|
Name |
Accession |
Description |
Interval |
E-value |
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
8-263 |
1.12e-126 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 359.81 E-value: 1.12e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 8 LLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVL 86
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTpSSGEVRLNGRPLAAWSPWELARRRAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 87 PQSSSLSFPFLCEEVVAMGRLPHSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQIWQAPEEPQq 166
Cdd:COG4559 81 PQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQLWEPVDGGP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 167 aRLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLYD 246
Cdd:COG4559 160 -RWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVYG 238
|
250
....*....|....*..
gi 743522756 247 YPAQVIHHPESGVPMVV 263
Cdd:COG4559 239 ADLRVLAHPEGGCPQVL 255
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
7-263 |
2.81e-118 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 338.67 E-value: 2.81e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 7 PLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGV 85
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSpDSGEVRLNGRPLADWSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 86 LPQSSSLSFPFLCEEVVAMGRLPHSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQIWQAPEEPq 165
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEPDGPP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 166 qaRLLLLDEPTSALDLKYQHQLLAMARALAG-RNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARL 244
Cdd:PRK13548 160 --RWLLLDEPTSALDLAHQHHVLRLARQLAHeRGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRV 237
|
250
....*....|....*....
gi 743522756 245 YDYPAQVIHHPESGVPMVV 263
Cdd:PRK13548 238 YGADVLVQPHPETGAPLVL 256
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
8-263 |
1.44e-101 |
|
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: 296.18 E-value: 1.44e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 8 LLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVL 86
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKpSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 87 PQSSSLSFPFLCEEVVAMGRLPHS---EPASRRD-EIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqape 162
Cdd:COG1120 81 PQEPPAPFGLTVRELVALGRYPHLglfGRPSAEDrEAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 163 epqQARLLLLDEPTSALDLKYQHQLLAMARALA-GRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELI 241
Cdd:COG1120 155 ---EPPLLLLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELL 231
|
250 260
....*....|....*....|..
gi 743522756 242 ARLYDYPAQVIHHPESGVPMVV 263
Cdd:COG1120 232 EEVYGVEARVIEDPVTGRPLVL 253
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-254 |
3.75e-70 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 216.11 E-value: 3.75e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 4 SPSPLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQT-RRGWagnalaH 81
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLFGKPpRRAR------R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 82 RVGVLPQSSSL--SFPFLCEEVVAMGRLPHS---EPASRRD-EIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLA 155
Cdd:COG1121 76 RIGYVPQRAEVdwDFPITVRDVVLMGRYGRRglfRRPSRADrEAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 156 QiwqapeepqQARLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLmADGNAGEV 235
Cdd:COG1121 156 Q---------DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEEV 225
|
250
....*....|....*....
gi 743522756 236 LTPELIARLYDYPAQVIHH 254
Cdd:COG1121 226 LTPENLSRAYGGPVALLAH 244
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
8-263 |
3.32e-64 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 201.98 E-value: 3.32e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 8 LLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELEH---------EGEIHLFGQTRRGWAGNA 78
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGggaprgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 79 LAHRVGVLPQSSSLSFPFLCEEVVAMGRLPHSEPA---SRRD-EIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVL 154
Cdd:PRK13547 81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAgalTHRDgEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 155 AQIWQAPEEPQQARLLLLDEPTSALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAG 233
Cdd:PRK13547 161 AQLWPPHDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
|
250 260 270
....*....|....*....|....*....|
gi 743522756 234 EVLTPELIARLYDYPAQVIHHPESGVPMVV 263
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVDAGDGVPPVIV 270
|
|
| F420-0_ABC_ATP |
TIGR03873 |
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ... |
13-263 |
2.03e-63 |
|
proposed F420-0 ABC transporter, ATP-binding protein; This small clade of ABC-type transporter ATP-binding protein components is found as a three gene cassette along with a periplasmic substrate-binding protein (TIGR03868) and a permease (TIGR03869). The organisms containing this cassette are all Actinobacteria and all contain numerous genes requiring the coenzyme F420. This model was defined based on five such organisms, four of which are lacking all F420 biosynthetic capability save the final side-chain polyglutamate attachment step (via the gene cofE: TIGR01916). In Jonesia denitrificans DSM 20603 and marine actinobacterium PHSC20C1 this cassette is in an apparent operon with the cofE gene and, in PHSC20C1, also with a F420-dependent glucose-6-phosphate dehydrogenase (TIGR03554). Based on these observations we propose that this ATP-binding protein is a component of an F420-0 (that is, F420 lacking only the polyglutamate tail) transporter.
Pssm-ID: 163585 [Multi-domain] Cd Length: 256 Bit Score: 199.27 E-value: 2.03e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 13 GLRLSR-----GNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVL 86
Cdd:TIGR03873 1 GLRLSRvswsaGGRLIVDGVDVTAPPGSLTGLLGPNGSGKSTLLRLLAGALRpDAGTVDLAGVDLHGLSRRARARRVALV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 87 PQSSSLSFPFLCEEVVAMGRLPH----SEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqape 162
Cdd:TIGR03873 81 EQDSDTAVPLTVRDVVALGRIPHrslwAGDSPHDAAVVDRALARTELSHLADRDMSTLSGGERQRVHVARALAQ------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 163 epqQARLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIA 242
Cdd:TIGR03873 155 ---EPKLLLLDEPTNHLDVRAQLETLALVRELAATGVTVVAALHDLNLAASYCDHVVVLDGGRVVAAGPPREVLTPALIR 231
|
250 260
....*....|....*....|.
gi 743522756 243 RLYDYPAQVIHHPESGVPMVV 263
Cdd:TIGR03873 232 AVYGVDATVLTHPDTGRPIIA 252
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
10-230 |
2.85e-62 |
|
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: 193.42 E-value: 2.85e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 10 SCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQ 88
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKpSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 89 ssslsfpflceevvamgrlphsepasrrdeivraAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQAR 168
Cdd:cd03214 81 ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQ---------EPP 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 169 LLLLDEPTSALDLKYQHQLLAMARALAG-RNTAVLVVLHDLNLAARYADRLVMLEQGRLMADG 230
Cdd:cd03214 118 ILLLDEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
33-263 |
2.75e-60 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 191.00 E-value: 2.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGWAGNALAHRVGVLPQSSSLSFPFLCEEVVAMGRLPHSE 111
Cdd:PRK11231 27 TGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVRELVAYGRSPWLS 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 ---PASRRDE-IVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQL 187
Cdd:PRK11231 107 lwgRLSAEDNaRVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ---------DTPVVLLDEPTTYLDINHQVEL 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743522756 188 LAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLYDYPAQVIHHPESGVPMVV 263
Cdd:PRK11231 178 MRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAEIHPEPVSGTPMCV 253
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-262 |
5.69e-55 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 181.96 E-value: 5.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 7 PLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGWAGNALAHRVGV 85
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTaGTVLVAGDDVEALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 86 LPQSSSLSFPFLCEEVVAMGRLPHSEPASRRDE----IVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwQAP 161
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTEtdraAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQ--ATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 162 eepqqarLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELI 241
Cdd:PRK09536 160 -------VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTL 232
|
250 260
....*....|....*....|.
