvkRAMNIVGLDYedYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIK 188
|
170
....*....|....*
gi 1278501429 255 K-HGSEKECAVVVEH 268
Cdd:PRK13637 189 ElHKEYNMTIILVSH 203
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
103-242 |
6.63e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 52.03 E-value: 6.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDffkGTEAQNYFEKLYTTgletsyKPQYVEQIPRIFKGSVKal 182
Cdd:TIGR00958 512 LVGPSGSGKSTVAALLQNLYQPT--------GGQVLLD---GVPLVQYDHHYLHR------QVALVGQEPVLFSGSVR-- 572
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 183 lNKISEG----------DVNKVCN--------ELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLD 242
Cdd:TIGR00958 573 -ENIAYGltdtpdeeimAAAKAANahdfimefPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
349-494 |
7.19e-07 |
|
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: 52.05 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKpgilmRNEIIGVLGENGTGKTTFAKILAGMIKPDKG-------------KTDTSVKISYKPQ--YV----- 408
Cdd:TIGR01193 490 LSDISLTIK-----MNSKTTIVGMSGSGKSTLAKLLVGFFQARSGeillngfslkdidRHTLRQFINYLPQepYIfsgsi 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 409 ----------QVENDDFVRSVLMKTPPSMIERLDLShlLKRKLSE----LSGGELQRVAIAECLSRDADVYLLDEPSAHL 474
Cdd:TIGR01193 565 lenlllgakeNVSQDEIWAACEIAEIKDDIENMPLG--YQTELSEegssISGGQKQRIALARALLTDSKVLILDESTSNL 642
|
170 180
....*....|....*....|
gi 1278501429 475 DVeqrLNVAKILRDVIKKKE 494
Cdd:TIGR01193 643 DT---ITEKKIVNNLLNLQD 659
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
105-269 |
7.19e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 50.10 E-value: 7.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 105 GVNGIGKSTCLNILSGQLKPnlgnDFGEVegqkiidFFKGTEaqnyfeklYTTGLETSYKPQ--YVEQIPRIFKGSVKAl 182
Cdd:PRK10247 40 GPSGCGKSTLLKIVASLISP----TSGTL-------LFEGED--------ISTLKPEIYRQQvsYCAQTPTLFGDTVYD- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 183 lNKI-------SEGDVNKVCNEL---GI-KHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVAN 251
Cdd:PRK10247 100 -NLIfpwqirnQQPDPAIFLDDLerfALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNE 178
|
170
....*....|....*....
gi 1278501429 252 LLRKHGSEKECAVV-VEHD 269
Cdd:PRK10247 179 IIHRYVREQNIAVLwVTHD 197
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
347-490 |
7.36e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 7.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 347 KKLGDFKLKVKPGILMRN--------EIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVKISYKPQYVQVENDDfVRS 418
Cdd:PTZ00243 661 KMKTDDFFELEPKVLLRDvsvsvprgKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQAWIMNAT-VRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 419 VLMKTPPSMIERL-----------DLSHL---LKRKLSE----LSGGELQRVAIAECLSRDADVYLLDEPSAHLD--VEQ 478
Cdd:PTZ00243 740 NILFFDEEDAARLadavrvsqleaDLAQLgggLETEIGEkgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDahVGE 819
|
170
....*....|..
gi 1278501429 479 RlnvakILRDVI 490
Cdd:PTZ00243 820 R-----VVEECF 826
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
99-269 |
7.78e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 51.65 E-value: 7.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPNLGNdfGEVEGQKIIDFFKGTEAQ---NYFEKLYTTGLETSY--KPQYVEqIPR 173
Cdd:PRK10535 35 EMVAIVGASGSGKSTLMNILGCLDKPTSGT--YRVAGQDVATLDADALAQlrrEHFGFIFQRYHLLSHltAAQNVE-VPA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 174 IFKGSVKallnKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLL 253
Cdd:PRK10535 112 VYAGLER----KQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAIL 187
|
170
....*....|....*.
gi 1278501429 254 RKHGSEKECAVVVEHD 269
Cdd:PRK10535 188 HQLRDRGHTVIIVTHD 203
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
349-488 |
8.08e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 51.73 E-value: 8.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPG--ILMRneiigvlGENGTGKTTFAKILAG--------MIKPDKGKT----------DTSVK--ISYkPQ 406
Cdd:COG4178 379 LEDLSLSLKPGerLLIT-------GPSGSGKSTLLRAIAGlwpygsgrIARPAGARVlflpqrpylpLGTLReaLLY-PA 450
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 407 YVQVENDDFVRSVLmktppsmiERLDLSHLLKRkLSE-------LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQR 479
Cdd:COG4178 451 TAEAFSDAELREAL--------EAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENE 521
|
....*....
gi 1278501429 480 LNVAKILRD 488
Cdd:COG4178 522 AALYQLLRE 530
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
96-286 |
8.22e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 50.60 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKP--------------NLGNDFGEVEGQKIIDFFKGTEAQnYFEKlytTGLET 161
Cdd:PRK13641 31 EEGSFVALVGHTGSGKSTLMQHFNALLKPssgtitiagyhitpETGNKNLKKLRKKVSLVFQFPEAQ-LFEN---TVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 162 sykpqyVEQIPRIFKGSVKALLNKisegdVNKVCNELGIKH-VLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSY 240
Cdd:PRK13641 107 ------VEFGPKNFGFSEDEAKEK-----ALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1278501429 241 LDIKQRLKVANLLRKHGSEKECAVVVEHDL-IMLDYLADVEHIMYGR 286
Cdd:PRK13641 176 LDPEGRKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGK 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
190-255 |
8.42e-07 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 50.05 E-value: 8.42e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 190 DVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRK 255
Cdd:COG2884 117 RVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEE 182
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
210-278 |
8.58e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.47 E-value: 8.58e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 210 DISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAV-VVEHDLIMLDYLAD 278
Cdd:PRK10418 140 EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMlLVTHDMGVVARLAD 209
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
98-256 |
9.68e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 49.49 E-value: 9.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 98 KQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEGQKiidffKGTEAQNYFEKLYTTGLETSYKPQY-VEQIPRI-- 174
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPP----AAGTIKLDG-----GDIDDPDVAEACHYLGHRNAMKPALtVAENLEFwa 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 175 -FKGSvkallnkiSEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIK-QRLkVANL 252
Cdd:PRK13539 99 aFLGG--------EELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAaVAL-FAEL 169
|
....
gi 1278501429 253 LRKH 256
Cdd:PRK13539 170 IRAH 173
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
198-288 |
9.92e-07 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 50.01 E-value: 9.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 198 LGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEhdLIMLDY-L 276
Cdd:PRK09984 140 VGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVT--LHQVDYaL 217
|
90
....*....|..
gi 1278501429 277 ADVEHIMYGRAG 288
Cdd:PRK09984 218 RYCERIVALRQG 229
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
212-286 |
1.00e-06 |
|
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: 50.44 E-value: 1.00e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 212 SGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDLIMLDYLADVEHIMY-GR 286
Cdd:COG0444 152 SGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILfITHDLGVVAEIADRVAVMYaGR 228
|
|
| COG1149 |
COG1149 |
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ... |
42-69 |
1.04e-06 |
|
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];
Pssm-ID: 440763 [Multi-domain] Cd Length: 68 Bit Score: 46.26 E-value: 1.04e-06
10 20
....*....|....*....|....*...
gi 1278501429 42 KIVVEEELCIGCGICVNKCPFDAVKVVN 69
Cdd:COG1149 5 IPVIDEEKCIGCGLCVEVCPEGAIKLDD 32
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
354-492 |
1.04e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 50.08 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 354 LKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVK-ISY-KPQYVQV--------ENDD---FVRSVL 420
Cdd:PRK13639 23 FKAEKG-----EMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpIKYdKKSLLEVrktvgivfQNPDdqlFAPTVE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 421 ---------MKTPPSMIE--------RLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVA 483
Cdd:PRK13639 98 edvafgplnLGLSKEEVEkrvkealkAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIM 177
|
....*....
gi 1278501429 484 KILRDVIKK 492
Cdd:PRK13639 178 KLLYDLNKE 186
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
90-286 |
1.12e-06 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 49.06 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 90 FNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgndfgEVEGQKIIdfFKGTEaqnyfeklyTTGLETSYK----- 164
Cdd:cd03217 19 VNLTIK-KGEVHALMGPNGSGKSTLAKTIMGHPKY-------EVTEGEIL--FKGED---------ITDLPPEERarlgi 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 165 ---PQYVEQIPRIfkgSVKALLNKISEGdvnkvcnelgikhvlnrkvgdISGGELQRVAIAGALLKKSDFLFIDEPSSYL 241
Cdd:cd03217 80 flaFQYPPEIPGV---KNADFLRYVNEG---------------------FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1278501429 242 DIKQRLKVANLLRKHGSEKECAVVVEHDLIMLDYL-ADVEHIMY-GR 286
Cdd:cd03217 136 DIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYdGR 182
|
|
| HdrA |
COG1148 |
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion]; |
5-73 |
1.13e-06 |
|
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
Pssm-ID: 440762 [Multi-domain] Cd Length: 563 Bit Score: 51.01 E-value: 1.13e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278501429 5 VVNKKKCTagkGCDyVCMNFCPINrtgkdCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVVNLPDE 73
Cdd:COG1148 492 EVDPEKCT---GCG-RCVEVCPYG-----AISIDEKGVAEVNPALCKGCGTCAAACPSGAISLKGFTDD 551
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
99-270 |
1.28e-06 |
|
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: 51.55 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPNLGNdfGEVEGQKIIdffkgTEAQNYFEKLyttgletSYKPQYvEQIPRIFKGS 178
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTGDTTVTSGD--ATVAGKSIL-----TNISDVHQNM-------GYCPQF-DAIDDLLTGR 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 179 ----VKALLNKISEGDVNKVCN----ELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVA 250
Cdd:TIGR01257 2031 ehlyLYARLRGVPAEEIEKVANwsiqSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110
|
170 180
....*....|....*....|
gi 1278501429 251 NLLRKHGSEKECAVVVEHDL 270
Cdd:TIGR01257 2111 NTIVSIIREGRAVVLTSHSM 2130
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
344-477 |
1.32e-06 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 49.57 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 344 NIEKK--LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGmikpDKGKTDTSVKISYK----------------- 404
Cdd:TIGR01978 9 SVEDKeiLKGVNLTVKKG-----EIHAIMGPNGSGKSTLSKTIAG----HPSYEVTSGTILFKgqdllelepderaragl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 405 ---PQYVQ----VENDDFVRSVL-------MKTPPSM----------IERLDLS-HLLKRKLSE-LSGGELQRVAIAECL 458
Cdd:TIGR01978 80 flaFQYPEeipgVSNLEFLRSALnarrsarGEEPLDLldfekllkekLALLDMDeEFLNRSVNEgFSGGEKKRNEILQMA 159
|
170
....*....|....*....
gi 1278501429 459 SRDADVYLLDEPSAHLDVE 477
Cdd:TIGR01978 160 LLEPKLAILDEIDSGLDID 178
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
365-482 |
1.32e-06 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 49.79 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 365 EIIGVLGENGTGKTTFAKILAGMIKPDKGK---TDTSV----------KISYKPQYVQVENDDFVRS-VLMKTPP----- 425
Cdd:PRK10575 38 KVTGLIGHNGSGKSTLLKMLGRHQPPSEGEillDAQPLeswsskafarKVAYLPQQLPAAEGMTVRElVAIGRYPwhgal 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278501429 426 ------------SMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNV 482
Cdd:PRK10575 118 grfgaadrekveEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDV 186
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
204-270 |
1.33e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 50.08 E-value: 1.33e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 204 LNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDL 270
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDL 225
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
99-242 |
1.34e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 51.03 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKpnlGNDFgevEGQKIIDFFKGTEaqnyfEKLYTTGLETSYKPQY----------- 167
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQ---GNNF---TGTILANNRKPTK-----QILKRTGFVTQDDILYphltvretlvf 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 168 --VEQIPRIFKGSVKALLnkisegdVNKVCNELGIKHVLNRKVGD-----ISGGELQRVAIAGALLKKSDFLFIDEPSSY 240
Cdd:PLN03211 164 csLLRLPKSLTKQEKILV-------AESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
..
gi 1278501429 241 LD 242
Cdd:PLN03211 237 LD 238
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
100-270 |
1.34e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 49.58 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 100 IMGLVGVNGIGKST---CLNILSgqlKPNLGNDFgeVEGQKIiDFFKGTEAQ-NYFEK----LYTTGLETSYKP----QY 167
Cdd:PRK10619 33 VISIIGSSGSGKSTflrCINFLE---KPSEGSIV--VNGQTI-NLVRDKDGQlKVADKnqlrLLRTRLTMVFQHfnlwSH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 168 VEQIPRIFKGSVKAL-LNKISEGD-VNKVCNELGIKHVLNRKV-GDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIK 244
Cdd:PRK10619 107 MTVLENVMEAPIQVLgLSKQEARErAVKYLAKVGIDERAQGKYpVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE 186
|
170 180
....*....|....*....|....*.
gi 1278501429 245 QRLKVANLLRKHGSEKECAVVVEHDL 270
Cdd:PRK10619 187 LVGEVLRIMQQLAEEGKTMVVVTHEM 212
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
100-270 |
1.35e-06 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 49.95 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 100 IMGLvgvNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIIDFFK-----------GTEAQNYFEKLYTTGLETSYKPQYV 168
Cdd:cd03294 55 IMGL---SGSGKSTLLRCINRLIEPTSGKVL--IDGQDIAAMSRkelrelrrkkiSMVFQSFALLPHRTVLENVAFGLEV 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 169 EQIPRifkgsvkallnKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLK 248
Cdd:cd03294 130 QGVPR-----------AEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180
....*....|....*....|...
gi 1278501429 249 VAN-LLRKHGSEKECAVVVEHDL 270
Cdd:cd03294 199 MQDeLLRLQAELQKTIVFITHDL 221
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
203-489 |
1.37e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.01 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 203 VLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDLIMLDYLADVEH 281
Cdd:PRK10261 161 ILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIfITHDMGVVAEIADRVL 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 282 IMY-GRAGVYGIVSKSLSIRE--CINTYLEGYIREDNMRFRSEEIKF--------EVKAPTKALNNI----PIIEWSNIE 346
Cdd:PRK10261 241 VMYqGEAVETGSVEQIFHAPQhpYTRALLAAVPQLGAMKGLDYPRRFplislehpAKQEPPIEQDTVvdgePILQVRNLV 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 347 KklgdfKLKVKPGILMR-----------------NEIIGVLGENGTGKTTFAKIL-------AGMIKPDKGKTDT----- 397
Cdd:PRK10261 321 T-----RFPLRSGLLNRvtrevhavekvsfdlwpGETLSLVGESGSGKSTTGRALlrlvesqGGEIIFNGQRIDTlspgk 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 398 ------SVKISYKPQYVQVENDDFVRSVLMKtpPSMIERL--------DLSHLLK----------RKLSELSGGELQRVA 453
Cdd:PRK10261 396 lqalrrDIQFIFQDPYASLDPRQTVGDSIME--PLRVHGLlpgkaaaaRVAWLLErvgllpehawRYPHEFSGGQRQRIC 473
|
330 340 350
....*....|....*....|....*....|....*.
