|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
28-613 |
6.59e-137 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 412.90 E-value: 6.59e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 28 KKPEKkSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVSG---------KIEIGKARKLCGYIMQDDHFFP 98
Cdd:TIGR00955 34 ERPRK-HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGsgsvllngmPIDAKEMRAISAYVQQDDLFIP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 99 YFTVEETMLMAATLKISNQcVSLKEKRTLIDYLLNSLKLTKTRQTK------CSNLSGGQKKRLSIALELIDNPAVLFLD 172
Cdd:TIGR00955 113 TLTVREHLMFQAHLRMPRR-VTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 173 EPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIYNLFNLVYVLSAGRCTYQGTPQNTVMFLSSVGLECPPYHNP 252
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLGHPCPENYNP 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 253 ADFLLECANGDYGDQTEALAEAAKDIRwrydqqlmqgEDADAPSETQV-AKFNESQSPGQVQVQvqkiEIQNMESSkdlt 331
Cdd:TIGR00955 272 ADFYVQVLAVIPGSENESRERIEKICD----------SFAVSDIGRDMlVNTNLWSGKAGGLVK----DSENMEGI---- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 332 khTYPPTEYMRLWLLIGRCHLQFFRDWTLTYLKLGIHVLCSILIGLFFGDSGSNATKQISNVGMIMIHCVYLWYTTIMPG 411
Cdd:TIGR00955 334 --GYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMTFQNVFPV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 412 ILRYPAEIEIIRKETFNNWYKLRTYYLATIITSTPVHIIFSTVYITIGYLMTDQPVEMDRFVKYLLSAVVVTICADGLGV 491
Cdd:TIGR00955 412 INVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGY 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 492 FLGTVLNPVN-GTFVGAVSTSCMLMFSGFLILLNHIPAAMRFMAYISPLRYALENMVISLYGN-QRGQLICPPTEFYCHF 569
Cdd:TIGR00955 492 LISCAFSSTSmALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDvDNIECTSANTTGPCPS 571
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 442625523 570 kNAVTVLRQFGMEDGDFGHNILMILIQIAIFKVLSYFTLKHKIK 613
Cdd:TIGR00955 572 -SGEVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIR 614
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-230 |
1.31e-77 |
|
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: 244.38 E-value: 1.31e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 12 GIDIHFEDLVYQVNVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKS-GVSGKIEIG-------KA 83
Cdd:cd03213 1 GVTLSFRNLTVTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlGVSGEVLINgrpldkrSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 84 RKLCGYIMQDDHFFPYFTVEETMLMAAtlkisnqcvslkekrtlidyllnslkltktrqtKCSNLSGGQKKRLSIALELI 163
Cdd:cd03213 81 RKIIGYVPQDDILHPTLTVRETLMFAA---------------------------------KLRGLSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442625523 164 DNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIYNLFNLVYVLSAGRCTYQG 230
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
4-552 |
9.13e-64 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 222.06 E-value: 9.13e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 4 SKLLKNVYGIDIHFEDLVYQVNVPKKP-----------------------EKKSVLKGIKGTFKSGELTAIMGPSGAGKS 60
Cdd:PLN03211 29 SLLLSSCYPITLKFMDVCYRVKFENMKnkgsnikrilghkpkisdetrqiQERTILNGVTGMASPGEILAVLGPSGSGKS 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 61 SLMNILTG-LTKSGVSGKIEIGKAR------KLCGYIMQDDHFFPYFTVEETMLMAATLKISNQcVSLKEKRTLIDYLLN 133
Cdd:PLN03211 109 TLLNALAGrIQGNNFTGTILANNRKptkqilKRTGFVTQDDILYPHLTVRETLVFCSLLRLPKS-LTKQEKILVAESVIS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 134 SLKLTKTRQTKCSN-----LSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPS 208
Cdd:PLN03211 188 ELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPS 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 209 TNIYNLFNLVYVLSAGRCTYQGTPQNTVMFLSSVGLECPPYHNPADFLLECANGDYgdQTEALAEAAK-DIRwrydQQLM 287
Cdd:PLN03211 268 SRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLANGVC--QTDGVSEREKpNVK----QSLV 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 288 QGEDADAPSETQVAkFNESQSPGQVQVQVQKIEIQNMESSKDLTKHTYppteYMRLWLLIGRChLQFFRDWTLTYLKLGI 367
Cdd:PLN03211 342 ASYNTLLAPKVKAA-IEMSHFPQANARFVGSASTKEHRSSDRISISTW----FNQFSILLQRS-LKERKHESFNTLRVFQ 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 368 HVLCSILIGLFFGDSGSNATKqiSNVGMIMIHCVYLWYTTIMPGILRYPAEIEIIRKETFNNWYKLRTYYLATIITSTPV 447
Cdd:PLN03211 416 VIAAALLAGLMWWHSDFRDVQ--DRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERASGMYTLSSYFMARIVGDLPM 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 448 HIIFSTVYITIGYLMTDQPVEMDRFVKYLLSAVVVTICADGLGVFLGTVLnpVNGTFVGAVSTSCMLMF---SGFLIllN 524
Cdd:PLN03211 494 ELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAI--MDAKKASTIVTVTMLAFvltGGFYV--H 569
|
570 580
....*....|....*....|....*...
gi 442625523 525 HIPAAMRFMAYISPLRYALENMVISLYG 552
Cdd:PLN03211 570 KLPSCMAWIKYISTTFYSYRLLINVQYG 597
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-564 |
8.32e-60 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 216.51 E-value: 8.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 4 SKLLKNVYGIDI-HFEDLVYQVNVpkKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGV-SGKIEIG 81
Cdd:TIGR00956 748 EKDMEKESGEDIfHWRNLTYEVKI--KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGViTGGDRLV 825
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 82 KARKL-------CGYIMQDDHFFPYFTVEETMLMAATLKISNQcVSLKEKRTLIDYLLNSLKLTKTRQ----TKCSNLSG 150
Cdd:TIGR00956 826 NGRPLdssfqrsIGYVQQQDLHLPTSTVRESLRFSAYLRQPKS-VSKSEKMEYVEEVIKLLEMESYADavvgVPGEGLNV 904
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 151 GQKKRLSIALELIDNPAVL-FLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIYNLFN-LVYVLSAGRCTY 228
Cdd:TIGR00956 905 EQRKRLTIGVELVAKPKLLlFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDrLLLLQKGGQTVY 984
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 229 QG----TPQNTVMFLSSVGL-ECPPYHNPADFLLECANgdygdqteALAEAAKDIRWrYDqqlmqgedadapsetqvaKF 303
Cdd:TIGR00956 985 FGdlgeNSHTIINYFEKHGApKCPEDANPAEWMLEVIG--------AAPGAHANQDY-HE------------------VW 1037
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 304 NESQSPGQVQVQVQKIE--IQNMESSKDLTKHTYPPTEYMRLWLLIgrCHLQFFRDW-TLTYL--KLGIHVLCSILIGLF 378
Cdd:TIGR00956 1038 RNSSEYQAVKNELDRLEaeLSKAEDDNDPDALSKYAASLWYQFKLV--LWRTFQQYWrTPDYLysKFFLTIFAALFIGFT 1115
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 379 FGDSGSNA---TKQISNVGMIMIhcvylWYTTIMPGILRYPAEIEII--RKETFNNWYKLRTYYLATIITSTPVHIIFST 453
Cdd:TIGR00956 1116 FFKVGTSLqglQNQMFAVFMATV-----LFNPLIQQYLPPFVAQRDLyeVRERPSRTFSWLAFIAAQITVEIPYNLVAGT 1190
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 454 VYITIGYLM-------TDQPVEMDRFVKYLLSAVVVTICADGLGVFLgTVLNPVNGT---FVGAVSTSCmLMFSGFLILL 523
Cdd:TIGR00956 1191 IFFFIWYYPvgfywnaSKTGQVHERGVLFWLLSTMFFLYFSTLGQMV-ISFNPNADNaavLASLLFTMC-LSFCGVLAPP 1268
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 442625523 524 NHIPAAMRFMAYISPLRYALENMVISLYGNQrgQLICPPTE 564
Cdd:TIGR00956 1269 SRMPGFWIFMYRCSPFTYLVQALLSTGLADV--PVTCKVKE 1307
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
26-230 |
3.59e-59 |
|
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: 197.49 E-value: 3.59e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 26 VPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSG--VSGKI-------EIGKARKLCGYIMQDDHF 96
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgtTSGQIlfngqprKPDQFQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 FPYFTVEETMLMAATLKISNqCVSLKEKRTLI-DYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPT 175
Cdd:cd03234 93 LPGLTVRETLTYTAILRLPR-KSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442625523 176 TGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIYNLFNLVYVLSAGRCTYQG 230
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-230 |
2.58e-55 |
|
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: 185.91 E-value: 2.58e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNVPKKpeKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSG-VSGKIEI-GKARKLC----- 87
Cdd:cd03232 4 LTWKNLNYTVPVKGG--KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvITGEILInGRPLDKNfqrst 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 88 GYIMQDDHFFPYFTVEETMLMAATLKisnqcvslkekrtlidyllnslkltktrqtkcsNLSGGQKKRLSIALELIDNPA 167
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSALLR---------------------------------GLSVEQRKRLTIGVELAAKPS 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442625523 168 VLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIYNLFNLVYVL-SAGRCTYQG 230
Cdd:cd03232 129 ILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLkRGGKTVYFG 192
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
27-548 |
2.75e-53 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 197.25 E-value: 2.75e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 27 PKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLT---KSGVSGKI--------EIGKA-RKLCGYIMQDD 94
Cdd:TIGR00956 68 FRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfHIGVEGVItydgitpeEIKKHyRGDVVYNAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 95 HFFPYFTVEETMLMAATLKISN---QCVSLKEKRT-LIDYLLNSLKLTKTRQTKCSN-----LSGGQKKRLSIALELIDN 165
Cdd:TIGR00956 148 VHFPHLTVGETLDFAARCKTPQnrpDGVSREEYAKhIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 166 PAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIV-CTIHQPSTNIYNLFNLVYVLSAGRCTYQGTPQNTVMFLSSVGL 244
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTTPlVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKMGF 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 245 ECPPYHNPADFLLECAN-------GDYGDQTEALAEAAKDiRWRYD---QQLMqgEDADAPSEtQVAKFNESQSPGQVQV 314
Cdd:TIGR00956 308 KCPDRQTTADFLTSLTSpaerqikPGYEKKVPRTPQEFET-YWRNSpeyAQLM--KEIDEYLD-RCSESDTKEAYRESHV 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 315 QVQkieiqnmesskdlTKHTYPPTEY-----MRLWLLIGRCHLQFFRDWTLTYLKLGIHVLCSILIGLFFGDSGSNATKQ 389
Cdd:TIGR00956 384 AKQ-------------SKRTRPSSPYtvsfsMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDF 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 390 ISNVGMI---MIHCVYLWYTTIMPGILRYPaeieIIRKETFNNWYKLRTYYLATIITSTPVHIIFSTVYITIGYLMTDQP 466
Cdd:TIGR00956 451 YSRGGALffaILFNAFSSLLEIASMYEARP----IVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFR 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 467 VEMDRFVKYLLSAVVVTICADGLGVFLGTVLNpvngTFVGAVSTSCML-----MFSGFLILLNHIPAAMRFMAYISPLRY 541
Cdd:TIGR00956 527 RTAGRFFFYLLILFICTLAMSHLFRSIGAVTK----TLSEAMTPAAILllalsIYTGFAIPRPSMLGWSKWIYYVNPLAY 602
|
....*..
gi 442625523 542 ALENMVI 548
Cdd:TIGR00956 603 AFESLMV 609
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
32-234 |
6.46e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 172.94 E-value: 6.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 32 KKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG---------KARKLCGYIMQDDHFFPYFTV 102
Cdd:COG1131 12 DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRP-TSGEVRVLgedvardpaEVRRRIGYVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 103 EETMLMAATLKisnqCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSS 182
Cdd:COG1131 91 RENLRFFARLY----GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442625523 183 SFDTIQLLRGLANEGRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQGTPQN 234
Cdd:COG1131 167 RRELWELLRELAAEGKTVLLSTHYLEE-AERLCDRVAIIDKGRIVADGTPDE 217
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
25-233 |
7.83e-42 |
|
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: 151.16 E-value: 7.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG---------KARKLCGYIMQDDH 95
Cdd:COG4555 6 NLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD-SGSILIDgedvrkeprEARRQIGVLPDERG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 96 FFPYFTVEETMLMAATLkisnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPT 175
Cdd:COG4555 85 LYDRLTVRENIRYFAEL----YGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442625523 176 TGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQE-VEALCDRVVILHKGKVVAQGSLD 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
17-225 |
1.63e-40 |
|
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: 146.46 E-value: 1.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 17 FEDLVYQVNVPKKPekksVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI----------GKARKL 86
Cdd:cd03225 2 LKNLSFSYPDGARP----ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-TSGEVLVdgkdltklslKELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 87 CGYIMQD-DHFFPYFTVEETMlmAATLKisNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDN 165
Cdd:cd03225 77 VGLVFQNpDDQFFGPTVEEEV--AFGLE--NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 166 PAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTnIYNLFNLVYVLSAGR 225
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDL-LLELADRVIVLEDGK 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
25-233 |
2.24e-39 |
|
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: 143.80 E-value: 2.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKS--VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK--------SGVSGKIEIGKARKLCGYIMQDD 94
Cdd:cd03263 5 NLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRptsgtayiNGYSIRTDRKAARQSLGYCPQFD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 95 HFFPYFTVEETMLMAATLKisnqCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEP 174
Cdd:cd03263 85 ALFDELTVREHLRFYARLK----GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442625523 175 TTGLDSSSS---FDTIQLLRglanEGRTIVCTIHQPsTNIYNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:cd03263 161 TSGLDPASRraiWDLILEVR----KGRSIILTTHSM-DEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-258 |
5.16e-39 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 154.23 E-value: 5.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 17 FEDLVYQVNVPKKPEKKSV-------LKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSG-VSGKIEIGKARK--- 85
Cdd:PLN03140 870 FDDVNYFVDMPAEMKEQGVtedrlqlLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyIEGDIRISGFPKkqe 949
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 86 ----LCGYIMQDDHFFPYFTVEETMLMAATLKISNQcVSLKEKRTLIDYL-----LNSLKLTKTRQTKCSNLSGGQKKRL 156
Cdd:PLN03140 950 tfarISGYCEQNDIHSPQVTVRESLIYSAFLRLPKE-VSKEEKMMFVDEVmelveLDNLKDAIVGLPGVTGLSTEQRKRL 1028
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 157 SIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIYNLFN-LVYVLSAGRCTYQGT---- 231
Cdd:PLN03140 1029 TIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDeLLLMKRGGQVIYSGPlgrn 1108
|
250 260
....*....|....*....|....*....
gi 442625523 232 PQNTVMFLSSV-GL-ECPPYHNPADFLLE 258
Cdd:PLN03140 1109 SHKIIEYFEAIpGVpKIKEKYNPATWMLE 1137
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
15-233 |
7.77e-39 |
|
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: 142.47 E-value: 7.77e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVnvpkkPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKsGVSGKIEIG----------KAR 84
Cdd:COG1122 1 IELENLSFSY-----PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLK-PTSGEVLVDgkditkknlrELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQD-DH--FFPyfTVEEtmlmaatlKIS----NQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLS 157
Cdd:COG1122 75 RKVGLVFQNpDDqlFAP--TVEE--------DVAfgpeNLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442625523 158 IALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:COG1122 145 IAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADGTPR 219
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
346-549 |
9.01e-39 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 141.64 E-value: 9.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 346 LIGRCHLQFFRDWTLTYLKLGIHVLCSILIGLFFGDSGsNATKQISNVGMIMIHCVYLWYTTIMPGILRYPAEIEIIRKE 425
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLG-NQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 426 TFNNWYKLRTYYLATIITSTPVHIIFSTVYITIGYLMTDQPVEMDRFVKYLLSAVVVTICADGLGVFLGTVL-NPVNGTF 504
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALApSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442625523 505 VGAVSTSCMLMFSGFLILLNHIPAAMRFMAYISPLRYALENMVIS 549
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
15-208 |
9.98e-39 |
|
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: 141.86 E-value: 9.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNvpKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG------------- 81
Cdd:cd03255 1 IELKNLSKTYG--GGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRP-TSGEVRVDgtdisklsekela 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 82 --KARKLcGYIMQDDHFFPYFTVEETMLMAATLkisnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIA 159
Cdd:cd03255 78 afRRRHI-GFVFQSFNLLPDLTALENVELPLLL----AGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442625523 160 LELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQPS 208
Cdd:cd03255 153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPE 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
15-233 |
2.71e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 141.77 E-value: 2.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNvpkkpeKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI-----GKARKLCGY 89
Cdd:COG1121 7 IELENLTVSYG------GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-TSGTVRLfgkppRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 90 IMQDDHF---FPyFTVEETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNP 166
Cdd:COG1121 80 VPQRAEVdwdFP-ITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442625523 167 AVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTnIYNLFNLVYVLsAGRCTYQGTPQ 233
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLL-NRGLVAHGPPE 223
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
35-225 |
1.14e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 139.41 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK-SgvSGKIEIG-------KARKL-------CGYIMQDDHFFPY 99
Cdd:COG1136 23 ALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRpT--SGEVLIDgqdisslSERELarlrrrhIGFVFQFFNLLPE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 100 FTVEETMLMAATLkisnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:COG1136 101 LTALENVALPLLL----AGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442625523 180 SSSSFDTIQLLRGLANE-GRTIVCTIHQPstNIYNLFNLVYVLSAGR 225
Cdd:COG1136 177 SKTGEEVLELLRELNRElGTTIVMVTHDP--ELAARADRVIRLRDGR 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
23-230 |
3.81e-37 |
|
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: 137.01 E-value: 3.81e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 23 QVNVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKS--GVSGKI-----EIGKARKLCG----YIM 91
Cdd:cd03233 10 SFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvSVEGDIhyngiPYKEFAEKYPgeiiYVS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 92 QDDHFFPYFTVEETMLMAATLKiSNQCVSlkekrtlidyllnslkltktrqtkcsNLSGGQKKRLSIALELIDNPAVLFL 171
Cdd:cd03233 90 EEDVHFPTLTVRETLDFALRCK-GNEFVR--------------------------GISGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 172 DEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQPSTNIYNLFNLVYVLSAGRCTYQG 230
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
35-205 |
5.47e-35 |
|
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: 131.50 E-value: 5.47e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI-----GKARKLCGYIMQDDHFFPYF--TVEETML 107
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP-TSGSIRVfgkplEKERKRIGYVPQRRSIDRDFpiSVRDVVL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 108 MAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTI 187
Cdd:cd03235 93 MGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIY 172
|
170
....*....|....*...
gi 442625523 188 QLLRGLANEGRTIVCTIH 205
Cdd:cd03235 173 ELLRELRREGMTILVVTH 190
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
25-225 |
6.10e-35 |
|
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: 129.83 E-value: 6.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI---------GKARKLCGYIMQDDH 95
Cdd:cd03230 5 NLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKP-DSGEIKVlgkdikkepEEVKRRIGYLPEEPS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 96 FFPYFTVEETMlmaatlkisnqcvslkekrtlidyllnslkltktrqtkcsNLSGGQKKRLSIALELIDNPAVLFLDEPT 175
Cdd:cd03230 84 LYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442625523 176 TGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPStNIYNLFNLVYVLSAGR 225
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILE-EAERLCDRVAILNNGR 172
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
25-230 |
1.54e-34 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 130.01 E-value: 1.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGeLTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG---------KARKLCGYIMQDDH 95
Cdd:cd03264 5 NLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPP-SSGTIRIDgqdvlkqpqKLRRRIGYLPQEFG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 96 FFPYFTVEETMLMAATLKisnqCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPT 175
Cdd:cd03264 83 VYPNFTVREFLDYIAWLK----GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442625523 176 TGLDSSSSFDTIQLLRGLAnEGRTIVCTIHQPStNIYNLFNLVYVLSAGRCTYQG 230
Cdd:cd03264 159 AGLDPEERIRFRNLLSELG-EDRIVILSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
24-232 |
6.33e-33 |
|
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: 126.12 E-value: 6.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 24 VNVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG-----------KARKLCGYIMQ 92
Cdd:cd03218 4 ENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPD-SGKILLDgqditklpmhkRARLGIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 93 DDHFFPYFTVEETMLmaATLKIsnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLD 172
Cdd:cd03218 83 EASIFRKLTVEENIL--AVLEI--RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442625523 173 EPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHqpstNIYNLFNLV---YVLSAGRCTYQGTP 232
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDH----NVRETLSITdraYIIYEGKVLAEGTP 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
25-225 |
5.94e-32 |
|
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: 121.20 E-value: 5.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG----------KARKLCGYIMQdd 94
Cdd:cd00267 4 NLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-SGEILIDgkdiaklpleELRRRIGYVPQ-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 95 hffpyftveetmlmaatlkisnqcvslkekrtlidyllnslkltktrqtkcsnLSGGQKKRLSIALELIDNPAVLFLDEP 174
Cdd:cd00267 81 -----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442625523 175 TTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTnIYNLFNLVYVLSAGR 225
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPEL-AELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
15-233 |
7.32e-32 |
|
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: 124.00 E-value: 7.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNvpkkpeKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI-GK----------A 83
Cdd:COG1120 2 LEAENLSVGYG------GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-SGEVLLdGRdlaslsrrelA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 84 RKLcGYIMQDDHFFPYFTVEETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELI 163
Cdd:COG1120 75 RRI-AYVPQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442625523 164 DNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQPstniynlfNL-------VYVLSAGRCTYQGTPQ 233
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDL--------NLaaryadrLVLLKDGRIVAQGPPE 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
36-176 |
3.35e-31 |
|
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: 118.52 E-value: 3.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 36 LKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKsGVSGKIEIGK----------ARKLCGYIMQDDHFFPYFTVEET 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLS-PTEGTILLDGqdltdderksLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442625523 106 MLMAATLKIsnqcVSLKEKRTLIDYLLNSLKLTKTRQTKC----SNLSGGQKKRLSIALELIDNPAVLFLDEPTT 176
Cdd:pfam00005 80 LRLGLLLKG----LSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
29-549 |
1.94e-30 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 128.04 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 29 KPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTG-LTKS-GVSGKIEIGK-------ARKLCGYIMQDDHFFPY 99
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGkLDPSlKVSGEITYNGyrlnefvPRKTSAYISQNDVHVGV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 100 FTVEETmlmaatLKISNQC------------VSLKEKRTLI------------------------DYLLNSLKLTKTRQT 143
Cdd:PLN03140 254 MTVKET------LDFSARCqgvgtrydllseLARREKDAGIfpeaevdlfmkatamegvksslitDYTLKILGLDICKDT 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 144 KCSN-----LSGGQKKRLSIAlELIDNPA-VLFLDEPTTGLDSSSSFDTIQLLRGLA--NEGrTIVCTIHQPSTNIYNLF 215
Cdd:PLN03140 328 IVGDemirgISGGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQQIVhlTEA-TVLMSLLQPAPETFDLF 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 216 NLVYVLSAGRCTYQGTPQNTVMFLSSVGLECPPYHNPADFLLECANGDygDQTEALAEAAKDIRWrydqqlmqgedadap 295
Cdd:PLN03140 406 DDIILLSEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKK--DQEQYWADRNKPYRY--------------- 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 296 seTQVAKFNESQSPGQVQVQVQKiEI-------QNMESSKDLTKHTYPPTEYMRL-----WLLIGRcHLQFFRDWTLTYL 363
Cdd:PLN03140 469 --ISVSEFAERFKSFHVGMQLEN-ELsvpfdksQSHKAALVFSKYSVPKMELLKAcwdkeWLLMKR-NAFVYVFKTVQII 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 364 KLGIHVLCSILIGLFFGDSGSNATKQISNVGMIMIHCVYLWYTTIMPGILRYPAeieiirketfnnWYKLR--------T 435
Cdd:PLN03140 545 IVAAIASTVFLRTEMHTRNEEDGALYIGALLFSMIINMFNGFAELALMIQRLPV------------FYKQRdllfhppwT 612
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 436 YYLATIITSTPVHIIFSTVYITIGYLMTDQPVEMDRFVKYLLSAVVVTICADGLGVFLGTVLNP-VNGTFVGAVSTSCML 514
Cdd:PLN03140 613 FTLPTFLLGIPISIIESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTmIIANTGGALVLLLVF 692
|
570 580 590
....*....|....*....|....*....|....*
gi 442625523 515 MFSGFLILLNHIPAAMRFMAYISPLRYALENMVIS 549
Cdd:PLN03140 693 LLGGFILPKGEIPNWWEWAYWVSPLSYGFNALAVN 727
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
30-234 |
5.43e-30 |
|
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: 118.44 E-value: 5.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 30 PEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKsGVSGKIEIG-------------KARKLCGYIMQDDHF 96
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE-PTSGSVLIDgtdinklkgkalrQLRRQIGMIFQQFNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 FPYFTVEETMLMAA-----TLKISNQCVSLKEKRTLIdYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFL 171
Cdd:cd03256 90 IERLSVLENVLSGRlgrrsTWRSLFGLFPKEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442625523 172 DEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQPstniyNL----FNLVYVLSAGRCTYQGTPQN 234
Cdd:cd03256 169 DEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQV-----DLareyADRIVGLKDGRIVFDGPPAE 231
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
35-207 |
1.96e-29 |
|
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: 115.65 E-value: 1.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG---------KARKLCGYIMQDDHFFPYFTVEET 105
Cdd:COG4133 17 LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPP-SAGEVLWNgepirdareDYRRRLAYLGHADGLKPELTVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 106 MLMAATLKisnqcvSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFD 185
Cdd:COG4133 96 LRFWAALY------GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVAL 169
|
170 180
....*....|....*....|..