gi 743522756 242 ARLYDYPAQVIHHPESGVPMV 262
Cdd:PRK09536 233 RAAFDARTAVGTDPATGAPTV 253
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
33-263 |
5.88e-55 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 177.20 E-value: 5.88e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLSFPFLCEEVVAMGRLPHSE 111
Cdd:COG4604 26 KGGITALIGPNGAGKSTLLSMISRLLPpDSGEVLVDGLDVATTPSRELAKRLAILRQENHINSRLTVRELVAFGRFPYSK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 --PASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLA 189
Cdd:COG4604 106 grLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQ---------DTDYVLLDEPLNNLDMKHSVQMMK 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 190 MARALA---GRntAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLYDYPAQVIHHPesGVPMVV 263
Cdd:COG4604 177 LLRRLAdelGK--TVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEVEEID--GKRICV 249
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
33-230 |
1.18e-54 |
|
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: 175.41 E-value: 1.18e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQ-TRRGWagnalaHRVGVLPQSSSL--SFPFLCEEVVAMGRLP 108
Cdd:cd03235 24 PGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSIRVFGKpLEKER------KRIGYVPQRRSIdrDFPISVRDVVLMGLYG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HS---EPASRRD-EIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQ 184
Cdd:cd03235 98 HKglfRRLSKADkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQ---------DPDLLLLDEPFAGVDPKTQ 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 743522756 185 HQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEqGRLMADG 230
Cdd:cd03235 169 EDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
33-250 |
8.33e-49 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 161.55 E-value: 8.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEHEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLSFPFLCEEVVAMGRlphseP 112
Cdd:COG4138 21 AGELIHLIGPNGAGKSTLLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYLALHQ-----P 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 113 ASRRDEIVRAAMTHA----GVDHLANRLYPGLSGGERQRVQFARVLAQIWqaPEEPQQARLLLLDEPTSALDLKYQHQLL 188
Cdd:COG4138 96 AGASSEAVEQLLAQLaealGLEDKLSRPLTQLSGGEWQRVRLAAVLLQVW--PTINPEGQLLLLDEPMNSLDVAQQAALD 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743522756 189 AMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLYDYPAQ 250
Cdd:COG4138 174 RLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFR 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
32-237 |
4.81e-47 |
|
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: 156.34 E-value: 4.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQTRRGWAGNALAHRVGVLPQssslsFP---FLCEEV---VAM 104
Cdd:COG1122 25 EKGEFVAIIGPNGSGKSTLLRLLNGLLKPtSGEVLVDGKDITKKNLRELRRKVGLVFQ-----NPddqLFAPTVeedVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 105 G----RLPHSEpasrRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALD 180
Cdd:COG1122 100 GpenlGLPREE----IRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM------EPE---VLVLDEPTAGLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 181 LKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:COG1122 167 PRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFS 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
34-263 |
2.79e-46 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 155.53 E-value: 2.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLSFPFLCEEVVAMGRLPHSEP 112
Cdd:PRK10253 33 GHFTAIIGPNGCGKSTLLRTLSRLMTpAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQELVARGRYPHQPL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 113 ASR----RDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLL 188
Cdd:PRK10253 113 FTRwrkeDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQ---------ETAIMLLDEPTTWLDISHQIDLL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743522756 189 AMARALAGRNTAVLV-VLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLYDYPAQVIHHPESGVPMVV 263
Cdd:PRK10253 184 ELLSELNREKGYTLAaVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMIIDDPVAGTPLVV 259
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
33-261 |
3.33e-45 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 152.63 E-value: 3.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCL-TGELEHEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLSFPFLCEEVVAMGRLPHSE 111
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLgRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIGRYPWHG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASR----RDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQL 187
Cdd:PRK10575 116 ALGRfgaaDREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQ---------DSRCLLLDEPTSALDIAHQVDV 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743522756 188 LAMARALAG-RNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLYDYPAQVIHHPESGVPM 261
Cdd:PRK10575 187 LALVHRLSQeRGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPHPAGAAPV 261
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
33-236 |
7.69e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 148.29 E-value: 7.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAhRVGVLPQSSSLsFPFL-CEEVVA-MGRLpH 109
Cdd:COG1131 25 PGEIFGLLGPNGAGKTTTIRMLLGLLRpTSGEVRVLGEDVARDPAEVRR-RIGYVPQEPAL-YPDLtVRENLRfFARL-Y 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 110 SEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLA 189
Cdd:COG1131 102 GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLH---------DPELLILDEPTSGLDPEARRELWE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 743522756 190 MARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:COG1131 173 LLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
37-254 |
1.64e-43 |
|
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: 147.92 E-value: 1.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 37 TALLGPNGAGKSSLLKCLTGEL--EHEGEIHLFGQTRRGWAGNALAHRVGVLpqSSSLSFPFL----CEEVVA------M 104
Cdd:COG1119 32 WAILGPNGAGKSTLLSLITGDLppTYGNDVRLFGERRGGEDVWELRKRIGLV--SPALQLRFPrdetVLDVVLsgffdsI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 105 GRLPHSEPASRrdEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapEEPqqaRLLLLDEPTSALDLKYQ 184
Cdd:COG1119 110 GLYREPTDEQR--ERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV------KDP---ELLILDEPTAGLDLGAR 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743522756 185 HQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLYDYPAQVIHH 254
Cdd:COG1119 179 ELLLALLDKLAAEgAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEAFGLPVEVERR 249
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
32-225 |
1.34e-42 |
|