gi 1278501429 454 IAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDV 489
Cdd:PRK10261 474 IARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
3-61 |
1.47e-06 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 45.32 E-value: 1.47e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 3 IVVVNKKKCTagkGCdYVCMNFCPINRTGKDCIVEGADGKIVVEE-ELCIGCGICVNKCP 61
Cdd:pfam13237 1 KVVIDPDKCI---GC-GRCTAACPAGLTRVGAIVERLEGEAVRIGvWKCIGCGACVEACP 56
|
|
| DMSOR_beta_like |
cd16367 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
18-68 |
1.49e-06 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319889 [Multi-domain] Cd Length: 138 Bit Score: 47.69 E-value: 1.49e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 18 DYVCMNFCPINrtgkdcIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:cd16367 62 DPVCMIGCPTG------AIHRDDGGEVVISDACCGCGNCASACPYGAIQMV 106
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
369-493 |
1.60e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 49.60 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 369 VLGENGTGKTTFAKILAGMIKPDKGKT------------------------------DTSV-------KISYKPQYVQ-- 409
Cdd:PRK10253 38 IIGPNGCGKSTLLRTLSRLMTPAHGHVwldgehiqhyaskevarrigllaqnattpgDITVqelvargRYPHQPLFTRwr 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 410 VENDDFVRSVLMKTppsmierlDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDV 489
Cdd:PRK10253 118 KEDEEAVTKAMQAT--------GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSEL 189
|
....
gi 1278501429 490 IKKK 493
Cdd:PRK10253 190 NREK 193
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
370-492 |
1.65e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 49.74 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 370 LGENGTGKTTFAKILAGMIKPDKGK--------TDTSVKISYKPQYVQV-------ENDDFVRSVLM------------- 421
Cdd:PRK13649 39 IGHTGSGKSTIMQLLNGLHVPTQGSvrvddtliTSTSKNKDIKQIRKKVglvfqfpESQLFEETVLKdvafgpqnfgvsq 118
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 422 -KTPPSMIERLDL----SHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRlnvaKILRDVIKK 492
Cdd:PRK13649 119 eEAEALAREKLALvgisESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR----KELMTLFKK 190
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
103-270 |
1.81e-06 |
|
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: 48.68 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKST---CLNIL----SGQLkpnlgndfgEVEGQKIIDFFKGTEA---------QNY--FEKLytTGLETsyk 164
Cdd:cd03262 31 IIGPSGSGKSTllrCINLLeepdSGTI---------IIDGLKLTDDKKNINElrqkvgmvfQQFnlFPHL--TVLEN--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 165 pqyVEQIPRIFKGSVKALLNKISEGDVNKVcnelGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLD-- 242
Cdd:cd03262 97 ---ITLAPIKVKGMSKAEAEERALELLEKV----GLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDpe 169
|
170 180
....*....|....*....|....*....
gi 1278501429 243 -IKQRLKVANLLRKhgsEKECAVVVEHDL 270
Cdd:cd03262 170 lVGEVLDVMKDLAE---EGMTMVVVTHEM 195
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
196-291 |
1.82e-06 |
|
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: 48.79 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 196 NELGIKHV-LNRKVGDISGGELQRVAIAGALLKK-SDFLFI-DEPSSYL---DIKQRLKVANLLRKHGSEkecAVVVEHD 269
Cdd:cd03270 122 VDVGLGYLtLSRSAPTLSGGEAQRIRLATQIGSGlTGVLYVlDEPSIGLhprDNDRLIETLKRLRDLGNT---VLVVEHD 198
|
90 100
....*....|....*....|....*.
gi 1278501429 270 LIML---DYLADVehimyG-RAGVYG 291
Cdd:cd03270 199 EDTIraaDHVIDI-----GpGAGVHG 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
205-274 |
1.92e-06 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 49.95 E-value: 1.92e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 205 NRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVAN----LLRKHGSekeCAVVVEHD----LIMLD 274
Cdd:PRK09452 139 QRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNelkaLQRKLGI---TFVFVTHDqeeaLTMSD 213
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
342-495 |
2.08e-06 |
|
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: 48.29 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 342 WSNIEKK--LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGmikpDKGKTDTSVKISYKPQYV-QVENDDFVRS 418
Cdd:cd03217 7 HVSVGGKeiLKGVNLTIKKG-----EVHALMGPNGSGKSTLAKTIMG----HPKYEVTEGEILFKGEDItDLPPEERARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 419 ---VLMKTPPSmIERLDLSHLLkRKLSE-LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKE 494
Cdd:cd03217 78 gifLAFQYPPE-IPGVKNADFL-RYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGK 155
|
.
gi 1278501429 495 A 495
Cdd:cd03217 156 S 156
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
349-477 |
2.19e-06 |
|
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: 48.77 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKI-----------SYKPQYVQVENDDFVR 417
Cdd:cd03251 18 LRDISLDIPAG-----ETVALVGPSGSGKSTLVNLIPRFYDVDSG----RILIdghdvrdytlaSLRRQIGLVSQDVFLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 418 SVLMK----------TPPSMIERLDLSHLLK--RKLSE------------LSGGELQRVAIAECLSRDADVYLLDEPSAH 473
Cdd:cd03251 89 NDTVAeniaygrpgaTREEVEEAARAANAHEfiMELPEgydtvigergvkLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
....
gi 1278501429 474 LDVE 477
Cdd:cd03251 169 LDTE 172
|
|
| DMSOR_beta_like |
cd16374 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
21-67 |
2.32e-06 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319896 [Multi-domain] Cd Length: 139 Bit Score: 46.88 E-value: 2.32e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1278501429 21 CMNFCPINRTGKDCivegaDGKIVVEEELCIGCGICVNKCPFDAVKV 67
Cdd:cd16374 51 CMEVCPTGAIYRDE-----DGAVLVDPDKCIGCGMCAMACPFGVPRF 92
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
356-487 |
2.36e-06 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 48.01 E-value: 2.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 356 VKPGILmrneiIGVLGENGTGKTTFAKILAGmiKPDKGKTDTSVKISYKPQyvqveNDDFVRSVlmktppSMIERLDL-- 433
Cdd:cd03232 30 VKPGTL-----TALMGESGAGKTTLLDVLAG--RKTAGVITGEILINGRPL-----DKNFQRST------GYVEQQDVhs 91
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 434 -------SHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILR 487
Cdd:cd03232 92 pnltvreALRFSALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
91-270 |
2.67e-06 |
|
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: 48.97 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPQKKQImGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDFFKGTEAQNYFE---KL------------Y 155
Cdd:TIGR04520 22 SLSIEKGEFV-AIIGHNGSGKSTLAKLLNGLLLPT--------SGKVTVDGLDTLDEENLWEirkKVgmvfqnpdnqfvG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 156 TT-------GLETSYKPQyvEQIPRIfkgsvkallnkisegdVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKK 228
Cdd:TIGR04520 93 ATveddvafGLENLGVPR--EEMRKR----------------VDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1278501429 229 SDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDL 270
Cdd:TIGR04520 155 PDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVIsITHDM 197
|
|
| FDH-O_like |
cd10560 |
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes ... |
9-62 |
2.69e-06 |
|
beta subunit of formate dehydrogenase O (FDH-O) and similar proteins; This subfamily includes beta subunit of formate dehydrogenase family O (FDH-O), which is highly homologous to formate dehydrogenase N (FDH-N), a member of the DMSO reductase family. In E. coli three formate dehydrogenases are synthesized that are capable of oxidizing formate; Fdh-H, couples formate disproportionation to hydrogen and CO2, and is part of the cytoplasmically oriented formate hydrogenlyase complex, while FDH-N and FDH-O indicate their respective induction after growth with nitrate and oxygen. Little is known about FDH-O, although it shows formate oxidase activity during aerobic growth and is also synthesized during nitrate respiration, similar to FDH-N.
Pssm-ID: 319882 [Multi-domain] Cd Length: 225 Bit Score: 48.54 E-value: 2.69e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1278501429 9 KKCT-AGkgcdyvCMNFCPinrTGkdCIVEGADGKIVVEEELCIGCGICVNKCPF 62
Cdd:cd10560 79 KHCTdAG------CLEACP---TG--AIFRTEFGTVYIQPDICNGCGYCVAACPF 122
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
90-242 |
2.96e-06 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 48.42 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 90 FNLVIPQKKQIMGLvGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQkiiDFFKGTEAQ----------NYFEKLYttgl 159
Cdd:PRK10771 18 FDLTVERGERVAIL-GPSGAGKSTLLNLIAGFLTPASGSLT--LNGQ---DHTTTPPSRrpvsmlfqenNLFSHLT---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 160 etsykpqyVEQipRIFKGSVKAL-LNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPS 238
Cdd:PRK10771 88 --------VAQ--NIGLGLNPGLkLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
....
gi 1278501429 239 SYLD 242
Cdd:PRK10771 158 SALD 161
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
103-284 |
3.04e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 48.97 E-value: 3.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQLKPNLGNDfgEVEGQKIIDFFKGTEAQNYFEKLyttGLetsykpqyVEQIP--RIFKGSVK 180
Cdd:PRK13649 38 FIGHTGSGKSTIMQLLNGLHVPTQGSV--RVDDTLITSTSKNKDIKQIRKKV---GL--------VFQFPesQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 181 ALLN------KISEGDVNKVCNE----LGIKHVL-NRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKV 249
Cdd:PRK13649 105 KDVAfgpqnfGVSQEEAEALAREklalVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKEL 184
|
170 180 190
....*....|....*....|....*....|....*
gi 1278501429 250 ANLLRKHGSEKECAVVVEHdliMLDYLADVEHIMY 284
Cdd:PRK13649 185 MTLFKKLHQSGMTIVLVTH---LMDDVANYADFVY 216
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
349-489 |
3.25e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.67 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMI----KPDKGKTDTSVKISYKPQYV--------------QV 410
Cdd:PRK13547 17 LRDLSLRIEPG-----RVTALLGRNGAGKSTLLKALAGDLtgggAPRGARVTGDVTLNGEPLAAidaprlarlravlpQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 411 ENDDFVRS----VLMKTPP-----------------SMIERLDLSHLLKRKLSELSGGELQRVAIAECLS---------R 460
Cdd:PRK13547 92 AQPAFAFSareiVLLGRYPharragalthrdgeiawQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQ 171
|
170 180
....*....|....*....|....*....
gi 1278501429 461 DADVYLLDEPSAHLDVEQRLNVAKILRDV 489
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRL 200
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
18-66 |
3.37e-06 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 47.63 E-value: 3.37e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1278501429 18 DYVCMNFCPINRTGKDcivegADGKIVVEEELCIGCGICVNKCPFDAVK 66
Cdd:COG0437 65 DPPCVKVCPTGATYKR-----EDGIVLVDYDKCIGCRYCVAACPYGAPR 108
|
|
| rnfB |
TIGR01944 |
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ... |
2-68 |
3.40e-06 |
|
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]
Pssm-ID: 273887 [Multi-domain] Cd Length: 165 Bit Score: 47.10 E-value: 3.40e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 2 RIVVVNKKKCTagkGCDyVCMNFCPInrtgkDCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:TIGR01944 106 MVALIDEDNCI---GCT-KCIQACPV-----DAIVGAAKAMHTVIADECTGCDLCVEPCPTDCIEMI 163
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
3-68 |
3.41e-06 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319894 [Multi-domain] Cd Length: 125 Bit Score: 46.17 E-value: 3.41e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 3 IVVVNKKKCTagkGCdYVCMNFCPINrtgkdCIVEGADgkiVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:cd16372 71 VVMINKKLCV---GC-LMCVGFCPEG-----AMFKHED---YPEPFKCIACGICVKACPTGALELV 124
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
349-477 |
3.55e-06 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 49.72 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKISYKP--QY-----------VQVENDDF 415
Cdd:TIGR00958 497 LKGLTFTLHPG-----EVVALVGPSGSGKSTVAALLQNLYQPTGG----QVLLDGVPlvQYdhhylhrqvalVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 416 VRSV-------LMKTPPSMIE---RLDLSHLLKRKL------------SELSGGELQRVAIAECLSRDADVYLLDEPSAH 473
Cdd:TIGR00958 568 SGSVreniaygLTDTPDEEIMaaaKAANAHDFIMEFpngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
....
gi 1278501429 474 LDVE 477
Cdd:TIGR00958 648 LDAE 651
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
444-479 |
3.58e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 49.46 E-value: 3.58e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1278501429 444 LSGGELQRVAIAECLSRDADVYLLDEPSAHLDV--EQR 479
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAhsEQL 523
|
|
| RnfB |
COG2878 |
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ... |
14-84 |
3.66e-06 |
|
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase
Pssm-ID: 442125 [Multi-domain] Cd Length: 254 Bit Score: 48.45 E-value: 3.66e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 14 GKGCDYVCMNF------CPInrtgkDCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVVNLPDELesrMIHSYDK 84
Cdd:COG2878 132 PKGCEYGCIGCgdcikaCPF-----DAIVGAAKGMHTVDEDKCTGCGLCVEACPVDCIEMVPVSPTV---VVSSWDK 200
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
369-488 |
3.71e-06 |
|
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: 47.15 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 369 VLGENGTGKTTFAKILAGM--------IKPDKGKtdtsvkISYKPQ--YvqvenddFVRSVLmktppsmieRLDLSHLLK 438
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLwpwgsgriGMPEGED------LLFLPQrpY-------LPLGTL---------REQLIYPWD 89
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1278501429 439 RklsELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRD 488
Cdd:cd03223 90 D---VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE 136
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
433-499 |
3.73e-06 |
|
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: 48.20 E-value: 3.73e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 433 LSHL-LKRKLSEL-----SGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDviKKKEASAFV 499
Cdd:COG4778 136 LARLnLPERLWDLppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEE--AKARGTAII 206
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
211-270 |
4.05e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 48.09 E-value: 4.05e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 211 ISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDL 270
Cdd:COG4161 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEV 201
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
212-283 |
4.17e-06 |
|
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: 47.81 E-value: 4.17e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 212 SGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRkhgsEKE---CAVV-VEHDLIMLDYLADVEHIM 283
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIE----EAKargTAIIgIFHDEEVREAVADRVVDV 225
|
|
| Fer4 |
pfam00037 |
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ... |
43-66 |
4.17e-06 |
|
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 459642 [Multi-domain] Cd Length: 24 Bit Score: 43.01 E-value: 4.17e-06
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
212-291 |
4.18e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.57 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 212 SGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDLIMLDYLADVEHIMY-GRAGV 289
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYaGRTME 242
|
..