gi 442625523 186 TIQLLRGLANEGRTIVCTIHQP 207
Cdd:COG4133 170 LAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
35-233 |
2.00e-29 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 116.38 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG-------KARKLCGYIM----QDDHFFPYFTVE 103
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT-SGSVLFDgeditglPPHEIARLGIgrtfQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 104 ETMLMAATLK---ISNQCVSLKEKRTLIDY---LLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTG 177
Cdd:cd03219 94 ENVMVAAQARtgsGLLLARARREEREARERaeeLLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442625523 178 LDSSSSFDTIQLLRGLANEGRTIVCTIHqpstNIYNLFNL---VYVLSAGRCTYQGTPQ 233
Cdd:cd03219 174 LNPEETEELAELIRELRERGITVLLVEH----DMDVVMSLadrVTVLDQGRVIAEGTPD 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
35-230 |
4.81e-29 |
|
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: 115.30 E-value: 4.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI---------GKARKLCG----YIMQDDH--FFPY 99
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKP-TSGSIIFdgkdllklsRRLRKIRRkeiqMVFQDPMssLNPR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 100 FTVEEtmLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSN-LSGGQKKRLSIALELIDNPAVLFLDEPTTGL 178
Cdd:cd03257 99 MTIGE--QIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHeLSGGQRQRVAIARALALNPKLLIADEPTSAL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442625523 179 DSSSSFDTIQLLRGLANE-GRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQG 230
Cdd:cd03257 177 DVSVQAQILDLLKKLQEElGLTLLFITHDLGV-VAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
25-206 |
6.44e-29 |
|
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: 114.24 E-value: 6.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI--------GKARKLCGYIMQDDHF 96
Cdd:cd03268 5 DLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD-SGEITFdgksyqknIEALRRIGALIEAPGF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 FPYFTVEETMLMAATLKIsnqcvsLKEKRtlIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTT 176
Cdd:cd03268 84 YPNLTARENLRLLARLLG------IRKKR--IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190
....*....|....*....|....*....|
gi 442625523 177 GLDSSSSFDTIQLLRGLANEGRTIVCTIHQ 206
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHL 185
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
12-233 |
1.77e-28 |
|
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: 119.86 E-value: 1.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 12 GIDIHFEDLVYQvnvpkKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIGKA-------- 83
Cdd:COG4988 334 PPSIELEDVSFS-----YPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY-SGSILINGVdlsdldpa 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 84 --RKLCGYIMQDDHFFPYfTVEETMLMAatlkisNQCVSLKE-----KRTLIDYLLNSLK--LtktrQTKC----SNLSG 150
Cdd:COG4988 408 swRRQIAWVPQNPYLFAG-TIRENLRLG------RPDASDEEleaalEAAGLDEFVAALPdgL----DTPLgeggRGLSG 476
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 151 GQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLAnEGRT-IVCTiHQPSTniYNLFNLVYVLSAGRCTYQ 229
Cdd:COG4988 477 GQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTvILIT-HRLAL--LAQADRILVLDDGRIVEQ 552
|
....
gi 442625523 230 GTPQ 233
Cdd:COG4988 553 GTHE 556
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
25-233 |
4.01e-28 |
|
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: 112.60 E-value: 4.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG-------------KARKLCGYIM 91
Cdd:cd03261 5 GLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRP-DSGEVLIDgedisglseaelyRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 92 QDDHFFPYFTVEEtmlmaatlkisNQCVSLKEKRTL----IDYL----LNSLKLTKTRQTKCSNLSGGQKKRLSIALELI 163
Cdd:cd03261 84 QSGALFDSLTVFE-----------NVAFPLREHTRLseeeIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442625523 164 DNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDT-AFAIADRIAVLYDGKIVAEGTPE 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
30-205 |
7.68e-28 |
|
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: 111.19 E-value: 7.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 30 PEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIGKA-------RKLCGYIMQD--DHFFpyf 100
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKE-SSGSILLNGKpikakerRKSIGYVMQDvdYQLF--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 101 tvEETMlmAATLKISNQCVSLKEKRtlIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDS 180
Cdd:cd03226 86 --TDSV--REELLLGLKELDAGNEQ--AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDY 159
|
170 180
....*....|....*....|....*
gi 442625523 181 SSSFDTIQLLRGLANEGRTIVCTIH 205
Cdd:cd03226 160 KNMERVGELIRELAAQGKAVIVITH 184
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
15-225 |
9.57e-28 |
|
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: 109.78 E-value: 9.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNvpkkPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLtKSGVSGKIEIGKA----------R 84
Cdd:cd03228 1 IEFKNVSFSYP----GRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRL-YDPTSGEILIDGVdlrdldleslR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQDDHFFPyFTVEEtmlmaatlkisnqcvslkekrtlidyllnslkltktrqtkcsN-LSGGQKKRLSIALELI 163
Cdd:cd03228 76 KNIAYVPQDPFLFS-GTIRE------------------------------------------NiLSGGQRQRIAIARALL 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442625523 164 DNPAVLFLDEPTTGLDSSSSFDTIQLLRGLAnEGRTIVCTIHQPSTNIynLFNLVYVLSAGR 225
Cdd:cd03228 113 RDPPILILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIR--DADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
14-233 |
1.91e-27 |
|
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: 117.63 E-value: 1.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 14 DIHFEDLVYQVNvpkkPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIGKA---------- 83
Cdd:COG2274 473 DIELENVSFRYP----GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP-TSGRILIDGIdlrqidpasl 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 84 RKLCGYIMQDDHFF------------PYFTVEEtmLMAAtLKISNqcvslkekrtLIDYLLnslKLTKTRQTKC----SN 147
Cdd:COG2274 548 RRQIGVVLQDVFLFsgtirenitlgdPDATDEE--IIEA-ARLAG----------LHDFIE---ALPMGYDTVVgeggSN 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 148 LSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANeGRTIVCTIHQPSTNiyNLFNLVYVLSAGRCT 227
Cdd:COG2274 612 LSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTI--RLADRIIVLDKGRIV 688
|
....*.
gi 442625523 228 YQGTPQ 233
Cdd:COG2274 689 EDGTHE 694
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
32-230 |
1.96e-27 |
|
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: 109.06 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 32 KKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIGKaRKLcgyimqddhffpyftveETMlmaat 111
Cdd:cd03214 11 GRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-SGEILLDG-KDL-----------------ASL----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 112 lkisnqcvSLKEKRTLIDYLLNSLKLTKTRQTK---CSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQ 188
Cdd:cd03214 67 --------SPKELARKIAYVPQALELLGLAHLAdrpFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLE 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442625523 189 LLRGLANE-GRTIVCTIHQPstniynlfNL-------VYVLSAGRCTYQG 230
Cdd:cd03214 139 LLRRLARErGKTVVMVLHDL--------NLaaryadrVILLKDGRIVAQG 180
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
15-225 |
5.87e-27 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 108.75 E-value: 5.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNvpkkpeKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTkSGVSGKIEI-GKA---------R 84
Cdd:COG4619 1 LELEGLSFRVG------GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLD-PPTSGEIYLdGKPlsampppewR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQDDHFFPYfTVEETMLMAATLKisnqcvSLKEKRTLIDYLLNSLKLTK-TRQTKCSNLSGGQKKRLSIALELI 163
Cdd:COG4619 74 RQVAYVPQEPALWGG-TVRDNLPFPFQLR------ERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442625523 164 DNPAVLFLDEPTTGLDSSSSFDTIQLLRGL-ANEGRTIVCTIHQPsTNIYNLFNLVYVLSAGR 225
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDP-EQIERVADRVLTLEAGR 208
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
30-206 |
8.36e-27 |
|
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: 109.31 E-value: 8.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 30 PEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKI-------------EIGKARKLCGYIMQDDHF 96
Cdd:TIGR02315 12 PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEP-SSGSIllegtditklrgkKLRKLRRRIGMIFQHYNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 FPYFTVEETMLMAA-----TLKISNQCVSLKEKRTLIdYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFL 171
Cdd:TIGR02315 91 IERLTVLENVLHGRlgykpTWRSLLGRFSEEDKERAL-SALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILA 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 442625523 172 DEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQ 206
Cdd:TIGR02315 170 DEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQ 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
35-233 |
1.39e-26 |
|
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: 107.91 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG-----------KARKLCGYIMQDDHFFPYFTVE 103
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPP-RSGSIRFDgrditglppheRARAGIGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 104 ETMLMAATLKisnqcvSLKEKRTLIDYLLNSL-KLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSS 182
Cdd:cd03224 94 ENLLLGAYAR------RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 183 SFDTIQLLRGLANEGRTIVcTIHQpstniynlfNL---------VYVLSAGRCTYQGTPQ 233
Cdd:cd03224 168 VEEIFEAIRELRDEGVTIL-LVEQ---------NArfaleiadrAYVLERGRVVLEGTAA 217
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
30-205 |
2.14e-26 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 106.35 E-value: 2.14e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 30 PEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG------------KARKLCGYIMQ--DDH 95
Cdd:TIGR01166 2 PGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRP-QSGAVLIDgepldysrkgllERRQRVGLVFQdpDDQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 96 FFpYFTVEETMlmaaTLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPT 175
Cdd:TIGR01166 81 LF-AADVDQDV----AFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPT 155
|
170 180 190
....*....|....*....|....*....|
gi 442625523 176 TGLDSSSSFDTIQLLRGLANEGRTIVCTIH 205
Cdd:TIGR01166 156 AGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
30-234 |
2.16e-26 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 108.22 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 30 PEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKsGVSGKIEIG-------------KARKLCGYIMQDDHF 96
Cdd:COG3638 13 PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVE-PTSGEILVDgqdvtalrgralrRLRRRIGMIFQQFNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 FPYFTVEETMLMAA-----TLKISNQCVSLKEKRTLIDyLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFL 171
Cdd:COG3638 92 VPRLSVLTNVLAGRlgrtsTWRSLLGLFPPEDRERALE-ALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442625523 172 DEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQPstniyNL----FNLVYVLSAGRCTYQGTPQN 234
Cdd:COG3638 171 DEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQV-----DLarryADRIIGLRDGRVVFDGPPAE 233
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
25-225 |
3.49e-26 |
|
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: 105.35 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG------------KARKLCGYIMQ 92
Cdd:cd03229 5 NVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEP-DSGSILIDgedltdledelpPLRRRIGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 93 DDHFFPYFTVEETMLMAatlkisnqcvslkekrtlidyllnslkltktrqtkcsnLSGGQKKRLSIALELIDNPAVLFLD 172
Cdd:cd03229 84 DFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442625523 173 EPTTGLDSSSSFDTIQLLRGL-ANEGRTIVCTIHQPStNIYNLFNLVYVLSAGR 225
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLD-EAARLADRVVVLRDGK 178
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
15-233 |
4.02e-26 |
|
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: 106.99 E-value: 4.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNvpkkpeKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG------------- 81
Cdd:COG1127 6 IEVRNLTKSFG------DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRP-DSGEILVDgqditglsekely 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 82 KARKLCGYIMQDDHFFPYFTVEE----TMLMAATLkisnqcvSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLS 157
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSLTVFEnvafPLREHTDL-------SEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442625523 158 IALELIDNPAVLFLDEPTTGLD--SSSSFDtiQLLRGLANE-GRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDpiTSAVID--ELIRELRDElGLTSVVVTHDLDS-AFAIADRVAVLADGKIIAEGTPE 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
15-231 |
4.37e-26 |
|
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: 106.90 E-value: 4.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDL--VYQVNVPKKPekksVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK--SG---VSG-------KIEI 80
Cdd:cd03258 2 IELKNVskVFGDTGGKVT----ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERptSGsvlVDGtdltllsGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 81 GKARKLCGYIMQDDHFFPYFTVEETMlmAATLKISNqcVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIAL 160
Cdd:cd03258 78 RKARRRIGMIFQHFNLLSSRTVFENV--ALPLEIAG--VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442625523 161 ELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQGT 231
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEV-VKRICDRVAVMEKGEVVEEGT 224
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-233 |
4.41e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 109.54 E-value: 4.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 24 VNVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVsGKIEI---------GKARKLCGYIMQDD 94
Cdd:PRK13536 45 AGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA-GKITVlgvpvparaRLARARIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 95 HFFPYFTVEETMLMaatlkISNQC-VSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDE 173
Cdd:PRK13536 124 NLDLEFTVRENLLV-----FGRYFgMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 174 PTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQpSTNIYNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:PRK13536 199 PTTGLDPHARHLIWERLRSLLARGKTILLTTHF-MEEAERLCDRLCVLEAGRKIAEGRPH 257
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
27-231 |
5.88e-26 |
|
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: 106.02 E-value: 5.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 27 PKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK--SG---VSGKIEIGKARKlCGYIMQDDHFFPYFT 101
Cdd:cd03293 11 GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERptSGevlVDGEPVTGPGPD-RGYVFQQDALLPWLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 102 VEETMLMAatLKIsnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSS 181
Cdd:cd03293 90 VLDNVALG--LEL--QGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442625523 182 SSFDTIQLLRGLANE-GRTIVCTIHQPSTNIYnLFNLVYVLSAGRCTYQGT 231
Cdd:cd03293 166 TREQLQEELLDIWREtGKTVLLVTHDIDEAVF-LADRVVVLSARPGRIVAE 215
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
15-249 |
1.00e-25 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 107.15 E-value: 1.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDL--VYQvnvPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG----------- 81
Cdd:TIGR04521 1 IKLKNVsyIYQ---PGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPT-SGTVTIDgrditakkkkk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 82 --KARKLCGYIMQddhfFPyftveETMLMAAT-LK-I----SNQCVSLKEKRTLIDYLLNSLKLTKTRQTK-CSNLSGGQ 152
Cdd:TIGR04521 77 lkDLRKKVGLVFQ----FP-----EHQLFEETvYKdIafgpKNLGLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 153 KKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQPStNIYNLFNLVYVLSAGRCTYQGT 231
Cdd:TIGR04521 148 MRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSME-DVAEYADRVIVMHKGKIVLDGT 226
|
250 260
....*....|....*....|.
gi 442625523 232 PQNTVM---FLSSVGLECPPY 249
Cdd:TIGR04521 227 PREVFSdvdELEKIGLDVPEI 247
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
36-234 |
1.20e-25 |
|
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: 105.14 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 36 LKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK--------SGVSGKIEIGKARKLCGYIMQDDHFFPYFTVEETML 107
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKptsgratvAGHDVVREPREVRRRIGIVFQDLSVDDELTGWENLY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 108 MAATLkisnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTI 187
Cdd:cd03265 96 IHARL----YGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVW 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442625523 188 QLLRGL-ANEGRTIVCTIHqpstniY-----NLFNLVYVLSAGRCTYQGTPQN 234
Cdd:cd03265 172 EYIEKLkEEFGMTILLTTH------YmeeaeQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
35-207 |
1.22e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.24 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIGKARKLcGYIMQ---DDHFFPyFTVEETMLMAAT 111
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRP-TSGTVRRAGGARV-AYVPQrseVPDSLP-LTVRDLVAMGRW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 112 LKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLR 191
Cdd:NF040873 84 ARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLA 163
|
170
....*....|....*.
gi 442625523 192 GLANEGRTIVCTIHQP 207
Cdd:NF040873 164 EEHARGATVVVVTHDL 179
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
35-201 |
8.08e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 104.02 E-value: 8.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK--SG---VSGKIEIGKARKlCGYIMQDDHFFPYFTVEETMLMA 109
Cdd:COG1116 26 ALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKptSGevlVDGKPVTGPGPD-RGVVFQEPALLPWLTVLDNVALG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 110 atLKISNqcVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDsssSF--DTI 187
Cdd:COG1116 105 --LELRG--VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMDEPFGALD---ALtrERL 177
|
170
....*....|....*.
gi 442625523 188 Q--LLRGLANEGRTIV 201
Cdd:COG1116 178 QdeLLRLWQETGKTVL 193
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
14-233 |
8.70e-25 |
|
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: 103.07 E-value: 8.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 14 DIHFEDLVYQVNvpkkpEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK--------SGVSGK-IEIGKAR 84
Cdd:cd03254 2 EIEFENVNFSYD-----EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDpqkgqiliDGIDIRdISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQDDHFFPYfTVEETMLMaATLKISNQCVSLKEKRTLIDYLLNslKLTKTRQT----KCSNLSGGQKKRLSIAL 160
Cdd:cd03254 77 SMIGVVLQDTFLFSG-TIMENIRL-GRPNATDEEVIEAAKEAGAHDFIM--KLPNGYDTvlgeNGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442625523 161 ELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLaNEGRTIVCTIHQPSTnIYNLfNLVYVLSAGRCTYQGTPQ 233
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLST-IKNA-DKILVLDDGKIIEEGTHD 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
35-248 |
1.27e-24 |
|
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: 107.68 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSG--VSGKIEIG----------KARKLCGYIMQD--DHFFPYf 100
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgrISGEVLLDgrdllelseaLRGRRIGMVFQDpmTQLNPV- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 101 TVEETMLMAatlkISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDS 180
Cdd:COG1123 100 TVGDQIAEA----LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442625523 181 SSSFDTIQLLRGLANE-GRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQGTPQntVMFLSSVGLECPP 248
Cdd:COG1123 176 TTQAEILDLLRELQRErGTTVLLITHDLGV-VAEIADRVVVMDDGRIVEDGPPE--EILAAPQALAAVP 241
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
25-225 |
1.40e-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: 101.83 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIGKARKLC--------GYIMQDDHF 96
Cdd:cd03259 5 GLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD-SGEILIDGRDVTGvpperrniGMVFQDYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 FPYFTVEETMLMAatLKisNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTT 176
Cdd:cd03259 84 FPHLTVAENIAFG--LK--LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442625523 177 GLDSSSSFDTIQLLRGL-ANEGRTIVCTIHQPStNIYNLFNLVYVLSAGR 225
Cdd:cd03259 160 ALDAKLREELREELKELqRELGITTIYVTHDQE-EALALADRIAVMNEGR 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
36-234 |
1.45e-24 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 104.39 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 36 LKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK--SG---VSGKIEIGKARKL---CGYIMQDDHFFPYFTVEETML 107
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRptSGtarVAGYDVVREPRKVrrsIGIVPQYASVDEDLTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 108 MAATLkisnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTI 187
Cdd:TIGR01188 89 MMGRL----YGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIW 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442625523 188 QLLRGLANEGRTIVCTIHqpstNIYN---LFNLVYVLSAGRCTYQGTPQN 234
Cdd:TIGR01188 165 DYIRALKEEGVTILLTTH----YMEEadkLCDRIAIIDHGRIIAEGTPEE 210
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
15-225 |
4.33e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 100.90 E-value: 4.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEdlvyqvNVPKK-PEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG-------KARKL 86
Cdd:COG2884 2 IRFE------NVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERP-TSGQVLVNgqdlsrlKRREI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 87 C------GYIMQDDHFFPYFTVEETMLMAatLKISNqcVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIAL 160
Cdd:COG2884 75 PylrrriGVVFQDFRLLPDRTVYENVALP--LRVTG--KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442625523 161 ELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHqpSTNIYNLFNL-VYVLSAGR 225
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH--DLELVDRMPKrVLELEDGR 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
25-206 |
4.81e-24 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 100.43 E-value: 4.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI-GK-----ARKLCGYIMQDDHFFP 98
Cdd:cd03269 5 NVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD-SGEVLFdGKpldiaARNRIGYLPEERGLYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 99 YFTVEETMLMAATLKisnqCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGL 178
Cdd:cd03269 84 KMKVIDQLVYLAQLK----GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGL 159
|
170 180
....*....|....*....|....*...
gi 442625523 179 DSSSSFDTIQLLRGLANEGRTIVCTIHQ 206
Cdd:cd03269 160 DPVNVELLKDVIRELARAGKTVILSTHQ 187
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
25-206 |
6.69e-24 |
|
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: 99.91 E-value: 6.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG------------KARKLCGYIMQ 92
Cdd:cd03262 5 NLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPD-SGTIIIDglkltddkkninELRQKVGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 93 DDHFFPYFTVEETmLMAATLKIsnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLD 172
Cdd:cd03262 84 QFNLFPHLTVLEN-ITLAPIKV--KGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190
....*....|....*....|....*....|....
gi 442625523 173 EPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQ 206
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE 194
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
45-230 |
1.82e-23 |
|
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: 98.91 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 45 SGELTAIMGPSGAGKSSLMNILTGLTKSGVsGKIEIG---------------KARKLcGYIMQDDHFFPYFTVEETMLMA 109
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDG-GTIVLNgtvlfdsrkkinlppQQRKI-GLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 110 ATLKisnqcvSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQL 189
Cdd:cd03297 100 LKRK------RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442625523 190 LRGLANE--GRTIVCTiHQPStNIYNLFNLVYVLSAGRCTYQG 230
Cdd:cd03297 174 LKQIKKNlnIPVIFVT-HDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
29-225 |
1.89e-23 |
|
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: 98.82 E-value: 1.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 29 KPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIGKA----------RKLCGYIMQDDHFFp 98
Cdd:cd03245 13 PNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT-SGSVLLDGTdirqldpadlRRNIGYVPQDVTLF- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 99 YFTVEETMLMAATLkISNQCVSLKEKRTLIDYLLNSLKLTKTRQT--KCSNLSGGQKKRLSIALELIDNPAVLFLDEPTT 176
Cdd:cd03245 91 YGTLRDNITLGAPL-ADDERILRAAELAGVTDFVNKHPNGLDLQIgeRGRGLSGGQRQAVALARALLNDPPILLLDEPTS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 442625523 177 GLDSSSSFDTIQLLRGLAnEGRTIVCTIHQPStnIYNLFNLVYVLSAGR 225
Cdd:cd03245 170 AMDMNSEERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGR 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
42-230 |
2.27e-23 |
|
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: 98.33 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKSSLMNILTGLtKSGVSGKIEIGK--------ARKLCGYIMQDDHFFPYFTVEETMLMAAT-- 111
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGF-ETPQSGRVLINGvdvtaappADRPVSMLFQENNLFAHLTVEQNVGLGLSpg 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 112 LKISnqcvslKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLR 191
Cdd:cd03298 99 LKLT------AEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442625523 192 GLANE-GRTIVCTIHQPStNIYNLFNLVYVLSAGRCTYQG 230
Cdd:cd03298 173 DLHAEtKMTVLMVTHQPE-DAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-233 |
4.01e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 100.26 E-value: 4.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI---------GKARKLCGYIMQDDH 95
Cdd:PRK13537 12 NVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPD-AGSISLcgepvpsraRHARQRVGVVPQFDN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 96 FFPYFTVEETMLMAATLKisnqCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPT 175
Cdd:PRK13537 91 LDPDFTVRENLLVFGRYF----GLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442625523 176 TGLDSSSSFDTIQLLRGLANEGRTIVCTIHQpSTNIYNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGKTILLTTHF-MEEAERLCDRLCVIEEGRKIAEGAPH 223
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
14-234 |
4.43e-23 |
|
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: 103.31 E-value: 4.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 14 DIHFEDLVYQVNvpkkPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG----------KA 83
Cdd:COG4987 333 SLELEDVSFRYP----GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP-QSGSITLGgvdlrdldedDL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 84 RKLCGYIMQDDHFFpYFTVEETMLMA---AT-------LKIsnqcVSLKEkrtLIDYLLNSLkltktrQTKC----SNLS 149
Cdd:COG4987 408 RRRIAVVPQRPHLF-DTTLRENLRLArpdATdeelwaaLER----VGLGD---WLAALPDGL------DTWLgeggRRLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 150 GGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLAnEGRTIVCTIHQPSTNiyNLFNLVYVLSAGRCTYQ 229
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGL--ERMDRILVLEDGRIVEQ 550
|
....*
gi 442625523 230 GTPQN 234
Cdd:COG4987 551 GTHEE 555
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
15-233 |
8.54e-23 |
|
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: 102.29 E-value: 8.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNVPKKPEKKsVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG------------- 81
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVR-AVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP-TSGSILFDgkdltklsrrslr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 82 KARKLCGYIMQD-DH-FFPYFTVEETMlmAATLKIsNQCVSLKEKRTLIDYLLNSLKLTKT------RQtkcsnLSGGQK 153
Cdd:COG1123 339 ELRRRVQMVFQDpYSsLNPRMTVGDII--AEPLRL-HGLLSRAERRERVAELLERVGLPPDladrypHE-----LSGGQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 154 KRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHqpstniynlfNL---------VYVLSA 223
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISH----------DLavvryiadrVAVMYD 480
|
250
....*....|
gi 442625523 224 GRCTYQGTPQ 233
Cdd:COG1123 481 GRIVEDGPTE 490
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
19-233 |
1.18e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 98.23 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 19 DLVYqvnvpKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG------------KARKL 86
Cdd:PRK13639 6 DLKY-----SYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKP-TSGEVLIKgepikydkksllEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 87 CGYIMQ--DDHFF-PyfTVEETMLMAA-TLKISNQCVslkEKRtlIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALEL 162
Cdd:PRK13639 80 VGIVFQnpDDQLFaP--TVEEDVAFGPlNLGLSKEEV---EKR--VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442625523 163 IDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQpsTNIYNLF-NLVYVLSAGRCTYQGTPQ 233
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEGTPK 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
31-209 |
3.34e-22 |
|
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: 93.82 E-value: 3.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 31 EKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIGKA----------RKLCGYIMQDDHFFPyf 100
Cdd:cd03246 13 AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRP-TSGRVRLDGAdisqwdpnelGDHVGYLPQDDELFS-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 101 tveetmlmaatlkisnqcvslkekRTLIDYLlnslkltktrqtkcsnLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDS 180
Cdd:cd03246 90 ------------------------GSIAENI----------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDV 129
|
170 180
....*....|....*....|....*....
gi 442625523 181 SSSFDTIQLLRGLANEGRTIVCTIHQPST 209
Cdd:cd03246 130 EGERALNQAIAALKAAGATRIVIAHRPET 158
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
15-247 |
3.94e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 96.60 E-value: 3.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNvpkkPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI----------GKAR 84
Cdd:PRK13632 8 IKVENVSFSYP----NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKP-QSGEIKIdgitiskenlKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQD-DHFFPYFTVEETMlmAATLKisNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELI 163
Cdd:PRK13632 83 KKIGIIFQNpDNQFIGATVEDDI--AFGLE--NKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 164 DNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEG-RTIVCTIHQPSTNIynLFNLVYVLSAGRCTYQGTPQ---NTVMFL 239
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI--LADKVIVFSEGKLIAQGKPKeilNNKEIL 236
|
....*...