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: 144.15 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGEL-EHEGEIHLFGQTRRGWAGNALAHRVGVLPQssslsFP---FLCEEV---VAM 104
Cdd:cd03225 25 KKGEFVLIVGPNGSGKSTLLRLLNGLLgPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ-----NPddqFFGPTVeeeVAF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 105 GRLPHSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQ 184
Cdd:cd03225 100 GLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM---------DPDILLLDEPTAGLDPAGR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 743522756 185 HQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGR 225
Cdd:cd03225 171 RELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-263 |
2.55e-40 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 139.68 E-value: 2.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEHEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLSFPFLCEEVVAMGRLPHSEP 112
Cdd:PRK03695 21 AGEILHLVGPNGAGKSTLLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLHQPDKTRT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 113 ASRRDEIVRAAmTHAGVDHLANRLYPGLSGGERQRVQFARVLAQIWqaPEEPQQARLLLLDEPTSALDLKYQHQLLAMAR 192
Cdd:PRK03695 101 EAVASALNEVA-EALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVW--PDINPAGQLLLLDEPMNSLDVAQQAALDRLLS 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743522756 193 ALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLYDYPAQviHHPESGVPMVV 263
Cdd:PRK03695 178 ELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFR--RLDVEGHPMLI 246
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
32-245 |
1.27e-38 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 135.00 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALA---HRVGVLPQSSSLSFPFLCEEVVAMGRL 107
Cdd:cd03256 25 NPGEFVALIGPSGAGKSTLLRCLNGLVEpTSGSVLIDGTDINKLKGKALRqlrRQIGMIFQQFNLIERLSVLENVLSGRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 PH-------SEPASRRD-EIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSAL 179
Cdd:cd03256 105 GRrstwrslFGLFPKEEkQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ---------QPKLILADEPVASL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 180 DLKYQHQLLAMARALA-GRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEvLTPELIARLY 245
Cdd:cd03256 176 DPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVLDEIY 241
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
32-237 |
2.68e-38 |
|
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: 140.04 E-value: 2.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGN---ALAHRVGVLPQ--SSSLsFPFL-CEEVVAM 104
Cdd:COG1123 289 RRGETLGLVGESGSGKSTLARLLLGLLRpTSGSILFDGKDLTKLSRRslrELRRRVQMVFQdpYSSL-NPRMtVGDIIAE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 105 G-RLPHSEPASRRDEIVRAAMTHAGVD-HLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALDL 181
Cdd:COG1123 368 PlRLHGLLSRAERRERVAELLERVGLPpDLADR-YPHeLSGGQRQRVAIARALAL------EP---KLLILDEPTSALDV 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 182 KYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:COG1123 438 SVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
33-236 |
1.78e-37 |
|
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: 131.90 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQ-TRRGWagNALAHRVGVLPQSSSLsFPFL-CEEVVAM-GRL- 107
Cdd:COG4555 26 DGEITGLLGPNGAGKTTLLRMLAGLLKPdSGSILIDGEdVRKEP--REARRQIGVLPDERGL-YDRLtVRENIRYfAELy 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 --PHSEPASRRDEIVRAAmthaGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQH 185
Cdd:COG4555 103 glFDEELKKRIEELIELL----GLEEFLDRRVGELSTGMKKKVALARALVH---------DPKVLLLDEPTNGLDVMARR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 743522756 186 QLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:COG4555 170 LLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
32-221 |
7.94e-37 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 128.89 E-value: 7.94e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEHEGeihlfGQTRRgwagnALAHRVGVLPQSSSL--SFPFLCEEVVAMGRLPH 109
Cdd:NF040873 16 PAGSLTAVVGPNGSGKSTLLKVLAGVLRPTS-----GTVRR-----AGGARVAYVPQRSEVpdSLPLTVRDLVAMGRWAR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 110 SEPASRRDEIVRAAMTHA----GVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQH 185
Cdd:NF040873 86 RGLWRRLTRDDRAAVDDAlervGLADLAGRQLGELSGGQRQRALLAQGLAQ---------EADLLLLDEPTTGLDAESRE 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 743522756 186 QLLAMARALAGRNTAVLVVLHDLNLAARyADRLVML 221
Cdd:NF040873 157 RIIALLAEEHARGATVVVVTHDLELVRR-ADPCVLL 191
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-262 |
2.30e-36 |
|
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: 134.65 E-value: 2.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 6 SPLLSCRGLRLS--RGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELEH----EGEIHLFGQTRRGWAGNAL 79
Cdd:COG1123 2 TPLLEVRDLSVRypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 80 AHRVGVLPQSSSLSF-PFLCEEVVAMGRLPHSEPASRRDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAqi 157
Cdd:COG1123 82 GRRIGMVFQDPMTQLnPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDR-YPHqLSGGQRQRVAIAMALA-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 158 wqapeepQQARLLLLDEPTSALDLKYQHQLLAMARAL-AGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:COG1123 159 -------LDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
250 260 270
....*....|....*....|....*....|
gi 743522756 237 T-PELIA---RLYDYPAQVIHHPESGVPMV 262
Cdd:COG1123 232 AaPQALAavpRLGAARGRAAPAAAAAEPLL 261
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
10-225 |
1.21e-35 |
|
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: 124.66 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 10 SCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQ 88
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 89 ssslsfpflceevvamgrlphsepasrrdeivraamthagvdhlanrlypgLSGGERQRVQFARVLAQiwqapeepqQAR 168
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLL---------NPD 100
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 169 LLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGR 225
Cdd:cd00267 101 LLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
32-237 |
3.15e-35 |
|
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: 126.01 E-value: 3.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHR--------VGVLPQSSSLsfpflceEVV 102
Cdd:cd03219 24 RPGEIHGLIGPNGAGKTTLFNLISGFLRpTSGSVLFDGEDITGLPPHEIARLgigrtfqiPRLFPELTVL-------ENV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 103 AMGRLPHS-------EPASRRDEIVRAAMTHA---GVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLL 172