gi 1278501429 290 YG 291
Cdd:PRK09473 243 YG 244
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
83-270 |
4.27e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 48.45 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 83 DKNGFKLFNLVIPQKKQImGLVGVNGIGKSTCLNILSGQLKPNLGND--FGEVEGQKIIDFFK---GTEAQN-------- 149
Cdd:PRK13632 21 ENNALKNVSFEINEGEYV-AILGHNGSGKSTISKILTGLLKPQSGEIkiDGITISKENLKEIRkkiGIIFQNpdnqfiga 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 150 YFEKLYTTGLETsykpqyvEQIPRifkGSVKALLNKISEgdvnkvcnELGIKHVLNRKVGDISGGELQRVAIAGALLKKS 229
Cdd:PRK13632 100 TVEDDIAFGLEN-------KKVPP---KKMKDIIDDLAK--------KVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1278501429 230 DFLFIDEPSSYLDIKQRLKVANLLRK-HGSEKECAVVVEHDL 270
Cdd:PRK13632 162 EIIIFDESTSMLDPKGKREIKKIMVDlRKTRKKTLISITHDM 203
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
365-487 |
4.55e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.04 E-value: 4.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 365 EIIGVLGENGTGKTTFAKILAGMIKPDKGK-------------TDTSVKISYKPQY----------VQVENDDFVRSVLM 421
Cdd:PRK10619 32 DVISIIGSSGSGKSTFLRCINFLEKPSEGSivvngqtinlvrdKDGQLKVADKNQLrllrtrltmvFQHFNLWSHMTVLE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 422 KTPPSMIERLDLS----------HLLKRKLSE---------LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNV 482
Cdd:PRK10619 112 NVMEAPIQVLGLSkqeareravkYLAKVGIDEraqgkypvhLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEV 191
|
....*
gi 1278501429 483 AKILR 487
Cdd:PRK10619 192 LRIMQ 196
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
212-286 |
4.57e-06 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 48.57 E-value: 4.57e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 212 SGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECA-VVVEHDLIMLDYLADVEHIMY-GR 286
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTyLFISHDLSVVRHISDRVAVMYlGK 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
96-476 |
4.86e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.14 E-value: 4.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIIdFFKGTEAQNyfeklytTGL-----ETSYKPQ---- 166
Cdd:PRK11288 28 RAGQVHALMGENGAGKSTLLKILSGNYQPDAGSIL--IDGQEMR-FASTTAALA-------AGVaiiyqELHLVPEmtva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 167 ---YVEQIPRIFkGSV-KALLNKisegDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYL- 241
Cdd:PRK11288 98 enlYLGQLPHKG-GIVnRRLLNY----EAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLs 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 242 --DIKQRLKVANLLRKHGsekecAVV--VEHDLIMLDYLADVEHIMygRAGVYgivskslsirecINTY--LEGYIRED- 314
Cdd:PRK11288 173 arEIEQLFRVIRELRAEG-----RVIlyVSHRMEEIFALCDAITVF--KDGRY------------VATFddMAQVDRDQl 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 315 --NMRFRSeeikfevkaptkaLNNIpiieWSNIEKKLGDFKLKVK----PGI-------LMRNEIIGVLGENGTGKTTFA 381
Cdd:PRK11288 234 vqAMVGRE-------------IGDI----YGYRPRPLGEVRLRLDglkgPGLrepisfsVRAGEIVGLFGLVGAGRSELM 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 382 KILAGMIKPDKG-----------------------------KTD-----TSVK----ISYKPQYV----------QVEN- 412
Cdd:PRK11288 297 KLLYGATRRTAGqvyldgkpidirsprdairagimlcpedrKAEgiipvHSVAdninISARRHHLragclinnrwEAENa 376
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278501429 413 DDFVRSVLMKTPPSmierldlshllKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDV 476
Cdd:PRK11288 377 DRFIRSLNIKTPSR-----------EQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDV 429
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
91-255 |
4.87e-06 |
|
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: 47.58 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGNDfgEVEGQKIIDFfKGTEAQNyFEKlyttgletsykpqyveQ 170
Cdd:cd03258 25 SLSVP-KGEIFGIIGRSGAGKSTLIRCINGLERPTSGSV--LVDGTDLTLL-SGKELRK-ARR----------------R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 IPRIFKG-----SVKALLN--------KISEGDVNKVCNEL----GIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLF 233
Cdd:cd03258 84 IGMIFQHfnllsSRTVFENvalpleiaGVPKAEIEERVLELlelvGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180
....*....|....*....|..
gi 1278501429 234 IDEPSSYLDIKQRLKVANLLRK 255
Cdd:cd03258 164 CDEATSALDPETTQSILALLRD 185
|
|
| COG2768 |
COG2768 |
Uncharacterized Fe-S cluster protein [Function unknown]; |
39-69 |
4.99e-06 |
|
Uncharacterized Fe-S cluster protein [Function unknown];
Pssm-ID: 442050 [Multi-domain] Cd Length: 74 Bit Score: 44.34 E-value: 4.99e-06
10 20 30
....*....|....*....|....*....|.
gi 1278501429 39 ADGKIVVEEELCIGCGICVNKCPFDAVKVVN 69
Cdd:COG2768 2 SLGKPYVDEEKCIGCGACVKVCPVGAISIED 32
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
98-255 |
5.02e-06 |
|
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: 47.16 E-value: 5.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 98 KQIMGLVGVNGIGKSTCLNILSGQLKPnlGNDFGEV--EGQKIIDFfkgteaqnyfeklyttgletSYKPQ--YVEQ--- 170
Cdd:cd03213 35 GELTAIMGPSGAGKSTLLNALAGRRTG--LGVSGEVliNGRPLDKR--------------------SFRKIigYVPQddi 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 -IPrifkgsvkallnkisegdvnkvcnELGIKHVL--NRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRL 247
Cdd:cd03213 93 lHP------------------------TLTVRETLmfAAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
|
....*...
gi 1278501429 248 KVANLLRK 255
Cdd:cd03213 149 QVMSLLRR 156
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
91-268 |
5.06e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 47.99 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPQKkQIMGLVGVNGIGKSTCLNILSG--QLKPNlgndfGEVEGQKIIDffkgteAQNYFEklyTTGLETSYKPQYV 168
Cdd:PRK14247 23 NLEIPDN-TITALMGPSGSGKSTLLRVFNRliELYPE-----ARVSGEVYLD------GQDIFK---MDVIELRRRVQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 169 EQIPR------IFKGSVKAL-LNKI--SEGDVNKVCNEL--------GIKHVLNRKVGDISGGELQRVAIAGALLKKSDF 231
Cdd:PRK14247 88 FQIPNpipnlsIFENVALGLkLNRLvkSKKELQERVRWAlekaqlwdEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190
....*....|....*....|....*....|....*...
gi 1278501429 232 LFIDEPSSYLDIKQRLKVANLLRKhgSEKECAVV-VEH 268
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLE--LKKDMTIVlVTH 203
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
363-499 |
5.08e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 48.31 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKG-----------KTDTSVKISYK---------------------PQY--- 407
Cdd:PRK13631 51 KNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdKKNNHELITNPyskkiknfkelrrrvsmvfqfPEYqlf 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 408 -VQVENDDFVRSVLMKTPPSMIERLDLSHL---------LKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:PRK13631 131 kDTIEKDIMFGPVALGVKKSEAKKLAKFYLnkmglddsyLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK 210
|
170 180
....*....|....*....|..
gi 1278501429 478 QRLNVAKILRDViKKKEASAFV 499
Cdd:PRK13631 211 GEHEMMQLILDA-KANNKTVFV 231
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
91-282 |
5.11e-06 |
|
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: 47.46 E-value: 5.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPNlgndFGEVegqkiidFFKGTEAqnyfeklyttgletsykpqYVEQ 170
Cdd:cd03250 25 NLEVP-KGELVAIVGPVGSGKSSLLSALLGELEKL----SGSV-------SVPGSIA-------------------YVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 IPRIFKGSVK---------------------AL---LNKISEGDvNKVCNELGIkhvlnrkvgDISGGELQRVAIAGALL 226
Cdd:cd03250 74 EPWIQNGTIRenilfgkpfdeeryekvikacALepdLEILPDGD-LTEIGEKGI---------NLSGGQKQRISLARAVY 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 227 KKSDFLFIDEPSSYLDIK--QRLkVANLLRKHGSEKECAVVVEHdliMLDYLADVEHI 282
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHvgRHI-FENCILGLLLNNKTRILVTH---QLQLLPHADQI 197
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
81-242 |
6.49e-06 |
|
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: 47.23 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 81 SYDKNG---FKLFNLVIPQKKQImGLVGVNGIGKSTCLNILSgqlkpnlgnDFGEV-EGQKIIDffkGTEAQNYfeKLyt 156
Cdd:cd03251 9 RYPGDGppvLRDISLDIPAGETV-ALVGPSGSGKSTLVNLIP---------RFYDVdSGRILID---GHDVRDY--TL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 157 tgleTSYKPQ--YVEQIPRIFKGSVKallNKISEGDVN----------KVCN--------ELGIKHVLNRKVGDISGGEL 216
Cdd:cd03251 72 ----ASLRRQigLVSQDVFLFNDTVA---ENIAYGRPGatreeveeaaRAANahefimelPEGYDTVIGERGVKLSGGQR 144
|
170 180
....*....|....*....|....*.
gi 1278501429 217 QRVAIAGALLKKSDFLFIDEPSSYLD 242
Cdd:cd03251 145 QRIAIARALLKDPPILILDEATSALD 170
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
361-496 |
7.07e-06 |
|
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: 48.13 E-value: 7.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 361 LMRNEIIGVLGENGTGKTTFAKILAGMIKPdKGKTDTSV---------------------KISYKPQ------------Y 407
Cdd:COG0444 28 VRRGETLGLVGESGSGKSTLARAILGLLPP-PGITSGEIlfdgedllklsekelrkirgrEIQMIFQdpmtslnpvmtvG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 408 VQVEndDFVRSVLMKTPPSMIERLDlsHLLKR-KLS-----------ELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:COG0444 107 DQIA--EPLRIHGGLSKAEARERAI--ELLERvGLPdperrldryphELSGGMRQRVMIARALALEPKLLIADEPTTALD 182
|
170 180
....*....|....*....|.
gi 1278501429 476 VEQRLNVAKILRDVIKKKEAS 496
Cdd:COG0444 183 VTIQAQILNLLKDLQRELGLA 203
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
103-268 |
7.44e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 47.71 E-value: 7.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQLKPNLGN-DFGEVE-------------GQKIIDFFKGTEAQnYFEKlyTTGLETSYKPQYv 168
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQPTSGTvTIGERVitagkknkklkplRKKVGIVFQFPEHQ-LFEE--TVEKDICFGPMN- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 169 eqipriFKGSVKALLNKISEgdvnkVCNELGIKH-VLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRL 247
Cdd:PRK13634 114 ------FGVSEEDAKQKARE-----MIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180
....*....|....*....|..
gi 1278501429 248 KVANLLRKHGSEKECAVV-VEH 268
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVlVTH 204
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
104-266 |
7.60e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 7.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 104 VGVNGIGKSTCLNILSGQLKPnlgndfgeVEGQKIIDFFKGTEAQnyFEKLyttgletsykPQYVEQIpriFKGSVKALL 183
Cdd:PRK10938 35 VGANGSGKSALARALAGELPL--------LSGERQSQFSHITRLS--FEQL----------QKLVSDE---WQRNNTDML 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 184 NK------------ISEG-DVNKVCNEL----GIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQR 246
Cdd:PRK10938 92 SPgeddtgrttaeiIQDEvKDPARCEQLaqqfGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180
....*....|....*....|
gi 1278501429 247 LKVANLLRKHGSEKECAVVV 266
Cdd:PRK10938 172 QQLAELLASLHQSGITLVLV 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
338-474 |
8.56e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 48.12 E-value: 8.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKKLGdfKLKVKPGI---LMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKISYKPQY------- 407
Cdd:PRK15439 10 PLLCARSISKQYS--GVEVLKGIdftLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSG----TLEIGGNPCArltpaka 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 408 -------VQVE-----NDDFVRSVLMKTPPSMierlDLSHLLKRKLSEL--------SGGEL-----QRVAIAECLSRDA 462
Cdd:PRK15439 84 hqlgiylVPQEpllfpNLSVKENILFGLPKRQ----ASMQKMKQLLAALgcqldldsSAGSLevadrQIVEILRGLMRDS 159
|
170
....*....|..
gi 1278501429 463 DVYLLDEPSAHL 474
Cdd:PRK15439 160 RILILDEPTASL 171
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
347-475 |
8.57e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 47.70 E-value: 8.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 347 KKLGDFKLKVKpgilmRNEIIGVLGENGTGKTTFAKILAGMIKPDKGKT---DTSVKISYK------------------P 405
Cdd:PRK13645 25 KALNNTSLTFK-----KNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgDYAIPANLKkikevkrlrkeiglvfqfP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 406 QYvQVENDDFVRSV-------------LMKTPPSMIERLDLSH-LLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPS 471
Cdd:PRK13645 100 EY-QLFQETIEKDIafgpvnlgenkqeAYKKVPELLKLVQLPEdYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
....
gi 1278501429 472 AHLD 475
Cdd:PRK13645 179 GGLD 182
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
74-253 |
8.80e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 47.14 E-value: 8.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 74 LESRMIHSY--DKNGFKLFNLVIPQKKqIMGLVGVNGIGKSTCLNILSGQLKPNlgnDFGEVEGqkiidffkgtEAQNYF 151
Cdd:PRK14267 5 IETVNLRVYygSNHVIKGVDLKIPQNG-VFALMGPSGCGKSTLLRTFNRLLELN---EEARVEG----------EVRLFG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 152 EKLYTTG---LETSYKPQYVEQIPRIF---------------KGSVKAL--LNKISEGDVNKVCNELGIKHVLNRKVGDI 211
Cdd:PRK14267 71 RNIYSPDvdpIEVRREVGMVFQYPNPFphltiydnvaigvklNGLVKSKkeLDERVEWALKKAALWDEVKDRLNDYPSNL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1278501429 212 SGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLL 253
Cdd:PRK14267 151 SGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELL 192
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
355-494 |
9.56e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 47.34 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 355 KVKPGILM---RNEIIGVLGENGTGKTTFAKIL------------------------------------AGMIKPDKGKT 395
Cdd:PRK14258 21 KILEGVSMeiyQSKVTAIIGPSGCGKSTFLKCLnrmnelesevrvegrveffnqniyerrvnlnrlrrqVSMVHPKPNLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 396 DTSV--KISYKPQYV----QVENDDFVRSVLMKTppsmiERLD-LSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLD 468
Cdd:PRK14258 101 PMSVydNVAYGVKIVgwrpKLEIDDIVESALKDA-----DLWDeIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMD 175
|
170 180
....*....|....*....|....*.
gi 1278501429 469 EPSAHLDVEQRLNVAKILRDVIKKKE 494
Cdd:PRK14258 176 EPCFGLDPIASMKVESLIQSLRLRSE 201
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
349-475 |
9.78e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 9.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGILmrneiIGVLGENGTGKTTFAKILAGMIKPDKgktDTSVKI----SYKPQYVQVENDDFVRSVLM--K 422
Cdd:PLN03232 633 LSDINLEIPVGSL-----VAIVGGTGEGKTSLISAMLGELSHAE---TSSVVIrgsvAYVPQVSWIFNATVRENILFgsD 704
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 423 TPPSMIERL--------DLSHLLKRKLSEL-------SGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:PLN03232 705 FESERYWRAidvtalqhDLDLLPGRDLTEIgergvniSGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| porD |
PRK09624 |
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed |
7-68 |
1.03e-05 |
|
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 170017 [Multi-domain] Cd Length: 105 Bit Score: 44.25 E-value: 1.03e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 7 NKKKCTAgkgCdYVCMNFCPinrtgKDCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:PRK09624 49 NRDKCVR---C-YLCYIYCP-----EPAIYLDEEGYPVFDYDYCKGCGICANECPTKAIEMV 101
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
361-476 |
1.11e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 47.42 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 361 LMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGK-----TDTSV--KISYKP-----QYV-QvenDDF--------VRSV 419
Cdd:COG4608 41 IRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEilfdgQDITGlsGRELRPlrrrmQMVfQ---DPYaslnprmtVGDI 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278501429 420 L--------MKTPPSMIER---------LDLSHLlKRKLSELSGGELQRVAIAECLSRDADVYLLDEP-SAhLDV 476
Cdd:COG4608 118 IaeplrihgLASKAERRERvaellelvgLRPEHA-DRYPHEFSGGQRQRIGIARALALNPKLIVCDEPvSA-LDV 190
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
82-346 |
1.11e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 47.08 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 82 YDKNGFKLFNLVIPQKKqIMGLVGVNGIGKSTCLNILSGQLKPNLGN-DFGEVE-------------GQKIIDFFKGTEA 147
Cdd:PRK13646 18 YEHQAIHDVNTEFEQGK-YYAIVGQTGSGKSTLIQNINALLKPTTGTvTVDDITithktkdkyirpvRKRIGMVFQFPES 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 148 QnyfekLYTTGLEtsykpQYVEQIPRIFKGSVKALLNKisegdVNKVCNELGI-KHVLNRKVGDISGGELQRVAIAGALL 226
Cdd:PRK13646 97 Q-----LFEDTVE-----REIIFGPKNFKMNLDEVKNY-----AHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 227 KKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDliMLDYLADVEHIMYGRAGvyGIVSKSlSIRECIN- 304
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIIlVSHD--MNEVARYADEVIVMKEG--SIVSQT-SPKELFKd 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1278501429 305 -TYLEGYIRE--DNMRFRSE-EIKFEVKAPTKALNNIPII----EWSNIE 346
Cdd:PRK13646 237 kKKLADWHIGlpEIVQLQYDfEQKYQTKLKDIALTEEEFVslykEWQHEK 286
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
361-492 |
1.17e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 47.01 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 361 LMRNEIIGVLGENGTGKTTFAKILAGMIKPDKG--KTDTS----------------VKISYKPQYVQ----------VEN 412
Cdd:PRK13642 30 ITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGkvKIDGElltaenvwnlrrkigmVFQNPDNQFVGatveddvafgMEN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 413 DDFVRSVLMKTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKK 492
Cdd:PRK13642 110 QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEK 189
|
|
| MtMvhB_like |
cd10549 |
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ... |
43-69 |
1.17e-05 |
|
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.