gi 442625523 240 SSVGLECP 247
Cdd:PRK13632 237 EKAKIDSP 244
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
27-201 |
7.78e-22 |
|
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: 94.87 E-value: 7.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 27 PKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKsGVSGKIEI-GKA---------RKLCGYIMQDdhf 96
Cdd:COG1124 12 GQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLER-PWSGEVTFdGRPvtrrrrkafRRRVQMVFQD--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 fPY------FTVEETMlmAATLKISNqcvsLKEKRTLIDYLLNSLKLTKT------RQtkcsnLSGGQKKRLSIALELID 164
Cdd:COG1124 88 -PYaslhprHTVDRIL--AEPLRIHG----LPDREERIAELLEQVGLPPSfldrypHQ-----LSGGQRQRVAIARALIL 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 442625523 165 NPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE-GRTIV 201
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYL 193
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
27-207 |
1.31e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.41 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 27 PKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIGKA--------------RKLCGYIMQ 92
Cdd:PRK10535 15 PSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKP-TSGTYRVAGQdvatldadalaqlrREHFGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 93 DDHFFPYFTVEETMLMAATLKisnqCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLD 172
Cdd:PRK10535 94 RYHLLSHLTAAQNVEVPAVYA----GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169
|
170 180 190
....*....|....*....|....*....|....*
gi 442625523 173 EPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQP 207
Cdd:PRK10535 170 EPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
15-237 |
1.33e-21 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 94.41 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNvpkkpeKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTG-LTKSgvSGKIEI-GK---------- 82
Cdd:COG4559 2 LEAENLSVRLG------GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGeLTPS--SGEVRLnGRplaawspwel 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 83 ARKLCgyIM-QDDHF-FPyFTVEETMLM---------AATLKISNQCVSlkekRTLIDYLLNSLKLTktrqtkcsnLSGG 151
Cdd:COG4559 74 ARRRA--VLpQHSSLaFP-FTVEEVVALgraphgssaAQDRQIVREALA----LVGLAHLAGRSYQT---------LSGG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 152 QKKRLSIALELI-------DNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHqpstniyNLfNL------- 217
Cdd:COG4559 138 EQQRVQLARVLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLH-------DL-NLaaqyadr 209
|
250 260
....*....|....*....|
gi 442625523 218 VYVLSAGRCTYQGTPQnTVM 237
Cdd:COG4559 210 ILLLHQGRLVAQGTPE-EVL 228
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
15-233 |
1.94e-21 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 93.76 E-value: 1.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYqvNVPKKPEKKsVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTkSGVSGKIEIG----------KAR 84
Cdd:cd03249 1 IEFKNVSF--RYPSRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFY-DPTSGEILLDgvdirdlnlrWLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQDDHFF------------PYFTVEETMLMAATLKISNQCVSLKEK-RTLIDyllnslkltktrqTKCSNLSGG 151
Cdd:cd03249 77 SQIGLVSQEPVLFdgtiaenirygkPDATDEEVEEAAKKANIHDFIMSLPDGyDTLVG-------------ERGSQLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 152 QKKRLSIALELIDNPAVLFLDEPTTGLDSSSSfDTIQLLRGLANEGRTIVCTIHQPSTnIYNLfNLVYVLSAGRCTYQGT 231
Cdd:cd03249 144 QKQRIAIARALLRNPKILLLDEATSALDAESE-KLVQEALDRAMKGRTTIVIAHRLST-IRNA-DLIAVLQNGQVVEQGT 220
|
..
gi 442625523 232 PQ 233
Cdd:cd03249 221 HD 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
15-256 |
1.96e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.80 E-value: 1.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNvPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK-------------SGVSGKIEIG 81
Cdd:PRK13643 2 IKFEKVNYTYQ-PNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQptegkvtvgdivvSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 82 KARKLCGYIMQddhfFPYFTV-EETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCS-NLSGGQKKRLSIA 159
Cdd:PRK13643 81 PVRKKVGVVFQ----FPESQLfEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 160 LELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQpSTNIYNLFNLVYVLSAGRCTYQGTPQNT---V 236
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHL-MDDVADYADYVYLLEKGHIISCGTPSDVfqeV 235
|
250 260
....*....|....*....|
gi 442625523 237 MFLSSVGLECPPYHNPADFL 256
Cdd:PRK13643 236 DFLKAHELGVPKATHFADQL 255
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
35-206 |
3.50e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 93.15 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTgLTKSGVSGKIEIGKA----------------RKLCGYIMQDDHFFP 98
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLN-LLETPDSGQLNIAGHqfdfsqkpsekairllRQKVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 99 YFTVEETmLMAATLKISNQcvSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGL 178
Cdd:COG4161 96 HLTVMEN-LIEAPCKVLGL--SKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180
....*....|....*....|....*...
gi 442625523 179 DSSSSFDTIQLLRGLANEGRTIVCTIHQ 206
Cdd:COG4161 173 DPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
32-201 |
3.50e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 32 KKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIGKARKLcGYIMQDDHFFPYFTVEETMLMA-- 109
Cdd:COG0488 10 GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD-SGEVSIPKGLRI-GYLPQEPPLDDDLTVLDTVLDGda 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 110 -----------ATLKISNQCVSLKEKRTL---------------IDYLLNSLKLTKT-RQTKCSNLSGGQKKRLSIALEL 162
Cdd:COG0488 88 elraleaeleeLEAKLAEPDEDLERLAELqeefealggweaearAEEILSGLGFPEEdLDRPVSELSGGWRRRVALARAL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442625523 163 IDNPAVLFLDEPTTGLDssssFDTIQLLRG-LANEGRTIV 201
Cdd:COG0488 168 LSEPDLLLLDEPTNHLD----LESIEWLEEfLKNYPGTVL 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
15-234 |
3.55e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 93.30 E-value: 3.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNvpkkpeKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG-------KARKLC 87
Cdd:PRK13548 3 LEARNLSVRLG------GRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-SGEVRLNgrpladwSPAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 88 GY--IM-QDDHF-FPyFTVEETMLM-AATLKISNQcvslkEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALEL 162
Cdd:PRK13548 76 RRraVLpQHSSLsFP-FTVEEVVAMgRAPHGLSRA-----EDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 163 I------DNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHqpstniyNLfNL-------VYVLSAGRCTY 228
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLH-------DL-NLaaryadrIVLLHQGRLVA 221
|
....*.
gi 442625523 229 QGTPQN 234
Cdd:PRK13548 222 DGTPAE 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
25-208 |
3.61e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 93.28 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTgLTKSGVSGKIEIG------------------KARKL 86
Cdd:PRK11264 8 NLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCIN-LLEQPEAGTIRVGditidtarslsqqkglirQLRQH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 87 CGYIMQDDHFFPYFTVEETMlmaatlkISNQCVSLKEKR----TLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALEL 162
Cdd:PRK11264 87 VGFVFQNFNLFPHRTVLENI-------IEGPVIVKGEPKeeatARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442625523 163 IDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPS 208
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMS 205
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-233 |
3.89e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 93.76 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVnvpkkPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG------------K 82
Cdd:PRK13636 6 LKVEELNYNY-----SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP-SSGRILFDgkpidysrkglmK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 83 ARKLCGYIMQD-DH-FFPYFTVEETMLMAATLKISNqcvslKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIAL 160
Cdd:PRK13636 80 LRESVGMVFQDpDNqLFSASVYQDVSFGAVNLKLPE-----DEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442625523 161 ELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHqpSTNIYNLF-NLVYVLSAGRCTYQGTPQ 233
Cdd:PRK13636 155 VLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATH--DIDIVPLYcDNVFVMKEGRVILQGNPK 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
15-248 |
4.74e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.33 E-value: 4.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNVPKKpekksVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK--SG---VSG----KIEIGKARK 85
Cdd:PRK13652 4 IETRDLCYSYSGSKE-----ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKptSGsvlIRGepitKENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 86 LCGYIMQ--DDHFFPYfTVEETMLMAAT-LKISNQCVSLKekrtlIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALEL 162
Cdd:PRK13652 79 FVGLVFQnpDDQIFSP-TVEQDIAFGPInLGLDEETVAHR-----VSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 163 IDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQGTPQNTVM---F 238
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTVEEIFLqpdL 231
|
250
....*....|
gi 442625523 239 LSSVGLECPP 248
Cdd:PRK13652 232 LARVHLDLPS 241
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
32-233 |
5.40e-21 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 92.40 E-value: 5.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 32 KKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG-----------KARKLCGYIMQDDHFFPYF 100
Cdd:COG1137 15 KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD-SGRIFLDgedithlpmhkRARLGIGYLPQEASIFRKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 101 TVEETMLmaATLKISNqcVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDS 180
Cdd:COG1137 94 TVEDNIL--AVLELRK--LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442625523 181 SSSFDtIQ-LLRGLANEGRTIVCTIHqpstNIYNLFNLV---YVLSAGRCTYQGTPQ 233
Cdd:COG1137 170 IAVAD-IQkIIRHLKERGIGVLITDH----NVRETLGICdraYIISEGKVLAEGTPE 221
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
35-231 |
6.18e-21 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 91.82 E-value: 6.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKsGVSGKIEIG-----------KARKLCGYIMQDDHFFPYFTVE 103
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLP-VKSGSIRLDgeditklppheRARAGIAYVPQGREIFPRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 104 ETMLM-AATLKisnqcvslKEKRTLIDYLLNSLK-LTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSS 181
Cdd:TIGR03410 94 ENLLTgLAALP--------RRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442625523 182 SSFDTIQLLRGLANEGRTIVCTIHQPSTNIYNLFNLVYVLSAGRCTYQGT 231
Cdd:TIGR03410 166 IIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
13-247 |
9.32e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 92.78 E-value: 9.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 13 IDIHFEDL--VYQvnvPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG--------- 81
Cdd:PRK13634 1 MDITFQKVehRYQ---YKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQP-TSGTVTIGervitagkk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 82 -----KARKLCGYIMQddhfFP---YFtvEETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCS-NLSGGQ 152
Cdd:PRK13634 77 nkklkPLRKKVGIVFQ----FPehqLF--EETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 153 KKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQpSTNIYNLFNLVYVLSAGRCTYQGT 231
Cdd:PRK13634 151 MRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHS-MEDAARYADQIVVMHKGTVFLQGT 229
|
250 260
....*....|....*....|.
gi 442625523 232 PQNtvMF-----LSSVGLECP 247
Cdd:PRK13634 230 PRE--IFadpdeLEAIGLDLP 248
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
35-233 |
1.23e-20 |
|
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: 91.20 E-value: 1.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKI-----EIGK------ARKLCGYIMQDDHFFPYFTVE 103
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPP-RSGSIrfdgeDITGlpphriARLGIGYVPEGRRIFPSLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 104 ETMLMAATLKISNQCVS------------LKEKRtlidyllnslkltktRQtKCSNLSGGQKKRLSIALELIDNPAVLFL 171
Cdd:COG0410 97 ENLLLGAYARRDRAEVRadlervyelfprLKERR---------------RQ-RAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 172 DEPTTGLdsssS-------FDTIqllRGLANEGRTIVctihqpstniynlfnLV--------------YVLSAGRCTYQG 230
Cdd:COG0410 161 DEPSLGL----ApliveeiFEII---RRLNREGVTIL---------------LVeqnarfaleiadraYVLERGRIVLEG 218
|
...
gi 442625523 231 TPQ 233
Cdd:COG0410 219 TAA 221
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-247 |
1.35e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.11 E-value: 1.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDL--VYQVNVPKKpekKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGL---TKSGV----------SGKIE 79
Cdd:PRK13649 3 INLQNVsyTYQAGTPFE---GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLhvpTQGSVrvddtlitstSKNKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 80 IGKARKLCGYIMQddhfFPYFTV-EETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCS-NLSGGQKKRLS 157
Cdd:PRK13649 80 IKQIRKKVGLVFQ----FPESQLfEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPfELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 158 IALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQpSTNIYNLFNLVYVLSAGRCTYQGTPQNT-- 235
Cdd:PRK13649 156 IAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHL-MDDVANYADFVYVLEKGKLVLSGKPKDIfq 234
|
250
....*....|...
gi 442625523 236 -VMFLSSVGLECP 247
Cdd:PRK13649 235 dVDFLEEKQLGVP 247
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
25-205 |
4.00e-20 |
|
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: 89.00 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKK-PEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI---------GKA----RKLCGYI 90
Cdd:cd03292 5 NVTKTyPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELP-TSGTIRVngqdvsdlrGRAipylRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 91 MQDDHFFPYFTVEETMLMAatLKISNqcVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLF 170
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFA--LEVTG--VPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190
....*....|....*....|....*....|....*
gi 442625523 171 LDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIH 205
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
25-206 |
4.63e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 89.77 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLM---NILTGLTK-----SGVS---GKIEIGKARKLCGYIMQD 93
Cdd:PRK09493 6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKLEEITSgdlivDGLKvndPKVDERLIRQEAGMVFQQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 94 DHFFPYFTVEETmLMAATLKISNQcvSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDE 173
Cdd:PRK09493 86 FYLFPHLTALEN-VMFGPLRVRGA--SKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190
....*....|....*....|....*....|...
gi 442625523 174 PTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQ 206
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
15-230 |
5.87e-20 |
|
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: 88.96 E-value: 5.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNVPKKPEKksVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG---------KARK 85
Cdd:cd03266 2 ITADALTKRFRDVKKTVQ--AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDgfdvvkepaEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 86 LCGYIMQDDHFFPYFTVEETMLMAATLKisnqcvSLK--EKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELI 163
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFAGLY------GLKgdELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442625523 164 DNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPStNIYNLFNLVYVLSAGRCTYQG 230
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQ-EVERLCDRVVVLHRGRVVYEG 218
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
42-179 |
6.94e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 88.31 E-value: 6.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKSSLMNILTGLTKSG--VSGKIEIG---------KARKLcGYIMQDDHFFPYFTVEETMLMAA 110
Cdd:COG4136 23 TVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsASGEVLLNgrrltalpaEQRRI-GILFQDDLLFPHLSVGENLAFAL 101
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442625523 111 TLKISNQcvslkEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:COG4136 102 PPTIGRA-----QRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLD 165
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
30-247 |
1.30e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 89.28 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 30 PEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKI-----------EIGKARKLCGYIMQD-DHFF 97
Cdd:PRK13644 12 PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQ-KGKVlvsgidtgdfsKLQGIRKLVGIVFQNpETQF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 98 PYFTVEETMLMAAtlkiSNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTG 177
Cdd:PRK13644 91 VGRTVEEDLAFGP----ENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442625523 178 LDSSSSFDTIQLLRGLANEGRTIVCTIHqpstNIYNLF--NLVYVLSAGRCTYQGTPQNTV--MFLSSVGLECP 247
Cdd:PRK13644 167 LDPDSGIAVLERIKKLHEKGKTIVYITH----NLEELHdaDRIIVMDRGKIVLEGEPENVLsdVSLQTLGLTPP 236
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
33-201 |
1.36e-19 |
|
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: 88.60 E-value: 1.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVSGKIEI-----GKA-----RKLCGYI---MQDDhFFPY 99
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLfgerrGGEdvwelRKRIGLVspaLQLR-FPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 100 FTVEETMLMA--ATLKISNQcVSlKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTG 177
Cdd:COG1119 95 ETVLDVVLSGffDSIGLYRE-PT-DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAG 172
|
170 180
....*....|....*....|....*
gi 442625523 178 LDSSSSFDTIQLLRGLANEG-RTIV 201
Cdd:COG1119 173 LDLGARELLLALLDKLAAEGaPTLV 197
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
29-230 |
1.59e-19 |
|
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: 88.16 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 29 KPEKKSV--LKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG---------KARKLCGYIM-QDDHF 96
Cdd:cd03267 28 KRKYREVeaLKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQP-TSGEVRVAglvpwkrrkKFLRRIGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 FPYFTVEETM-LMAATLKISNQcvslkEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPT 175
Cdd:cd03267 107 WWDLPVIDSFyLLAAIYDLPPA-----RFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442625523 176 TGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQpSTNIYNLFNLVYVLSAGRCTYQG 230
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRErGTTVLLTSHY-MKDIEALARRVLVIDKGRLLYDG 236
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
14-237 |
2.11e-19 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 92.24 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 14 DIHFEDLVYQVNvpkkPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIGKA---------- 83
Cdd:TIGR03375 463 EIEFRNVSFAYP----GQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQP-TEGSVLLDGVdirqidpadl 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 84 RKLCGYIMQDDHFFpYFTVEETMLMAATLkISNQCVSLKEKRTLIDYLLNSLKLTKTRQT--KCSNLSGGQKKRLSIALE 161
Cdd:TIGR03375 538 RRNIGYVPQDPRLF-YGTLRDNIALGAPY-ADDEEILRAAELAGVTEFVRRHPDGLDMQIgeRGRSLSGGQRQAVALARA 615
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442625523 162 LIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLAnEGRTIVCTIHQPStniynLFNLV---YVLSAGRCTYQGtPQNTVM 237
Cdd:TIGR03375 616 LLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTS-----LLDLVdriIVMDNGRIVADG-PKDQVL 687
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
35-206 |
2.49e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 87.76 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTgLTKSGVSGKIEIG------------KA----RKLCGYIMQDDHFFP 98
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLN-LLEMPRSGTLNIAgnhfdfsktpsdKAirelRRNVGMVFQQYNLWP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 99 YFTVEETmLMAATLKISNqcVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGL 178
Cdd:PRK11124 96 HLTVQQN-LIEAPCRVLG--LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172
|
170 180
....*....|....*....|....*...
gi 442625523 179 DSSSSFDTIQLLRGLANEGRTIVCTIHQ 206
Cdd:PRK11124 173 DPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-233 |
3.63e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 87.26 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI-----------GKARKLCGYIMQD 93
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD-AGNIIIddedisllplhARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 94 DHFFPYFTVEETMLmaATLKISNQcVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDE 173
Cdd:PRK10895 87 ASIFRRLSVYDNLM--AVLQIRDD-LSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 174 PTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIyNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHGTPT 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
15-247 |
3.82e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 88.18 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYqVNVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG------------K 82
Cdd:PRK13637 3 IKIENLTH-IYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKP-TSGKIIIDgvditdkkvklsD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 83 ARKLCGYIMQddhfFP-YFTVEETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCS--NLSGGQKKRLSIA 159
Cdd:PRK13637 81 IRKKVGLVFQ----YPeYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSpfELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 160 LELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIYNLFNLVYVLSAGRCTYQGTPQ---NTV 236
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRevfKEV 236
|
250
....*....|.
gi 442625523 237 MFLSSVGLECP 247
Cdd:PRK13637 237 ETLESIGLAVP 247
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-232 |
4.58e-19 |
|
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: 86.52 E-value: 4.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNvPKKPekksVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG----------KAR 84
Cdd:cd03253 1 IEFENVTFAYD-PGRP----VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS-SGSILIDgqdirevtldSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQDDHFF------------PYFTVEETMLMAATLKISNQCVSLKEK-RTLIDyllnslkltkTRQTKcsnLSGG 151
Cdd:cd03253 75 RAIGVVPQDTVLFndtigynirygrPDATDEEVIEAAKAAQIHDKIMRFPDGyDTIVG----------ERGLK---LSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 152 QKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANeGRTIVCTIHQPSTnIYNLfNLVYVLSAGRCTYQGT 231
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLST-IVNA-DKIIVLKDGRIVERGT 218
|
.
gi 442625523 232 P 232
Cdd:cd03253 219 H 219
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
39-233 |
4.96e-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: 89.02 E-value: 4.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 39 IKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVsGKIEIG------KARKLC--------GYIMQDDHFFPYFTVEE 104
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDE-GEIVLNgrtlfdSRKGIFlppekrriGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 105 TMLMAATLkisnqcVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSF 184
Cdd:TIGR02142 95 NLRYGMKR------ARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 442625523 185 DTIQLLRGLANEGRTIVCTIHQPSTNIYNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIA 217
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
32-234 |
5.77e-19 |
|
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: 86.24 E-value: 5.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 32 KKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIGKA--------RKLCGYIMQDDHFFPYFTVE 103
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKP-DSGKILLNGKditnlppeKRDISYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 104 ETMlmAATLKISNQCVSLKEKRTL-------IDYLLNSLKLTktrqtkcsnLSGGQKKRLSIALELIDNPAVLFLDEPTT 176
Cdd:cd03299 90 KNI--AYGLKKRKVDKKEIERKVLeiaemlgIDHLLNRKPET---------LSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442625523 177 GLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIYNLFNLVYVLSAGRCTYQGTPQN 234
Cdd:cd03299 159 ALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEE 216
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
35-205 |
5.93e-19 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 86.20 E-value: 5.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK--SG---VSG------KIEIGKARKLCGYIMQddHF--FPYFT 101
Cdd:COG1126 16 VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEpdSGtitVDGedltdsKKDINKLRRKVGMVFQ--QFnlFPHLT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 102 VEETmLMAATLKIsnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSS 181
Cdd:COG1126 94 VLEN-VTLAPIKV--KKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPE 170
|
170 180
....*....|....*....|....
gi 442625523 182 SSFDTIQLLRGLANEGRTIVCTIH 205
Cdd:COG1126 171 LVGEVLDVMRDLAKEGMTMVVVTH 194
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
28-248 |
6.47e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.98 E-value: 6.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 28 KKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG-------------------------- 81
Cdd:PRK13631 34 KQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSK-YGTIQVGdiyigdkknnhelitnpyskkiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 82 KARKLCGYIMQddhfFPYF-----TVE-ETMLMAATLKISNQcvslkEKRTLIDYLLNSLKLTKTRQTKCS-NLSGGQKK 154
Cdd:PRK13631 113 ELRRRVSMVFQ----FPEYqlfkdTIEkDIMFGPVALGVKKS-----EAKKLAKFYLNKMGLDDSYLERSPfGLSGGQKR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 155 RLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQpSTNIYNLFNLVYVLSAGRCTYQGTPQN 234
Cdd:PRK13631 184 RVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTGTPYE 262
|
250
....*....|....*..
gi 442625523 235 TVM---FLSSVGLECPP 248
Cdd:PRK13631 263 IFTdqhIINSTSIQVPR 279
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
29-232 |
1.29e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 90.84 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 29 KPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG---------KARKLCGYIMQDDHFFPY 99
Cdd:TIGR01257 939 EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPP-TSGTVLVGgkdietnldAVRQSLGMCPQHNILFHH 1017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 100 FTVEETMLMAATLKISNQcvslKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:TIGR01257 1018 LTVAEHILFYAQLKGRSW----EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVD 1093
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442625523 180 SSSSFDTIQLLRGLaNEGRTIV-CTIHQPSTNIynLFNLVYVLSAGRCTYQGTP 232
Cdd:TIGR01257 1094 PYSRRSIWDLLLKY-RSGRTIImSTHHMDEADL--LGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
32-205 |
1.87e-18 |
|
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: 84.54 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 32 KKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGL----TKSGVSGKIEI-GKA-----------RKLCGYIMQDDH 95
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndliPGAPDEGEVLLdGKDiydldvdvlelRRRVGMVFQKPN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 96 FFPyFTVEETMlmAATLKIsNQCVSLKEKRTLIDYLLNSLKLTK--TRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDE 173
Cdd:cd03260 92 PFP-GSIYDNV--AYGLRL-HGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARALANEPEVLLLDE 167
|
170 180 190
....*....|....*....|....*....|..
gi 442625523 174 PTTGLDSSSSFDTIQLLRGLANEgRTIVCTIH 205
Cdd:cd03260 168 PTSALDPISTAKIEELIAELKKE-YTIVIVTH 198
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
42-233 |
2.00e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 84.81 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI-GK--------ARKLcGYIMQDDHFFPYFTVEETML--MAA 110
Cdd:COG3840 21 TIAAGERVAILGPSGAGKSTLLNLIAGFLPPD-SGRILWnGQdltalppaERPV-SMLFQENNLFPHLTVAQNIGlgLRP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 111 TLKISnqcvslKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLL 190
Cdd:COG3840 99 GLKLT------AEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442625523 191 RGLANE-GRTIVCTIHQPStNIYNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:COG3840 173 DELCRErGLTVLMVTHDPE-DAARIADRVLLVADGRIAADGPTA 215
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
18-232 |
2.24e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 84.73 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 18 EDLVYQVnvpkkpEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGV-SGKIEI-GK----------ARK 85
Cdd:COG0396 4 KNLHVSV------EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEVtSGSILLdGEdilelspderARA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 86 LCGYIMQDdhffPyftVE------ETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSN--LSGGQKKRLS 157
Cdd:COG0396 78 GIFLAFQY----P---VEipgvsvSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNegFSGGEKKRNE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 158 IALELIDNPAVLFLDEPTTGLDssssFDTIQLLRG----LANEGRTIVCTIHQPstniyNLFNL-----VYVLSAGRCTY 228
Cdd:COG0396 151 ILQMLLLEPKLAILDETDSGLD----IDALRIVAEgvnkLRSPDRGILIITHYQ-----RILDYikpdfVHVLVDGRIVK 221
|
....
gi 442625523 229 QGTP 232
Cdd:COG0396 222 SGGK 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
32-237 |
2.64e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 85.07 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 32 KKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG-------KARKLCGYI--MQDDHFFPY-FT 101
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP-QSGTVFLGdkpismlSSRQLARRLalLPQHHLTPEgIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 102 VEEtmLMAATlkiSNQCVSL-----KEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTT 176
Cdd:PRK11231 93 VRE--LVAYG---RSPWLSLwgrlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442625523 177 GLDSSSSFDTIQLLRGLANEGRTIVCTIH---QPSTNIYNLFnlvyVLSAGRCTYQGTPQNtVM 237
Cdd:PRK11231 168 YLDINHQVELMRLMRELNTQGKTVVTVLHdlnQASRYCDHLV----VLANGHVMAQGTPEE-VM 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
30-209 |
2.75e-18 |
|
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: 88.50 E-value: 2.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 30 PEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIGKA----------RKLCGYIMQDDHFFPY 99
Cdd:TIGR02857 332 PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT-EGSIAVNGVpladadadswRDQIAWVPQHPFLFAG 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 100 fTVEETMLMAaTLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQ--TKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTG 177
Cdd:TIGR02857 411 -TIAENIRLA-RPDASDAEIREALERAGLDEFVAALPQGLDTPigEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190
....*....|....*....|....*....|..