Cdd:cd03219 97 MVAAQARTgsglllaRARREEREARERAEELLervGLADLADRPAGELSYGQQRRLEIARALAT---------DPKLLLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743522756 173 DEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:cd03219 168 DEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
32-226 |
4.20e-35 |
|
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: 125.29 E-value: 4.20e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQTRRGWAGNALAH----RVGVLPQSSSLsFPFL-CEEVVAM 104
Cdd:cd03255 28 EKGEFVAIVGPSGSGKSTLLNILGG-LDRptSGEVRVDGTDISKLSEKELAAfrrrHIGFVFQSFNL-LPDLtALENVEL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 105 GRLPHSEPASRRDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKY 183
Cdd:cd03255 106 PLLLAGVPKKERRERAEELLERVGLGDRLNH-YPSeLSGGQQQRVAIARALA---------NDPKIILADEPTGNLDSET 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 743522756 184 QHQLLAMARALA-GRNTAVLVVLHDLNLaARYADRLVMLEQGRL 226
Cdd:cd03255 176 GKEVMELLRELNkEAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
32-236 |
1.01e-34 |
|
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: 124.92 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLSF-PF------LCEEVVA 103
Cdd:COG1124 29 APGESFGLVGESGSGKSTLLRALAGLERPwSGEVTFDGRPVTRRRRKAFRRRVQMVFQDPYASLhPRhtvdriLAEPLRI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 104 MGRLphsepasRRDEIVRAAMTHAGVD-HLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALDL 181
Cdd:COG1124 109 HGLP-------DREERIAELLEQVGLPpSFLDR-YPHqLSGGQRQRVAIARALIL------EP---ELLLLDEPTSALDV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743522756 182 KYQHQLLAMARAL-AGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:COG1124 172 SVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
33-226 |
1.55e-34 |
|
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: 122.12 E-value: 1.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQtRRGWAGNALAHRVGVLPQSSSLsFPFlceevvamgrlphse 111
Cdd:cd03230 25 KGEIYGLLGPNGAGKTTLIKIILGLLKpDSGEIKVLGK-DIKKEPEEVKRRIGYLPEEPSL-YEN--------------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 pasrrdeivraaMThaGVDHLAnrlypgLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLAMA 191
Cdd:cd03230 88 ------------LT--VRENLK------LSGGMKQRLALAQALLH---------DPELLILDEPTSGLDPESRREFWELL 138
|
170 180 190
....*....|....*....|....*....|....*
gi 743522756 192 RALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRL 226
Cdd:cd03230 139 RELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
12-235 |
1.83e-34 |
|
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: 123.83 E-value: 1.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 12 RGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTG------ELEHEGEIHLFGQTRRGWAGNALAHR--V 83
Cdd:cd03260 4 RDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndlipGAPDEGEVLLDGKDIYDLDVDVLELRrrV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 84 GVLPQSSSLsFPFLCEEVVAMG-RLPHSEPASRRDEIVRAAMTHAGV-DHLANRLYP-GLSGGERQRVQFARVLAQiwqa 160
Cdd:cd03260 84 GMVFQKPNP-FPGSIYDNVAYGlRLHGIKLKEELDERVEEALRKAALwDEVKDRLHAlGLSGGQQQRLCLARALAN---- 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 161 peEPqqaRLLLLDEPTSALDlkyQHQLLAMARALA--GRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEV 235
Cdd:cd03260 159 --EP---EVLLLDEPTSALD---PISTAKIEELIAelKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-237 |
7.80e-34 |
|
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: 122.40 E-value: 7.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 4 SPSPLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAG---NAL 79
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRpDSGEILVDGQDITGLSEkelYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 80 AHRVGVLPQS----SSLSfpflCEEVVAM-----GRLPHSEpasrRDEIVRAAMTHAGVDHLANrLYPG-LSGGERQRVQ 149
Cdd:COG1127 81 RRRIGMLFQGgalfDSLT----VFENVAFplrehTDLSEAE----IRELVLEKLELVGLPGAAD-KMPSeLSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 150 FARVLAQiwqapeEPQqarLLLLDEPTSALD-----------LKYQHQLlamaralagrNTAVLVVLHDLNLAARYADRL 218
Cdd:COG1127 152 LARALAL------DPE---ILLYDEPTAGLDpitsavideliRELRDEL----------GLTSVVVTHDLDSAFAIADRV 212
|
250
....*....|....*....
gi 743522756 219 VMLEQGRLMADGNAGEVLT 237
Cdd:COG1127 213 AVLADGKIIAEGTPEELLA 231
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
32-229 |
8.39e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 122.07 E-value: 8.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQTRRGWAGNALA----HRVGVLPQSSSLsFPFL-CEEVVAM 104
Cdd:COG1136 32 EAGEFVAIVGPSGSGKSTLLNILGG-LDRptSGEVLIDGQDISSLSERELArlrrRHIGFVFQFFNL-LPELtALENVAL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 105 GRLPHSEPASRRDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKY 183
Cdd:COG1136 110 PLLLAGVSRKERRERARELLERVGLGDRLDH-RPSqLSGGQQQRVAIARALV---------NRPKLILADEPTGNLDSKT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 743522756 184 QHQLLAMARALAGR-NTAVLVVLHDLNLAArYADRLVMLEQGRLMAD 229
Cdd:COG1136 180 GEEVLELLRELNRElGTTIVMVTHDPELAA-RADRVIRLRDGRIVSD 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
9-237 |
1.86e-33 |
|
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: 121.45 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 9 LSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGWAGNALAH---RVG 84
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEVLIDGEDISGLSEAELYRlrrRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 85 VLPQS----SSLSfpflCEEVVAMGRLPHSE-PASRRDEIVRAAMTHAGVDHLANrLYPG-LSGGERQRVQFARVLAqiw 158
Cdd:cd03261 81 MLFQSgalfDSLT----VFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAED-LYPAeLSGGMKKRVALARALA--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 159 qapEEPQqarLLLLDEPTSALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:cd03261 153 ---LDPE---LLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
9-226 |
7.94e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 118.77 E-value: 7.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 9 LSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQTRRGWAGNALAHRVGVLP 87
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADlDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 88 QSSS---------LSFPFlceevvamgRLPHSEPasrRDEIVRAAMTHAGVDH-LANRLYPGLSGGERQRVQFARVLAQi 157
Cdd:COG4619 81 QEPAlwggtvrdnLPFPF---------QLRERKF---DRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLL- 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 158 wqapeEPqqaRLLLLDEPTSALDLKYQHQLLAM-ARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRL 226
Cdd:COG4619 148 -----QP---DVLLLDEPTSALDPENTRRVEELlREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
32-229 |
2.57e-32 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 119.04 E-value: 2.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQTRRGwagnaLAHRVGVLPQSSSLsFPFL-CEEVVAMGRLP 108