Pssm-ID: 319871 [Multi-domain] Cd Length: 128 Bit Score: 44.70 E-value: 1.17e-05
10 20
....*....|....*....|....*..
gi 1278501429 43 IVVEEELCIGCGICVNKCPFDAVKVVN 69
Cdd:cd10549 1 LKYDPEKCIGCGICVKACPTDAIELGP 27
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
340-475 |
1.28e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 47.66 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKKLGDFKLKVKPG--ILMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGK-------TDTSVKISYKPQYVQV 410
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVGPInlTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEilldgkpVTAEQPEDYRKLFSAV 402
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278501429 411 ENDDFVRSVLM---KTPP------SMIERLDLSHLLK---RKLS--ELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:PRK10522 403 FTDFHLFDQLLgpeGKPAnpalveKWLERLKMAHKLEledGRISnlKLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
101-270 |
1.31e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 101 MGLVGVNGIGKSTC----LNILSGQlkpnlgndfGEVegqkiidFFKGTEAQNYFEKLYttgLETSYKPQYVEQIPrifK 176
Cdd:PRK15134 315 LGLVGESGSGKSTTglalLRLINSQ---------GEI-------WFDGQPLHNLNRRQL---LPVRHRIQVVFQDP---N 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 177 GSVKALLNK---ISEG---------------DVNKVCNELGI----KHvlnRKVGDISGGELQRVAIAGALLKKSDFLFI 234
Cdd:PRK15134 373 SSLNPRLNVlqiIEEGlrvhqptlsaaqreqQVIAVMEEVGLdpetRH---RYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278501429 235 DEPSSYLDIKQRLKVANLLRKHGSEKECA-VVVEHDL 270
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLAyLFISHDL 486
|
|
| PRK13795 |
PRK13795 |
hypothetical protein; Provisional |
10-61 |
1.31e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237510 [Multi-domain] Cd Length: 636 Bit Score: 47.68 E-value: 1.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 10 KCTagkGCDyVCMNFCPINrtgkdCI-VEGADGKIVVEEELCIGCGICVNKCP 61
Cdd:PRK13795 582 ECV---GCG-VCVGACPTG-----AIrIEEGKRKISVDEEKCIHCGKCTEVCP 625
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
338-487 |
1.34e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.80 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 338 PIIEWSNIEKKL--GDFKLKVKPGILMR---NEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtsvkiSYK--PQYVQV 410
Cdd:PRK10535 3 ALLELKDIRRSYpsGEEQVEVLKGISLDiyaGEMVAIVGASGSGKSTLMNILGCLDKPTSG--------TYRvaGQDVAT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 411 ENDD-------------FVRSVLM------------------------KTPPSMIERLDLSHLLKRKLSELSGGELQRVA 453
Cdd:PRK10535 75 LDADalaqlrrehfgfiFQRYHLLshltaaqnvevpavyaglerkqrlLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVS 154
|
170 180 190
....*....|....*....|....*....|....
gi 1278501429 454 IAECLSRDADVYLLDEPSAHLDVEQRLNVAKILR 487
Cdd:PRK10535 155 IARALMNGGQVILADEPTGALDSHSGEEVMAILH 188
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
332-499 |
1.35e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 332 KALNNIPIIEWSNIEKKLGDFK-------LKVKPGILMRNEIIGVLGENGTGKTTFAKILAGmiKPDKGKTDTSVKISY- 403
Cdd:TIGR00956 48 PTFPNALLKILTRGFRKLKKFRdtktfdiLKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS--NTDGFHIGVEGVITYd 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 404 -------KPQY-----VQVEND------------DFvrSVLMKTP---PSMIERLD--------------LSHLLKRKLS 442
Cdd:TIGR00956 126 gitpeeiKKHYrgdvvYNAETDvhfphltvgetlDF--AARCKTPqnrPDGVSREEyakhiadvymatygLSHTRNTKVG 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 443 E-----LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEASAFV 499
Cdd:TIGR00956 204 NdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLV 265
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
2-69 |
1.41e-05 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 46.85 E-value: 1.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 2 RIVVVNKKKCTagkGCDyVCMNFCP---INRTGKDCIVEGA-----DGKIV--VEEELCIGCGICVNKCPFDAVKVVN 69
Cdd:PRK07118 161 GLPVVDEDKCT---GCG-ACVKACPrnvIELIPKSARVFVAcnskdKGKAVkkVCEVGCIGCGKCVKACPAGAITMEN 234
|
|
| IOR_alpha |
TIGR03336 |
indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin ... |
6-65 |
1.71e-05 |
|
indolepyruvate ferredoxin oxidoreductase, alpha subunit; Indolepyruvate ferredoxin oxidoreductase (IOR) is an alpha 2/beta 2 tetramer related to ketoacid oxidoreductases for pyruvate (1.2.7.1, POR), 2-ketoglutarate (1.2.7.3, KOR), and 2-oxoisovalerate (1.2.7.7, VOR). These multi-subunit enzymes typically are found in anaerobes and are inactiviated by oxygen. IOR in Pyrococcus acts in fermentation of all three aromatic amino acids, following removal of the amino group by transamination. In Methanococcus maripaludis, by contrast, IOR acts in the opposite direction, in pathways of amino acid biosynthesis from phenylacetate, indoleacetate, and p-hydroxyphenylacetate. In M. maripaludis and many other species, iorA and iorB are found next to an apparent phenylacetate-CoA ligase.
Pssm-ID: 274526 [Multi-domain] Cd Length: 595 Bit Score: 47.41 E-value: 1.71e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 6 VNKKKCTAGKGCdyvcmnfcpINRTGKDCIVEgaDGKIVVEEELCIGCGICVNKCPFDAV 65
Cdd:TIGR03336 547 VDQDKCIGCKKC---------IKELGCPAIEP--EDKEAVIDPLCTGCGVCAQICPFDAI 595
|
|
| PRK10330 |
PRK10330 |
electron transport protein HydN; |
6-71 |
1.77e-05 |
|
electron transport protein HydN;
Pssm-ID: 182382 [Multi-domain] Cd Length: 181 Bit Score: 45.27 E-value: 1.77e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 6 VNKKKCTAGKGC-DYVCMNFCP---INRTGkdcivegadGKIVVEEELCIGCGICVNKCPFDAVKVVNLP 71
Cdd:PRK10330 50 VNVSTATVCRQCeDAPCANVCPngaISRDK---------GFVHVMQERCIGCKTCVVACPYGAMEVVVRP 110
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
87-242 |
1.85e-05 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 45.55 E-value: 1.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 87 FKLFNLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFgEVEGQKIIDffkGTEaqnyfeklyTTGLetsykPQ 166
Cdd:COG4136 17 LAPLSLTVA-PGEILTLMGPSGSGKSTLLAAIAGTLSP----AF-SASGEVLLN---GRR---------LTAL-----PA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 167 YVEQIPRIFKG-------SVK-----ALLNKISEGD----VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSD 230
Cdd:COG4136 74 EQRRIGILFQDdllfphlSVGenlafALPPTIGRAQrrarVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPR 153
|
170
....*....|..
gi 1278501429 231 FLFIDEPSSYLD 242
Cdd:COG4136 154 ALLLDEPFSKLD 165
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
427-488 |
1.91e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.71 E-value: 1.91e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278501429 427 MIERLD------LSHL-LKRKLSELSGGELQRVAIAECLSRDAD--VYLLDEPSAHL---DVEQRLNVAKILRD 488
Cdd:cd03270 114 IRERLGflvdvgLGYLtLSRSAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLhprDNDRLIETLKRLRD 187
|
|
| Fer4_21 |
pfam14697 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
21-61 |
2.15e-05 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 434137 [Multi-domain] Cd Length: 59 Bit Score: 41.88 E-value: 2.15e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1278501429 21 CMNFCPinRTGKDCIVEGADGKIVVEEELCIGCGICVNKCP 61
Cdd:pfam14697 14 CYIACP--DTSHQAIVGDGKRHHTVIEDECTGCNLCVSVCP 52
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
86-270 |
2.28e-05 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 46.29 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 86 GFKL---FNLVIPQKkQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVegqkiidFFKGTEA--------------- 147
Cdd:COG1118 14 SFTLlddVSLEIASG-ELVALLGPSGSGKTTLLRIIAGLETP----DSGRI-------VLNGRDLftnlpprerrvgfvf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 148 QNY-------------FeklyttGLETsyKPQYVEQIprifKGSVKALLNKIsegdvnkvcnelGIKHVLNRKVGDISGG 214
Cdd:COG1118 82 QHYalfphmtvaeniaF------GLRV--RPPSKAEI----RARVEELLELV------------QLEGLADRYPSQLSGG 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 215 ELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDL 270
Cdd:COG1118 138 QRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVfVTHDQ 194
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
91-288 |
2.28e-05 |
|
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: 45.78 E-value: 2.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPQKKQIMgLVGVNGIGKSTCLNILSGQLkpnlgndfgevegQKIIDFFKGTEAQNYFEKLYTTGLETSYKPQYVEQ 170
Cdd:cd03290 21 NIRIPTGQLTM-IVGQVGCGKSSLLLAILGEM-------------QTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 IPRIFKGSVK------ALLNKISEGDVNKVCN--------ELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDE 236
Cdd:cd03290 87 KPWLLNATVEenitfgSPFNKQRYKAVTDACSlqpdidllPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1278501429 237 PSSYLDI--KQRLKVANLLRKHGSEKECAVVVEHDlimLDYLADVEHIMYGRAG 288
Cdd:cd03290 167 PFSALDIhlSDHLMQEGILKFLQDDKRTLVLVTHK---LQYLPHADWIIAMKDG 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
99-238 |
2.35e-05 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 45.74 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPNLGndfgevegqKIIdfFKGTEaqnyfeklyTTGLETSYKPQ----YVEQIPRI 174
Cdd:COG0410 30 EIVALLGRNGAGKTTLLKAISGLLPPRSG---------SIR--FDGED---------ITGLPPHRIARlgigYVPEGRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 175 FKG-SVK-----ALLNKISEGDVNKVcnelgIKHVL----------NRKVGDISGGELQRVAIAGALLKKSDFLFIDEPS 238
Cdd:COG0410 90 FPSlTVEenlllGAYARRDRAEVRAD-----LERVYelfprlkerrRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
349-491 |
2.50e-05 |
|
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: 45.61 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKIL-------AGMIKPDkGKTDTSVKIS-YKPQ--YVQVENDDFVRS 418
Cdd:cd03249 19 LKGLSLTIPPG-----KTVALVGSSGCGKSTVVSLLerfydptSGEILLD-GVDIRDLNLRwLRSQigLVSQEPVLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 419 V-----LMKTPPSMIE-----RLDLSHLLKRKL------------SELSGGELQRVAIAECLSRDADVYLLDEPSAHLDV 476
Cdd:cd03249 93 IaenirYGKPDATDEEveeaaKKANIHDFIMSLpdgydtlvgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170
....*....|....*
gi 1278501429 477 EQRLNVAKILRDVIK 491
Cdd:cd03249 173 ESEKLVQEALDRAMK 187
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
369-487 |
2.60e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 45.93 E-value: 2.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 369 VLGENGTGKTTFAKILAGMIKPDKGKTDTS-VKISYKPQyvqvenDDFVRSVLMKT------PPSM-----IER------ 430
Cdd:PRK13646 38 IVGQTGSGKSTLIQNINALLKPTTGTVTVDdITITHKTK------DKYIRPVRKRIgmvfqfPESQlfedtVEReiifgp 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 431 ------------------LDLS---HLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILR 487
Cdd:PRK13646 112 knfkmnldevknyahrllMDLGfsrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLK 189
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
212-283 |
2.69e-05 |
|
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: 46.60 E-value: 2.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 212 SGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLR----KHG------SekecavvveHDLIMLDYLADveH 281
Cdd:COG4172 427 SGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRdlqrEHGlaylfiS---------HDLAVVRALAH--R 495
|
..
gi 1278501429 282 IM 283
Cdd:COG4172 496 VM 497
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-291 |
2.86e-05 |
|
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: 46.93 E-value: 2.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 133 VEGQKIIDF--FKGTEAQNYFEKLYTTGLETsykpQYVEQIPRIFKGSVKALLNkisegdvnkvcneLGIKHV-LNRKVG 209
Cdd:TIGR00630 425 VGGKSIADVseLSIREAHEFFNQLTLTPEEK----KIAEEVLKEIRERLGFLID-------------VGLDYLsLSRAAG 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 210 DISGGELQRVAIA---GALLkkSDFLFI-DEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIML---DYLADvehi 282
Cdd:TIGR00630 488 TLSGGEAQRIRLAtqiGSGL--TGVLYVlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIraaDYVID---- 561
|
....*....
gi 1278501429 283 MYGRAGVYG 291
Cdd:TIGR00630 562 IGPGAGEHG 570
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
96-272 |
2.88e-05 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 45.75 E-value: 2.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGN---DFGEVEG---QKI-----IDFFkgteaQN--YFEKLytTGLETS 162
Cdd:PRK11300 29 REQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTillRGQHIEGlpgHQIarmgvVRTF-----QHvrLFREM--TVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 163 YKPQYVEQIPRIFKGSVKALLNKISEGDVNKVC----NELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPS 238
Cdd:PRK11300 102 LVAQHQQLKTGLFSGLLKTPAFRRAESEALDRAatwlERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 1278501429 239 SYLDIKQRLKVANLLRKHGSEKECAV-VVEHD--LIM 272
Cdd:PRK11300 182 AGLNPKETKELDELIAELRNEHNVTVlLIEHDmkLVM 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
102-277 |
2.97e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 45.83 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 102 GLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVegqkiidFFKGTEaqnyfeklyTTGLETSYKPQYVEQIPRIFKGSVKA 181
Cdd:PRK10419 42 ALLGRSGCGKSTLARLLVGLESP----SQGNV-------SWRGEP---------LAKLNRAQRKAFRRDIQMVFQDSISA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 182 L----------------LNKISEGD----VNKVCNELGIK-HVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSY 240
Cdd:PRK10419 102 VnprktvreiireplrhLLSLDKAErlarASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 1278501429 241 LDIKQRLKVANLLRKHGSEKECA-VVVEHDLIMLDYLA 277
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFC 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
444-496 |
2.98e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 46.55 E-value: 2.98e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 444 LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILrDVIKKKEAS 496
Cdd:PRK11176 481 LSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAAL-DELQKNRTS 532
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
91-243 |
3.14e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 46.55 E-value: 3.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPQKKQImGLVGVNGIGKSTCLNILsgqlkpnlgNDFGEV-EGQKIIDffkGTEAQNYfeKLyttgleTSYKPQY-- 167
Cdd:PRK11176 363 NFKIPAGKTV-ALVGRSGSGKSTIANLL---------TRFYDIdEGEILLD---GHDLRDY--TL------ASLRNQVal 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 168 VEQIPRIFKGSVK-----ALLNKISEGDVNKVCNEL-------GIKHVLNRKVGD----ISGGELQRVAIAGALLKKSDF 231
Cdd:PRK11176 422 VSQNVHLFNDTIAnniayARTEQYSREQIEEAARMAyamdfinKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPI 501
|
170
....*....|..
gi 1278501429 232 LFIDEPSSYLDI 243
Cdd:PRK11176 502 LILDEATSALDT 513
|
|
| PRK14993 |
PRK14993 |
tetrathionate reductase subunit TtrB; |
21-64 |
3.37e-05 |
|
tetrathionate reductase subunit TtrB;
Pssm-ID: 184955 [Multi-domain] Cd Length: 244 Bit Score: 45.25 E-value: 3.37e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1278501429 21 CMNFCPINRTgkdciVEGADGKIVVEEELCIGCGICVNKCPFDA 64
Cdd:PRK14993 108 CVPVCPVQAT-----FQREDGIVVVDNKRCVGCAYCVQACPYDA 146
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
96-255 |
3.43e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 45.46 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDFFKGTEAQNYFEKLYTTGLetsykpqyveqiprIF 175
Cdd:PRK13633 34 KKGEFLVILGRNGSGKSTIAKHMNALLIPS--------EGKVYVDGLDTSDEENLWDIRNKAGM--------------VF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 176 KGSVKALLNKISEGDVNKVCNELGIKHVLNRKVGD------------------ISGGELQRVAIAGALLKKSDFLFIDEP 237
Cdd:PRK13633 92 QNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDeslkkvgmyeyrrhaphlLSGGQKQRVAIAGILAMRPECIIFDEP 171
|
170
....*....|....*...
gi 1278501429 238 SSYLDIKQRLKVANLLRK 255
Cdd:PRK13633 172 TAMLDPSGRREVVNTIKE 189
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
416-488 |
3.52e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 416 VRSVL--MKTPPSMIERLDLSHL-LKRKLSELSGGELQRVAIAECLSRD--ADVYLLDEPSAHL---DVEQRLNVAKILR 487
Cdd:PRK00635 446 IEEVLqgLKSRLSILIDLGLPYLtPERALATLSGGEQERTALAKHLGAEliGITYILDEPSIGLhpqDTHKLINVIKKLR 525
|
.
gi 1278501429 488 D 488
Cdd:PRK00635 526 D 526
|
|
| Fer4_7 |
pfam12838 |
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ... |
16-64 |
3.54e-05 |
|
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.