gi 442625523 178 LDSSSSFDTIQLLRGLAnEGRTIVCTIHQPST 209
Cdd:TIGR02857 489 LDAETEAEVLEALRALA-QGRTVLLVTHRLAL 519
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-180 |
2.80e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.91 E-value: 2.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 24 VNVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI-GKA-------RklcGYIMQDDH 95
Cdd:COG4525 11 VRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS-SGEITLdGVPvtgpgadR---GVVFQKDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 96 FFPYFTVEETMlmAATLKIsnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPT 175
Cdd:COG4525 87 LLPWLNVLDNV--AFGLRL--RGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPF 162
|
....*
gi 442625523 176 TGLDS 180
Cdd:COG4525 163 GALDA 167
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
32-247 |
2.83e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 85.24 E-value: 2.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 32 KKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGL--------TKSGVSGkIEIGK-----ARKLCGYIMQD-DHFF 97
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpddnpnSKITVDG-ITLTAktvwdIREKVGIVFQNpDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 98 PYFTVEETMlmaaTLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTG 177
Cdd:PRK13640 98 VGATVGDDV----AFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSM 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442625523 178 LDSSSSFDTIQLLRGLANE-GRTIVCTIHqpSTNIYNLFNLVYVLSAGRCTYQGTPQ---NTVMFLSSVGLECP 247
Cdd:PRK13640 174 LDPAGKEQILKLIRKLKKKnNLTVISITH--DIDEANMADQVLVLDDGKLLAQGSPVeifSKVEMLKEIGLDIP 245
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
25-233 |
3.79e-18 |
|
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: 83.83 E-value: 3.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG--------KARKLCGYIMQDDHF 96
Cdd:cd03300 5 NVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPT-SGEILLDgkditnlpPHKRPVNTVFQNYAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 FPYFTVEETMLMAATLKISNQcvslKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTT 176
Cdd:cd03300 84 FPHLTVFENIAFGLRLKKLPK----AEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442625523 177 GLDSSSSFDTIQLLRGLANE-GRTIVCTIHQPSTNIyNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:cd03300 160 ALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEAL-TMSDRIAVMNKGKIQQIGTPE 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
36-233 |
4.23e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.68 E-value: 4.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 36 LKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVS---------------GKI--EIGKARKLCGYIMQDDHFFP 98
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSagshiellgrtvqreGRLarDIRKSRANTGYIFQQFNLVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 99 YFTVEETMLMAA--TLKISNQCVS----LKEKRTLidYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLD 172
Cdd:PRK09984 100 RLSVLENVLIGAlgSTPFWRTCFSwftrEQKQRAL--QALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442625523 173 EPTTGLDSSSSFDTIQLLRGL-ANEGRTIVCTIHQPSTNIYNLFNLVyVLSAGRCTYQGTPQ 233
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIV-ALRQGHVFYDGSSQ 238
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
24-233 |
7.02e-18 |
|
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: 83.16 E-value: 7.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 24 VNVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG---------KARKLcGYIMQDD 94
Cdd:cd03296 6 RNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD-SGTILFGgedatdvpvQERNV-GFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 95 HFFPYFTVEETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEP 174
Cdd:cd03296 84 ALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 175 TTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQPSTNIyNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:cd03296 164 FGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEAL-EVADRVVVMNKGRIEQVGTPD 222
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
31-232 |
7.22e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.90 E-value: 7.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 31 EKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVSGKIEIGKA-----------RKLCGYIMQD-DHFFP 98
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldyskrgllalRQQVATVFQDpEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 99 YFTVEETMlmaaTLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGL 178
Cdd:PRK13638 92 YTDIDSDI----AFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442625523 179 DSSSSFDTIQLLRGLANEGRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQGTP 232
Cdd:PRK13638 168 DPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHGAP 220
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
35-190 |
8.29e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.94 E-value: 8.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLtKSGVSGKIeIGKARKL---------------CGYIMQDDHFFPY 99
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-DTPTSGDV-IFNGQPMsklssaakaelrnqkLGFIYQFHHLLPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 100 FTVEETMLMAatLKISNQCVSLKEKRTLidYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:PRK11629 102 FTALENVAMP--LLIGKKKPAEINSRAL--EMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170
....*....|.
gi 442625523 180 SSSSFDTIQLL 190
Cdd:PRK11629 178 ARNADSIFQLL 188
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
35-201 |
1.03e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 86.23 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI-GK---------ARKL-CGYIMQDDHFFPYFTVE 103
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD-SGEILLdGEpvrfrsprdAQAAgIAIIHQELNLVPNLSVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 104 ETMLMAATLKisnqcvslkeKRTLIDY---------LLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEP 174
Cdd:COG1129 98 ENIFLGREPR----------RGGLIDWramrrrareLLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEP 167
|
170 180 190
....*....|....*....|....*....|
gi 442625523 175 TTGLDSSSS---FDtiqLLRGLANEGRTIV 201
Cdd:COG1129 168 TASLTEREVerlFR---IIRRLKAQGVAII 194
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
36-205 |
1.23e-17 |
|
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: 82.51 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 36 LKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVSGKIEIGKARKLCG----YIMQDDHFFPYFTVEETMLMAat 111
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGpdrmVVFQNYSLLPWLTVRENIALA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 112 LKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLR 191
Cdd:TIGR01184 79 VDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170
....*....|....*
gi 442625523 192 GLANEGR-TIVCTIH 205
Cdd:TIGR01184 159 QIWEEHRvTVLMVTH 173
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
35-180 |
1.30e-17 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 84.43 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG----------KARKlCGYIMQddHF--FPYFTV 102
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPD-SGRIVLNgrdlftnlppRERR-VGFVFQ--HYalFPHMTV 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442625523 103 EETmlMAATLKIsnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDS 180
Cdd:COG1118 93 AEN--IAFGLRV--RPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
42-201 |
1.32e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 82.86 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKI-------------EI---GKARKlcgyimqddhF-----FPYF 100
Cdd:COG4674 32 YVDPGELRVIIGPNGAGKTTLMDVITGKTRPD-SGSVlfggtdltgldehEIarlGIGRK----------FqkptvFEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 101 TVEETMLMA--------ATL--KISnqcvslKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLF 170
Cdd:COG4674 101 TVFENLELAlkgdrgvfASLfaRLT------AEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLL 174
|
170 180 190
....*....|....*....|....*....|.
gi 442625523 171 LDEPTTGLDSSSSFDTIQLLRGLAnEGRTIV 201
Cdd:COG4674 175 LDEPVAGMTDAETERTAELLKSLA-GKHSVV 204
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-207 |
1.41e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 82.79 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGL-----TKSGVSGK----------IEIGKARKLCGYIMQDDHFF 97
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydSKIKVDGKvlyfgkdifqIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 98 PYFTVEETMlmAATLKiSNQCVSLKEKRTLIDYLLNSLKLTKT----RQTKCSNLSGGQKKRLSIALELIDNPAVLFLDE 173
Cdd:PRK14246 103 PHLSIYDNI--AYPLK-SHGIKEKREIKKIVEECLRKVGLWKEvydrLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190
....*....|....*....|....*....|....
gi 442625523 174 PTTGLDSSSSFDTIQLLRGLANEgRTIVCTIHQP 207
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNP 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
14-233 |
2.65e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 85.60 E-value: 2.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 14 DIHFEDLV--YqvnvpkkPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGL---TksgvSGKIEIGKA----- 83
Cdd:COG1132 339 EIEFENVSfsY-------PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFydpT----SGRILIDGVdirdl 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 84 -----RKLCGYIMQDDHFF------------PYFTVEEtmLMAAtLKISNqcvsLKEkrtLIDYLLNSLkltktrQTKC- 145
Cdd:COG1132 408 tleslRRQIGVVPQDTFLFsgtirenirygrPDATDEE--VEEA-AKAAQ----AHE---FIEALPDGY------DTVVg 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 146 ---SNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLAnEGRTIVcTI-HQPSTnIYNlFNLVYVL 221
Cdd:COG1132 472 ergVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTI-VIaHRLST-IRN-ADRILVL 547
|
250
....*....|..
gi 442625523 222 SAGRCTYQGTPQ 233
Cdd:COG1132 548 DDGRIVEQGTHE 559
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-208 |
2.79e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.81 E-value: 2.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLM---NILTGLTKSG-VSGKIEI-GK-----------ARKLCGYIMQDDHFFP 98
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEArVEGEVRLfGRniyspdvdpieVRREVGMVFQYPNPFP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 99 YFTVEETMlmAATLKISNQCVSLKEKRTLIDYLLNSLKL---TKTR-QTKCSNLSGGQKKRLSIALELIDNPAVLFLDEP 174
Cdd:PRK14267 99 HLTIYDNV--AIGVKLNGLVKSKKELDERVEWALKKAALwdeVKDRlNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190
....*....|....*....|....*....|....
gi 442625523 175 TTGLDSSSSFDTIQLLRGLANEgRTIVCTIHQPS 208
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKE-YTIVLVTHSPA 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
25-234 |
4.66e-17 |
|
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: 80.81 E-value: 4.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKK-PEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG----------KARKLCGYIMQD 93
Cdd:cd03295 5 NVTKRyGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP-TSGEIFIDgedireqdpvELRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 94 DHFFPYFTVEETMLMAATLkisnQCVSLKEKRTLIDYLLNSLKL--TKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFL 171
Cdd:cd03295 84 IGLFPHMTVEENIALVPKL----LKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442625523 172 DEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHqpstNIYNLFNL---VYVLSAGRCTYQGTPQN 234
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTH----DIDEAFRLadrIAIMKNGEIVQVGTPDE 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
28-233 |
8.10e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.78 E-value: 8.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 28 KKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSG----------------------VSGKIEIGKARK 85
Cdd:PRK10619 13 KRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSegsivvngqtinlvrdkdgqlkVADKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 86 LCGYIMQDDHFFPYFTVEETmLMAATLKISNqcVSLKEKRTLIDYLLNSLKLTKTRQTKC-SNLSGGQKKRLSIALELID 164
Cdd:PRK10619 93 RLTMVFQHFNLWSHMTVLEN-VMEAPIQVLG--LSKQEARERAVKYLAKVGIDERAQGKYpVHLSGGQQQRVSIARALAM 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442625523 165 NPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:PRK10619 170 EPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGF-ARHVSSHVIFLHQGKIEEEGAPE 237
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
17-225 |
1.18e-16 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 83.17 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 17 FEDLVYQVNVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIGKAR----------KL 86
Cdd:TIGR01842 315 GHLSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPP-TSGSVRLDGADlkqwdretfgKH 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 87 CGYIMQDDHFFPYFTVE-----------ETMLMAATLKISNQcvslkekrtLIdyllnsLKLTKTRQTKC----SNLSGG 151
Cdd:TIGR01842 394 IGYLPQDVELFPGTVAEniarfgenadpEKIIEAAKLAGVHE---------LI------LRLPDGYDTVIgpggATLSGG 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442625523 152 QKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPStnIYNLFNLVYVLSAGR 225
Cdd:TIGR01842 459 QRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPS--LLGCVDKILVLQDGR 530
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
35-179 |
1.69e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 81.27 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK-SgvSGKIEIG---------KARKLcGYIMQDDHFFPYFTVEE 104
Cdd:COG3839 18 ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDpT--SGEILIGgrdvtdlppKDRNI-AMVFQSYALYPHMTVYE 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442625523 105 TMLMAatLKISNqcVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:COG3839 95 NIAFP--LKLRK--VPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
42-230 |
1.99e-16 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 78.36 E-value: 1.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI--------GKARKLCGYIMQDDHFFPYFTVEETMLMAATlk 113
Cdd:TIGR01277 20 NVADGEIVAIMGPSGAGKSTLLNLIAGFIEP-ASGSIKVndqshtglAPYQRPVSMLFQENNLFAHLTVRQNIGLGLH-- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 114 isnqcVSLKekrtlidylLNSLKLTKTRQTKCS------------NLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSS 181
Cdd:TIGR01277 97 -----PGLK---------LNAEQQEKVVDAAQQvgiadyldrlpeQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442625523 182 SSFDTIQLLRGLANE-GRTIVCTIHQPSTNIyNLFNLVYVLSAGRCTYQG 230
Cdd:TIGR01277 163 LREEMLALVKQLCSErQRTLLMVTHHLSDAR-AIASQIAVVSQGKIKVVS 211
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
45-205 |
2.16e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.54 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 45 SGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI-----GKARK--LCGYIMQD---DHFFPYFtVEETMLMAATLKI 114
Cdd:PRK15056 32 GGSIAALVGVNGSGKSTLFKALMGFVRLA-SGKISIlgqptRQALQknLVAYVPQSeevDWSFPVL-VEDVVMMGRYGHM 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 115 SNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLA 194
Cdd:PRK15056 110 GWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELR 189
|
170
....*....|.
gi 442625523 195 NEGRTIVCTIH 205
Cdd:PRK15056 190 DEGKTMLVSTH 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
33-190 |
2.20e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.42 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIGKARKLcGYIMQD-DHFFPYFTVEETMLMAAt 111
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEP-DSGTVKLGETVKI-GYFDQHqEELDPDKTVLDELRDGA- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 112 lkisnqcvSLKEKRTLIDYlLNSLKLTKTRQ-TKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDssssFDTIQLL 190
Cdd:COG0488 405 --------PGGTEQEVRGY-LGRFLFSGDDAfKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLD----IETLEAL 471
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
15-242 |
3.75e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 80.12 E-value: 3.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDL--VYqvnvPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG----------- 81
Cdd:COG1135 2 IELENLskTF----PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPT-SGSVLVDgvdltalsere 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 82 --KARKLCGYIMQddHF--FPYFTVEETMlmAATLKISNqcVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLS 157
Cdd:COG1135 77 lrAARRKIGMIFQ--HFnlLSSRTVAENV--ALPLEIAG--VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 158 IALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLaNE--GRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQGT---- 231
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSILDLLKDI-NRelGLTIVLITHEMDV-VRRICDRVAVLENGRIVEQGPvldv 228
|
250
....*....|....*.
gi 442625523 232 ---PQN--TVMFLSSV 242
Cdd:COG1135 229 fanPQSelTRRFLPTV 244
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
15-302 |
3.95e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 79.84 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDL--VYQVNVPKKPekksVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG----------- 81
Cdd:PRK11153 2 IELKNIskVFPQGGRTIH----ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERP-TSGRVLVDgqdltalseke 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 82 --KARKLCGYIMQddHF--FPYFTVEETMLMAatLKISNqcVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLS 157
Cdd:PRK11153 77 lrKARRQIGMIFQ--HFnlLSSRTVFDNVALP--LELAG--TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 158 IALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQGT----- 231
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDV-VKRICDRVAVIDAGRLVEQGTvsevf 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442625523 232 --PQN--TVMFLSSV-GLECPPYhnpadfLLECANGDYGDQTEALaeaakdIRWRYdqqlmQGEDADAPSETQVAK 302
Cdd:PRK11153 230 shPKHplTREFIQSTlHLDLPED------YLARLQAEPTTGSGPL------LRLEF-----TGESVDAPLLSETAR 288
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
15-209 |
4.46e-16 |
|
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: 77.90 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYqvNVPKKPEKKsVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI-GKArklcgyIMQD 93
Cdd:cd03248 12 VKFQNVTF--AYPTRPDTL-VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQP-QGGQVLLdGKP------ISQY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 94 DHFFPYFTV----EETMLMAATLK---------ISNQCVSLKEKRTLIDYLLNSLKL---TKTRQtKCSNLSGGQKKRLS 157
Cdd:cd03248 82 EHKYLHSKVslvgQEPVLFARSLQdniayglqsCSFECVKEAAQKAHAHSFISELASgydTEVGE-KGSQLSGGQKQRVA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442625523 158 IALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGlANEGRTIVCTIHQPST 209
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLST 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
25-179 |
6.91e-16 |
|
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: 76.91 E-value: 6.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG---------KARKLcGYIMQDDH 95
Cdd:cd03301 5 NVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT-SGRIYIGgrdvtdlppKDRDI-AMVFQNYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 96 FFPYFTVEETMLMAATLKISNQcVSLKEK-----RTL-IDYLLNSlkltKTRQtkcsnLSGGQKKRLSIALELIDNPAVL 169
Cdd:cd03301 83 LYPHMTVYDNIAFGLKLRKVPK-DEIDERvrevaELLqIEHLLDR----KPKQ-----LSGGQRQRVALGRAIVREPKVF 152
|
170
....*....|
gi 442625523 170 FLDEPTTGLD 179
Cdd:cd03301 153 LMDEPLSNLD 162
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
35-207 |
7.13e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 76.24 E-value: 7.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKI-----EIGKARKL----CGYIMQDDHFFPYFTVEET 105
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP-DSGEVrwngtPLAEQRDEphenILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 106 MLMAATLkisnqcvsLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFD 185
Cdd:TIGR01189 94 LHFWAAI--------HGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|..
gi 442625523 186 TIQLLRGLANEGRTIVCTIHQP 207
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLLTTHQD 187
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-231 |
7.52e-16 |
|
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: 77.27 E-value: 7.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNvpkkPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILT---GLTksgvSGKIEI----------G 81
Cdd:cd03251 1 VEFKNVTFRYP----GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPrfyDVD----SGRILIdghdvrdytlA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 82 KARKLCGYIMQDDHFFpYFTVEETMLMA---ATLKISNQCVSLKEKRTLIDyllnslKLTKTRQTKC----SNLSGGQKK 154
Cdd:cd03251 73 SLRRQIGLVSQDVFLF-NDTVAENIAYGrpgATREEVEEAARAANAHEFIM------ELPEGYDTVIgergVKLSGGQRQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442625523 155 RLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLAnEGRTIVCTIHQPSTnIYNLFNLVyVLSAGRCTYQGT 231
Cdd:cd03251 146 RIAIARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLST-IENADRIV-VLEDGKIVERGT 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
15-247 |
8.41e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 77.85 E-value: 8.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYqvnvpKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTG--LTKSG---VSGKiEIGKA-----R 84
Cdd:PRK13647 5 IEVEDLHF-----RYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiyLPQRGrvkVMGR-EVNAEnekwvR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQD--DHFFPYfTVEETMLMAATlkisNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALEL 162
Cdd:PRK13647 79 SKVGLVFQDpdDQVFSS-TVWDDVAFGPV----NMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 163 IDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIyNLFNLVYVLSAGRCTYQGTPQ--NTVMFLS 240
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEGDKSllTDEDIVE 232
|
....*..
gi 442625523 241 SVGLECP 247
Cdd:PRK13647 233 QAGLRLP 239
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
34-233 |
9.83e-16 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 79.50 E-value: 9.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 34 SVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG----------KARKLCGYIMQDDHFFPYFTVE 103
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPT-AGTVLVAgddvealsarAASRRVASVPQDTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 104 ETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSS 183
Cdd:PRK09536 96 QVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442625523 184 FDTIQLLRGLANEGRTIVCTIHqpSTNIYNLF-NLVYVLSAGRCTYQGTPQ 233
Cdd:PRK09536 176 VRTLELVRRLVDDGKTAVAAIH--DLDLAARYcDELVLLADGRVRAAGPPA 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
34-208 |
1.02e-15 |
|
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: 76.70 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 34 SVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGL-TKSgvSGKIEI-----------GKAR---KLCGYIMQDDHFFP 98
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPT--SGTVRLagqdlfaldedARARlraRHVGFVFQSFQLLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 99 YFTVEETMLMAATLKisnqcvSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGL 178
Cdd:COG4181 104 TLTALENVMLPLELA------GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNL 177
|
170 180 190
....*....|....*....|....*....|.
gi 442625523 179 DSSSSFDTIQLLRGLANE-GRTIVCTIHQPS 208
Cdd:COG4181 178 DAATGEQIIDLLFELNRErGTTLVLVTHDPA 208
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
49-179 |
1.17e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 78.76 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 49 TAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIGK------ARKLC--------GYIMQDDHFFPYFTVEETML--MAATL 112
Cdd:PRK11144 27 TAIFGRSGAGKTSLINAISGLTRPQ-KGRIVLNGrvlfdaEKGIClppekrriGYVFQDARLFPHYKVRGNLRygMAKSM 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442625523 113 KIS-NQCVSLkekrtL-IDYLLNSLKLTktrqtkcsnLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:PRK11144 106 VAQfDKIVAL-----LgIEPLLDRYPGS---------LSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
15-234 |
1.54e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.56 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYqVNVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG------------- 81
Cdd:PRK13641 3 IKFENVDY-IYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPS-SGTITIAgyhitpetgnknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 82 -KARKLCGYIMQddhfFPYFTV-EETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCS-NLSGGQKKRLSI 158
Cdd:PRK13641 81 kKLRKKVSLVFQ----FPEAQLfENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442625523 159 ALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQpSTNIYNLFNLVYVLSAGRCTYQGTPQN 234
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHN-MDDVAEYADDVLVLEHGKLIKHASPKE 231
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
31-225 |
1.89e-15 |
|
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: 76.15 E-value: 1.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 31 EKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGV-SGKIEIG-----------KARKLCGYIMQDDHFFP 98
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHPSYEVtSGTILFKgqdllelepdeRARAGLFLAFQYPEEIP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 99 YFTVEE---TMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSN--LSGGQKKRLSIALELIDNPAVLFLDE 173
Cdd:TIGR01978 91 GVSNLEflrSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNegFSGGEKKRNEILQMALLEPKLAILDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 174 PTTGLDSSS---SFDTIQLLRglaNEGRTIVCTIHQPstniyNLFNL-----VYVLSAGR 225
Cdd:TIGR01978 171 IDSGLDIDAlkiVAEGINRLR---EPDRSFLIITHYQ-----RLLNYikpdyVHVLLDGR 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
35-207 |
2.18e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 75.30 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKI-------EIGKARKLCGYIMQDDHFFPYFTVEETML 107
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-AAGTIkldggdiDDPDVAEACHYLGHRNAMKPALTVAENLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 108 MAATLkisnqcvsLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSsfdtI 187
Cdd:PRK13539 96 FWAAF--------LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA----V 163
|
170 180
....*....|....*....|....
gi 442625523 188 QLLRGL----ANEGRTIVCTIHQP 207
Cdd:PRK13539 164 ALFAELirahLAQGGIVIAATHIP 187
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-233 |
2.22e-15 |
|
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: 79.41 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNVPKKPekksVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIGKA----------R 84
Cdd:COG4618 331 LSVENLTVVPPGSKRP----ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPP-TAGSVRLDGAdlsqwdreelG 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQDDHFFPYfTVEE-----------TMLMAATLkisnqcVSLKEkrtLIdyllnsLKLTKTRQTKC----SNLS 149
Cdd:COG4618 406 RHIGYLPQDVELFDG-TIAEniarfgdadpeKVVAAAKL------AGVHE---MI------LRLPDGYDTRIgeggARLS 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 150 GGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPStnIYNLFNLVYVLSAGRCTYQ 229
Cdd:COG4618 470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS--LLAAVDKLLVLRDGRVQAF 547
|
....
gi 442625523 230 GTPQ 233
Cdd:COG4618 548 GPRD 551
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
14-232 |
2.69e-15 |
|
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: 75.22 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 14 DIHFEDlvyqVNVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTkSGVSGKIEIG----------KA 83
Cdd:cd03244 2 DIEFKN----VSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLV-ELSSGSILIDgvdiskiglhDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 84 RKLCGYIMQDDHFF---------PYFTVEETMLMAATLKisnqcVSLKEkrtlidYLLNSLKLTKTRQTKC-SNLSGGQK 153
Cdd:cd03244 77 RSRISIIPQDPVLFsgtirsnldPFGEYSDEELWQALER-----VGLKE------FVESLPGGLDTVVEEGgENLSVGQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 154 KRLSIALELIDNPAVLFLDEPTTGLDsSSSFDTIQ-LLRGlANEGRTIVCTIHQPSTNIYnlFNLVYVLSAGRCTYQGTP 232
Cdd:cd03244 146 QLLCLARALLRKSKILVLDEATASVD-PETDALIQkTIRE-AFKDCTVLTIAHRLDTIID--SDRILVLDKGRVVEFDSP 221
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-207 |
3.18e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 75.72 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLT----KSGVSG----------KIEIGKARKLCGYIMQDDHFFPYF 100
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypEARVSGevyldgqdifKMDVIELRRRVQMVFQIPNPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 101 TVEETMlmAATLKISNQCVSLKEKRTLIDYLLNSLKL---TKTR-QTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTT 176
Cdd:PRK14247 98 SIFENV--ALGLKLNRLVKSKKELQERVRWALEKAQLwdeVKDRlDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190
....*....|....*....|....*....|.
gi 442625523 177 GLDSSSSFDTIQLLRGLANEgRTIVCTIHQP 207
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKD-MTIVLVTHFP 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
25-206 |
4.31e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 76.30 E-value: 4.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI-GK-----ARKLCGYI-------- 90
Cdd:COG4152 6 GLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD-SGEVLWdGEpldpeDRRRIGYLpeerglyp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 91 -MqddhffpyfTVEETMLMAATLKisnqCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVL 169
Cdd:COG4152 85 kM---------KVGEQLVYLARLK----GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 442625523 170 FLDEPTTGLDSSSSfDTI-QLLRGLANEGRTIVCTIHQ 206
Cdd:COG4152 152 ILDEPFSGLDPVNV-ELLkDVIRELAAKGTTVIFSSHQ 188
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
42-201 |
4.58e-15 |
|
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: 76.63 E-value: 4.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKSSLMNILTGLTKSG--VSGKI-----EIGKA-----RKLCG----YIMQD--DHFFPYFTVE 103
Cdd:COG0444 27 DVRRGETLGLVGESGSGKSTLARAILGLLPPPgiTSGEIlfdgeDLLKLsekelRKIRGreiqMIFQDpmTSLNPVMTVG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 104 ETMlmAATLKISNQcVSLKEKRTLIDYLLNSLKLTKTRQTKCS---NLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDS 180
Cdd:COG0444 107 DQI--AEPLRIHGG-LSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQRVMIARALALEPKLLIADEPTTALDV 183
|
170 180
....*....|....*....|..