Cdd:COG1116 35 AAGEFVALVGPSGCGKSTLLRLIAG-LEKptSGEVLVDGKPVTG-----PGPDRGVVFQEPAL-LPWLtVLDNVALGLEL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSEPASRRDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALD----LKY 183
Cdd:COG1116 108 RGVPKAERRERARELLELVGLAGFEDA-YPHqLSGGMRQRVAIARALA---------NDPEVLLMDEPFGALDaltrERL 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 743522756 184 QHQLLAMARAlagRNTAVLVVLHDLNLAARYADRLVMLEQ--GRLMAD 229
Cdd:COG1116 178 QDELLRLWQE---TGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
32-242 |
4.58e-32 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 118.22 E-value: 4.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRvGVLP--QSSSLsFPFL-CEEVVAMGRL 107
Cdd:COG0411 28 ERGEIVGLIGPNGAGKTTLFNLITGFYRpTSGRILFDGRDITGLPPHRIARL-GIARtfQNPRL-FPELtVLENVLVAAH 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 PHSE----------PASRRDEI-----VRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPqqaRLLLL 172
Cdd:COG0411 106 ARLGrgllaallrlPRARREERearerAEELLERVGLADRADEPAGNLSYGQQRRLEIARALAT------EP---KLLLL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743522756 173 DEPTSALDLKYQHQLLAMARAL-AGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT-PELIA 242
Cdd:COG0411 177 DEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRAdPRVIE 248
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
33-249 |
5.29e-32 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 120.25 E-value: 5.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQTrrgWAGNALAH--RVGVLPQSSSLsFPFL-CEEVVAMG-- 105
Cdd:COG1118 27 SGELVALLGPSGSGKTTLLRIIAG-LETpdSGRIVLNGRD---LFTNLPPRerRVGFVFQHYAL-FPHMtVAENIAFGlr 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 RLPHSEPASRRD-----EIVRAamthagvDHLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSAL 179
Cdd:COG1118 102 VRPPSKAEIRARveellELVQL-------EGLADR-YPSqLSGGQRQRVALARALAV------EP---EVLLLDEPFGAL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743522756 180 DLKYQHQLLAMARAL--AGRNTAVLVVlHDLNLAARYADRLVMLEQGRLMADGNAGEVltpeliarlYDYPA 249
Cdd:COG1118 165 DAKVRKELRRWLRRLhdELGGTTVFVT-HDQEEALELADRVVVMNQGRIEQVGTPDEV---------YDRPA 226
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
32-240 |
2.80e-31 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 115.33 E-value: 2.80e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQT-RRGWAgnalahRVGVLPQSSSLS--FPFLCEEVVAMGRL 107
Cdd:TIGR03771 4 DKGELLGLLGPNGAGKTTLLRAILGLIPPaKGTVKVAGASpGKGWR------HIGYVPQRHEFAwdFPISVAHTVMSGRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 PHSEP--ASRRDEI--VRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKY 183
Cdd:TIGR03771 78 GHIGWlrRPCVADFaaVRDALRRVGLTELADRPVGELSGGQRQRVLVARALAT------RPS---VLLLDEPFTGLDMPT 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 184 QHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLeQGRLMADGNAGEVLTPEL 240
Cdd:TIGR03771 149 QELLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLL-NGRVIADGTPQQLQDPAP 204
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
32-249 |
3.71e-31 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.28 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQT-------RRGwagnalahrVGVLPQSSSLsFPFL-CEEV 101
Cdd:COG3842 29 EPGEFVALLGPSGCGKTTLLRMIAG-FETpdSGRILLDGRDvtglppeKRN---------VGMVFQDYAL-FPHLtVAEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 102 VAMG-RLpHSEPASRRDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSAL 179
Cdd:COG3842 98 VAFGlRM-RGVPKAEIRARVAELLELVGLEGLADR-YPHqLSGGQQQRVALARALAP------EP---RVLLLDEPLSAL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743522756 180 DLK----YQHQLLAMARALagrNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGnagevlTPEliaRLYDYPA 249
Cdd:COG3842 167 DAKlreeMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQVG------TPE---EIYERPA 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
32-177 |
3.92e-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: 112.74 E-value: 3.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFL-CEEVVAMGRLPH 109
Cdd:pfam00005 9 NPGEILALVGPNGAGKSTLLKLIAGLLSPtEGTILLDGQDLTDDERKSLRKEIGYVFQDPQL-FPRLtVRENLRLGLLLK 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743522756 110 SEPASRRDEIVRAAMTHAGVDHLANRL----YPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTS 177
Cdd:pfam00005 88 GLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALL---------TKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
32-236 |
4.19e-31 |
|
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: 120.63 E-value: 4.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAMGRlphs 110
Cdd:COG4988 361 PPGERVALVGPSGAGKSTLLNLLLGFLPpYSGSILINGVDLSDLDPASWRRQIAWVPQNPYL-FAGTIRENLRLGR---- 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 ePASRRDEIVRAAMThAGVDHLANRLyP------------GLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSA 178
Cdd:COG4988 436 -PDASDEELEAALEA-AGLDEFVAAL-PdgldtplgeggrGLSGGQAQRLALARALLR---------DAPLLLLDEPTAH 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 743522756 179 LDLKYQHQLL-AMARALAGRntAVLVVLHDLNLAARyADRLVMLEQGRLMADGNAGEVL 236
Cdd:COG4988 504 LDAETEAEILqALRRLAKGR--TVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELL 559
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
33-230 |
5.47e-31 |
|
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: 114.15 E-value: 5.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQTRRGWAgnalAHR--VGVLPQSSSLsFPFL-CEEVVAMGRL 107
Cdd:cd03259 25 PGEFLALLGPSGCGKTTLLRLIAG-LERpdSGEILIDGRDVTGVP----PERrnIGMVFQDYAL-FPHLtVAENIAFGLK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 PHSEPASRRDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQ 186
Cdd:cd03259 99 LRGVPKAEIRARVRELLELVGLEGLLNR-YPHeLSGGQQQRVALARALA---------REPSLLLLDEPLSALDAKLREE 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 743522756 187 LLAMARAL--AGRNTAVLVVlHDLNLAARYADRLVMLEQGRLMADG 230
Cdd:cd03259 169 LREELKELqrELGITTIYVT-HDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
33-258 |
1.58e-30 |
|
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: 116.35 E-value: 1.58e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQTrrgWAGNALAH-------RVGVLPQSSSLsFPFLceeVV- 102
Cdd:COG4148 24 GRGVTALFGPSGSGKTTLLRAIAG-LERpdSGRIRLGGEV---LQDSARGIflpphrrRIGYVFQEARL-FPHL---SVr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 103 -----AMGRLPHSEPASRRDEIVraAMThaGVDHLANRlYPG-LSGGERQRVQFARVLAqiwQAPeepqqaRLLLLDEPT 176
Cdd:COG4148 96 gnllyGRKRAPRAERRISFDEVV--ELL--GIGHLLDR-RPAtLSGGERQRVAIGRALL---SSP------RLLLMDEPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 177 SALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT-PELIARLYDYPAQVI-- 252
Cdd:COG4148 162 AALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSrPDLLPLAGGEEAGSVle 241
|
250
....*....|.