Pssm-ID: 463724 [Multi-domain] Cd Length: 51 Bit Score: 41.36 E-value: 3.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1278501429 16 GCDYvCMNFCPINRTGKDC-IVEGADGKIVVEEELCIGCGICVNKCPFDA 64
Cdd:pfam12838 3 GCGA-CVAACPVGAITLDEvGEKKGTKTVVIDPERCVGCGACVAVCPTGA 51
|
|
| PRK12769 |
PRK12769 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
2-71 |
3.58e-05 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183733 [Multi-domain] Cd Length: 654 Bit Score: 46.28 E-value: 3.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1278501429 2 RIVVVNKKKCTAGKGC----DYVCMNFCPinrtgKDCIVEGADGkIVVEEELCIGCGICVNKCPFDAVKVVNLP 71
Cdd:PRK12769 41 RITVIKHQQQRSAVTChhceDAPCARSCP-----NGAISHVDDS-IQVNQQKCIGCKSCVVACPFGTMQIVLTP 108
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
356-495 |
3.92e-05 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 46.55 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 356 VKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGK------------TDTSVKISYKPQYVQVenDD--------F 415
Cdd:TIGR01257 1962 VRPG-----ECFGLLGVNGAGKTTTFKMLTGDTTVTSGDatvagksiltniSDVHQNMGYCPQFDAI--DDlltgrehlY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 416 VRSVLMKTPPSMIER--------LDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILR 487
Cdd:TIGR01257 2035 LYARLRGVPAEEIEKvanwsiqsLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIV 2114
|
....*...
gi 1278501429 488 DVIKKKEA 495
Cdd:TIGR01257 2115 SIIREGRA 2122
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
211-242 |
4.05e-05 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 45.01 E-value: 4.05e-05
10 20 30
....*....|....*....|....*....|..
gi 1278501429 211 ISGGELQRVAIAGALLKKSDFLFIDEPSSYLD 242
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
211-278 |
4.07e-05 |
|
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: 46.16 E-value: 4.07e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 211 ISGGELQRVAIAGALLKKSD--FLFI-DEPSSYL---DIKQRLKVANLLRKHGSEkecAVVVEHDLIML---DYLAD 278
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSKRSTgrTLYIlDEPTTGLhfdDIKKLLEVLQRLVDKGNT---VVVIEHNLDVIktaDYIID 903
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
349-482 |
4.49e-05 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 44.39 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 349 LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPD---KGKT---DTSV--------KISYKPQyvqvenDD 414
Cdd:COG4136 17 LAPLSLTVAPG-----EILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVllnGRRLtalpaeqrRIGILFQ------DD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 415 --F-----VRSVLMKTPPS------------MIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:COG4136 86 llFphlsvGENLAFALPPTigraqrrarveqALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
....*..
gi 1278501429 476 VEQRLNV 482
Cdd:COG4136 166 AALRAQF 172
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
103-254 |
4.55e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 4.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQLKPNLGNDFGEV-----EGQKIIDFFKG-----TEAQNYFEKLyTTG--LETSYKPQYVEQ 170
Cdd:TIGR00956 92 VLGRPGSGCSTLLKTIASNTDGFHIGVEGVItydgiTPEEIKKHYRGdvvynAETDVHFPHL-TVGetLDFAARCKTPQN 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 ipRIFKGSVKALLNKISegDVnkVCNELGIKHVLNRKVGD-----ISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQ 245
Cdd:TIGR00956 171 --RPDGVSREEYAKHIA--DV--YMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT 244
|
....*....
gi 1278501429 246 RLKVANLLR 254
Cdd:TIGR00956 245 ALEFIRALK 253
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
363-475 |
4.62e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 45.11 E-value: 4.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKGktdtSVKISykPQYVQVENDDFVRS------------------------ 418
Cdd:PRK13647 30 EGSKTALLGPNGAGKSTLLLHLNGIYLPQRG----RVKVM--GREVNAENEKWVRSkvglvfqdpddqvfsstvwddvaf 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 419 --VLMKTPPSMIER--------LDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:PRK13647 104 gpVNMGLDKDEVERrveealkaVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLD 170
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
442-483 |
4.89e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 45.72 E-value: 4.89e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1278501429 442 SELSGGELQRVAIAECLSRDADVYLLDEPSAHLDV--EQRLNVA 483
Cdd:PRK13657 470 RQLSGGERQRLAIARALLKDPPILILDEATSALDVetEAKVKAA 513
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
91-296 |
4.98e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 46.12 E-value: 4.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPQKkQIMGLVGVNGIGKSTCLNILSGQLKPnlgndfgeVEGQKIIdfFKGTEAqnyfeklyttgletsykpqYVEQ 170
Cdd:PLN03232 637 NLEIPVG-SLVAIVGGTGEGKTSLISAMLGELSH--------AETSSVV--IRGSVA-------------------YVPQ 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 IPRIFKGSVKALL---NKISEGDVNKVCNELGIKHVLNRKVG-----------DISGGELQRVAIAGALLKKSDFLFIDE 236
Cdd:PLN03232 687 VSWIFNATVRENIlfgSDFESERYWRAIDVTALQHDLDLLPGrdlteigergvNISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 237 PSSYLDIKQRLKVANLLRKHGSEKECAVVVE---HDLIMLDYLADVEHIMYGRAGVYGIVSKS 296
Cdd:PLN03232 767 PLSALDAHVAHQVFDSCMKDELKGKTRVLVTnqlHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
428-485 |
5.05e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 44.90 E-value: 5.05e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 428 IERLDLSHLLKRKL----SELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEqrlNVAKI 485
Cdd:PRK14247 127 LEKAQLWDEVKDRLdapaGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPE---NTAKI 185
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
361-496 |
5.08e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 45.17 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 361 LMRNEIIGVLGENGTGKTTFAKILAGMIKPDKGK---TDTSVKI---SYKPQYVQVENDDFVRSVlmkTPPSMIER-LDL 433
Cdd:PRK15112 36 LREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGElliDDHPLHFgdySYRSQRIRMIFQDPSTSL---NPRQRISQiLDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 434 SHLLKRKLSE---------------------------LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKIL 486
Cdd:PRK15112 113 PLRLNTDLEPeqrekqiietlrqvgllpdhasyyphmLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLM 192
|
170
....*....|
gi 1278501429 487 RDVIKKKEAS 496
Cdd:PRK15112 193 LELQEKQGIS 202
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
212-242 |
5.55e-05 |
|
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: 45.58 E-value: 5.55e-05
10 20 30
....*....|....*....|....*....|.
gi 1278501429 212 SGGELQRVAIAGALLKKSDFLFIDEPSSYLD 242
Cdd:COG5265 496 SGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
92-270 |
6.18e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 44.77 E-value: 6.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 92 LVIPqKKQIMGLVGVNGIGKSTCLNILsgqlkpNLGNDFGE---VEGqKIidFFKGTEaqnyfekLYTTGL---ETSYKP 165
Cdd:PRK14243 31 LDIP-KNQITAFIGPSGCGKSTILRCF------NRLNDLIPgfrVEG-KV--TFHGKN-------LYAPDVdpvEVRRRI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 166 QYVEQIPRIFKGSVK---ALLNKIS--EGDVNKVCNELGIKHVLNRKVGD--------ISGGELQRVAIAGALLKKSDFL 232
Cdd:PRK14243 94 GMVFQKPNPFPKSIYdniAYGARINgyKGDMDELVERSLRQAALWDEVKDklkqsglsLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 1278501429 233 FIDEPSSYLDIKQRLKVANLLRKHGsEKECAVVVEHDL 270
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNM 210
|
|
| FDH-N |
cd10558 |
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ... |
21-63 |
6.75e-05 |
|
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups.
Pssm-ID: 319880 [Multi-domain] Cd Length: 208 Bit Score: 43.92 E-value: 6.75e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1278501429 21 CMNFCPinrtGKDCIVEGADGKIVVEEELCIGCGICVNKCPFD 63
Cdd:cd10558 78 CLKACP----SPGAIVQYANGIVDFQSDKCIGCGYCIKGCPFD 116
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
91-270 |
7.61e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 44.30 E-value: 7.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPqKKQIMGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEVEgqkiIDffkgteaqnyfeklyttGLE-TSYKPQYVE 169
Cdd:COG4604 21 SLTIP-KGGITALIGPNGAGKSTLLSMISRLLPP----DSGEVL----VD-----------------GLDvATTPSRELA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 170 QIPRIFKGS--------VKAL------------LNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKS 229
Cdd:COG4604 75 KRLAILRQEnhinsrltVRELvafgrfpyskgrLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1278501429 230 DFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDL 270
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVViVLHDI 196
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
100-274 |
7.92e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 43.79 E-value: 7.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 100 IMGLVGVNGIGKSTCLNILSGQLKPNLGNDFgeVEGQKIidffkGTEAQNYFEKLYTTGLETSYKPQYVEQIPRIFKGSV 179
Cdd:PRK13540 29 LLHLKGSNGAGKTTLLKLIAGLLNPEKGEIL--FERQSI-----KKDLCTYQKQLCFVGHRSGINPYLTLRENCLYDIHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 180 KALLNKISEgdvnkVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSE 259
Cdd:PRK13540 102 SPGAVGITE-----LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAK 176
|
170
....*....|....*
gi 1278501429 260 KECAVVVEHDLIMLD 274
Cdd:PRK13540 177 GGAVLLTSHQDLPLN 191
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
212-270 |
8.35e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 45.40 E-value: 8.35e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 212 SGGELQRVAIAGALLKKS--DFLFI-DEPSSYL---DIKQRLKVANLLRKHG-SekecAVVVEHDL 270
Cdd:COG0178 828 SGGEAQRVKLASELSKRStgKTLYIlDEPTTGLhfhDIRKLLEVLHRLVDKGnT----VVVIEHNL 889
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
211-249 |
8.73e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 44.95 E-value: 8.73e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1278501429 211 ISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKV 249
Cdd:PRK13657 472 LSGGERQRLAIARALLKDPPILILDEATSALDVETEAKV 510
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
97-288 |
9.38e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 44.31 E-value: 9.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 97 KKQIMGLVGVNGIGKSTCLNILSGQlkpnlgndFGEVEGQKIIDFFKGTeAQNYFEKLYTTGL-----ETSYKPQYVEQ- 170
Cdd:PRK13642 32 KGEWVSIIGQNGSGKSTTARLIDGL--------FEEFEGKVKIDGELLT-AENVWNLRRKIGMvfqnpDNQFVGATVEDd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 171 ---------IPRifkgsvKALLNKISEGDVnkVCNELGIKhvlNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYL 241
Cdd:PRK13642 103 vafgmenqgIPR------EEMIKRVDEALL--AVNMLDFK---TREPARLSGGQKQRVAVAGIIALRPEIIILDESTSML 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1278501429 242 DIKQRLKVANLLRKHGSEKECAVV-VEHDlimLDYLADVEHIMYGRAG 288
Cdd:PRK13642 172 DPTGRQEIMRVIHEIKEKYQLTVLsITHD---LDEAASSDRILVMKAG 216
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
99-242 |
1.04e-04 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 45.04 E-value: 1.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPNL-GNDFGEVEGQKI-IDFFKGTEAQNYFEKLYTTGLeTSYKPQYVE---QIPR 173
Cdd:TIGR00955 52 ELLAVMGSSGAGKTTLMNALAFRSPKGVkGSGSVLLNGMPIdAKEMRAISAYVQQDDLFIPTL-TVREHLMFQahlRMPR 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278501429 174 IFKGSVKALLnkisegdVNKVCNELGIKHVLNRKVGD------ISGGELQRVAIAGALLKKSDFLFIDEPSSYLD 242
Cdd:TIGR00955 131 RVTKKEKRER-------VDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
371-479 |
1.07e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.32 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 371 GENGTGKTTFAKILAGMIKPDKGK----------------TDTSVKISYKPQYVQVENDDFVRSVL--MKTPPSMIERLD 432
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNiyykncninniakpycTYIGHNLGLKLEMTVFENLKFWSEIYnsAETLYAAIHYFK 112
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1278501429 433 LSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQR 479
Cdd:PRK13541 113 LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
336-477 |
1.08e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.86 E-value: 1.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 336 NIPIIEWSNIEKKLGDFK------LKVKPGilmrnEIIGVLGENGTGKTTFAKILAG-----MIKPD---KGKTDTSVK- 400
Cdd:CHL00131 4 NKPILEIKNLHASVNENEilkglnLSINKG-----EIHAIMGPNGSGKSTLSKVIAGhpaykILEGDilfKGESILDLEp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 401 -------ISYKPQY----VQVENDDFVRSV---------LMKTPP----SMI-ERLDL----SHLLKRKLSE-LSGGELQ 450
Cdd:CHL00131 79 eerahlgIFLAFQYpieiPGVSNADFLRLAynskrkfqgLPELDPleflEIInEKLKLvgmdPSFLSRNVNEgFSGGEKK 158
|
170 180
....*....|....*....|....*..
gi 1278501429 451 RVAIAECLSRDADVYLLDEPSAHLDVE 477
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLDID 185
|
|
| PsrB |
cd10551 |
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial ... |
21-64 |
1.11e-04 |
|
polysulfide reductase beta (PsrB) subunit; This family includes the beta subunit of bacterial polysulfide reductase (PsrABC), an integral membrane-bound enzyme responsible for quinone-coupled reduction of polysulfides, a process important in extreme environments such as deep-sea vents and hot springs. Polysulfide reductase contains three subunits: a catalytic subunit PsrA, an electron transfer PsrB subunit and the hydrophobic transmembrane PsrC subunit. PsrB belongs to the DMSO reductase superfamily that contains [4Fe-4S] clusters which transfer the electrons from the A subunit to the hydrophobic integral membrane C subunit via the B subunit. In Shewanella oneidensis, which has highly diverse anaerobic respiratory pathways, PsrABC is responsible for H2S generation as well as its regulation via respiration of sulfur species. PsrB transfers electrons from PsrC (serving as quinol oxidase) to the catalytic subunit PsrA for reduction of corresponding electron acceptors. It has been shown that T. thermophilus polysulfide reductase could be a key energy-conserving enzyme of the respiratory chain, using polysulfide as the terminal electron acceptor and pumping protons across the membrane.