gi 442625523 181 SSSFDTIQLLRGLANE-GRTIV 201
Cdd:COG0444 184 TIQAQILNLLKDLQRElGLAIL 205
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
21-230 |
4.67e-15 |
|
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: 73.50 E-value: 4.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 21 VYQVNVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIGKarklcgyimqddhfFPYF 100
Cdd:cd03247 3 INNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ-QGEITLDG--------------VPVS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 101 TVEETMlmAATLKISNQCVslkekrtlidYLLNslklTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDS 180
Cdd:cd03247 68 DLEKAL--SSLISVLNQRP----------YLFD----TTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442625523 181 SSSFdtiQLLRGLAN--EGRTIVCTIHQpSTNIYNlFNLVYVLSAGRCTYQG 230
Cdd:cd03247 132 ITER---QLLSLIFEvlKDKTLIWITHH-LTGIEH-MDKILFLENGKIIMQG 178
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
31-225 |
4.69e-15 |
|
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: 74.10 E-value: 4.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 31 EKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVSGkieigkarklcGYIMQDDHFFPYFTVEETMLMAA 110
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVTE-----------GEILFKGEDITDLPPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 111 TLkiSNQCVSLKEKRTLIDYL--LNslkltktrqtkcSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQ 188
Cdd:cd03217 80 FL--AFQYPPEIPGVKNADFLryVN------------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAE 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 442625523 189 LLRGLANEGRTIVCTIHQPSTNIYNLFNLVYVLSAGR 225
Cdd:cd03217 146 VINKLREEGKSVLIITHYQRLLDYIKPDRVHVLYDGR 182
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
15-206 |
4.95e-15 |
|
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: 74.04 E-value: 4.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNvPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTG-LTKsgVSGKIEIGKArklCGYIMQd 93
Cdd:cd03250 1 ISVEDASFTWD-SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGeLEK--LSGSVSVPGS---IAYVSQ- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 94 dhfFPYftveetmLMAATLKiSNQCVSLK--EKR--TLIDY--LLNSLK-LTKTRQT----KCSNLSGGQKKRLSIALEL 162
Cdd:cd03250 74 ---EPW-------IQNGTIR-ENILFGKPfdEERyeKVIKAcaLEPDLEiLPDGDLTeigeKGINLSGGQKQRISLARAV 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 442625523 163 IDNPAVLFLDEPTTGLDSSSS---FDtiQLLRGLANEGRTIVCTIHQ 206
Cdd:cd03250 143 YSDADIYLLDDPLSAVDAHVGrhiFE--NCILGLLLNNKTRILVTHQ 187
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
25-233 |
7.03e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 76.28 E-value: 7.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLtKSGVSGKIEIG---------KARKLcGYIMQDDH 95
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGL-EHQTSGHIRFHgtdvsrlhaRDRKV-GFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 96 FFPYFTVEETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPT 175
Cdd:PRK10851 85 LFRHMTVFDNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 442625523 176 TGLDSSSSFDTIQLLRGLANEGR-TIVCTIHQPSTNIyNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAM-EVADRVVVMSQGNIEQAGTPD 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
35-201 |
8.72e-15 |
|
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: 72.08 E-value: 8.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI-GKArklcgyimqddhfFPYFTVEEtmlmAATLK 113
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD-SGEILVdGKE-------------VSFASPRD----ARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 114 IsnQCVSlkekrtlidyllnslkltktrQtkcsnLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGL 193
Cdd:cd03216 77 I--AMVY---------------------Q-----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL 128
|
....*...
gi 442625523 194 ANEGRTIV 201
Cdd:cd03216 129 RAQGVAVI 136
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
33-205 |
8.85e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.76 E-value: 8.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKI-------------EIGKARKLCGYIMQDDHFFPY 99
Cdd:PRK10908 15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPS-AGKIwfsghditrlknrEVPFLRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 100 FTVEETMlmAATLKISNqcVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:PRK10908 94 RTVYDNV--AIPLIIAG--ASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
170 180
....*....|....*....|....*.
gi 442625523 180 SSSSFDTIQLLRGLANEGRTIVCTIH 205
Cdd:PRK10908 170 DALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
8-209 |
1.01e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 77.45 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 8 KNVYGIdIHFEDLVYqvNVPKKPEKKsVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIGKARklc 87
Cdd:TIGR00958 473 LNLEGL-IEFQDVSF--SYPNRPDVP-VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQP-TGGQVLLDGVP--- 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 88 gyIMQDDHFFPYFTV----EETMLMAATLKiSNQCVSLKekRTLIDYLLNSLK----------LTKTRQTKC----SNLS 149
Cdd:TIGR00958 545 --LVQYDHHYLHRQValvgQEPVLFSGSVR-ENIAYGLT--DTPDEEIMAAAKaanahdfimeFPNGYDTEVgekgSQLS 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 150 GGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFdTIQLLRGLAneGRTIVCTIHQPST 209
Cdd:TIGR00958 620 GGQKQRIAIARALVRKPRVLILDEATSALDAECEQ-LLQESRSRA--SRTVLLIAHRLST 676
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
30-207 |
1.20e-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: 77.02 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 30 PEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGL--------TKSGVS-GKIEIGKARKLCGYIMQDDHFFPYf 100
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLldplqgevTLDGVPvSSLDQDEVRRRVSVCAQDAHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 101 TVEETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTR-QTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:TIGR02868 424 TVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVlGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*...
gi 442625523 180 SSSSFDTIQLLRGlANEGRTIVCTIHQP 207
Cdd:TIGR02868 504 AETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
42-235 |
1.38e-14 |
|
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: 75.52 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKSSLMNILTGLTKsGVSGKIEIG------KARKLC--------GYIMQDDHFFPYFTVEETML 107
Cdd:COG4148 21 TLPGRGVTALFGPSGSGKTTLLRAIAGLER-PDSGRIRLGgevlqdSARGIFlpphrrriGYVFQEARLFPHLSVRGNLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 108 MAAT-LKISNQCVSLKEKRTL--IDYLLNslkltktRQTkcSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSF 184
Cdd:COG4148 100 YGRKrAPRAERRISFDEVVELlgIGHLLD-------RRP--ATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 442625523 185 DTIQLLRGLANEGRT-IVCTIHQPsTNIYNLFNLVYVLSAGRCTYQGTPQNT 235
Cdd:COG4148 171 EILPYLERLRDELDIpILYVSHSL-DEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
25-242 |
1.38e-14 |
|
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: 76.76 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK-SGVSGKI-----------------EIGKARKL 86
Cdd:TIGR03269 5 NLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyEPTSGRIiyhvalcekcgyverpsKVGEPCPV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 87 CGYIMQDDHFfPYFTVEETMLMAATLKIS---NQCVSLKEKRTLIDYLLNSLK-------------LTKTRQTKCS---- 146
Cdd:TIGR03269 85 CGGTLEPEEV-DFWNLSDKLRRRIRKRIAimlQRTFALYGDDTVLDNVLEALEeigyegkeavgraVDLIEMVQLShrit 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 147 ----NLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSfDTIQ--LLRGLANEGRTIVCTIHQPSTnIYNLFNLVYV 220
Cdd:TIGR03269 164 hiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTA-KLVHnaLEEAVKASGISMVLTSHWPEV-IEDLSDKAIW 241
|
250 260
....*....|....*....|...
gi 442625523 221 LSAGRCTYQGTPQNTV-MFLSSV 242
Cdd:TIGR03269 242 LENGEIKEEGTPDEVVaVFMEGV 264
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
33-207 |
1.61e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 72.53 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKI---------EIGKARKLCGYIMQDDHFFPYFTVE 103
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP-LAGRVllnggpldfQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 104 ETMLMAATLKISNQCVSLkekrtlidylLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSS 183
Cdd:cd03231 92 ENLRFWHADHSDEQVEEA----------LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|....
gi 442625523 184 FDTIQLLRGLANEGRTIVCTIHQP 207
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-247 |
1.72e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.97 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSL---MNILTGLTKSGV-------SGKIEIGKAR 84
Cdd:PRK13633 5 IKCKNVSYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPSEGKVyvdgldtSDEENLWDIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQD-DHFFPYFTVEETMLMAAtlkiSNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELI 163
Cdd:PRK13633 85 NKAGMVFQNpDNQIVATIVEEDVAFGP----ENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 164 DNPAVLFLDEPTTGLDSSSSFDTIQLLRGL-ANEGRTIVCTIHQPSTNIYNlfNLVYVLSAGRCTYQGTPQNT---VMFL 239
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEA--DRIIVMDSGKVVMEGTPKEIfkeVEMM 238
|
....*...
gi 442625523 240 SSVGLECP 247
Cdd:PRK13633 239 KKIGLDVP 246
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
29-233 |
1.98e-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: 73.29 E-value: 1.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 29 KPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGL--TKSG---VSGK----IEIGKARKLCGYIMQDDHFFPY 99
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyvPENGrvlVDGHdlalADPAWLRRQVGVVLQENVLFNR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 100 FTVEETMLM--AATLKISNQCVSLKEKRTLIdyllnsLKLTKTRQT----KCSNLSGGQKKRLSIALELIDNPAVLFLDE 173
Cdd:cd03252 91 SIRDNIALAdpGMSMERVIEAAKLAGAHDFI------SELPEGYDTivgeQGAGLSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 174 PTTGLDSSSSFDTIQLLRGLAnEGRTIVCTIHQPSTnIYNLfNLVYVLSAGRCTYQGTPQ 233
Cdd:cd03252 165 ATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLST-VKNA-DRIIVMEKGRIVEQGSHD 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
15-205 |
2.21e-14 |
|
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: 70.56 E-value: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVnvpkkpEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIGKARKLcGYIMQdd 94
Cdd:cd03221 1 IELENLSKTY------GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEP-DEGIVTWGSTVKI-GYFEQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 95 hffpyftveetmlmaatlkisnqcvslkekrtlidyllnslkltktrqtkcsnLSGGQKKRLSIALELIDNPAVLFLDEP 174
Cdd:cd03221 71 -----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|..
gi 442625523 175 TTGLDSsssfDTIQLL-RGLANEGRTIVCTIH 205
Cdd:cd03221 98 TNHLDL----ESIEALeEALKEYPGTVILVSH 125
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
33-180 |
2.47e-14 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 73.20 E-value: 2.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI--------GKARklcGYIMQDDHFFPYFTVEE 104
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLdgkpvegpGAER---GVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442625523 105 TMLMAATLkisnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDS 180
Cdd:PRK11248 90 NVAFGLQL----AGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
35-179 |
2.79e-14 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 74.36 E-value: 2.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK-SgvSGKIEI-GK--------ARKLcGYIMQDDHFFPYFTVEE 104
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETpD--SGRILLdGRdvtglppeKRNV-GMVFQDYALFPHLTVAE 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442625523 105 TmlMAATLKIsnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:COG3842 97 N--VAFGLRM--RGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
44-205 |
2.92e-14 |
|
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: 76.59 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 44 KSGELTAIMGPSGAGKSSLMNILTGLT--KSG---VSGK---IEIGKARKLCGYIMQDDHFFPYFTVEETMLMAATLKis 115
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTGDTtvTSGdatVAGKsilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLR-- 2040
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 116 nqCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLAN 195
Cdd:TIGR01257 2041 --GVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR 2118
|
170
....*....|
gi 442625523 196 EGRTIVCTIH 205
Cdd:TIGR01257 2119 EGRAVVLTSH 2128
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
34-207 |
2.93e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.50 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 34 SVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLtKSGVSGKI-----------EIGKAR---KLCGYIMQDDHFFPY 99
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGL-DDGSSGEVslvgqplhqmdEEARAKlraKHVGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 100 FTVEETMLMAATLKISNQcvslKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:PRK10584 103 LNALENVELPALLRGESS----RQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180
....*....|....*....|....*....
gi 442625523 180 SSSSFDTIQLLRGLANE-GRTIVCTIHQP 207
Cdd:PRK10584 179 RQTGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
32-203 |
3.68e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 72.50 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 32 KKSVLKGIKGTFKSGELTAIMGPSGAGKSSL------MNILT-GLTKSGV---------SGKIEIGKARKLCGYIMQDDH 95
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsinrMNDLNpEVTITGSivynghniySPRTDTVDLRKEIGMVFQQPN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 96 FFPyFTVEETMLMAATLKisnqcvSLKEKRTLIDYLLNSLK------LTKTR-QTKCSNLSGGQKKRLSIALELIDNPAV 168
Cdd:PRK14239 97 PFP-MSIYENVVYGLRLK------GIKDKQVLDEAVEKSLKgasiwdEVKDRlHDSALGLSGGQQQRVCIARVLATSPKI 169
|
170 180 190
....*....|....*....|....*....|....*
gi 442625523 169 LFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCT 203
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT 204
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
32-236 |
6.57e-14 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 72.33 E-value: 6.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 32 KKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTkSGVSGKIEIGK-----------ARKLcGYIMQDDHFFPYF 100
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-TPAHGHVWLDGehiqhyaskevARRI-GLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 101 TVEEtmlMAATLKISNQCVSL---KEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTG 177
Cdd:PRK10253 97 TVQE---LVARGRYPHQPLFTrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 178 LDSSSSFDTIQLLRGLANE-GRTIVCTIHQPSTNIYNLFNLVyVLSAGRCTYQGTPQNTV 236
Cdd:PRK10253 174 LDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLI-ALREGKIVAQGAPKEIV 232
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
15-205 |
7.35e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.81 E-value: 7.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVNvPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGL----------------------TKS 72
Cdd:PRK13651 3 IKVKNIVKIFN-KKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkdeknkkktkEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 73 GVSGKIEIGKA-----------RKLCGYIMQddhFFPYFTVEET-----MLMAATLKISNQCVSLKEKRTL------IDY 130
Cdd:PRK13651 82 KVLEKLVIQKTrfkkikkikeiRRRVGVVFQ---FAEYQLFEQTiekdiIFGPVSMGVSKEEAKKRAAKYIelvgldESY 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442625523 131 LlnslkltktrQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIH 205
Cdd:PRK13651 159 L----------QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
35-206 |
1.40e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG----------KARKLCGYIM-QDDHFFPYFTVE 103
Cdd:PRK15439 26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD-SGTLEIGgnpcarltpaKAHQLGIYLVpQEPLLFPNLSVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 104 ETMLmaatLKISNQCVSLKEKRTLIDYLLNSLKLtktrQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSS 183
Cdd:PRK15439 105 ENIL----FGLPKRQASMQKMKQLLAALGCQLDL----DSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAET 176
|
170 180
....*....|....*....|...
gi 442625523 184 FDTIQLLRGLANEGRTIVCTIHQ 206
Cdd:PRK15439 177 ERLFSRIRELLAQGVGIVFISHK 199
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
25-208 |
1.81e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.86 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSG----VSGKIEIGKARKLCGYIMQDDHFFPYF 100
Cdd:PRK11247 17 AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSagelLAGTAPLAEAREDTRLMFQDARLLPWK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 101 TVeetmlmaatlkISNQCVSLKEK-RTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:PRK11247 97 KV-----------IDNVGLGLKGQwRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALD 165
|
170 180 190
....*....|....*....|....*....|
gi 442625523 180 SSSSFDTIQLLRGLANE-GRTIVCTIHQPS 208
Cdd:PRK11247 166 ALTRIEMQDLIESLWQQhGFTVLLVTHDVS 195
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
42-201 |
3.09e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI-GK---------ARKLcGYIM--QddHF--FPYFTVEETML 107
Cdd:COG3845 27 TVRPGEIHALLGENGAGKSTLMKILYGLYQPD-SGEILIdGKpvrirsprdAIAL-GIGMvhQ--HFmlVPNLTVAENIV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 108 MAATlKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLdssssfdTI 187
Cdd:COG3845 103 LGLE-PTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL-------TP 174
|
170 180
....*....|....*....|.
gi 442625523 188 Q-------LLRGLANEGRTIV 201
Cdd:COG3845 175 QeadelfeILRRLAAEGKSII 195
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
44-254 |
3.43e-13 |
|
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: 69.98 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 44 KSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI-GKA-------------RKLCGYIMQddHF--FPYFTVEETml 107
Cdd:cd03294 48 REGEIFVIMGLSGSGKSTLLRCINRLIEP-TSGKVLIdGQDiaamsrkelrelrRKKISMVFQ--SFalLPHRTVLEN-- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 108 maATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSsssfdTI 187
Cdd:cd03294 123 --VAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP-----LI 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442625523 188 ------QLLRGLANEGRTIVCTIHQPSTNIyNLFNLVYVLSAGRCTYQGTPQNTVMflssvglecppyhNPAD 254
Cdd:cd03294 196 rremqdELLRLQAELQKTIVFITHDLDEAL-RLGDRIAIMKDGRLVQVGTPEEILT-------------NPAN 254
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
27-183 |
3.77e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 69.73 E-value: 3.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 27 PKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG----------KARKLCGYIMQDdhf 96
Cdd:COG1101 13 PGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPD-SGSILIDgkdvtklpeyKRAKYIGRVFQD--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 fPY------FTVEETMLMAA------TLKISNqcvsLKEKRTLIDYLLNSLKL-TKTR-QTKCSNLSGGQKKRLSIALEL 162
Cdd:COG1101 89 -PMmgtapsMTIEENLALAYrrgkrrGLRRGL----TKKRRELFRELLATLGLgLENRlDTKVGLLSGGQRQALSLLMAT 163
|
170 180
....*....|....*....|.
gi 442625523 163 IDNPAVLFLDEPTTGLDSSSS 183
Cdd:COG1101 164 LTKPKLLLLDEHTAALDPKTA 184
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
11-207 |
4.17e-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: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 11 YGIDIHFE---DLVYQV-------NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSG-VSGKIE 79
Cdd:COG2401 11 MRVTKVYSsvlDLSERVaivleafGVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTpVAGCVD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 80 IgkarklcgyimQDDHFFPyftvEETMLmaatlkisnQCVSLKEKRTLIDYLLNSLKLTK--TRQTKCSNLSGGQKKRLS 157
Cdd:COG2401 91 V-----------PDNQFGR----EASLI---------DAIGRKGDFKDAVELLNAVGLSDavLWLRRFKELSTGQKFRFR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 442625523 158 IALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQP 207
Cdd:COG2401 147 LALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHY 197
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
15-233 |
4.58e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 70.04 E-value: 4.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVnvpkKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG----------KAR 84
Cdd:PRK13635 6 IRVEHISFRY----PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPE-AGTITVGgmvlseetvwDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQD-DHFFPYFTVEETMLMAatlkISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELI 163
Cdd:PRK13635 81 RQVGMVFQNpDNQFVGATVQDDVAFG----LENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442625523 164 DNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIhqpstnIYNL-----FNLVYVLSAGRCTYQGTPQ 233
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSI------THDLdeaaqADRVIVMNKGEILEEGTPE 225
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
51-233 |
5.41e-13 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 70.22 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 51 IMGPSGAGKSSLMNILTGLTKSGvSGKIEIGKA--------RKLCGYIMQDDHFFPYFTVEETMlmAATLKIsnQCVSLK 122
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPD-SGSIMLDGEdvtnvpphLRHINMVFQSYALFPHMTVEENV--AFGLKM--RKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 123 EKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSfDTIQL-LRGLANE-GRTI 200
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLR-DQMQLeLKTIQEQlGITF 154
|
170 180 190
....*....|....*....|....*....|...
gi 442625523 201 VCTIHQPSTNIyNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:TIGR01187 155 VFVTHDQEEAM-TMSDRIAIMRKGKIAQIGTPE 186
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
46-247 |
5.94e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.39 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 46 GELTAIMGPSGAGKSSLMNILTGLTKSGvSGKI----------EIGKARKLCGYIMQ--DDHFfpyftVEETMLMAATLK 113
Cdd:PRK13648 35 GQWTSIVGHNGSGKSTIAKLMIGIEKVK-SGEIfynnqaitddNFEKLRKHIGIVFQnpDNQF-----VGSIVKYDVAFG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 114 ISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGL 193
Cdd:PRK13648 109 LENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKV 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442625523 194 -ANEGRTIVCTIHQPSTNIYNlfNLVYVLSAGRCTYQGTPQ---NTVMFLSSVGLECP 247
Cdd:PRK13648 189 kSEHNITIISITHDLSEAMEA--DHVIVMNKGTVYKEGTPTeifDHAEELTRIGLDLP 244
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-206 |
6.80e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.35 E-value: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 18 EDLVYQVNVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI-GKA-----RKLC---- 87
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEP-TKGTITInNINynkldHKLAaqlg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 88 -GYIMQDDHFFPYFTVEETMLMA--ATLKISN-QCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELI 163
Cdd:PRK09700 82 iGIIYQELSVIDELTVLENLYIGrhLTKKVCGvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442625523 164 DNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQ 206
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHK 204
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
38-232 |
6.92e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.86 E-value: 6.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 38 GIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI-GK----------ARKLCGYIMQDDHFFPYFTVEETM 106
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKP-TGGTILLrGQhieglpghqiARMGVVRTFQHVRLFREMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 107 LMA-----------ATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPT 175
Cdd:PRK11300 102 LVAqhqqlktglfsGLLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 442625523 176 TGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIYNLFNLVYVLSAGRCTYQGTP 232
Cdd:PRK11300 182 AGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
15-234 |
9.16e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 69.04 E-value: 9.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDL--VYQVNVPKKPEkksVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG----------- 81
Cdd:PRK13646 3 IRFDNVsyTYQKGTPYEHQ---AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKP-TTGTVTVDditithktkdk 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 82 ---KARKLCGYIMQddhfFP---YF--TVEETMLMAAtlkiSNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCS-NLSGGQ 152
Cdd:PRK13646 79 yirPVRKRIGMVFQ----FPesqLFedTVEREIIFGP----KNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 153 KKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGL-ANEGRTIVCTIHQpSTNIYNLFNLVYVLSAGRCTYQGT 231
Cdd:PRK13646 151 MRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHD-MNEVARYADEVIVMKEGSIVSQTS 229
|
...
gi 442625523 232 PQN 234
Cdd:PRK13646 230 PKE 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
33-225 |
9.18e-13 |
|
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: 67.07 E-value: 9.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI----------GKARKL-CGYIMQDDH---FFP 98
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPP-ASGEITLdgkpvtrrspRDAIRAgIAYVPEDRKregLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 99 YFTVEETMLmaatlkisnqcvslkekrtlidylLNSLkltktrqtkcsnLSGGQKKRLSIALELIDNPAVLFLDEPTTGL 178
Cdd:cd03215 92 DLSVAENIA------------------------LSSL------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442625523 179 DSSSSFDTIQLLRGLANEGRTIVCTihqpSTNIYNLFNL---VYVLSAGR 225
Cdd:cd03215 136 DVGAKAEIYRLIRELADAGKAVLLI----SSELDELLGLcdrILVMYEGR 181
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-203 |
1.50e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.20 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK--SGV--SGKIEIG-----------KARKLCGYIMQDDHFF 97
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvSGYrySGDVLLGgrsifnyrdvlEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 98 PyFTVEETMLMAATlkiSNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSN----LSGGQKKRLSIALELIDNPAVLFLDE 173
Cdd:PRK14271 114 P-MSIMDNVLAGVR---AHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDE 189
|
170 180 190
....*....|....*....|....*....|
gi 442625523 174 PTTGLDSSSSFDTIQLLRGLANEGRTIVCT 203
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLADRLTVIIVT 219
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
35-233 |
1.50e-12 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 67.90 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSL---MNIL-------------TGLTKSGVSGKIEIGKARKL------CGYIMQ 92
Cdd:COG4598 23 VLKGVSLTARKGDVISIIGSSGSGKSTFlrcINLLetpdsgeirvggeEIRLKPDRDGELVPADRRQLqrirtrLGMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 93 ddHF--FPYFTVEETMLMAAT--LKIS-NQCVSLKEKrtlidyLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPA 167
Cdd:COG4598 103 --SFnlWSHMTVLENVIEAPVhvLGRPkAEAIERAEA------LLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPE 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442625523 168 VLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPStniynlF-----NLVYVLSAGRCTYQGTPQ 233
Cdd:COG4598 175 VMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMG------FardvsSHVVFLHQGRIEEQGPPA 239
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-206 |
1.66e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.26 E-value: 1.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 12 GIDIHFEDLVYqvnvpKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTG-------LTKSGVS-GKIEIGKA 83
Cdd:PRK11174 347 PVTIEAEDLEI-----LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpyqgsLKINGIElRELDPESW 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 84 RKLCGYIMQDDHFFPYfTVEETMLMAATlKISNQCVSLKEKRTLIDYLLNSLK--LTKTRQTKCSNLSGGQKKRLSIALE 161
Cdd:PRK11174 422 RKHLSWVGQNPQLPHG-TLRDNVLLGNP-DASDEQLQQALENAWVSEFLPLLPqgLDTPIGDQAAGLSVGQAQRLALARA 499
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 442625523 162 LIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTiHQ 206
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQ 543
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-208 |
1.85e-12 |
|
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: 65.64 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVnvpkkPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEigkarKLCGyimqDD 94
Cdd:cd03223 1 IELENLSLAT-----PDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG-SGRIG-----MPEG----ED 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 95 HFF----PYFTveetmlmAATLkisnqcvslkekRTLIDYLLNSlkltktrqtkcsNLSGGQKKRLSIALELIDNPAVLF 170
Cdd:cd03223 66 LLFlpqrPYLP-------LGTL------------REQLIYPWDD------------VLSGGEQQRLAFARLLLHKPKFVF 114
|
170 180 190
....*....|....*....|....*....|....*...