gi 743522756 253 -----HHPESG 258
Cdd:COG4148 242 atvaaHDPDYG 252
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
32-236 |
1.83e-30 |
|
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: 113.30 E-value: 1.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHR-VGVLPQSSSLsFPFL-CEE--VVAMGR 106
Cdd:cd03224 24 PEGEIVALLGRNGAGKTTLLKTIMGLLPpRSGSIRFDGRDITGLPPHERARAgIGYVPEGRRI-FPELtVEEnlLLGAYA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 107 LPHSEPASRRDEIVR-----AAMTH--AGVdhlanrlypgLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSAL 179
Cdd:cd03224 103 RRRAKRKARLERVYElfprlKERRKqlAGT----------LSGGEQQMLAIARALMS---------RPKLLLLDEPSEGL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 180 DLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:cd03224 164 APKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
32-236 |
1.95e-30 |
|
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: 119.55 E-value: 1.95e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsfpF---LcEEVVAMGRl 107
Cdd:COG2274 499 KPGERVAIVGRSGSGKSTLLKLLLGLYEpTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFL---FsgtI-RENITLGD- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 phsePASRRDEIVRAAMThAGVDHLANRLyP------------GLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEP 175
Cdd:COG2274 574 ----PDATDEEIIEAARL-AGLHDFIEAL-PmgydtvvgeggsNLSGGQRQRLAIARALL---------RNPRILILDEA 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743522756 176 TSALDLKYQHQLL-AMARALAGRntAVLVVLHDLNLaARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:COG2274 639 TSALDAETEAIILeNLRRLLKGR--TVIIIAHRLST-IRLADRIIVLDKGRIVEDGTHEELL 697
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
32-225 |
2.30e-30 |
|
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: 111.32 E-value: 2.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsfpFlceevvamgrlphs 110
Cdd:cd03228 26 KPGEKVAIVGPSGSGKSTLLKLLLRLYDpTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFL---F-------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 ePASRRDEIvraamthagvdhlanrlypgLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLAM 190
Cdd:cd03228 89 -SGTIRENI--------------------LSGGQRQRIAIARALLR---------DPPILILDEATSALDPETEALILEA 138
|
170 180 190
....*....|....*....|....*....|....*
gi 743522756 191 ARALAGRNTaVLVVLHDLNLaARYADRLVMLEQGR 225
Cdd:cd03228 139 LRALAKGKT-VIVIAHRLST-IRDADRIIVLDDGR 171
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
32-230 |
3.76e-30 |
|
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: 112.60 E-value: 3.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGeLEHE--GEIHLFGQTRRGWAG---NALAHRVGVLPQ--SSSLSFPFLCEEVVAM 104
Cdd:cd03257 29 KKGETLGLVGESGSGKSTLARAILG-LLKPtsGSIIFDGKDLLKLSRrlrKIRRKEIQMVFQdpMSSLNPRMTIGEQIAE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 105 GRLPH--SEPASRRDEIVRAAMTHAG-VDHLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALD 180
Cdd:cd03257 108 PLRIHgkLSKKEARKEAVLLLLVGVGlPEEVLNR-YPHeLSGGQRQRVAIARALAL------NP---KLLIADEPTSALD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 743522756 181 LKYQHQLLAMARAL-AGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADG 230
Cdd:cd03257 178 VSVQAQILDLLKKLqEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
32-221 |
6.37e-30 |
|
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: 111.79 E-value: 6.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQTRRGwagnaLAHRVGVLPQSSSLsFPFL-CEEVVAMGRLP 108
Cdd:cd03293 28 EEGEFVALVGPSGCGKSTLLRIIAG-LERptSGEVLVDGEPVTG-----PGPDRGYVFQQDAL-LPWLtVLDNVALGLEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSEPASRRDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALD----LKY 183
Cdd:cd03293 101 QGVPKAEARERAEELLELVGLSGFENA-YPHqLSGGMRQRVALARALAV------DP---DVLLLDEPFSALDaltrEQL 170
|
170 180 190
....*....|....*....|....*....|....*...