Pssm-ID: 319873 [Multi-domain] Cd Length: 185 Bit Score: 42.90 E-value: 1.11e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1278501429 21 CMNFCPINRTGKDcivegADGKIVVEEELCIGCGICVNKCPFDA 64
Cdd:cd10551 61 CVKVCPTGATYKR-----EDGIVLVDYDKCIGCRYCMAACPYGA 99
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
212-278 |
1.16e-04 |
|
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: 43.76 E-value: 1.16e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 212 SGGELQRVAIAGALLKKS--DFLFI-DEPSSYL---DIKQRLKVANLLRKHGSEkecAVVVEHDLIML---DYLAD 278
Cdd:cd03271 171 SGGEAQRIKLAKELSKRStgKTLYIlDEPTTGLhfhDVKKLLEVLQRLVDKGNT---VVVIEHNLDVIkcaDWIID 243
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
71-282 |
1.23e-04 |
|
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: 43.36 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 71 PDELESRMIHSYDKNG----FKLFNLvipqkkqimgLVGVNGIGKST----CLNILSGQLKPNL-GNDF-------GEVE 134
Cdd:cd03240 1 IDKLSIRNIRSFHERSeiefFSPLTL----------IVGQNGAGKTTiieaLKYALTGELPPNSkGGAHdpklireGEVR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 135 GQKIIDFfkgteaQNYFEKLYTtgletsykpqyVEQIPRIFKGSVKallnkISEGDVNKVcnelgikhvLNRKVGDISGG 214
Cdd:cd03240 71 AQVKLAF------ENANGKKYT-----------ITRSLAILENVIF-----CHQGESNWP---------LLDMRGRCSGG 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 215 E------LQRVAIAGALLKKSDFLFIDEPSSYLDIKQR-LKVANLLRKHGSEK-ECAVVVEHDLIMLDYLADVEHI 282
Cdd:cd03240 120 EkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENIeESLAEIIEERKSQKnFQLIVITHDEELVDAADHIYRV 195
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
92-270 |
1.24e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 43.96 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 92 LVIPQKKQImGLVGVNGIGKSTCLNILSGQLKPNLGNDfgEVEGQKIidffkgtEAQNYFEKLYTTGLetsykpqyVEQI 171
Cdd:PRK13647 26 LSIPEGSKT-ALLGPNGAGKSTLLLHLNGIYLPQRGRV--KVMGREV-------NAENEKWVRSKVGL--------VFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 172 P--RIFKGSVkalLNKISEGDVNKvcnELGIKHVLNRkVGD-----------------ISGGELQRVAIAGALLKKSDFL 232
Cdd:PRK13647 88 PddQVFSSTV---WDDVAFGPVNM---GLDKDEVERR-VEEalkavrmwdfrdkppyhLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 1278501429 233 FIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDL 270
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDV 198
|
|
| PreA |
COG1146 |
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ... |
41-64 |
1.24e-04 |
|
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];
Pssm-ID: 440761 [Multi-domain] Cd Length: 67 Bit Score: 40.08 E-value: 1.24e-04
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
364-492 |
1.33e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 43.50 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 364 NEIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVKISYKPQYV-QVENDDFVRSVLMK-TPPSMIERLDL-------- 433
Cdd:PRK14246 36 NSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIfQIDAIKLRKEVGMVfQQPNPFPHLSIydniaypl 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 434 -SHLLKRK---------------------------LSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKI 485
Cdd:PRK14246 116 kSHGIKEKreikkiveeclrkvglwkevydrlnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKL 195
|
....*..
gi 1278501429 486 LRDVIKK 492
Cdd:PRK14246 196 ITELKNE 202
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
91-242 |
1.51e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 44.02 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPqKKQIMGLVGVNGIGKST---CLNILSgqlKPNlgndfgevEGQKIIDffkGTEaqnyFEKLYTTGLETSYKpqy 167
Cdd:PRK11153 25 SLHIP-AGEIFGVIGASGAGKSTlirCINLLE---RPT--------SGRVLVD---GQD----LTALSEKELRKARR--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 168 veQIPRIFK-----------GSVkAL---LNKISEGDVNKVCNEL----GIKHVLNRKVGDISGGELQRVAIAGALLKKS 229
Cdd:PRK11153 83 --QIGMIFQhfnllssrtvfDNV-ALpleLAGTPKAEIKARVTELlelvGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170
....*....|...
gi 1278501429 230 DFLFIDEPSSYLD 242
Cdd:PRK11153 160 KVLLCDEATSALD 172
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
437-488 |
1.55e-04 |
|
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: 43.37 E-value: 1.55e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 437 LKRKLSELSGGELQRVAIAECLSRDAD---VYLLDEPSAHL---DVEQRLNVAKILRD 488
Cdd:cd03271 163 LGQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLhfhDVKKLLEVLQRLVD 220
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
211-269 |
1.62e-04 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 43.51 E-value: 1.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 211 ISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLK----VANLLRKHGSekeCAVVVEHD 269
Cdd:PRK11247 134 LSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEmqdlIESLWQQHGF---TVLLVTHD 193
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
363-469 |
1.79e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.11 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 363 RNEIIGVLGENGTGKTTFAKILAGMIKPDKGKTD-----TSVKIS--YKPQYVQVENDDfVRSVLM--------KTPPSM 427
Cdd:PRK13545 49 EGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDikgsaALIAISsgLNGQLTGIENIE-LKGLMMgltkekikEIIPEI 127
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1278501429 428 IERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDE 469
Cdd:PRK13545 128 IEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
340-489 |
1.87e-04 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 43.64 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 340 IEWSNIEKK----------LGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKtdtsvkisykpqyVQ 409
Cdd:PRK11153 2 IELKNISKVfpqggrtihaLNNVSLHIPAG-----EIFGVIGASGAGKSTLIRCINLLERPTSGR-------------VL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 410 VENDDFV-----------RSVLM------------------------KTPPSMI--------ERLDLSHLLKRKLSELSG 446
Cdd:PRK11153 64 VDGQDLTalsekelrkarRQIGMifqhfnllssrtvfdnvalplelaGTPKAEIkarvtellELVGLSDKADRYPAQLSG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1278501429 447 GELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDV 489
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDI 186
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
91-286 |
1.98e-04 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 43.13 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIPQKKqIMGLVGVNGIGKSTCLNILSGqlKPNLgndfgEVEGQKIIdfFKGteaQNYFEkLYTT-----GLETSYkp 165
Cdd:COG0396 20 NLTIKPGE-VHAIMGPNGSGKSTLAKVLMG--HPKY-----EVTSGSIL--LDG---EDILE-LSPDeraraGIFLAF-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 166 QYVEQIPRIfkgSV----KALLNKISEGD---------VNKVCNELGI-KHVLNRKV-GDISGGELQRVAIAGALLKKSD 230
Cdd:COG0396 84 QYPVEIPGV---SVsnflRTALNARRGEElsareflklLKEKMKELGLdEDFLDRYVnEGFSGGEKKRNEILQMLLLEPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278501429 231 FLFIDEPSSYLDIkQRLK-VANLLRKHGSEKECAVVVEHDLIMLDYL-ADVEHIMY-GR 286
Cdd:COG0396 161 LAILDETDSGLDI-DALRiVAEGVNKLRSPDRGILIITHYQRILDYIkPDFVHVLVdGR 218
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
198-285 |
2.01e-04 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 43.68 E-value: 2.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 198 LGIKHVLNRKVGDISGGELQRVAIAGALLKKSD-FLFiDEPSSYLDIKqrLKVA---NLLRKHGSEKECAVVVEHDLIML 273
Cdd:PRK11650 122 LELEPLLDRKPRELSGGQRQRVAMGRAIVREPAvFLF-DEPLSNLDAK--LRVQmrlEIQRLHRRLKTTSLYVTHDQVEA 198
|
90
....*....|..
gi 1278501429 274 DYLADVEHIMYG 285
Cdd:PRK11650 199 MTLADRVVVMNG 210
|
|
| Nar1 |
COG4624 |
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion]; |
7-69 |
2.11e-04 |
|
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
Pssm-ID: 443663 [Multi-domain] Cd Length: 450 Bit Score: 43.86 E-value: 2.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 7 NKKKCTAGKGCDYVCMNFCPINRTGKDCIVEGaDGKIVVEEELCIGCGICVNKCPFDAVKVVN 69
Cdd:COG4624 51 CPRCCLCCCCCCRCCVAISCIQVRGIIIIDKR-GPSIIRDKEKCKNCYPCVRACPVKAIKVDD 112
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
444-475 |
2.37e-04 |
|
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: 43.66 E-value: 2.37e-04
10 20 30
....*....|....*....|....*....|..
gi 1278501429 444 LSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALD 526
|
|
| PhsB_like |
cd10553 |
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This ... |
21-64 |
2.49e-04 |
|
uncharacterized beta subfamily of DMSO Reductase similar to Desulfonauticus sp PhsB; This family includes beta FeS subunits of anaerobic DMSO reductase (DMSOR) superfamily that have yet to be characterized. DMSOR consists of a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and the tungsten-containing formate dehydrogenase (FDH-T). Examples of heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319875 [Multi-domain] Cd Length: 146 Bit Score: 41.20 E-value: 2.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1278501429 21 CMNFCP---INRTGKDCIVegadgkiVVEEELCIGCGICVNKCPFDA 64
Cdd:cd10553 66 CVKACPtgaMQKREKDGIV-------YVDQELCIGCKACIEACPWGI 105
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
16-68 |
2.59e-04 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 42.86 E-value: 2.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 16 GCDyVCMNFCPInrtgkDCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:PRK06991 89 GCT-LCMQACPV-----DAIVGAPKQMHTVLADLCTGCDLCVPPCPVDCIDMV 135
|
|
| IorA |
COG4231 |
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ... |
42-69 |
2.60e-04 |
|
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];
Pssm-ID: 443375 [Multi-domain] Cd Length: 76 Bit Score: 39.64 E-value: 2.60e-04
10 20
....*....|....*....|....*...
gi 1278501429 42 KIVVEEELCIGCGICVNKCPFDAVKVVN 69
Cdd:COG4231 16 RYVIDEDKCTGCGACVKVCPADAIEEGD 43
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
347-487 |
2.67e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 43.56 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 347 KKLGDFKLKVKPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKTD-TSVKISYKPQYVQVEN------------- 412
Cdd:PRK10982 12 KALDNVNLKVRPH-----SIHALMGENGAGKSTLLKCLFGIYQKDSGSILfQGKEIDFKSSKEALENgismvhqelnlvl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 413 -----DD-----------FVRSVLM-KTPPSMIERLDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:PRK10982 87 qrsvmDNmwlgryptkgmFVDQDKMyRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170
....*....|..
gi 1278501429 476 VEQRLNVAKILR 487
Cdd:PRK10982 167 EKEVNHLFTIIR 178
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
198-242 |
2.69e-04 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 42.54 E-value: 2.69e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1278501429 198 LGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLD 242
Cdd:COG4525 122 VGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
73-243 |
2.83e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.34 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 73 ELESrMIHSYDKNG-FKLFNLVIPQKKQImGLVGVNGIGKSTCLNILSGQLKPnlgnDFGEV---EGQKIidffkGTEAQ 148
Cdd:PRK15064 321 EVEN-LTKGFDNGPlFKNLNLLLEAGERL-AIIGENGVGKTTLLRTLVGELEP----DSGTVkwsENANI-----GYYAQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 149 NY---FEKLYT-TGLETSYK-PQYVEQiprifkgSVKALLNKI--SEGDVNKvcnelgikhvlnrKVGDISGGELQRVAI 221
Cdd:PRK15064 390 DHaydFENDLTlFDWMSQWRqEGDDEQ-------AVRGTLGRLlfSQDDIKK-------------SVKVLSGGEKGRMLF 449
|
170 180
....*....|....*....|..
gi 1278501429 222 AGALLKKSDFLFIDEPSSYLDI 243
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDM 471
|
|
| flavo_MJ0208 |
TIGR02700 |
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of ... |
6-66 |
2.98e-04 |
|
archaeoflavoprotein, MJ0208 family; This model describes one of two paralogous families of archaealflavoprotein. The other, described by TIGR02699 and typified by the partially characterized AF1518 of Archaeoglobus fulgidus, is a homodimeric FMN-containing flavoprotein that accepts electrons from ferredoxin and can transfer them to various oxidoreductases. The function of this protein family is unknown. [Unknown function, General]
Pssm-ID: 131747 [Multi-domain] Cd Length: 234 Bit Score: 42.55 E-value: 2.98e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 6 VNKKKCtagKGCDyVCMNFCPinrtgKDCIVEgADGKIVVEEELCIGCGICVNKCPFDAVK 66
Cdd:TIGR02700 145 IDRKRC---KGCG-ICVDACP-----RSAIDM-VDGKAFIRLLKCVGCGKCKEACPYNAIH 195
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
180-284 |
3.03e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 42.73 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 180 KALLNKISEGDVNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSE 259
Cdd:PRK14246 123 KREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE 202
|
90 100
....*....|....*....|....*
gi 1278501429 260 KeCAVVVEHDLIMLDYLADVEHIMY 284
Cdd:PRK14246 203 I-AIVIVSHNPQQVARVADYVAFLY 226
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
371-491 |
3.14e-04 |
|
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: 41.82 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 371 GENGTGKTTFakILA---------------GMIKPD---KGKTDTSVKISYK----PQYVQVENDDFVRSVLMktppsmI 428
Cdd:cd03240 29 GQNGAGKTTI--IEAlkyaltgelppnskgGAHDPKlirEGEVRAQVKLAFEnangKKYTITRSLAILENVIF------C 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278501429 429 ERLDLSHLLKRKLSELSGGE------LQRVAIAECLSRDADVYLLDEPSAHLDVEqrlNVAKILRDVIK 491
Cdd:cd03240 101 HQGESNWPLLDMRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEE---NIEESLAEIIE 166
|
|
| DMSOR_beta_like |
cd10550 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
3-68 |
3.14e-04 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319872 [Multi-domain] Cd Length: 130 Bit Score: 40.64 E-value: 3.14e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 3 IVVVNKKKCTagkGCdYVCMNFCPINRTGKDcivegADGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:cd10550 74 AVVVDEDKCI---GC-GMCVEACPFGAIRVD-----PETGKAIKCDLCGGDPACVKVCPTGALEFV 130
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
437-475 |
3.18e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 42.52 E-value: 3.18e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1278501429 437 LKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:PRK14267 143 LNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANID 181
|
|
| PRK09898 |
PRK09898 |
ferredoxin-like protein; |
21-62 |
3.22e-04 |
|
ferredoxin-like protein;
Pssm-ID: 182135 [Multi-domain] Cd Length: 208 Bit Score: 42.13 E-value: 3.22e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1278501429 21 CMNFCPINRTGkdciVEGADGKIVVEEELCIGCGICVNKCPF 62
Cdd:PRK09898 131 CMNVCPIGAIT----WQQKEGCITVDHKRCIGCSACTTACPW 168
|
|
| PRK12809 |
PRK12809 |
putative oxidoreductase Fe-S binding subunit; Reviewed |
2-156 |
3.46e-04 |
|
putative oxidoreductase Fe-S binding subunit; Reviewed
Pssm-ID: 183762 [Multi-domain] Cd Length: 639 Bit Score: 43.09 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 2 RIVVVNKKKCTAGKGC----DYVCMNFCPINrtgkdcIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVV-NLPDELES 76
Cdd:PRK12809 41 RIHVVGKGQAANPVAChhcnNAPCVTACPVN------ALTFQSDSVQLDEQKCIGCKRCAIACPFGVVEMVdTIAQKCDL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 77 RMIHSydkNGFKLFNLVIP-QKKQIMGLVGVNGIGKSTCLNILSGQ----LKPNLGNDFGEVEGQKIIDFFKGTEAQNYF 151
Cdd:PRK12809 115 CNQRS---SGTQACIEVCPtQALRLMDDKGLQQIKVARQRKTAAGKassdAQPSRSAALLPVNSRKGADKISASERKTHF 191
|
....*
gi 1278501429 152 EKLYT 156
Cdd:PRK12809 192 GEIYC 196
|
|
| Fer |
COG1141 |
Ferredoxin [Energy production and conversion]; |
42-75 |
3.70e-04 |
|
Ferredoxin [Energy production and conversion];
Pssm-ID: 440756 [Multi-domain] Cd Length: 63 Bit Score: 38.71 E-value: 3.70e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1278501429 42 KIVVEEELCIGCGICVNKCP--FD-------AVKVVNLPDELE 75
Cdd:COG1141 2 KVTVDRDTCIGCGLCVALAPevFEldddgkaVVLDEEVPEELE 44
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
198-314 |
3.73e-04 |
|
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: 42.29 E-value: 3.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 198 LGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSE-KECAVVVEHDLIMLDYL 276
Cdd:cd03295 123 LDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRL 202
|
90 100 110
....*....|....*....|....*....|....*....