gi 442625523 171 LDEPTTGLDSSSSFDTIQLLRGlanEGRTIVCTIHQPS 208
Cdd:cd03223 115 LDEATSALDEESEDRLYQLLKE---LGITVISVGHRPS 149
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
32-231 |
2.14e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.21 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 32 KKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVSGKIEIGKA----------RKLCGYIMQDDHFFPYFT 101
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDitdwqtakimREAVAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 102 VEETMLMAATLKISNQcvslKEKRTLIDYLLNSlKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDS- 180
Cdd:PRK11614 97 VEENLAMGGFFAERDQ----FQERIKWVYELFP-RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPi 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442625523 181 --SSSFDTIQLLRglaNEGRTIVcTIHQPSTNIYNLFNLVYVLSAGRCTYQGT 231
Cdd:PRK11614 172 iiQQIFDTIEQLR---EQGMTIF-LVEQNANQALKLADRGYVLENGHVVLEDT 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
14-231 |
2.31e-12 |
|
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: 70.15 E-value: 2.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 14 DIHFEDLVYQVNVPKKpekksVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG----------KA 83
Cdd:TIGR01193 473 DIVINDVSYSYGYGSN-----ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR-SGEILLNgfslkdidrhTL 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 84 RKLCGYIMQDDHFFPYfTVEETMLMAATLKISN----QCVSLKEKRTLIDYLlnSLKLTKTRQTKCSNLSGGQKKRLSIA 159
Cdd:TIGR01193 547 RQFINYLPQEPYIFSG-SILENLLLGAKENVSQdeiwAACEIAEIKDDIENM--PLGYQTELSEEGSSISGGQKQRIALA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442625523 160 LELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANegRTIVCTIHQpsTNIYNLFNLVYVLSAGRCTYQGT 231
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHR--LSVAKQSDKIIVLDHGKIIEQGS 691
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
35-231 |
2.49e-12 |
|
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: 69.75 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKI----------EIGKARKLCGYIMQDDHFFPYfTVEE 104
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD-SGQIlldghdladyTLASLRRQVALVSQDVVLFND-TIAN 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 105 TMLMAATLKISNQCVslkeKRTLIDYLLNSL--KLTKTRQT----KCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGL 178
Cdd:TIGR02203 425 NIAYGRTEQADRAEI----ERALAAAYAQDFvdKLPLGLDTpigeNGVLLSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442625523 179 DSSSSFDTIQLLRGLAnEGRTIVCTIHQPSTnIYNLFNLVyVLSAGRCTYQGT 231
Cdd:TIGR02203 501 DNESERLVQAALERLM-QGRTTLVIAHRLST-IEKADRIV-VMDDGRIVERGT 550
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
36-209 |
2.66e-12 |
|
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: 65.42 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 36 LKGIKGTFKSGELTAIMGPSGAGKSSLmnILTGLTKSGvsgKIEIGKARKLcgyimqddhfFPYftveetmlmaatlkis 115
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASG---KARLISFLPK----------FSR---------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 116 NQCVSLKEKRTLIDYLLNSLKLTKTRQTkcsnLSGGQKKRLSIALELIDNP--AVLFLDEPTTGLDSSSSFDTIQLLRGL 193
Cdd:cd03238 60 NKLIFIDQLQFLIDVGLGYLTLGQKLST----LSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDINQLLEVIKGL 135
|
170
....*....|....*.
gi 442625523 194 ANEGRTIVCTIHQPST 209
Cdd:cd03238 136 IDLGNTVILIEHNLDV 151
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
44-179 |
2.77e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.53 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 44 KSGELTAIMGPSGAGKSSLMNILTG-LTKSgvSGKIEI-GK-------ARKLCGYIMQDDHFFPYFTVEETML--MAATL 112
Cdd:PRK10771 23 ERGERVAILGPSGAGKSTLLNLIAGfLTPA--SGSLTLnGQdhtttppSRRPVSMLFQENNLFSHLTVAQNIGlgLNPGL 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 113 KIS-NQCVSLKE--KRTLIDYLLNSLKltktrqtkcSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:PRK10771 101 KLNaAQREKLHAiaRQMGIEDLLARLP---------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-231 |
2.84e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 68.19 E-value: 2.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDL--VYQVNVPK-----------KPEKKSV--LKGIKGTFKSGELTAIMGPSGAGKSSLMNILTG-LTKSgvSGKI 78
Cdd:COG4586 2 IEVENLskTYRVYEKEpglkgalkglfRREYREVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGiLVPT--SGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 79 EI-GK---------ARKLcGYIM-QDDHFFPYFTVEET-MLMAATLKISNqcvslKEKRTLIDYLLNSLKL-----TKTR 141
Cdd:COG4586 80 RVlGYvpfkrrkefARRI-GVVFgQRSQLWWDLPAIDSfRLLKAIYRIPD-----AEYKKRLDELVELLDLgelldTPVR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 142 QtkcsnLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGL-ANEGRTIVCTIHQpSTNIYNLFNLVYV 220
Cdd:COG4586 154 Q-----LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHD-MDDIEALCDRVIV 227
|
250
....*....|.
gi 442625523 221 LSAGRCTYQGT 231
Cdd:COG4586 228 IDHGRIIYDGS 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-201 |
3.40e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.04 E-value: 3.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 4 SKLLKNVYGIDIHFEDLVYQV-NVPKKPEKKsvLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI-G 81
Cdd:PRK09700 248 NRFNAMKENVSNLAHETVFEVrNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKR-AGGEIRLnG 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 82 KA----------RKLCGYIMQ---DDHFFPYFTVEETMLMAATLKISNQCVSL------KEKRTLIDYL-LNSLKLTKTR 141
Cdd:PRK09700 325 KDisprspldavKKGMAYITEsrrDNGFFPNFSIAQNMAISRSLKDGGYKGAMglfhevDEQRTAENQReLLALKCHSVN 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 142 QTkCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIV 201
Cdd:PRK09700 405 QN-ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVIL 463
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
42-201 |
3.71e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 68.88 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKSSLMNILTG-LTKSgvSGKIEI-GKARKL--------CG--YIMQD---DHFFPYFTVEETM 106
Cdd:PRK10762 274 TLRKGEILGVSGLMGAGRTELMKVLYGaLPRT--SGYVTLdGHEVVTrspqdglaNGivYISEDrkrDGLVLGMSVKENM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 107 LMAATLKISNQCVSLK---EKRTLIDYL-LNSLKlTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSS 182
Cdd:PRK10762 352 SLTALRYFSRAGGSLKhadEQQAVSDFIrLFNIK-TPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGA 430
|
170
....*....|....*....
gi 442625523 183 SFDTIQLLRGLANEGRTIV 201
Cdd:PRK10762 431 KKEIYQLINQFKAEGLSII 449
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
25-179 |
4.30e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.05 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIG---------KARKLcGYIMQDDH 95
Cdd:PRK09452 19 GISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPD-SGRIMLDgqdithvpaENRHV-NTVFQSYA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 96 FFPYFTVEETMlmAATLKIsnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPT 175
Cdd:PRK09452 97 LFPHMTVFENV--AFGLRM--QKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL 172
|
....
gi 442625523 176 TGLD 179
Cdd:PRK09452 173 SALD 176
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
28-247 |
4.32e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.06 E-value: 4.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 28 KKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI-GKA---------RKLCGYIMQD-DHF 96
Cdd:PRK13650 15 KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAE-SGQIIIdGDLlteenvwdiRHKIGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 FPYFTVEETMlmaaTLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTT 176
Cdd:PRK13650 94 FVGATVEDDV----AFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442625523 177 GLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIyNLFNLVYVLSAGRCTYQGTPQNtvMF-----LSSVGLECP 247
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRE--LFsrgndLLQLGLDIP 242
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
14-247 |
5.45e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 66.96 E-value: 5.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 14 DIHFEDLVYQVNvPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGL--TKSGVS-----------GKI-E 79
Cdd:PRK13645 6 DIILDNVSYTYA-KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLiiSETGQTivgdyaipanlKKIkE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 80 IGKARKLCGYIMQddhfFP-YFTVEETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCS-NLSGGQKKRLS 157
Cdd:PRK13645 85 VKRLRKEIGLVFQ----FPeYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 158 IALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGL-ANEGRTIVCTIHQpSTNIYNLFNLVYVLSAGRCTYQGTP---Q 233
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHN-MDQVLRIADEVIVMHEGKVISIGSPfeiF 239
|
250
....*....|....
gi 442625523 234 NTVMFLSSVGLECP 247
Cdd:PRK13645 240 SNQELLTKIEIDPP 253
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
25-254 |
6.25e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 67.36 E-value: 6.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLtKSGVSGKIEIGKAR--------KLCGYIMQDDHF 96
Cdd:PRK11000 8 NVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL-EDITSGDLFIGEKRmndvppaeRGVGMVFQSYAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 FPYFTVEETMlmAATLKISNQCVSLKEKRtlIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTT 176
Cdd:PRK11000 87 YPHLSVAENM--SFGLKLAGAKKEEINQR--VNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442625523 177 GLDSSSSFDT-IQLLRGLANEGRTIVCTIHQpSTNIYNLFNLVYVLSAGRCTYQGTPqntvmflssvgLECppYHNPAD 254
Cdd:PRK11000 163 NLDAALRVQMrIEISRLHKRLGRTMIYVTHD-QVEAMTLADKIVVLDAGRVAQVGKP-----------LEL--YHYPAN 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
46-201 |
7.22e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.12 E-value: 7.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 46 GELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI-GKARKLC----------GYIMQDDH---FFPYFTVEETMLMAAT 111
Cdd:COG1129 278 GEILGIAGLVGAGRTELARALFGADPA-DSGEIRLdGKPVRIRsprdairagiAYVPEDRKgegLVLDLSIRENITLASL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 112 LKISNQC-VSLKEKRTLIDYLLNSLKL-TKTRQTKCSNLSGG--QKkrLSIALELIDNPAVLFLDEPTTGLDSSSSFDTI 187
Cdd:COG1129 357 DRLSRGGlLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGnqQK--VVLAKWLATDPKVLILDEPTRGIDVGAKAEIY 434
|
170
....*....|....
gi 442625523 188 QLLRGLANEGRTIV 201
Cdd:COG1129 435 RLIRELAAEGKAVI 448
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
35-179 |
1.30e-11 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 66.41 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLtKSGVSGKIEIG---------KARKlCGYIMQDDHFFPYFTVEET 105
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL-ERITSGEIWIGgrvvnelepADRD-IAMVFQNYALYPHMSVREN 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442625523 106 mlMAATLKISNqcVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:PRK11650 97 --MAYGLKIRG--MPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
31-205 |
2.48e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.29 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 31 EKKSVLKGIKGTFKSGELTAIMGPSGAGKSSL------MNILTGLTKsgVSGKIE------------IGKARKLCGYIMQ 92
Cdd:PRK14258 18 DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFlkclnrMNELESEVR--VEGRVEffnqniyerrvnLNRLRRQVSMVHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 93 DDHFFPYFTVEEtmlMAATLKIsnqcVSLKEKRTLIDYLLNSLKLT------KTRQTKCS-NLSGGQKKRLSIALELIDN 165
Cdd:PRK14258 96 KPNLFPMSVYDN---VAYGVKI----VGWRPKLEIDDIVESALKDAdlwdeiKHKIHKSAlDLSGGQQQRLCIARALAVK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442625523 166 PAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGR-TIVCTIH 205
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSH 209
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
124-222 |
2.78e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 66.98 E-value: 2.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 124 KRTLIDYLLNSL--KLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSF---DTIQLLRGlaNEGR 198
Cdd:PTZ00265 554 KKVLIHDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYlvqKTINNLKG--NENR 631
|
90 100
....*....|....*....|....
gi 442625523 199 TIVCTIHQPSTNIYNlfNLVYVLS 222
Cdd:PTZ00265 632 ITIIIAHRLSTIRYA--NTIFVLS 653
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
32-191 |
3.02e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.98 E-value: 3.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 32 KKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIGKARKLcGYIMQDDHFFPY--FTVEETMLMA 109
Cdd:PRK09544 16 QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD-EGVIKRNGKLRI-GYVPQKLYLDTTlpLTVNRFLRLR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 110 ATLKISNQCVSLKekRTLIDYLLnslkltktrQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSS---FDT 186
Cdd:PRK09544 94 PGTKKEDILPALK--RVQAGHLI---------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQvalYDL 162
|
....*
gi 442625523 187 IQLLR 191
Cdd:PRK09544 163 IDQLR 167
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
119-250 |
3.32e-11 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.14 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 119 VSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGR 198
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 442625523 199 TIVCTIhQPSTNIYNLFNLVYVLSAGRCTYQGTPQNTVMFLSSVGLECPPYH 250
Cdd:NF000106 196 TVLLTT-QYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAH 246
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
44-205 |
3.70e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 63.92 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 44 KSGELTAIMGPSGAGKSSLMNILTGLTKSGVsGKI-------EIGKARKlcGYIMQDdhffpYFT--VEETM-------- 106
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNL-GKFddppdwdEILDEFR--GSELQN-----YFTklLEGDVkvivkpqy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 107 --LMAATLKIS-NQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSS 183
Cdd:cd03236 96 vdLIPKAVKGKvGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQR 175
|
170 180
....*....|....*....|..
gi 442625523 184 FDTIQLLRGLANEGRTIVCTIH 205
Cdd:cd03236 176 LNAARLIRELAEDDNYVLVVEH 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-182 |
4.42e-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: 65.73 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 21 VYQVN-VPKK-PEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIGKARKlCGYIMQDDHFFP 98
Cdd:TIGR03719 4 IYTMNrVSKVvPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKD-FNGEARPQPGIK-VGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 99 YFTVEETMLMA-----ATLKISNQcVS-------------LKEKRTLIDYL---------------LNSLKLTKTrQTKC 145
Cdd:TIGR03719 82 TKTVRENVEEGvaeikDALDRFNE-ISakyaepdadfdklAAEQAELQEIIdaadawdldsqleiaMDALRCPPW-DADV 159
|
170 180 190
....*....|....*....|....*....|....*..
gi 442625523 146 SNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSS 182
Cdd:TIGR03719 160 TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
41-237 |
4.82e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 63.41 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 41 GTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgvSGKIEIG-------KARKLC---GYIMQDD------HFFPYFTvee 104
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLLPG--SGSIQFAgqpleawSAAELArhrAYLSQQQtppfamPVFQYLT--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 105 tmlmaatLKISNQCVsLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGG--QKKRLSIALELID---NPA--VLFLDEPTTG 177
Cdd:PRK03695 92 -------LHQPDKTR-TEAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQVWpdiNPAgqLLLLDEPMNS 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 178 LDSSSSFDTIQLLRGLANEGRTIVCTIHQPStNIYNLFNLVYVLSAGRCTYQGTPQNtVM 237
Cdd:PRK03695 164 LDVAQQAALDRLLSELCQQGIAVVMSSHDLN-HTLRHADRVWLLKQGKLLASGRRDE-VL 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-179 |
5.33e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.21 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 18 EDLVYQVNVPKK--PEKKSVLKGIKG---TFKSGELTAIMGPSGAGKSSLMNILTG-------------------LTKSG 73
Cdd:TIGR03269 277 EPIIKVRNVSKRyiSVDRGVVKAVDNvslEVKEGEIFGIVGTSGAGKTTLSKIIAGvleptsgevnvrvgdewvdMTKPG 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 74 VSGKieiGKARKLCGYIMQDDHFFPYFTVEETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQK 153
Cdd:TIGR03269 357 PDGR---GRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLELPDELARMKAVITLKMVGFDEEKAEEILDKYPDELSEGER 433
|
170 180
....*....|....*....|....*.
gi 442625523 154 KRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMD 459
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
34-233 |
6.35e-11 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 65.23 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 34 SVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTgLTKSGVSGKIEIGKA----------RKLCGYIMQDDHFFPYfTVE 103
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT-RAWDPQQGEILLNGQpiadyseaalRQAISVVSQRVHLFSA-TLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 104 ETMLMAATLKISNQCVSLKEKRTLiDYLLNSLKLTKT------RQtkcsnLSGGQKKRLSIALELIDNPAVLFLDEPTTG 177
Cdd:PRK11160 432 DNLLLAAPNASDEALIEVLQQVGL-EKLLEDDKGLNAwlgeggRQ-----LSGGEQRRLGIARALLHDAPLLLLDEPTEG 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 442625523 178 LDSSSSFDTIQLLRGLAnEGRTIVCTIHqpstNIYNL--FNLVYVLSAGRCTYQGTPQ 233
Cdd:PRK11160 506 LDAETERQILELLAEHA-QNKTVLMITH----RLTGLeqFDRICVMDNGQIIEQGTHQ 558
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
25-234 |
6.50e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.36 E-value: 6.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG---------KARKLCgYIMQDDH 95
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKP-TEGQIFIDgedvthrsiQQRDIC-MVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 96 FFPYFTVEETMlmAATLKIsnQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPT 175
Cdd:PRK11432 89 LFPHMSLGENV--GYGLKM--LGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442625523 176 TGLDssssfdtiqllrglANEGRTIVCTIH--QPSTNIYNLF------------NLVYVLSAGRCTYQGTPQN 234
Cdd:PRK11432 165 SNLD--------------ANLRRSMREKIRelQQQFNITSLYvthdqseafavsDTVIVMNKGKIMQIGSPQE 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
32-201 |
8.72e-11 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 62.75 E-value: 8.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 32 KKSVLKGIKGTFKSGELTAIMGPSGAGKSSL------MNILTGLTKsgVSGKIEIG------------KARKLCGYIMQD 93
Cdd:COG1117 23 DKQALKDINLDIPENKVTALIGPSGCGKSTLlrclnrMNDLIPGAR--VEGEILLDgediydpdvdvvELRRRVGMVFQK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 94 DHFFPyFTVEETmlMAATLKISNqcvsLKEKRTLIDYLLNSLKLT------KTR-QTKCSNLSGGQKKRLSIALELIDNP 166
Cdd:COG1117 101 PNPFP-KSIYDN--VAYGLRLHG----IKSKSELDEIVEESLRKAalwdevKDRlKKSALGLSGGQQQRLCIARALAVEP 173
|
170 180 190
....*....|....*....|....*....|....*
gi 442625523 167 AVLFLDEPTTGLDSSSSFDTIQLLRGLANEgRTIV 201
Cdd:COG1117 174 EVLLMDEPTSALDPISTAKIEELILELKKD-YTIV 207
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
14-224 |
1.05e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 64.44 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 14 DIHFEDLVYQvnvpkKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIGKARKLcgyimqd 93
Cdd:COG4178 362 ALALEDLTLR-----TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG-SGRIARPAGARV------- 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 94 dhFF----PYF---TVEETML------------MAATLkisnQCVSLkekrtliDYLLNSLKLTKTRQtkcSNLSGGQKK 154
Cdd:COG4178 429 --LFlpqrPYLplgTLREALLypataeafsdaeLREAL----EAVGL-------GHLAERLDEEADWD---QVLSLGEQQ 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 155 RLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGlANEGRTIVCTIHQPSTNiyNLFNLVYVLSAG 224
Cdd:COG4178 493 RLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLA--AFHDRVLELTGD 559
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-231 |
1.13e-10 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 64.21 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 7 LKNVYGiDIHFEDLVYqvnvpKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTgLTKSGVSGKIEIGKA--- 83
Cdd:PRK13657 328 LGRVKG-AVEFDDVSF-----SYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQ-RVFDPQSGRILIDGTdir 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 84 -------RKLCGYIMQDDHFF------------PYFTVEEtMLMAAtlkisnqcvslkEKRTLIDYLLNSLKLTKTR-QT 143
Cdd:PRK13657 401 tvtraslRRNIAVVFQDAGLFnrsiednirvgrPDATDEE-MRAAA------------ERAQAHDFIERKPDGYDTVvGE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 144 KCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSS------SFDTIQllrglanEGRTIVCTIHQPSTnIYNLfNL 217
Cdd:PRK13657 468 RGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETeakvkaALDELM-------KGRTTFIIAHRLST-VRNA-DR 538
|
250
....*....|....
gi 442625523 218 VYVLSAGRCTYQGT 231
Cdd:PRK13657 539 ILVFDNGRVVESGS 552
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
15-247 |
1.32e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.42 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVnvpKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG----------KAR 84
Cdd:PRK13642 5 LEVENLVFKY---EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE-FEGKVKIDgelltaenvwNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQD-DHFFPYFTVEETMlmaaTLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELI 163
Cdd:PRK13642 81 RKIGMVFQNpDNQFVGATVEDDV----AFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 164 DNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIYNlFNLVYVLSAGRCTYQGTPQNtvMFLSS-- 241
Cdd:PRK13642 157 LRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSE--LFATSed 233
|
....*....
gi 442625523 242 ---VGLECP 247
Cdd:PRK13642 234 mveIGLDVP 242
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
42-207 |
1.77e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.97 E-value: 1.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKSSLMNILTGLTkSGVSGKI-----EIGKarklcgyimQDDHFF-------------PYFTVE 103
Cdd:PRK13538 23 TLNAGELVQIEGPNGAGKTSLLRILAGLA-RPDAGEVlwqgePIRR---------QRDEYHqdllylghqpgikTELTAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 104 ETMLMAATLkisNQCVSlkekRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSS 183
Cdd:PRK13538 93 ENLRFYQRL---HGPGD----DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGV 165
|
170 180
....*....|....*....|....
gi 442625523 184 FDTIQLLRGLANEGRTIVCTIHQP 207
Cdd:PRK13538 166 ARLEALLAQHAEQGGMVILTTHQD 189
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
19-193 |
2.32e-10 |
|
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: 63.42 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 19 DLVYQV-NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIGKARKLcGYIMQD-DHF 96
Cdd:TIGR03719 320 DKVIEAeNLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPD-SGTIEIGETVKL-AYVDQSrDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 FPYFTVEETmlmaatlkISNQcvslkekrtlIDYLLNSLKLTKTR-------------QTKCSNLSGGQKKRLSIALELI 163
Cdd:TIGR03719 398 DPNKTVWEE--------ISGG----------LDIIKLGKREIPSRayvgrfnfkgsdqQKKVGQLSGGERNRVHLAKTLK 459
|
170 180 190
....*....|....*....|....*....|
gi 442625523 164 DNPAVLFLDEPTTGLDssssfdtIQLLRGL 193
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLD-------VETLRAL 482
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
25-179 |
2.75e-10 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 62.55 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLtKSGVSGKI--------EIGKARKLCGYIMQDDHF 96
Cdd:PRK11607 24 NLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGF-EQPTAGQImldgvdlsHVPPYQRPINMMFQSYAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 FPYFTVEETMlmAATLKISNqcVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTT 176
Cdd:PRK11607 103 FPHMTVEQNI--AFGLKQDK--LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
...
gi 442625523 177 GLD 179
Cdd:PRK11607 179 ALD 181
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
29-199 |
2.89e-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: 61.36 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 29 KPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKI------------EIGKA-RKLCGYIMQDDH 95
Cdd:TIGR02769 20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKP-AQGTVsfrgqdlyqldrKQRRAfRRDVQLVFQDSP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 96 --FFPYFTVEEtmLMAATLKisnQCVSLKEKRTL--IDYLLNSLKLTKTRQTKC-SNLSGGQKKRLSIALELIDNPAVLF 170
Cdd:TIGR02769 99 saVNPRMTVRQ--IIGEPLR---HLTSLDESEQKarIAELLDMVGLRSEDADKLpRQLSGGQLQRINIARALAVKPKLIV 173
|
170 180
....*....|....*....|....*....
gi 442625523 171 LDEPTTGLDSSSSFDTIQLLRGLANEGRT 199
Cdd:TIGR02769 174 LDEAVSNLDMVLQAVILELLRKLQQAFGT 202
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
35-201 |
2.96e-10 |
|
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: 60.53 E-value: 2.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTG--LTKSG------VSGKIEIGKA---------RKLCGYIMQDDHFF 97
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnyLPDSGsilvrhDGGWVDLAQAspreilalrRRTIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 98 PYFT----VEETMLMAATlkisNQCVSLKEKRTLIDYLlnslkltktrqtkcsNL------------SGGQKKRLSIALE 161
Cdd:COG4778 106 PRVSaldvVAEPLLERGV----DREEARARARELLARL---------------NLperlwdlppatfSGGEQQRVNIARG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 442625523 162 LIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIV 201
Cdd:COG4778 167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
33-179 |
4.20e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.49 E-value: 4.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGlTKSGVSGKIEIGKARKLcGYIMQddHFFPYFTVEETMLMAATl 112
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAG-ELAPVSGEIGLAKGIKL-GYFAQ--HQLEFLRADESPLQHLA- 399
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442625523 113 KISNQcvslKEKRTLIDYL----LNSLKLTKTrqtkCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:PRK10636 400 RLAPQ----ELEQKLRDYLggfgFQGDKVTEE----TRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
14-232 |
9.51e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 58.58 E-value: 9.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 14 DIHFEDLVyqvnVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI----------GKA 83
Cdd:cd03369 6 EIEVENLS----VRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEA-EEGKIEIdgidistiplEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 84 RKLCGYIMQDDHFF---------PYFTVEETMLMAAtLKISNqcvslkekrtlidyllnslkltktrqtKCSNLSGGQKK 154
Cdd:cd03369 81 RSSLTIIPQDPTLFsgtirsnldPFDEYSDEEIYGA-LRVSE---------------------------GGLNLSQGQRQ 132
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442625523 155 RLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANeGRTIVCTIHQPSTNIYnlFNLVYVLSAGRCTYQGTP 232
Cdd:cd03369 133 LLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIID--YDKILVMDAGEVKEYDHP 207
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-230 |
1.53e-09 |
|
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: 58.31 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 27 PKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIgkARKLCGYIMQDDHFFPYFTVEETM 106
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD-SGTVTV--RGRVSSLLGLGGGFNPELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 107 LMAATLKisnqCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDT 186
Cdd:cd03220 106 YLNGRLL----GLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 442625523 187 IQLLRGLANEGRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQG 230
Cdd:cd03220 182 QRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
36-202 |
2.27e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.94 E-value: 2.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 36 LKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGV-SGKIEIG----KARKLC-------GYIMQDDHFFPYFTVE 103
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyEGEIIFEgeelQASNIRdteragiAIIHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 104 ETMLMAATLkisnqcvslkEKRTLIDY---------LLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEP 174
Cdd:PRK13549 101 ENIFLGNEI----------TPGGIMDYdamylraqkLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEP 170
|
170 180
....*....|....*....|....*...