gi 743522756 184 QHQLLAMARalaGRNTAVLVVLHDLNLAARYADRLVML 221
Cdd:cd03293 171 QEELLDIWR---ETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
38-243 |
1.58e-29 |
|
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: 111.27 E-value: 1.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 38 ALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGWagNALAHRVGVLPQSSSLsFPFL-CEEVVAMGRLPHSEPASR 115
Cdd:cd03299 29 VILGPTGSGKSVLLETIAGFIKPDsGKILLNGKDITNL--PPEKRDISYVPQNYAL-FPHMtVYKNIAYGLKKRKVDKKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 116 RDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALDLKYQHQLLAM-ARA 193
Cdd:cd03299 106 IERKVLEIAEMLGIDHLLNR-KPEtLSGGEQQRVAIARALVV------NP---KILLLDEPFSALDVRTKEKLREElKKI 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 743522756 194 LAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVL---TPELIAR 243
Cdd:cd03299 176 RKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFkkpKNEFVAE 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
34-230 |
5.91e-29 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 108.92 E-value: 5.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQ----TRRGWAGNALAHRVGVLPQSSSLsFPFL-CEEVVAMGrL 107
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGlEKPDGGTIVLNGTvlfdSRKKINLPPQQRKIGLVFQQYAL-FPHLnVRENLAFG-L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 PHSEPASRRDEiVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQL 187
Cdd:cd03297 101 KRKRNREDRIS-VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALA---------AQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 743522756 188 LAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADG 230
Cdd:cd03297 171 LPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
33-247 |
4.34e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.49 E-value: 4.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTgELEH--EGEIHLFGQTRRGWAGNALAHR--VGVLPQSSSLsFPFLCE-EVVAMGRL 107
Cdd:PRK09493 26 QGEVVVIIGPSGSGKSTLLRCIN-KLEEitSGDLIVDGLKVNDPKVDERLIRqeAGMVFQQFYL-FPHLTAlENVMFGPL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 pHSEPASRRD--EIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQ 184
Cdd:PRK09493 104 -RVRGASKEEaeKQARELLAKVGLAERAHH-YPSeLSGGQQQRVAIARALAV---------KPKLMLFDEPTSALDPELR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 185 HQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLYDY 247
Cdd:PRK09493 173 HEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEF 235
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
33-247 |
4.47e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.15 E-value: 4.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQTRrgwAGNALAHR-VGVLPQSSSLsFPFLC-EEVVAMGRlph 109
Cdd:COG3840 24 AGERVAILGPSGAGKSTLLNLIAGfLPPDSGRILWNGQDL---TALPPAERpVSMLFQENNL-FPHLTvAQNIGLGL--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 110 sEPASRRDEIVRAAMTHA----GVDHLANRLYPGLSGGERQRVQFARVLAQiwQAPeepqqarLLLLDEPTSALDLKYQH 185
Cdd:COG3840 97 -RPGLKLTAEQRAQVEQAlervGLAGLLDRLPGQLSGGQRQRVALARCLVR--KRP-------ILLLDEPFSALDPALRQ 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 186 QLLAMARALAG-RNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLYDY 247
Cdd:COG3840 167 EMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
32-225 |
1.59e-27 |
|
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: 104.19 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHR--VGVLPQSSSLsFPFLceevvamgrlp 108
Cdd:cd03229 24 EAGEIVALLGPSGSGKSTLLRCIAGLEEpDSGSILIDGEDLTDLEDELPPLRrrIGMVFQDFAL-FPHL----------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 hsepaSRRDeivraamthagvdhlaNRLYPgLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLL 188
Cdd:cd03229 92 -----TVLE----------------NIALG-LSGGQQQRVALARALAM---------DPDVLLLDEPTSALDPITRREVR 140
|
170 180 190
....*....|....*....|....*....|....*...
gi 743522756 189 AMARAL-AGRNTAVLVVLHDLNLAARYADRLVMLEQGR 225
Cdd:cd03229 141 ALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
34-245 |
1.76e-27 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 106.51 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQ-TRRGWAGNALAHrvgvLPQSSSL--SFPFLCEEVVAMGRLPH 109
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRlASGKISILGQpTRQALQKNLVAY----VPQSEEVdwSFPVLVEDVVMMGRYGH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 110 ----SEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQH 185
Cdd:PRK15056 109 mgwlRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ---------QGQVILLDEPFTGVDVKTEA 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 186 QLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLeQGRLMADGNAGEVLTPELIARLY 245
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTAENLELAF 238
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
32-245 |
1.87e-27 |
|
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: 105.45 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHR-VGVLPQSSSLsFPFL-CEE---VVAMG 105
Cdd:COG0410 27 EEGEIVALLGRNGAGKTTLLKAISGLLPpRSGSIRFDGEDITGLPPHRIARLgIGYVPEGRRI-FPSLtVEEnllLGAYA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 RLPHSEPASRRDEIV-----------RAAMThagvdhlanrlypgLSGGERQRVQFARVLAqiwqapeepQQARLLLLDE 174
Cdd:COG0410 106 RRDRAEVRADLERVYelfprlkerrrQRAGT--------------LSGGEQQMLAIGRALM---------SRPKLLLLDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743522756 175 PTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLY 245
Cdd:COG0410 163 PSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAY 233
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
32-246 |
2.12e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 110.25 E-value: 2.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAMGRLPHS 110
Cdd:COG1132 364 PPGETVALVGPSGSGKSTLVNLLLRFYDPtSGRILIDGVDIRDLTLESLRRQIGVVPQDTFL-FSGTIRENIRYGRPDAT 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 EpasrrDEIVRAAmTHAGVDHLANRLYPG-----------LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSAL 179
Cdd:COG1132 443 D-----EEVEEAA-KAAQAHEFIEALPDGydtvvgergvnLSGGQRQRIAIARALL---------KDPPILILDEATSAL 507
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743522756 180 DLKYQHQLL-AMARALAGRntAVLVVLHDLNlAARYADRLVMLEQGRLMADGNAGEVL-TPELIARLYD 246
Cdd:COG1132 508 DTETEALIQeALERLMKGR--TTIVIAHRLS-TIRNADRILVLDDGRIVEQGTHEELLaRGGLYARLYR 573
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
32-224 |
2.59e-27 |
|
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: 104.26 E-value: 2.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGEL-EHEGEIHLFGQTRRGWAgnaLAHRVGVLPQSSSLSFpFlcEEVVAMGRLPHS 110
Cdd:cd03226 24 YAGEIIALTGKNGAGKTTLAKILAGLIkESSGSILLNGKPIKAKE---RRKSIGYVMQDVDYQL-F--TDSVREELLLGL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 EPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLAM 190
Cdd:cd03226 98 KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS---------GKDLLIFDEPTSGLDYKNMERVGEL 168
|
170 180 190
....*....|....*....|....*....|....