gi 1278501429 277 ADVEHIMY-GRAGVYGivSKSLSIRECINTYLEGYIRED 314
Cdd:cd03295 203 ADRIAIMKnGEIVQVG--TPDEILRSPANDFVAEFVGAD 239
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
431-482 |
4.48e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.28 E-value: 4.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1278501429 431 LDLSHL-LKRKLSELSGGELQRVAIAECL---SRDADVYLLDEPSAHL---DVEQRLNV 482
Cdd:PRK00635 796 LGLDYLpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLhthDIKALIYV 854
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
198-270 |
4.75e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 198 LGIKHV-LNRKVGDISGGELQRVAIAGALL---KKSDFLFIDEPSSYL---DIKQRLKVANLLRKHGsekECAVVVEHDL 270
Cdd:PRK00635 796 LGLDYLpLGRPLSSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLhthDIKALIYVLQSLTHQG---HTVVIIEHNM 872
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
96-284 |
5.09e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 41.92 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 96 QKKQIMGLVGVNGIGKSTCLNILSGQLKPNLGN----DFGEVEGQKIIDFFKGTEAQnyfeklytTGLETSYkPQYveqi 171
Cdd:PRK13645 35 KKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQtivgDYAIPANLKKIKEVKRLRKE--------IGLVFQF-PEY---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 172 pRIFKGSVKallNKISEGDVN----------KVCNELGI----KHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEP 237
Cdd:PRK13645 102 -QLFQETIE---KDIAFGPVNlgenkqeaykKVPELLKLvqlpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1278501429 238 SSYLDIKQRLKVANL-LRKHGSEKECAVVVEHDLIMLDYLADVEHIMY 284
Cdd:PRK13645 178 TGGLDPKGEEDFINLfERLNKEYKKRIIMVTHNMDQVLRIADEVIVMH 225
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
437-488 |
5.33e-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: 42.69 E-value: 5.33e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 437 LKRKLSELSGGELQRVAIAECLSRDAD---VYLLDEPSAHL---DVEQRLNVAKILRD 488
Cdd:TIGR00630 823 LGQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLhfdDIKKLLEVLQRLVD 880
|
|
| PRK08764 |
PRK08764 |
Rnf electron transport complex subunit RnfB; |
16-68 |
5.46e-04 |
|
Rnf electron transport complex subunit RnfB;
Pssm-ID: 181550 [Multi-domain] Cd Length: 135 Bit Score: 40.29 E-value: 5.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 16 GCDYvCMNFCPInrtgkDCIVEGADGKIVVEEELCIGCGICVNKCPFDAVKVV 68
Cdd:PRK08764 89 GCTK-CIQACPV-----DAIVGGAKHMHTVIAPLCTGCELCVPACPVDCIELH 135
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
212-242 |
5.63e-04 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 41.52 E-value: 5.63e-04
10 20 30
....*....|....*....|....*....|.
gi 1278501429 212 SGGELQRVAIAGALLKKSDFLFIDEPSSYLD 242
Cdd:COG1126 138 SGGQQQRVAIARALAMEPKVMLFDEPTSALD 168
|
|
| sulfite_red_C |
TIGR02912 |
sulfite reductase, subunit C; Members of this protein family include the C subunit, one of ... |
16-64 |
5.78e-04 |
|
sulfite reductase, subunit C; Members of this protein family include the C subunit, one of three subunits, of the anaerobic sulfite reductase of Salmonella, and close homologs from various Clostridum species, where the three-gene neighborhood is preserved. Two such gene clusters are found in Clostridium perfringens, but it may be that these sets of genes correspond to the distinct assimilatory and dissimilatory forms as seen in Clostridium pasteurianum. Note that any one of these enzymes may have secondary substates such as NH2OH, SeO3(2-), and SO3(2-). Heterologous expression of the anaerobic sulfite reductase of Salmonella confers on Escherichia coli the ability to produce hydrogen sulfide gas from sulfite. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 131958 [Multi-domain] Cd Length: 314 Bit Score: 42.16 E-value: 5.78e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1278501429 16 GCDyVCMNFCPINRTGKdciVEGADGKIVVEEELCIGCGICVNKCPFDA 64
Cdd:TIGR02912 173 GCG-ACVKVCKKKAVGA---LSFENYKVVRDHSKCIGCGECVLKCPTGA 217
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
69-284 |
6.00e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 41.81 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 69 NLPDELESR--MIHSYDKngfklFNLVIpQKKQIMGLVGVNGIGKSTCLNILSGQLKPNL----------GNDF------ 130
Cdd:COG4170 8 NLTIEIDTPqgRVKAVDR-----VSLTL-NEGEIRGLVGESGSGKSLIAKAICGITKDNWhvtadrfrwnGIDLlklspr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 131 --GEVEGQKIIDFFKgtEAQNYFEKLYTTGletsykPQYVEQIPRI-FKGS-----------VKALLNKIsegdvnkvcn 196
Cdd:COG4170 82 erRKIIGREIAMIFQ--EPSSCLDPSAKIG------DQLIEAIPSWtFKGKwwqrfkwrkkrAIELLHRV---------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 197 elGIK---HVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVV-VEHDLIM 272
Cdd:COG4170 144 --GIKdhkDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILlISHDLES 221
|
250
....*....|..
gi 1278501429 273 LDYLADVEHIMY 284
Cdd:COG4170 222 ISQWADTITVLY 233
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
99-257 |
6.00e-04 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 41.42 E-value: 6.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILSGQLKPNlgndfgevEGQKIIDffkgtEAQNYFEKLYTTGLE-TSYKPQYVEQIPR--IF 175
Cdd:PRK10895 30 EIVGLLGPNGAGKTTTFYMVVGIVPRD--------AGNIIID-----DEDISLLPLHARARRgIGYLPQEASIFRRlsVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 176 KGSVKAL-----LNKISEGD-VNKVCNELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDE------PSSYLDI 243
Cdd:PRK10895 97 DNLMAVLqirddLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEpfagvdPISVIDI 176
|
170
....*....|....
gi 1278501429 244 KqrlKVANLLRKHG 257
Cdd:PRK10895 177 K---RIIEHLRDSG 187
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
212-278 |
6.04e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 42.75 E-value: 6.04e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 212 SGGELQRVAIAGALLKKSD--FLFI-DEPSSYL---DIKQRLKVANLLRKHGSEkecAVVVEHDLIML---DYLAD 278
Cdd:PRK00349 832 SGGEAQRVKLAKELSKRSTgkTLYIlDEPTTGLhfeDIRKLLEVLHRLVDKGNT---VVVIEHNLDVIktaDWIID 904
|
|
| oorD |
PRK09626 |
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed |
4-99 |
7.07e-04 |
|
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed
Pssm-ID: 236597 [Multi-domain] Cd Length: 103 Bit Score: 38.93 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 4 VVVNKKKCtagKGCDyVCMNFCPINRTGKDCIVEGADGKI--VVEEELCIGCGICVNKCPFDAVKVVnlpdelesrmihs 81
Cdd:PRK09626 11 VWVDESRC---KACD-ICVSVCPAGVLAMRIDPHAVLGKMikVVHPESCIGCRECELHCPDFAIYVA------------- 73
|
90
....*....|....*...
gi 1278501429 82 yDKNGFKlFNLVIPQKKQ 99
Cdd:PRK09626 74 -DRKEFK-FAKLSKEAKE 89
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
444-491 |
7.41e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 7.41e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 444 LSGGELQRVAIAECLSRDAD---VYLLDEPSAHL---DVEQRLNVAKILR-------------DVIK 491
Cdd:COG0178 827 LSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhfhDIRKLLEVLHRLVdkgntvvviehnlDVIK 893
|
|
| Fer4_6 |
pfam12837 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
42-64 |
7.53e-04 |
|
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 432822 [Multi-domain] Cd Length: 24 Bit Score: 36.82 E-value: 7.53e-04
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
444-488 |
8.30e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 8.30e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 444 LSGGELQRVAIAECLSRDAD---VYLLDEPSAHL---DVEQRLNVAKILRD 488
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLhfeDIRKLLEVLHRLVD 881
|
|
| DMSOR_beta_like |
cd16369 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
20-72 |
8.42e-04 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319891 [Multi-domain] Cd Length: 172 Bit Score: 40.45 E-value: 8.42e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 20 VCMNFCPInrtgkDCIVEGADGkiVVE---EELCIGCGICVNKCPFDAVKVVNLPD 72
Cdd:cd16369 58 TCAEVCPA-----DAIKVTEDG--VVQsalKPRCIGCSNCVNACPFGVPKYDEERN 106
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
211-275 |
8.45e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 8.45e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 211 ISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRK-HGSEKECAVVVEHDLIMLDY 275
Cdd:PTZ00265 580 LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNlKGNENRITIIIAHRLSTIRY 645
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
444-496 |
9.12e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 41.94 E-value: 9.12e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 444 LSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKKEAS 496
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKT 1411
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
445-488 |
1.02e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.10 E-value: 1.02e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1278501429 445 SGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRD 488
Cdd:PRK11308 156 SGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMD 199
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
97-246 |
1.05e-03 |
|
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: 39.66 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 97 KKQIMGLVGVNGIGKSTCLNILSGQLKPNLGndfgeveGQKIIDffkgteAQNYFEKLYttgletsykpqyveqiprifk 176
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGG-------GVIYID------GEDILEEVL--------------------- 46
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 177 gsvkallnkisegdvnkvcnELGIKHVLNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQR 246
Cdd:smart00382 47 --------------------DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQE 96
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
444-475 |
1.14e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 40.91 E-value: 1.14e-03
10 20 30
....*....|....*....|....*....|..
gi 1278501429 444 LSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
91-283 |
1.35e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 91 NLVIpQKKQIMGLVGVNGIGKSTCLNILSGQlkPNLGNDFGEV--EGQKIIDFFKGTEAQnyfeklytTGLETSYkpQYV 168
Cdd:CHL00131 27 NLSI-NKGEIHAIMGPNGSGKSTLSKVIAGH--PAYKILEGDIlfKGESILDLEPEERAH--------LGIFLAF--QYP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 169 EQIP--------RIFKGSVKALLNKiSEGD-------VNKVCNELGIK-HVLNRKVGD-ISGGELQRVAIAGALLKKSDF 231
Cdd:CHL00131 94 IEIPgvsnadflRLAYNSKRKFQGL-PELDplefleiINEKLKLVGMDpSFLSRNVNEgFSGGEKKRNEILQMALLDSEL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 232 LFIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIMLDYLA-DVEHIM 283
Cdd:CHL00131 173 AILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHVM 225
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
197-291 |
1.38e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 197 ELGIKHV-LNRKVGDISGGELQRVAIA---GALLKKSDFLfIDEPSSYLDIKQRLKVANLLRKHGSEKECAVVVEHDLIM 272
Cdd:PRK00635 462 DLGLPYLtPERALATLSGGEQERTALAkhlGAELIGITYI-LDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQM 540
|
90
....*....|....*....
gi 1278501429 273 LDyLADVEHIMYGRAGVYG 291
Cdd:PRK00635 541 IS-LADRIIDIGPGAGIFG 558
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
170-275 |
1.39e-03 |
|
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: 40.17 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 170 QIPRIFKGSVKALL---NKISEGDVNKVCNELGIKHVLNRKVG-----------DISGGELQRVAIAGALLKKSDFLFID 235
Cdd:cd03244 85 QDPVLFSGTIRSNLdpfGEYSDEELWQALERVGLKEFVESLPGgldtvveeggeNLSVGQRQLLCLARALLRKSKILVLD 164
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1278501429 236 EPSSYLDIKQRLKVANLLRKHgsEKECAVV-VEHDL-IMLDY 275
Cdd:cd03244 165 EATASVDPETDALIQKTIREA--FKDCTVLtIAHRLdTIIDS 204
|
|
| PorD |
COG1144 |
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ... |
42-69 |
1.48e-03 |
|
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation
Pssm-ID: 440759 [Multi-domain] Cd Length: 84 Bit Score: 37.72 E-value: 1.48e-03
10 20
....*....|....*....|....*...
gi 1278501429 42 KIVVEEELCIGCGICVNKCPFDAVKVVN 69
Cdd:COG1144 24 RPVVDEDKCIGCGLCWIVCPDGAIRVDD 51
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
8-76 |
1.56e-03 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 40.30 E-value: 1.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1278501429 8 KKKCTAG-KGCDyVCMNFCPinrtgKDCI-VEgaDGKIVVEEELCIGCGICVNKCPFDAVKVVNLPDELES 76
Cdd:PRK07118 208 KKVCEVGcIGCG-KCVKACP-----AGAItME--NNLAVIDQEKCTSCGKCVEKCPTKAIRILNKPPKVKE 270
|
|
| NapF_like |
cd10564 |
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ... |
44-70 |
1.70e-03 |
|
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319886 [Multi-domain] Cd Length: 139 Bit Score: 38.76 E-value: 1.70e-03
10 20
....*....|....*....|....*..
gi 1278501429 44 VVEEELCIGCGICVNKCPFDAVKVVNL 70
Cdd:cd10564 113 ELDADACTGCGACVSVCPVGAITLTPL 139
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
103-255 |
1.76e-03 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 39.55 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQLKPNLGND----FGEVEGQKIIDFFKGteaqnyfeklyttglETSYKPQYVEQIPRIfkgS 178
Cdd:cd03233 38 VLGRPGSGCSTLLKALANRTEGNVSVEgdihYNGIPYKEFAEKYPG---------------EIIYVSEEDVHFPTL---T 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 179 VKALLnkisegDVNKVCNElgikhvlNRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRK 255
Cdd:cd03233 100 VRETL------DFALRCKG-------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKCIRT 163
|
|
| HybA |
COG0437 |
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and ... |
3-77 |
1.81e-03 |
|
Fe-S-cluster-containing dehydrogenase component (DMSO reductase) [Energy production and conversion];
Pssm-ID: 440206 [Multi-domain] Cd Length: 184 Bit Score: 39.54 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 3 IVVVNKKKCTagkGCDYvCMNFCP-----INRTgkdcivegaDGKIvveeELCIGCG---------ICVNKCPFDAVKVV 68
Cdd:COG0437 84 IVLVDYDKCI---GCRY-CVAACPygaprFNPE---------TGVV----EKCTFCAdrldegllpACVEACPTGALVFG 146
|
....*....
gi 1278501429 69 NLpDELESR 77
Cdd:COG0437 147 DL-DDPESE 154
|
|
| PRK07118 |
PRK07118 |
Fe-S cluster domain-containing protein; |
15-61 |
1.92e-03 |
|
Fe-S cluster domain-containing protein;
Pssm-ID: 235941 [Multi-domain] Cd Length: 280 Bit Score: 40.30 E-value: 1.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 15 KGCDYVCM------NFCPInrtgkdciveGA----DGKIVVEEELCIGCGICVNKCP 61
Cdd:PRK07118 135 KGCSYGCLglgscvAACPF----------DAihieNGLPVVDEDKCTGCGACVKACP 181
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
44-65 |
2.01e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 40.16 E-value: 2.01e-03
|
| CooF_like |
cd10563 |
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the ... |
21-66 |
2.13e-03 |
|
CooF, iron-sulfur subunit of carbon monoxide dehydrogenase; This family includes CooF, the iron-sulfur subunit of carbon monoxide dehydrogenase (CODH), found in anaerobic bacteria and archaea. Carbon monoxide dehydrogenase is a key enzyme for carbon monoxide (CO) metabolism, where CooF is the proposed mediator of electron transfer between CODH and the CO-induced hydrogenase, catalyzing the reaction that uses CO as a single carbon and energy source, and producing only H2 and CO2. The ion-sulfur subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons in the protein complex during reaction.