gi 442625523 175 TTGLDSSSSFDTIQLLRGLANEGrtIVC 202
Cdd:PRK13549 171 TASLTESETAVLLDIIRDLKAHG--IAC 196
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
34-206 |
2.85e-09 |
|
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: 57.73 E-value: 2.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 34 SVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKI--------------EIGKARKLCGYIMQDdhffPY 99
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQT-LEGKVhwsnknesepsfeaTRSRNRYSVAYAAQK----PW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 100 F---TVEETMLMAATL-----KISNQCVSLKEKRTLIDYllnslkltkTRQTKCS----NLSGGQKKRLSIALELIDNPA 167
Cdd:cd03290 90 LlnaTVEENITFGSPFnkqryKAVTDACSLQPDIDLLPF---------GDQTEIGergiNLSGGQRQRICVARALYQNTN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 442625523 168 VLFLDEPTTGLDSSSSFDTIQ--LLRGLANEGRTIVCTIHQ 206
Cdd:cd03290 161 IVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHK 201
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
46-205 |
3.42e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 46 GELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIE-IGKARKLCG----------YIMQDDHFFPYFTVEETMLMAATLKI 114
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRD-AGSILyLGKEVTFNGpkssqeagigIIHQELNLIPQLTIAENIFLGREFVN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 115 SNQCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGL---DSSSSFDTIQLLR 191
Cdd:PRK10762 109 RFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtdtETESLFRVIRELK 188
|
170
....*....|....
gi 442625523 192 glaNEGRTIVCTIH 205
Cdd:PRK10762 189 ---SQGRGIVYISH 199
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
33-230 |
6.24e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 6.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgvSGKIEI-GKA------RKLCGY------IMQDDH--FF 97
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS--QGEIWFdGQPlhnlnrRQLLPVrhriqvVFQDPNssLN 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 98 PYFTVEEtmLMAATLKISNQCVSLKEKRTLIDYLLNSLKL-TKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTT 176
Cdd:PRK15134 377 PRLNVLQ--IIEEGLRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442625523 177 GLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIYNLFNLVYVLSAGRCTYQG 230
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQG 508
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
44-201 |
6.38e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 58.64 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 44 KSGELTAIMGPSGAGKSSLMNILTGLTKSGVsGKIEiGKA------RKLCGYIMQDdhffpYFTveetMLMAATLKIS-- 115
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNL-GDYD-EEPswdevlKRFRGTELQD-----YFK----KLANGEIKVAhk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 116 NQCV------------SLKEK---RTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDS 180
Cdd:COG1245 166 PQYVdlipkvfkgtvrELLEKvdeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
|
170 180
....*....|....*....|.
gi 442625523 181 SSSFDTIQLLRGLANEGRTIV 201
Cdd:COG1245 246 YQRLNVARLIRELAEEGKYVL 266
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
36-201 |
7.24e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.38 E-value: 7.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 36 LKGIKG---------TFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI-GKARK-------------LCGYIMQ 92
Cdd:PRK11288 260 LDGLKGpglrepisfSVRAGEIVGLFGLVGAGRSELMKLLYGATRR-TAGQVYLdGKPIDirsprdairagimLCPEDRK 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 93 DDHFFPYFTVEETMLMAATLKISNQCVSLKEKR--TLIDYLLNSLKL-TKTRQTKCSNLSGG--QKKRLSIAL-ELIDnp 166
Cdd:PRK11288 339 AEGIIPVHSVADNINISARRHHLRAGCLINNRWeaENADRFIRSLNIkTPSREQLIMNLSGGnqQKAILGRWLsEDMK-- 416
|
170 180 190
....*....|....*....|....*....|....*
gi 442625523 167 aVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIV 201
Cdd:PRK11288 417 -VILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVL 450
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
33-199 |
8.53e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.00 E-value: 8.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK-------------SGVSGKiEIGKARKLCGYIMQD--DHFF 97
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpsqgnvswrgeplAKLNRA-QRKAFRRDIQMVFQDsiSAVN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 98 PYFTV----EETMLMAATLKISNQCVSLKEkrtlidyLLNSLKLTKTRQTKC-SNLSGGQKKRLSIALELIDNPAVLFLD 172
Cdd:PRK10419 104 PRKTVreiiREPLRHLLSLDKAERLARASE-------MLRAVDLDDSVLDKRpPQLSGGQLQRVCLARALAVEPKLLILD 176
|
170 180
....*....|....*....|....*..
gi 442625523 173 EPTTGLDSSSSFDTIQLLRGLANEGRT 199
Cdd:PRK10419 177 EAVSNLDLVLQAGVIRLLKKLQQQFGT 203
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
36-225 |
1.25e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 36 LKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEI-GKARKL----------CGYIMQDDHFFPYFTVEE 104
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD-AGSILIdGQEMRFasttaalaagVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 105 TMLMAAtlkisnqcvsLKEKRTLIDY---------LLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPT 175
Cdd:PRK11288 99 NLYLGQ----------LPHKGGIVNRrllnyeareQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442625523 176 TGLDSSSSFDTIQLLRGLANEGRTIVCTIHQpSTNIYNLFNLVYVLSAGR 225
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSHR-MEEIFALCDAITVFKDGR 217
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
31-230 |
1.50e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.95 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 31 EKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVSGKIEIGKARKLCGyimqddhFFPYFTVEETMLMAA 110
Cdd:PRK09580 12 EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEVTGGTVEFKGKDLLE-------LSPEDRAGEGIFMAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 111 TLK-----ISNQC---VSLKEKRT--------------LIDYLLNSLKLTKTRQTKCSNL--SGGQKKRLSIALELIDNP 166
Cdd:PRK09580 85 QYPveipgVSNQFflqTALNAVRSyrgqepldrfdfqdLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAVLEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442625523 167 AVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIYNLFNLVYVLSAGRCTYQG 230
Cdd:PRK09580 165 ELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVHVLYQGRIVKSG 228
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
47-205 |
1.59e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.94 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 47 ELTAIMGPSGAGKSSLM---NILTGLTKSG-VSGKIEIG------------KARKLCGYIMQDDHFFPYFTVEEtmlMAA 110
Cdd:PRK14243 37 QITAFIGPSGCGKSTILrcfNRLNDLIPGFrVEGKVTFHgknlyapdvdpvEVRRRIGMVFQKPNPFPKSIYDN---IAY 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 111 TLKISNQCVSLKE--KRTLIDYLLNSLKLTKTRQTKCSnLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQ 188
Cdd:PRK14243 114 GARINGYKGDMDElvERSLRQAALWDEVKDKLKQSGLS-LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEE 192
|
170
....*....|....*..
gi 442625523 189 LLRGLAnEGRTIVCTIH 205
Cdd:PRK14243 193 LMHELK-EQYTIIIVTH 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-234 |
1.94e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.17 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 1 MDSSKLLKnVYGIDIHFEDLVYQVnvpkkpekkSVLKGIKGTFKSGELTAIMGPSGAGKS----SLMNILTGLTKSGVSG 76
Cdd:PRK10261 7 LDARDVLA-VENLNIAFMQEQQKI---------AAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 77 K----------IEIG-----KARKLCG----YIMQD--DHFFPYFTVEETMlmAATLKIsNQCVSLKEKRTLIDYLLNSL 135
Cdd:PRK10261 77 KmllrrrsrqvIELSeqsaaQMRHVRGadmaMIFQEpmTSLNPVFTVGEQI--AESIRL-HQGASREEAMVEAKRMLDQV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 136 KLTKTrQTKCS----NLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNI 211
Cdd:PRK10261 154 RIPEA-QTILSryphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVV 232
|
250 260
....*....|....*....|...
gi 442625523 212 YNLFNLVYVLSAGRCTYQGTPQN 234
Cdd:PRK10261 233 AEIADRVLVMYQGEAVETGSVEQ 255
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
30-193 |
3.86e-08 |
|
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: 56.23 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 30 PEKKSVLKGIKGTFKS----------GELTAIMGPSGAGKSSLMNILTGLTKSgvSGKIEI---------GKA----RKL 86
Cdd:COG4172 286 PIKRGLFRRTVGHVKAvdgvsltlrrGETLGLVGESGSGKSTLGLALLRLIPS--EGEIRFdgqdldglsRRAlrplRRR 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 87 CGYIMQDdhffPY------FTVEEtmLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTK-TRQTKCSNLSGGQKKRLSIA 159
Cdd:COG4172 364 MQVVFQD----PFgslsprMTVGQ--IIAEGLRVHGPGLSAAERRARVAEALEEVGLDPaARHRYPHEFSGGQRQRIAIA 437
|
170 180 190
....*....|....*....|....*....|....
gi 442625523 160 LELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGL 193
Cdd:COG4172 438 RALILEPKLLVLDEPTSALDVSVQAQILDLLRDL 471
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
40-180 |
3.96e-08 |
|
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: 54.72 E-value: 3.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 40 KGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVSgkiEIGKARKLCGYIMQddhffpYFTVEETMLMAATL-KISNQC 118
Cdd:cd03237 19 GGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG---DIEIELDTVSYKPQ------YIKADYEGTVRDLLsSITKDF 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442625523 119 VSLKEKRTLIdylLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDS 180
Cdd:cd03237 90 YTHPYFKTEI---AKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
44-201 |
4.31e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 44 KSGELTAIMGPSGAGKSSLMNILTGLTK------SGVSGKIEIGKARKlcGYIMQDdhffpYFTveetMLMAATLKIS-- 115
Cdd:PRK13409 97 KEGKVTGILGPNGIGKTTAVKILSGELIpnlgdyEEEPSWDEVLKRFR--GTELQN-----YFK----KLYNGEIKVVhk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 116 NQCVSL---------KE------KRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDS 180
Cdd:PRK13409 166 PQYVDLipkvfkgkvREllkkvdERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDI 245
|
170 180
....*....|....*....|.
gi 442625523 181 SSSFDTIQLLRGLAnEGRTIV 201
Cdd:PRK13409 246 RQRLNVARLIRELA-EGKYVL 265
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
42-232 |
6.83e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 54.02 E-value: 6.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKSSLMNILtGLTKSGVSGKIEIGK-----------ARKLcGYIMQDDHFFPYFTVEETMLMA- 109
Cdd:PRK10575 33 TFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAqpleswsskafARKV-AYLPQQLPAAEGMTVRELVAIGr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 110 -----ATLKISnqcvslKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSF 184
Cdd:PRK10575 111 ypwhgALGRFG------AADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 442625523 185 DTIQLLRGLANE-GRTIVCTIHQPSTNIYNLFNLVyVLSAGRCTYQGTP 232
Cdd:PRK10575 185 DVLALVHRLSQErGLTVIAVLHDINMAARYCDYLV-ALRGGEMIAQGTP 232
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-182 |
8.81e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 8.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 21 VYQVN-VPKK-PEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKsgvsgkiEI-GKARKL----CGYIMQD 93
Cdd:PRK11819 6 IYTMNrVSKVvPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK-------EFeGEARPApgikVGYLPQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 94 DHFFPYFTVEET-------------------MLMAATLKISNQCvsLKEKRTLIDYL---------------LNSLKLTK 139
Cdd:PRK11819 79 PQLDPEKTVRENveegvaevkaaldrfneiyAAYAEPDADFDAL--AAEQGELQEIIdaadawdldsqleiaMDALRCPP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 442625523 140 tRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSS 182
Cdd:PRK11819 157 -WDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
51-179 |
8.97e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.12 E-value: 8.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 51 IMGPSGAGKSSLMNILTGLTKSGvSGKIEIGKARKLcGYIMQD-DHFFPYFTVEETmlmaatlkISNQCVSLKekrtLID 129
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEQPD-SGTIKIGETVKL-AYVDQSrDALDPNKTVWEE--------ISGGLDIIK----VGN 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442625523 130 YLLNSlkltktR-------------QTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:PRK11819 421 REIPS------RayvgrfnfkggdqQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
138-241 |
1.56e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.35 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 138 TKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVcTIHQPSTNIYNLFNL 217
Cdd:PRK10982 382 TPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII-IISSEMPELLGITDR 460
|
90 100
....*....|....*....|....*...
gi 442625523 218 VYVLSAGRCT----YQGTPQNTVMFLSS 241
Cdd:PRK10982 461 ILVMSNGLVAgivdTKTTTQNEILRLAS 488
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
149-196 |
2.10e-07 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 52.62 E-value: 2.10e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 442625523 149 SGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE 196
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRE 200
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
148-234 |
2.34e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.56 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 148 LSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE-GRTIVCTIHQPSTnIYNLFNLVYVLSAGRC 226
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSI-VRKLADRVAVMQNGRC 235
|
....*...
gi 442625523 227 TYQGTPQN 234
Cdd:PRK15134 236 VEQNRAAT 243
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-202 |
2.47e-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: 53.68 E-value: 2.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 25 NVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGV-SGKIEIGKA-----------RKLCGYIMQ 92
Cdd:TIGR02633 6 GIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwDGEIYWSGSplkasnirdteRAGIVIIHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 93 DDHFFPYFTVEETMLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTKTRQTK-CSNLSGGQKKRLSIALELIDNPAVLFL 171
Cdd:TIGR02633 86 ELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLIL 165
|
170 180 190
....*....|....*....|....*....|.
gi 442625523 172 DEPTTGLDSSSSFDTIQLLRGLANEGrtIVC 202
Cdd:TIGR02633 166 DEPSSSLTEKETEILLDIIRDLKAHG--VAC 194
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
41-180 |
2.56e-07 |
|
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: 53.63 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 41 GTFKSGELTAIMGPSGAGKSSLMNILTGLTK--SG-VSGKIEIG-KARklcgYIMQDdhfFPYfTVEETMLMAATLKISN 116
Cdd:COG1245 361 GEIREGEVLGIVGPNGIGKTTFAKILAGVLKpdEGeVDEDLKISyKPQ----YISPD---YDG-TVEEFLRSANTDDFGS 432
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442625523 117 qcvSLKEKRtlidyLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDS 180
Cdd:COG1245 433 ---SYYKTE-----IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
33-233 |
3.22e-07 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.07 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKI-------------EIGKARKLCGYIMQDDHFFPY 99
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-HGEIlfdgenipamsrsRLYTVRKRMSMLFQSGALFTD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 100 FTVEEtmlmaatlkisNQCVSLKEKRTLIDYLLNSLKLTKTR--------QTKCSNLSGGQKKRLSIALELIDNPAVLFL 171
Cdd:PRK11831 99 MNVFD-----------NVAYPLREHTQLPAPLLHSTVMMKLEavglrgaaKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442625523 172 DEPTTGLDSSssfdTIQLLRGLANE-----GRTIVCTIHQpSTNIYNLFNLVYVLSAGRCTYQGTPQ 233
Cdd:PRK11831 168 DEPFVGQDPI----TMGVLVKLISElnsalGVTCVVVSHD-VPEVLSIADHAYIVADKKIVAHGSAQ 229
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-209 |
3.61e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 53.10 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 2 DSSKL-LKNVYGiDIHFEDLVYQVNVPKKPekksVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKI-- 78
Cdd:PRK11176 329 DEGKRvIERAKG-DIEFRNVTFTYPGKEVP----ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDID-EGEIll 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 79 --------EIGKARKLCGYIMQDDHFFPYfTVEETMLMAATLKISNQCVslkEKRTLIDYLLNSL-KLTKTRQT----KC 145
Cdd:PRK11176 403 dghdlrdyTLASLRNQVALVSQNVHLFND-TIANNIAYARTEQYSREQI---EEAARMAYAMDFInKMDNGLDTvigeNG 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 146 SNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSS------SFDTIQllrglanEGRTIVCTIHQPST 209
Cdd:PRK11176 479 VLLSGGQRQRIAIARALLRDSPILILDEATSALDTESeraiqaALDELQ-------KNRTSLVIAHRLST 541
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
36-233 |
4.27e-07 |
|
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: 53.41 E-value: 4.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 36 LKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIgkaRKLCGYI-----MQDDhffpyfTVEETMLMAA 110
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDK-VEGHVHM---KGSVAYVpqqawIQND------SLRENILFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 111 TLKISNQCVSLKEKRTLIDY-LLNSLKLTKTRQtKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSS---FDT 186
Cdd:TIGR00957 724 ALNEKYYQQVLEACALLPDLeILPSGDRTEIGE-KGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGkhiFEH 802
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 442625523 187 IQLLRG-LANEGRTIVC--TIHQPSTNIynlfnlVYVLSAGRCTYQGTPQ 233
Cdd:TIGR00957 803 VIGPEGvLKNKTRILVThgISYLPQVDV------IIVMSGGKISEMGSYQ 846
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-231 |
4.47e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 51.57 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 1 MDSSKLLKnvygidihFEDLVYQVNvpkkpeKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGV-SGKIE 79
Cdd:CHL00131 2 NKNKPILE--------IKNLHASVN------ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKIlEGDIL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 80 IgKARKLCgYIMQDDH-----F--FPYfTVE------ETMLMAA--TLKISNQCVSLK--EKRTLIDYLLNSLKLTKTRQ 142
Cdd:CHL00131 68 F-KGESIL-DLEPEERahlgiFlaFQY-PIEipgvsnADFLRLAynSKRKFQGLPELDplEFLEIINEKLKLVGMDPSFL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 143 TKCSN--LSGGQKKRLSIALELIDNPAVLFLDEPTTGLDssssfdtIQLLR-------GLANEGRTIVCTIHQPSTNIYN 213
Cdd:CHL00131 145 SRNVNegFSGGEKKRNEILQMALLDSELAILDETDSGLD-------IDALKiiaeginKLMTSENSIILITHYQRLLDYI 217
|
250
....*....|....*...
gi 442625523 214 LFNLVYVLSAGRCTYQGT 231
Cdd:CHL00131 218 KPDYVHVMQNGKIIKTGD 235
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
33-233 |
4.90e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 52.80 E-value: 4.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTG---LTKsgvsGKIEI----------GKARKLCGYIMQD-----D 94
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGyypLTE----GEIRLdgrplsslshSVLRQGVAMVQQDpvvlaD 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 95 HFFPYFT----VEETMLMAATlkisnQCVSLKE-KRTLIDYLLNSLKltktrqTKCSNLSGGQKKRLSIALELIDNPAVL 169
Cdd:PRK10790 430 TFLANVTlgrdISEEQVWQAL-----ETVQLAElARSLPDGLYTPLG------EQGNNLSVGQKQLLALARVLVQTPQIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 442625523 170 FLDEPTTGLDSSSSfDTIQLLRGLANEGRTIVCTIHQPSTNIYNlfNLVYVLSAGRCTYQGTPQ 233
Cdd:PRK10790 499 ILDEATANIDSGTE-QAIQQALAAVREHTTLVVIAHRLSTIVEA--DTILVLHRGQAVEQGTHQ 559
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
15-173 |
5.70e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.67 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVnvpkkPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI-GKA---------R 84
Cdd:PRK10522 323 LELRNVTFAY-----QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQP-QSGEILLdGKPvtaeqpedyR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQDDHFF-----PYFTVEETMLMAATLKISNqcvsLKEKRTLIDYLLNSLKLTKtrqtkcsnlsgGQKKRLSIA 159
Cdd:PRK10522 397 KLFSAVFTDFHLFdqllgPEGKPANPALVEKWLERLK----MAHKLELEDGRISNLKLSK-----------GQKKRLALL 461
|
170
....*....|....
gi 442625523 160 LELIDNPAVLFLDE 173
Cdd:PRK10522 462 LALAEERDILLLDE 475
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
15-231 |
6.08e-07 |
|
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: 52.51 E-value: 6.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLV--YQvnvPKKPekksVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGL---TksgvSGKIEIGKA------ 83
Cdd:COG5265 358 VRFENVSfgYD---PERP----ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFydvT----SGRILIDGQdirdvt 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 84 ----RKLCGYIMQDdhffpyfTV------------------EETMLMAATL-KISNQCVSLKEK-------Rtlidylln 133
Cdd:COG5265 427 qaslRAAIGIVPQD-------TVlfndtiayniaygrpdasEEEVEAAARAaQIHDFIESLPDGydtrvgeR-------- 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 134 SLKLtktrqtkcsnlSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLAnEGRTIVCTIHQPST---- 209
Cdd:COG5265 492 GLKL-----------SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHRLSTivda 559
|
250 260
....*....|....*....|...
gi 442625523 210 -NIynlfnlvYVLSAGRCTYQGT 231
Cdd:COG5265 560 dEI-------LVLEAGRIVERGT 575
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
27-232 |
8.25e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.47 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 27 PKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK--SG---VSGKI----EIGKArklcgyimqddhFF 97
Cdd:COG1134 33 RTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEptSGrveVNGRVsallELGAG------------FH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 98 PYFTVEE-TMLMAATLKISNQcvSLKEKRTLI-------DYLLNSLKltktrqtkcsNLSGGQKKRL--SIALELidNPA 167
Cdd:COG1134 101 PELTGREnIYLNGRLLGLSRK--EIDEKFDEIvefaelgDFIDQPVK----------TYSSGMRARLafAVATAV--DPD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442625523 168 VLFLDEPT-TGldssssfDT------IQLLRGLANEGRTIVCTIHQPSTnIYNLFNLVYVLSAGRCTYQGTP 232
Cdd:COG1134 167 ILLVDEVLaVG-------DAafqkkcLARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMDGDP 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
45-179 |
1.07e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.05 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 45 SGELTAIMGPSGAGKSSLMNILTGlTKSGVSGKIE-----IGKAR---KLCGYIMqddhFFP-------YFT--VEETML 107
Cdd:NF033858 26 AGCMVGLIGPDGVGKSSLLSLIAG-ARKIQQGRVEvlggdMADARhrrAVCPRIA----YMPqglgknlYPTlsVFENLD 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 442625523 108 MAATLKISNQcvslKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:NF033858 101 FFGRLFGQDA----AERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
42-208 |
1.20e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.48 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKI-----EIGKARKL-CGYIMQDDHFFPYFTVEETMLMAAtlKIS 115
Cdd:PRK13541 22 TFLPSAITYIKGANGCGKSSLLRMIAGIMQPS-SGNIyykncNINNIAKPyCTYIGHNLGLKLEMTVFENLKFWS--EIY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 116 NQCvslkekrTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLAN 195
Cdd:PRK13541 99 NSA-------ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMKAN 171
|
170
....*....|...
gi 442625523 196 EGRTIVCTIHQPS 208
Cdd:PRK13541 172 SGGIVLLSSHLES 184
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
27-227 |
1.32e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 27 PKKPEKKsVLKGIKGTFKSGELTAIMGPSGAGKSSL-MNI--------LTG-LTKSG-------VSGKIEIGKA-----R 84
Cdd:NF040905 268 PLHPERK-VVDDVSLNVRRGEIVGIAGLMGAGRTELaMSVfgrsygrnISGtVFKDGkevdvstVSDAIDAGLAyvtedR 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQDDhffpyftVEETMLMAATLKISNQCV--SLKEKRTLIDYLlNSLKL-TKTRQTKCSNLSGGQKKRLSIALE 161
Cdd:NF040905 347 KGYGLNLIDD-------IKRNITLANLGKVSRRGVidENEEIKVAEEYR-KKMNIkTPSVFQKVGNLSGGNQQKVVLSKW 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442625523 162 LIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVcTIhqpSTNIYNLFNL---VYVLSAGRCT 227
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVI-VI---SSELPELLGMcdrIYVMNEGRIT 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
33-179 |
1.65e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVSGKIEI-GKAR----------KLCGYIMQDDHFfpYFT 101
Cdd:PRK10938 273 RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLfGRRRgsgetiwdikKHIGYVSSSLHL--DYR 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 102 VEETMLmaaTLKISN--------QCVSLKEkRTLIDYLLNSLKLTKtRQTKCS--NLSGGQKKRLSIALELIDNPAVLFL 171
Cdd:PRK10938 351 VSTSVR---NVILSGffdsigiyQAVSDRQ-QKLAQQWLDILGIDK-RTADAPfhSLSWGQQRLALIVRALVKHPTLLIL 425
|
....*...
gi 442625523 172 DEPTTGLD 179
Cdd:PRK10938 426 DEPLQGLD 433
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
436-613 |
1.85e-06 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 49.04 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 436 YYLATIITSTPVHIIFSTVYITIGYLMTDQPVEMDRFVKYLLSAVVVTICADGLGVFLGTVL-NPVNGTFVGAVSTSCML 514
Cdd:COG0842 48 ILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLLLLLLVLLLFALAFSGLGLLISTLArSQEQASAISNLVILPLT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 515 MFSGFLILLNHIPAAMRFMAYISPLRYALENMVISLYGnqrgqlicpptefychfknavtvlrqfGMEDGDFGHNILMIL 594
Cdd:COG0842 128 FLSGAFFPIESLPGWLQAIAYLNPLTYFVEALRALFLG---------------------------GAGLADVWPSLLVLL 180
|
170
....*....|....*....
gi 442625523 595 IQIAIFKVLSYFTLKHKIK 613
Cdd:COG0842 181 AFAVVLLALALRLFRRRLR 199
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
27-201 |
1.96e-06 |
|
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: 50.59 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 27 PKKPEKKSVlKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVSGKIEI-GK--ARKLC------GYIM-----Q 92
Cdd:TIGR02633 268 VINPHRKRV-DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFInGKpvDIRNPaqairaGIAMvpedrK 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 93 DDHFFPYFTVEETMLMAATLKISNQCVSLKEKRT-LIDYLLNSLKL-TKTRQTKCSNLSGGQKKRLSIALELIDNPAVLF 170
Cdd:TIGR02633 347 RHGIVPILGVGKNITLSVLKSFCFKMRIDAAAELqIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190
....*....|....*....|....*....|.
gi 442625523 171 LDEPTTGLDSSSSFDTIQLLRGLANEGRTIV 201
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQEGVAII 457
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-201 |
2.40e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 50.31 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 27 PKKPEKKSVlKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVSGKIEI-GK-----------ARKLCgYIMQD- 93
Cdd:PRK13549 270 PVNPHIKRV-DDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIdGKpvkirnpqqaiAQGIA-MVPEDr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 94 --DHFFPYFTVEETMLMAATLKISNQCV--SLKEKRTlIDYLLNSLKL-TKTRQTKCSNLSGGQKKRLSIALELIDNPAV 168
Cdd:PRK13549 348 krDGIVPVMGVGKNITLAALDRFTGGSRidDAAELKT-ILESIQRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190
....*....|....*....|....*....|...
gi 442625523 169 LFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIV 201
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVQQGVAII 459
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
28-225 |
2.52e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.41 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 28 KKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEIG----------KARKL-CGYIMQDDH- 95
Cdd:COG3845 266 RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP-ASGSIRLDgeditglsprERRRLgVAYIPEDRLg 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 96 --FFPYFTVEETMLMaatLKISNQCVSlkeKRTLIDY---LLNSLKL-------TKTRQTKCSNLSGG--QKkrLSIALE 161
Cdd:COG3845 345 rgLVPDMSVAENLIL---GRYRRPPFS---RGGFLDRkaiRAFAEELieefdvrTPGPDTPARSLSGGnqQK--VILARE 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442625523 162 LIDNPAVLFLDEPTTGLD-SSSSFdtI-QLLRGLANEGRTIVCtIhqpSTNIYNLFNL---VYVLSAGR 225
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDvGAIEF--IhQRLLELRDAGAAVLL-I---SEDLDEILALsdrIAVMYEGR 479
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
42-231 |
3.30e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.34 E-value: 3.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKS----SLMNILTGLTKSGVSGKI-----------EIGKAR-KLCGYIMQD--DHFFPYFTVE 103
Cdd:PRK09473 38 SLRAGETLGIVGESGSGKSqtafALMGLLAANGRIGGSATFngreilnlpekELNKLRaEQISMIFQDpmTSLNPYMRVG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 104 ETMLMAATL--KISNQCVSLKEKRtlidyLLNSLKLTKTRQTKC---SNLSGGQKKRLSIALELIDNPAVLFLDEPTTGL 178
Cdd:PRK09473 118 EQLMEVLMLhkGMSKAEAFEESVR-----MLDAVKMPEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442625523 179 DSSSSFDTIQLLRGLANEGRTIVCTIHQPSTNIYNLFNLVYVLSAGRCTYQGT 231
Cdd:PRK09473 193 DVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGN 245
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
44-199 |
3.31e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 44 KSGELTAIMGPSGAGKSSLMNILTGLTKSGV-SGKIEI-GKARKLCGY----------IMQDDHFFPYFTVEETMLmaat 111
Cdd:NF040905 25 REGEIHALCGENGAGKSTLMKVLSGVYPHGSyEGEILFdGEVCRFKDIrdsealgiviIHQELALIPYLSIAENIF---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 112 lkISNQcvslKEKRTLIDY---------LLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSS 182
Cdd:NF040905 101 --LGNE----RAKRGVIDWnetnrrareLLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEED 174
|
170
....*....|....*..
gi 442625523 183 SFDTIQLLRGLANEGRT 199
Cdd:NF040905 175 SAALLDLLLELKAQGIT 191
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-193 |
3.39e-06 |
|
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: 50.07 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 1 MDSSKLLKnvygidihFEDLvyQVNVPKKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKS----SLMNILTGlTKSGVSG 76
Cdd:COG4172 1 MMSMPLLS--------VEDL--SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPD-PAAHPSG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 77 KI-----EIGKA-----RKLCG----YIMQD-----DhffPYFTVEETMlmAATLKIsNQCVSLKEKRTLIDYLLNSLKL 137
Cdd:COG4172 70 SIlfdgqDLLGLserelRRIRGnriaMIFQEpmtslN---PLHTIGKQI--AEVLRL-HRGLSGAAARARALELLERVGI 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442625523 138 T--KTR------QtkcsnLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSsssfdTIQ-----LLRGL 193
Cdd:COG4172 144 PdpERRldayphQ-----LSGGQRQRVMIAMALANEPDLLIADEPTTALDV-----TVQaqildLLKDL 202
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
13-206 |
3.78e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.41 E-value: 3.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 13 IDIHFEdLVYQVNVPkkpekksVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILT------------------------- 67
Cdd:PTZ00265 1169 MDVNFR-YISRPNVP-------IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMrfydlkndhhivfknehtndmtneq 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 68 ------------------GLTKSGV----------SGKIEIGKArKLCGYIMQDDHFFPYFTVEETMLMAATL----KIS 115
Cdd:PTZ00265 1241 dyqgdeeqnvgmknvnefSLTKEGGsgedstvfknSGKILLDGV-DICDYNLKDLRNLFSIVSQEPMLFNMSIyeniKFG 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 116 NQCVSLKE-----KRTLIDYLLNSL--KLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSF---D 185
Cdd:PTZ00265 1320 KEDATREDvkracKFAAIDEFIESLpnKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKlieK 1399
|
250 260
....*....|....*....|.
gi 442625523 186 TIQLLRGLANegRTIVCTIHQ 206
Cdd:PTZ00265 1400 TIVDIKDKAD--KTIITIAHR 1418
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
31-196 |
3.98e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 49.32 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 31 EKKSVLKGIKG-TFK--SGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIE-IGK------------ARKLCGYIMQDD 94
Cdd:PRK15079 29 QPPKTLKAVDGvTLRlyEGETLGVVGESGCGKSTFARAIIGLVKA-TDGEVAwLGKdllgmkddewraVRSDIQMIFQDP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 95 --HFFPYFTVEEtmLMAATLKISNQCVSLKEKRTLIDYLLNSLKLTktrqtkcSNL--------SGGQKKRLSIALELID 164
Cdd:PRK15079 108 laSLNPRMTIGE--IIAEPLRTYHPKLSRQEVKDRVKAMMLKVGLL-------PNLinryphefSGGQCQRIGIARALIL 178
|
170 180 190
....*....|....*....|....*....|..
gi 442625523 165 NPAVLFLDEPTTGLDSSSSFDTIQLLRGLANE 196
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQRE 210
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
122-201 |
4.17e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 122 KEKRTLIDY--LLNsLKLTKTRQTkCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRT 199
Cdd:PRK15439 378 RENAVLERYrrALN-IKFNHAEQA-ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVA 455
|
..
gi 442625523 200 IV 201
Cdd:PRK15439 456 VL 457
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
31-232 |
4.30e-06 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 49.26 E-value: 4.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 31 EKKSVLKGIKGT---FKSGELTAIMGPSGAGKSSLMNILTGLTKSG-----VSGkIEIGKA---------RKLCGYIMQD 93
Cdd:PRK10070 36 EKTGLSLGVKDAslaIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTrgqvlIDG-VDIAKIsdaelrevrRKKIAMVFQS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 94 DHFFPYFTVEETMLMAATLKisnqCVSLKEKRTLIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDE 173
Cdd:PRK10070 115 FALMPHMTVLDNTAFGMELA----GINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 174 PTTGLDSSSSFDTI-QLLRGLANEGRTIVCTIHQPSTNIyNLFNLVYVLSAGRCTYQGTP 232
Cdd:PRK10070 191 AFSALDPLIRTEMQdELVKLQAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVGTP 249
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
42-207 |
6.00e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.58 E-value: 6.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKSSLMN----ILTGLTKSGVSGKIEigkarkLCGYIMQDDHFFPYFTveetmlmaatlkisnq 117
Cdd:cd03227 17 TFGEGSLTIITGPNGSGKSTILDaiglALGGAQSATRRRSGV------KAGCIVAAVSAELIFT---------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 118 cvslkekrtlidyllnslkltktrqtkCSNLSGGQKKRLSIALELI---DNPAVLF-LDEPTTGLDSSSSFDTIQLLRGL 193
Cdd:cd03227 75 ---------------------------RLQLSGGEKELSALALILAlasLKPRPLYiLDEIDRGLDPRDGQALAEAILEH 127
|
170
....*....|....
gi 442625523 194 ANEGRTIVCTIHQP 207
Cdd:cd03227 128 LVKGAQVIVITHLP 141
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
31-230 |
8.24e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.01 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 31 EKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGltksgvsgKIEIGKARKLC----------GYIM----QDDHF 96
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLS--------QFEISEGRVWAersiayvpqqAWIMnatvRGNIL 742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 97 FpyFTVEEtmlmAATLKISNQCVSLKEkrtliDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTT 176
Cdd:PTZ00243 743 F--FDEED----AARLADAVRVSQLEA-----DLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 442625523 177 GLDSSSSFDTIQ--LLRGLAneGRTIVCTIHQpsTNIYNLFNLVYVLSAGRCTYQG 230
Cdd:PTZ00243 812 ALDAHVGERVVEecFLGALA--GKTRVLATHQ--VHVVPRADYVVALGDGRVEFSG 863
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
46-193 |
1.11e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 46 GELTAIMGPSGAGKSSLMNILTG----------LTKSGVSGKIEIGKARKLCG----YIM-----QDDHFFPYFTVEETM 106
Cdd:PRK11147 29 NERVCLVGRNGAGKSTLMKILNGevllddgriiYEQDLIVARLQQDPPRNVEGtvydFVAegieeQAEYLKRYHDISHLV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 107 LMAATLKISNQCVSLKEK---------RTLIDYLLNSLKLTKtrQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTG 177
Cdd:PRK11147 109 ETDPSEKNLNELAKLQEQldhhnlwqlENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNH 186
|
170
....*....|....*.
gi 442625523 178 LDssssFDTIQLLRGL 193
Cdd:PRK11147 187 LD----IETIEWLEGF 198
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-180 |
1.24e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.43 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGVSGKIEIgkaRKLCGYIMQDDHFFPYfTVEETMLMAATL 112
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVI---RGSVAYVPQVSWIFNA-TVRENILFGSDF 705
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 113 KISN--QCVSLKEKRTLIDyLLNSLKLTKTRQtKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDS 180
Cdd:PLN03232 706 ESERywRAIDVTALQHDLD-LLPGRDLTEIGE-RGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
35-206 |
1.59e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 46.10 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIE-----IGKAR-----KLCgYIMQDDHFFPYFTVEE 104
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE-KGEILferqsIKKDLctyqkQLC-FVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 105 TMLMaaTLKISNQCVSlkekrtlIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSF 184
Cdd:PRK13540 94 NCLY--DIHFSPGAVG-------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLL 164
|
170 180
....*....|....*....|..
gi 442625523 185 DTIQLLRGLANEGRTIVCTIHQ 206
Cdd:PRK13540 165 TIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
146-205 |
1.89e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.90 E-value: 1.89e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 442625523 146 SNLSGGQKKRLSIALELI---DNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIH 205
Cdd:PRK00635 808 SSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
45-211 |
2.63e-05 |
|
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: 44.67 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 45 SGELTAIMGPSGAGKSSLmniltgltksgvsgkieigkARKLCGYIMQDDHFFPYFTVEETMlmaatlkisnqcvslkek 124
Cdd:smart00382 1 PGEVILIVGPPGSGKTTL--------------------ARALARELGPPGGGVIYIDGEDIL------------------ 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 125 rtliDYLLNSLKLTKTRQTKcsnLSGGQKKRLSIALELID--NPAVLFLDEPTTGLDSSSSF------DTIQLLRGLANE 196
Cdd:smart00382 43 ----EEVLDQLLLIIVGGKK---ASGSGELRLRLALALARklKPDVLILDEITSLLDAEQEAllllleELRLLLLLKSEK 115
|
170
....*....|....*
gi 442625523 197 GRTIVCTIHQPSTNI 211
Cdd:smart00382 116 NLTVILTTNDEKDLG 130
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
33-208 |
5.64e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 46.24 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 33 KSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIgKARKLcgYIMQDDHFFPYFTVEETMLMAATL 112
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS-EGDIRF-HDIPL--TKLQLDSWRSRLAVVSQTPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 113 KISNQCV---------SLKEKRTLIDYLLNSLKLTKTRQTKCSN----LSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:PRK10789 404 TVANNIAlgrpdatqqEIEHVARLASVHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
170 180
....*....|....*....|....*....
gi 442625523 180 SSSSFDTIQLLRGLAnEGRTIVCTIHQPS 208
Cdd:PRK10789 484 GRTEHQILHNLRQWG-EGRTVIISAHRLS 511
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
46-196 |
6.30e-05 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 45.49 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 46 GELTAIMGPSGAGKSSLMNILTGLTKSgVSGKI-----EIGKA--------RKLCGYIMQDdhffPY------FTVEETM 106
Cdd:COG4608 44 GETLGLVGESGCGKSTLGRLLLRLEEP-TSGEIlfdgqDITGLsgrelrplRRRMQMVFQD----PYaslnprMTVGDII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 107 lmAATLKISNQcVSLKEKRTLIDYLLNSLKLtktrqtkcsN----------LSGGQKKRLSIALELIDNPAVLFLDEPTT 176
Cdd:COG4608 119 --AEPLRIHGL-ASKAERRERVAELLELVGL---------RpehadrypheFSGGQRQRIGIARALALNPKLIVCDEPVS 186
|
170 180
....*....|....*....|....*
gi 442625523 177 GLDSSssfdtIQ-----LLRGLANE 196
Cdd:COG4608 187 ALDVS-----IQaqvlnLLEDLQDE 206
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
15-234 |
6.99e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.27 E-value: 6.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 15 IHFEDLVYQVnvpkKPEKKSVLKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGvSGKI-----EIGK-----AR 84
Cdd:PLN03130 1238 IKFEDVVLRY----RPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE-RGRIlidgcDISKfglmdLR 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 85 KLCGYIMQDDHFF---------PYFTVEETMLMAATlkisnqcvslkEKRTLIDYLL-NSLKLTKTRQTKCSNLSGGQKK 154
Cdd:PLN03130 1313 KVLGIIPQAPVLFsgtvrfnldPFNEHNDADLWESL-----------ERAHLKDVIRrNSLGLDAEVSEAGENFSVGQRQ 1381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 155 RLSIALELIDNPAVLFLDEPTTGLDSSSSfDTIQllRGLANEGRTivCTI----HQPSTNIYNlfNLVYVLSAGRCTYQG 230
Cdd:PLN03130 1382 LLSLARALLRRSKILVLDEATAAVDVRTD-ALIQ--KTIREEFKS--CTMliiaHRLNTIIDC--DRILVLDAGRVVEFD 1454
|
....
gi 442625523 231 TPQN 234
Cdd:PLN03130 1455 TPEN 1458
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
42-182 |
1.05e-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: 43.75 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGeLTAIMGPSGAGKSSLMN-ILTGLTKSGVSGKIEIGKARKLCG--------YImqddhffpYFTVEETMLMAATL 112
Cdd:cd03240 19 EFFSP-LTLIVGQNGAGKTTIIEaLKYALTGELPPNSKGGAHDPKLIRegevraqvKL--------AFENANGKKYTITR 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442625523 113 KIS--NQCVSLKEKRtlIDYLLnslKLTKTRqtkcsnLSGGQKKRLSIALEL------IDNPAVLFLDEPTTGLDSSS 182
Cdd:cd03240 90 SLAilENVIFCHQGE--SNWPL---LDMRGR------CSGGEKVLASLIIRLalaetfGSNCGILALDEPTTNLDEEN 156
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
393-606 |
1.14e-04 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 44.69 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 393 VGMIMIHCVYLWYTTIMPGILRypAEIEIIRKETFNNWYKLRTYYLATIITSTPVHIIFSTVYItigYLMTDQPVEMDRF 472
Cdd:pfam12698 164 VGLILMIIILIGAAIIAVSIVE--EKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIIL---LLLFGIGIPFGNL 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 473 VKYLLSAVVVTICADGLGVFLGTVL-NPVNGTFVGAVSTSCMLMFSGFLILLNHIPAAMRFMAYISPLrYALENMVISLY 551
Cdd:pfam12698 239 GLLLLLFLLYGLAYIALGYLLGSLFkNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPF-FSPIDGLLRLI 317
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 442625523 552 gnqrgqlicpptefychfknavtvlrqFGMEDGDFGHNILMILIQIAIFKVLSYF 606
Cdd:pfam12698 318 ---------------------------YGDSLWEIAPSLIILLLFAVVLLLLALL 345
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
36-181 |
1.15e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.57 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 36 LKGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTK--SG----------VSGKIEIGKARKLCGYIMQDdhffPY---- 99
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETptGGelyyqgqdllKADPEAQKLLRQKIQIVFQN----PYgsln 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 100 ------FTVEETMLMAATLkisnqcvSLKEKRTLIDYLLNSLKLtKTRQTK--CSNLSGGQKKRLSIALELIDNPAVLFL 171
Cdd:PRK11308 107 prkkvgQILEEPLLINTSL-------SAAERREKALAMMAKVGL-RPEHYDryPHMFSGGQRQRIAIARALMLDPDVVVA 178
|
170
....*....|
gi 442625523 172 DEPTTGLDSS 181
Cdd:PRK11308 179 DEPVSALDVS 188
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
37-196 |
1.25e-04 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 43.92 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 37 KGIKGTFKSGELTAIMGPSGAGKSSLMNILTGLTKSGV---SGKIEI-GKARKLCGY-------IMQDDH--FFPYFT-- 101
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVrqtAGRVLLdGKPVAPCALrgrkiatIMQNPRsaFNPLHTmh 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 102 --VEETMLMA------ATLKISNQCVSLKEKRTLidyllnsLKLTKTRqtkcsnLSGGQKKRLSIALELIDNPAVLFLDE 173
Cdd:PRK10418 100 thARETCLALgkpaddATLTAALEAVGLENAARV-------LKLYPFE------MSGGMLQRMMIALALLCEAPFIIADE 166
|
170 180
....*....|....*....|...
gi 442625523 174 PTTGLDSSSSFDTIQLLRGLANE 196
Cdd:PRK10418 167 PTTDLDVVAQARILDLLESIVQK 189
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
125-205 |
1.27e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.00 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 125 RTLIDYLLNSLKLTKTRQTkcsnLSGGQKKRLSIALEL---IDNPAVLFLDEPTTGLdsssSFDTIQLL----RGLANEG 197
Cdd:TIGR00630 811 QTLCDVGLGYIRLGQPATT----LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGL----HFDDIKKLlevlQRLVDKG 882
|
....*...
gi 442625523 198 RTIVCTIH 205
Cdd:TIGR00630 883 NTVVVIEH 890
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
53-196 |
2.42e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 53 GPSGAGKSSLMNILTG-LTKSgvSGKIEIGKARKLcGYIMQDDHFFPYFTVEETMLMAATlkisnQCVSLKEKRTLI--- 128
Cdd:PRK15064 34 GANGCGKSTFMKILGGdLEPS--AGNVSLDPNERL-GKLRQDQFAFEEFTVLDTVIMGHT-----ELWEVKQERDRIyal 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 129 ------DY------------------------LLNSLKL-TKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTG 177
Cdd:PRK15064 106 pemseeDGmkvadlevkfaemdgytaearageLLLGVGIpEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNN 185
|
170
....*....|....*....
gi 442625523 178 LDssssFDTIQLLRGLANE 196
Cdd:PRK15064 186 LD----INTIRWLEDVLNE 200
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
45-82 |
2.45e-04 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 42.77 E-value: 2.45e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 442625523 45 SGELTAIMGPSGAGKSSLMNILTG---LTKSGVSGKIEIGK 82
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPelvLATGEISEKLGRGR 124
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
41-198 |
2.55e-04 |
|
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: 42.17 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 41 GTFKSGELTAIMGPSGAGKSSLMNILTGLTKSgvsgkieigkarklcgyimqddhffpyfTVEETMLMAATLKISNQCVS 120
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGQLIP----------------------------NGDNDEWDGITPVYKPQYID 71
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442625523 121 LkekrtlidyllnslkltktrqtkcsnlSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGR 198
Cdd:cd03222 72 L---------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
35-201 |
2.65e-04 |
|
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: 43.31 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 35 VLKGIKGTFKSGELTAIMGPSGAGKSS-LMNILTGLTKSgvSGKIEIGKARKLC---GYIMQDdhffpyfTVEETMLMAA 110
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSlLMLILGELEPS--EGKIKHSGRISFSsqfSWIMPG-------TIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 111 T-----LKISNQCVSLKEkrtlidyllNSLKLTKTRQTKCS----NLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSS 181
Cdd:cd03291 123 SydeyrYKSVVKACQLEE---------DITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
170 180
....*....|....*....|...
gi 442625523 182 SS---FDTIqLLRGLANEGRTIV 201
Cdd:cd03291 194 TEkeiFESC-VCKLMANKTRILV 215
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
7-190 |
3.42e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 43.19 E-value: 3.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 7 LKNVYGIDIHFEDlvyqvnvpKKPEKKSVLKgIKGTFKSGELTAIMGPSGAGKS-SLMNILTGLTKSG-VSG-------- 76
Cdd:PRK11022 3 LLNVDKLSVHFGD--------ESAPFRAVDR-ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGrVMAeklefngq 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 77 ---KIEIGKARKLCG----YIMQD--DHFFPYFTVEETMLMAatLKIsNQCVSLKEKRTLIDYLLNSLKLTKTR---QTK 144
Cdd:PRK11022 74 dlqRISEKERRNLVGaevaMIFQDpmTSLNPCYTVGFQIMEA--IKV-HQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVY 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 442625523 145 CSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLL 190
Cdd:PRK11022 151 PHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELL 196
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
42-173 |
3.54e-04 |
|
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: 43.63 E-value: 3.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 42 TFKSGELTAIMGPSGAGKSSLMNILTGLTKSgVSGKIEI-GKA---------RKLCGYIMQDDHFFpyftveETMLMAAT 111
Cdd:COG4615 354 TIRRGELVFIVGGNGSGKSTLAKLLTGLYRP-ESGEILLdGQPvtadnreayRQLFSAVFSDFHLF------DRLLGLDG 426
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442625523 112 LkisnqcvslkEKRTLIDYLLNSLKLtktrQTKCS---------NLSGGQKKRLSIALELIDNPAVLFLDE 173
Cdd:COG4615 427 E----------ADPARARELLERLEL----DHKVSvedgrfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
46-179 |
3.99e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 3.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 46 GELTAIMGPSGAGKSSLMNILTGLT-----------KSGVSGKIEIgkaRKLCGYIMQDdhFFPY--FTVEETMLMAATL 112
Cdd:NF033858 292 GEIFGFLGSNGCGKSTTMKMLTGLLpasegeawlfgQPVDAGDIAT---RRRVGYMSQA--FSLYgeLTVRQNLELHARL 366
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442625523 113 kisnqcVSLKEKRT--LIDYLLNSLKLTKTRQTKCSNLSGGQKKRLSIALELIDNPAVLFLDEPTTGLD 179
Cdd:NF033858 367 ------FHLPAAEIaaRVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
45-82 |
6.63e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 40.99 E-value: 6.63e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 442625523 45 SGELTAIMGPSGAGKSSLMNILTG---LTKSGVSGKIEIGK 82
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPeldLRTGEISEKLGRGR 145
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
148-201 |
9.53e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 9.53e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442625523 148 LSGGQKKRLSIALEL--IDNPAVLF-LDEPTTGLdsssSFDTIQLL----RGLANEGRTIV 201
Cdd:COG0178 827 LSGGEAQRVKLASELskRSTGKTLYiLDEPTTGL----HFHDIRKLlevlHRLVDKGNTVV 883
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
146-208 |
2.30e-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: 40.45 E-value: 2.30e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442625523 146 SNLSGGQKK---RLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIVCTIHQPS 208
Cdd:pfam13304 235 FELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
125-206 |
2.40e-03 |
|
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: 40.29 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 125 RTLIDYLLNSLKLTKTRQTkcsnLSGGQKKRLSIALEL--IDNPAVLF-LDEPTTGLdsssSFDTIQ----LLRGLANEG 197
Cdd:cd03271 151 QTLCDVGLGYIKLGQPATT----LSGGEAQRIKLAKELskRSTGKTLYiLDEPTTGL----HFHDVKklleVLQRLVDKG 222
|
....*....
gi 442625523 198 RTIVCTIHQ 206
Cdd:cd03271 223 NTVVVIEHN 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
148-201 |
2.65e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 2.65e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 442625523 148 LSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLRGLANEGRTIV 201
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLV 189
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
46-257 |
3.46e-03 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 40.22 E-value: 3.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 46 GELTAIMGPSGAGKSSLMNILTGLTKSGvSGKIEIGKAR--KLCGYIMQ----DDHFF---PYFTVEETMLMAAT----L 112
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQ-GGEIIFNGQRidTLSPGKLQalrrDIQFIfqdPYASLDPRQTVGDSimepL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 113 KISNqCVSLKEKRTLIDYLLNSLKLTKTRQTKCSN-LSGGQKKRLSIALELIDNPAVLFLDEPTTGLDSSSSFDTIQLLR 191
Cdd:PRK10261 429 RVHG-LLPGKAAAARVAWLLERVGLLPEHAWRYPHeFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLL 507
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442625523 192 GLANEGRTIVCTIHQPSTNIYNLFNLVYVLSAGRCTYQG-------TPQN--TVMFLSSVGLECPPYHNPADFLL 257
Cdd:PRK10261 508 DLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGprravfeNPQHpyTRKLMAAVPVADPSRQRPQRVLL 582
|
|
| PhnN |
COG3709 |
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism]; |
45-66 |
4.51e-03 |
|
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
Pssm-ID: 442923 Cd Length: 188 Bit Score: 38.64 E-value: 4.51e-03
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
126-205 |
5.89e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 5.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442625523 126 TLIDYLLNSLKLTKTRQTkcsnLSGGQKKRLSIALELidnPAVLF-----LDEPTTGLDSSSSFDTIQLLRGLANEGRTI 200
Cdd:PRK00635 459 ILIDLGLPYLTPERALAT----LSGGEQERTALAKHL---GAELIgityiLDEPSIGLHPQDTHKLINVIKKLRDQGNTV 531
|
....*
gi 442625523 201 VCTIH 205
Cdd:PRK00635 532 LLVEH 536
|
|
| MnmE_helical |
pfam12631 |
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An ... |
36-68 |
8.07e-03 |
|
MnmE helical domain; The tRNA modification GTPase MnmE consists of three domains. An N-terminal domain, a helical domain and a GTPase domain which is nested within the helical domain. This family represents the helical domain.
Pssm-ID: 463649 [Multi-domain] Cd Length: 326 Bit Score: 38.62 E-value: 8.07e-03
10 20 30
....*....|....*....|....*....|....*....
gi 442625523 36 LKGIKGTFKSGEL------TAIMGPSGAGKSSLMNILTG 68
Cdd:pfam12631 78 LEKLLATADRGRIlregikVVIVGKPNVGKSSLLNALLG 116
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
23-66 |
9.09e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 9.09e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 442625523 23 QVNVPK---KPEKKSV---------LKGIKGTFKSGELTAIMGPSGAGKSSLMN-IL 66
Cdd:COG0178 596 RIPVPKkrrKGNGKFLtikgarennLKNVDVEIPLGVLTCVTGVSGSGKSTLVNdIL 652
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
36-66 |
9.19e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 9.19e-03
10 20 30
....*....|....*....|....*....|..
gi 442625523 36 LKGIKGTFKSGELTAIMGPSGAGKSSLMN-IL 66
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINeTL 656
|
|
| |