Pssm-ID: 319885 [Multi-domain] Cd Length: 140 Bit Score: 38.39 E-value: 2.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1278501429 21 CMNFCPinrTG---KDciveGADGKIVVEEELCIGCGICVNKCPFDAVK 66
Cdd:cd10563 65 CVKACM---SGamhKD----PETGIVIHDEEKCVGCWMCVMVCPYGAIR 106
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
207-246 |
2.16e-03 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 40.17 E-value: 2.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 1278501429 207 KVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQR 246
Cdd:PRK13537 135 KVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQAR 174
|
|
| Fer4_10 |
pfam13237 |
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ... |
42-71 |
2.29e-03 |
|
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 404174 [Multi-domain] Cd Length: 56 Bit Score: 36.46 E-value: 2.29e-03
10 20 30
....*....|....*....|....*....|
gi 1278501429 42 KIVVEEELCIGCGICVNKCPFDAVKVVNLP 71
Cdd:pfam13237 1 KVVIDPDKCIGCGRCTAACPAGLTRVGAIV 30
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
16-66 |
2.45e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319892 [Multi-domain] Cd Length: 131 Bit Score: 38.02 E-value: 2.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 16 GCDY-VCMNFCPInrtgkDCIVEGADGKIVVEEELCIGCGICVNKCPFDAVK 66
Cdd:cd16370 55 ACEDpPCAEACPT-----GALEPRKGGGVVLDKEKCIGCGNCVKACIVGAIF 101
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
103-242 |
2.57e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 39.47 E-value: 2.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 103 LVGVNGIGKSTCLNILSGQLKPNLGndfgevegqKIidFFKGTEaqnyfeklyTTGLETSYKPQYVEQIPRIFKG----- 177
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAG---------KI--WFSGHD---------ITRLKNREVPFLRRQIGMIFQDhhllm 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1278501429 178 --------SVKALLNKISEGDVNK-VCNELGIKHVLNRKVG---DISGGELQRVAIAGALLKKSDFLFIDEPSSYLD 242
Cdd:PRK10908 93 drtvydnvAIPLIIAGASGDDIRRrVSAALDKVGLLDKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| Fer4_2 |
pfam12797 |
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ... |
41-62 |
2.70e-03 |
|
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.
Pssm-ID: 463711 [Multi-domain] Cd Length: 22 Bit Score: 35.07 E-value: 2.70e-03
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
351-475 |
2.71e-03 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 39.47 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 351 DFKLKvkPGilmrnEIIGVLGENGTGKTTFAKILAGMIKPDKGKT-----DTS-VKISYKP----QYVQVENDDFV---R 417
Cdd:PRK10908 22 TFHMR--PG-----EMAFLTGHSGAGKSTLLKLICGIERPSAGKIwfsghDITrLKNREVPflrrQIGMIFQDHHLlmdR 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1278501429 418 SVLMKTPPSMIERLDLSHLLKRKLS-----------------ELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIRRRVSaaldkvglldkaknfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
205-273 |
2.73e-03 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 39.68 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 205 NRKVGDISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRK--HGSEK---------ECAVVVEHDLIML 273
Cdd:PRK11248 123 KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKqvllithdiEEAVFMATELVLL 202
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
437-489 |
2.86e-03 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 39.38 E-value: 2.86e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 437 LKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDV 489
Cdd:PRK14243 145 LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL 197
|
|
| Fer4_9 |
pfam13187 |
4Fe-4S dicluster domain; |
50-79 |
3.08e-03 |
|
4Fe-4S dicluster domain;
Pssm-ID: 463801 [Multi-domain] Cd Length: 50 Bit Score: 35.61 E-value: 3.08e-03
10 20 30
....*....|....*....|....*....|
gi 1278501429 50 CIGCGICVNKCPFDAVKVVNLPDELESRMI 79
Cdd:pfam13187 2 CTGCGACVAACPAGAIVPDLVGQTIRGDIA 31
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
433-488 |
3.10e-03 |
|
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: 40.38 E-value: 3.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 433 LSHL-LKRKLSELSGGELQRVAIAECL-SRDADV-YLLDEPSAHL---DVEQRLNVAKILRD 488
Cdd:TIGR00630 477 LDYLsLSRAAGTLSGGEAQRIRLATQIgSGLTGVlYVLDEPSIGLhqrDNRRLINTLKRLRD 538
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
99-250 |
3.16e-03 |
|
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: 39.45 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 99 QIMGLVGVNGIGKSTCLNILsgqLKpnLGNDFGEVEgqkiIDffkGTEAQnyfeklyTTGLETSYK-----PQYVeqipR 173
Cdd:cd03289 31 QRVGLLGRTGSGKSTLLSAF---LR--LLNTEGDIQ----ID---GVSWN-------SVPLQKWRKafgviPQKV----F 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 174 IFKGSVKALLN---KISEGDVNKVCNELGIKHVLNRKVGDI-----------SGGELQRVAIAGALLKKSDFLFIDEPSS 239
Cdd:cd03289 88 IFSGTFRKNLDpygKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
170
....*....|....*..
gi 1278501429 240 YLD------IKQRLKVA 250
Cdd:cd03289 168 HLDpityqvIRKTLKQA 184
|
|
| porD |
PRK09625 |
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed |
5-61 |
3.28e-03 |
|
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
Pssm-ID: 236596 [Multi-domain] Cd Length: 133 Bit Score: 37.80 E-value: 3.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1278501429 5 VVNKKKCTagkGCDYvCMNFCPinrtgkDCIVEGADGKIV-VEEELCIGCGICVNKCP 61
Cdd:PRK09625 55 VHNNEICI---NCFN-CWVYCP------DAAILSRDKKLKgVDYSHCKGCGVCVEVCP 102
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
168-242 |
3.32e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.40 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 168 VEQIPRIFKGSV----KALLNKISEGDVNKVCNELGIKHVL-------NRKVG----DISGGELQRVAIAGALLKKSDFL 232
Cdd:PTZ00265 1301 VSQEPMLFNMSIyeniKFGKEDATREDVKRACKFAAIDEFIeslpnkyDTNVGpygkSLSGGQKQRIAIARALLREPKIL 1380
|
90
....*....|
gi 1278501429 233 FIDEPSSYLD 242
Cdd:PTZ00265 1381 LLDEATSSLD 1390
|
|
| Fer4_16 |
pfam13484 |
4Fe-4S double cluster binding domain; |
50-105 |
3.45e-03 |
|
4Fe-4S double cluster binding domain;
Pssm-ID: 463893 [Multi-domain] Cd Length: 65 Bit Score: 35.93 E-value: 3.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 50 CIGCGICVNKCPFDAVKVVnlPDELESRMIHSYDKNGFKLFNLVIPQKKQIMGLVG 105
Cdd:pfam13484 1 CGSCGKCIDACPTGAIVGP--EGVLDARRCISYLTIEKKGLIPDELRCLLGNRCYG 54
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
443-488 |
3.87e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 39.69 E-value: 3.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1278501429 443 ELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRD 488
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRE 201
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
437-475 |
4.24e-03 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 38.86 E-value: 4.24e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1278501429 437 LKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLD 475
Cdd:COG1117 148 LKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD 186
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
212-286 |
4.48e-03 |
|
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: 38.18 E-value: 4.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278501429 212 SGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHgSEKECAVVV---EHDLIMldYLADVEHIMY-GR 286
Cdd:cd03215 106 SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLissELDELL--GLCDRILVMYeGR 181
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
438-487 |
4.69e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 38.82 E-value: 4.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 438 KRKLSELSGGelQRVAIAECL------SRDADVYLLDEPSAHLDVEQRLNVAKILR 487
Cdd:cd03273 161 KESLTELSGG--QRSLVALSLilalllFKPAPMYILDEVDAALDLSHTQNIGRMIK 214
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
119-274 |
4.72e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 38.91 E-value: 4.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 119 SGQLKPNLGNDFGEVEGQKIIDFFKGTEAQNYFEKLYTTGLETSYKPQYVEQIPRIF-------KGSVKALLNKISEGDV 191
Cdd:pfam13304 140 SGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLADlnlsdlgEGIEKSLLVDDRLRER 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 192 NKVCNELGIKHVLNrkVGDISGGELQRVAIAGALL---KKSDFLFIDEPSSYLDIKQRLKVANLLRKHgSEKECAVVVE- 267
Cdd:pfam13304 220 GLILLENGGGGELP--AFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKEL-SRNGAQLILTt 296
|
....*..
gi 1278501429 268 HDLIMLD 274
Cdd:pfam13304 297 HSPLLLD 303
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
395-489 |
4.92e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 39.63 E-value: 4.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 395 TDTSVKISYKPQYVQVENDDFV---RSVLMKTPPSMI-ERLDLshLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEP 470
Cdd:PTZ00265 529 TDSNELIEMRKNYQTIKDSEVVdvsKKVLIHDFVSALpDKYET--LVGSNASKLSGGQKQRISIARAIIRNPKILILDEA 606
|
90
....*....|....*....
gi 1278501429 471 SAHLDVEQRLNVAKILRDV 489
Cdd:PTZ00265 607 TSSLDNKSEYLVQKTINNL 625
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
444-491 |
5.10e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 39.50 E-value: 5.10e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1278501429 444 LSGGELQ------RVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIK 491
Cdd:PRK01156 802 LSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLK 855
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
204-291 |
5.16e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.62 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 204 LNRKVGDISGGELQRVAIAGAL---LkkSDFLFI-DEPSSYL---DIkQRLkVANL--LRKHGSekeCAVVVEHDL-IML 273
Cdd:COG0178 479 LDRSAGTLSGGEAQRIRLATQIgsgL--VGVLYVlDEPSIGLhqrDN-DRL-IETLkrLRDLGN---TVIVVEHDEdTIR 551
|
90 100
....*....|....*....|.
gi 1278501429 274 --DYLADVehimyG-RAGVYG 291
Cdd:COG0178 552 aaDYIIDI-----GpGAGEHG 567
|
|
| DMSOR_beta_like |
cd16372 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
21-69 |
5.33e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319894 [Multi-domain] Cd Length: 125 Bit Score: 36.93 E-value: 5.33e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1278501429 21 CMNFCPINRTGKDcivegADGKIVVEEELCIGCGICVNKCPFDAVKVVN 69
Cdd:cd16372 55 CIDVCPTGAITRD-----ANGVVMINKKLCVGCLMCVGFCPEGAMFKHE 98
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
211-285 |
5.39e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 38.95 E-value: 5.39e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1278501429 211 ISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLLRKHGSEKECA-VVVEHDLIMldyLADVEH---IMYG 285
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMAlVLITHDLAL---VAEAAHkiiVMYA 229
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
371-417 |
5.46e-03 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 39.33 E-value: 5.46e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1278501429 371 GENGTGKTTFAKILAGmIKPDKGKTDTSVKISYK------PQYVQVENDDFVR 417
Cdd:COG4694 31 GENGSGKSTLSRILRS-LELGDTSSEVIAEFEIEaggsapNPSVRVFNRDFVE 82
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
91-127 |
5.49e-03 |
|
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: 38.28 E-value: 5.49e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1278501429 91 NLVIPQKKQImGLVGVNGIGKSTCLNILSGQLKPNLG 127
Cdd:cd03220 42 SFEVPRGERI-GLIGRNGAGKSTLLRLLAGIYPPDSG 77
|
|
| PRK13984 |
PRK13984 |
putative oxidoreductase; Provisional |
48-72 |
5.76e-03 |
|
putative oxidoreductase; Provisional
Pssm-ID: 172486 [Multi-domain] Cd Length: 604 Bit Score: 39.36 E-value: 5.76e-03
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
210-284 |
5.80e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 39.02 E-value: 5.80e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 210 DISGGELQRVAIAGALLKKSDFLFIDEPSSYLDIKQRLKVANLL-RKHGSEKECAVVVEHDLIMLDYLADVEHIMY 284
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLtRLNQNNNTTILLISHDLQMLSQWADKINVLY 233
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
438-476 |
7.20e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.07 E-value: 7.20e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1278501429 438 KRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDV 476
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
432-493 |
7.62e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 38.14 E-value: 7.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1278501429 432 DLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDEPSAHLDVEQRLNVAKILRDVIKKK 493
Cdd:PRK10418 129 NAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKR 190
|
|
| DMSOR_beta_like |
cd16370 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
4-63 |
7.96e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319892 [Multi-domain] Cd Length: 131 Bit Score: 36.48 E-value: 7.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 4 VVVNKKKCTagkGCDYvCMNFCPINRTGKDciveGADGKIVVeeelCIGCGICVNKCPFD 63
Cdd:cd16370 78 VVLDKEKCI---GCGN-CVKACIVGAIFWD----EETNKPII----CIHCGYCARYCPHD 125
|
|
| DMSOR_beta_like |
cd16373 |
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ... |
15-65 |
8.12e-03 |
|
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.
Pssm-ID: 319895 [Multi-domain] Cd Length: 154 Bit Score: 37.23 E-value: 8.12e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1278501429 15 KGCDYvCMNFC----PinrTG--KDCIVEGAD---GKIVVEEELCI------GCGICVNKCPFDAV 65
Cdd:cd16373 53 GPCDL-CCDACvevcP---TGalRPLDLEEQKvkmGVAVIDKDRCLawqggtDCGVCVEACPTEAI 114
|
|
| PRK06273 |
PRK06273 |
ferredoxin; Provisional |
45-70 |
9.82e-03 |
|
ferredoxin; Provisional
Pssm-ID: 235764 [Multi-domain] Cd Length: 165 Bit Score: 37.00 E-value: 9.82e-03
10 20
....*....|....*....|....*.
gi 1278501429 45 VEEELCIGCGICVNKCPFDAVKVVNL 70
Cdd:PRK06273 46 VFEELCIGCGGCANVCPTKAIEMIPV 71
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
365-469 |
9.83e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 37.87 E-value: 9.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1278501429 365 EIIGVLGENGTGKTTFAKILAGMIKPDKGKTDTSVKIS-------YKPQYVQVENDDF-------VRSVLMKTPPSMIER 430
Cdd:PRK13546 51 DVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSviaisagLSGQLTGIENIEFkmlcmgfKRKEIKAMTPKIIEF 130
|
90 100 110
....*....|....*....|....*....|....*....
gi 1278501429 431 LDLSHLLKRKLSELSGGELQRVAIAECLSRDADVYLLDE 469
Cdd:PRK13546 131 SELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
|
| |