gi 743522756 191 ARALAGRNTAVLVVLHDLNLAARYADRLVMLEQG 224
Cdd:cd03226 169 IRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
32-236 |
2.96e-27 |
|
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: 109.86 E-value: 2.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQ-----SSSLsfpflcEEVVAMG 105
Cdd:COG4987 359 PPGERVAIVGPSGSGKSTLLALLLRFLDpQSGSITLGGVDLRDLDEDDLRRRIAVVPQrphlfDTTL------RENLRLA 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 RlphsEPASrrDEIVRAAMTHAGVDHLANRLYPGL-----------SGGERQRVQFARVLAQiwqapeepqQARLLLLDE 174
Cdd:COG4987 433 R----PDAT--DEELWAALERVGLGDWLAALPDGLdtwlgeggrrlSGGERRRLALARALLR---------DAPILLLDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 175 PTSALDLKYQHQLLA-MARALAGRntAVLVVLHDLNLAARyADRLVMLEQGRLMADGNAGEVL 236
Cdd:COG4987 498 PTEGLDAATEQALLAdLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELL 557
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
32-242 |
4.95e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.95 E-value: 4.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQ-TRRGWAGNALAHRVGVLPQSSSLsFPFL-CEEVVAMGRLP 108
Cdd:COG1129 28 RPGEVHALLGENGAGKSTLMKILSGVYQPdSGEILLDGEpVRFRSPRDAQAAGIAIIHQELNL-VPNLsVAENIFLGREP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSEPASRRDEIVRAA---MTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQH 185
Cdd:COG1129 107 RRGGLIDWRAMRRRArelLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR---------DARVLILDEPTASLTEREVE 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 186 QLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIA 242
Cdd:COG1129 178 RLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVR 234
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
32-229 |
1.63e-26 |
|
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: 100.97 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQTRRGW-AGNALAHRVGVLPQssslsfpflceevvamgrlph 109
Cdd:cd03216 24 RRGEVHALLGENGAGKSTLMKILSGLYKPdSGEILVDGKEVSFAsPRDARRAGIAMVYQ--------------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 110 sepasrrdeivraamthagvdhlanrlypgLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLA 189
Cdd:cd03216 83 ------------------------------LSVGERQMVEIARALAR---------NARLLILDEPTAALTPAEVERLFK 123
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 743522756 190 MARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMAD 229
Cdd:cd03216 124 VIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
7-220 |
3.28e-26 |
|
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: 101.40 E-value: 3.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 7 PLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQ----TRRGWAGNA--L 79
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPpSAGEVLWNGEpirdAREDYRRRLayL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 80 AHRVGVLPQsssLSfpfLCEEVVAMGRLpHSEPASRRDeiVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwq 159
Cdd:COG4133 81 GHADGLKPE---LT---VRENLRFWAAL-YGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLL---- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743522756 160 apeepQQARLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLnLAARYADRLVM 220
Cdd:COG4133 148 -----SPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQP-LELAAARVLDL 202
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
37-236 |
4.88e-26 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 104.42 E-value: 4.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 37 TALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQT----RRGWAGNALAHRVGVLPQSSSLsFPFLCEE---VVAMGRLP 108
Cdd:TIGR02142 26 TAIFGRSGSGKTTLIRLIAGLTRpDEGEIVLNGRTlfdsRKGIFLPPEKRRIGYVFQEARL-FPHLSVRgnlRYGMKRAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSEPASRRDEIVRAAmthaGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQLL 188
Cdd:TIGR02142 105 PSERRISFERVIELL----GIGHLLGRLPGRLSGGEKQRVAIGRALL---------SSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 743522756 189 AMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:TIGR02142 172 PYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
32-237 |
5.07e-26 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 101.99 E-value: 5.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQ--TRRGWAGNALAHRVGVLPQSSSLsFPFL-----CEE-- 100
Cdd:COG1126 25 EKGEVVVIIGPSGSGKSTLLRCINL-LEEpdSGTITVDGEdlTDSKKDINKLRRKVGMVFQQFNL-FPHLtvlenVTLap 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 101 VVAMGRlphsepasRRDEIVRAAM---THAGVDHLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPT 176
Cdd:COG1126 103 IKVKKM--------SKAEAEERAMellERVGLADKADA-YPAqLSGGQQQRVAIARALAM------EP---KVMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743522756 177 SALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:COG1126 165 SALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
33-221 |
3.83e-25 |
|
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: 103.52 E-value: 3.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSsslsfPFLCEEVVAmGRLPHSE 111
Cdd:TIGR02857 347 PGERVALVGPSGAGKSTLLNLLLGFVDpTEGSIAVNGVPLADADADSWRDQIAWVPQH-----PFLFAGTIA-ENIRLAR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAAMThAGVDHLANRLYPG-----------LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALD 180
Cdd:TIGR02857 421 PDASDAEIREALER-AGLDEFVAALPQGldtpigeggagLSGGQAQRLALARAFL---------RDAPLLLLDEPTAHLD 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 743522756 181 LKYQHQLLAMARALAGRNTaVLVVLHDLNLAARyADRLVML 221
Cdd:TIGR02857 491 AETEAEVLEALRALAQGRT-VLLVTHRLALAAL-ADRIVVL 529
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
33-226 |
3.94e-25 |
|
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: 98.76 E-value: 3.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGeLE--HEGEIHLFGQ--TRRGWAGNALAHRVGVLPQSSSLsFPFLC--EEVVAMGR 106
Cdd:cd03262 25 KGEVVVIIGPSGSGKSTLLRCINL-LEepDSGTIIIDGLklTDDKKNINELRQKVGMVFQQFNL-FPHLTvlENITLAPI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 107 LPHSEPASRRDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQH 185
Cdd:cd03262 103 KVKGMSKAEAEERALELLEKVGLADKADA-YPAqLSGGQQQRVAIARALA---------MNPKVMLFDEPTSALDPELVG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 743522756 186 QLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRL 226
Cdd:cd03262 173 EVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
32-234 |
4.23e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 98.97 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAH---RVGVLPQssslSFPFL----CEEVVA 103
Cdd:COG2884 26 EKGEFVFLTGPSGAGKSTLLKLLYGEERpTSGQVLVNGQDLSRLKRREIPYlrrRIGVVFQ----DFRLLpdrtVYENVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 104 -----MGRlPHSEPASRrdeiVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSA 178
Cdd:COG2884 102 lplrvTGK-SRKEIRRR----VREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN------RPE---LLLADEPTGN 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743522756 179 LDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGE 234
Cdd:COG2884 168 LDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
33-230 |
4.73e-25 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 98.72 E-value: 4.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQTrrgWAGNALAHR-VGVLPQSSSLsFPFL-CEEVVAMGRLPH 109
Cdd:cd03298 23 QGEITAIVGPSGSGKSTLLNLIAGfETPQSGRVLINGVD---VTAAPPADRpVSMLFQENNL-FAHLtVEQNVGLGLSPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 110 SEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapEEPqqarLLLLDEPTSALDLKYQHQLLA 189
Cdd:cd03298 99 LKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVR-----DKP----VLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 743522756 190 MARAL-AGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADG 230
Cdd:cd03298 170 LVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
34-237 |
7.97e-25 |
|
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: 98.91 E-value: 7.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLC--EEVVAMGRLPHs 110
Cdd:cd03295 27 GEFLVLIGPSGSGKTTTMKMINRLIEPtSGEIFIDGEDIREQDPVELRRKIGYVIQQIGL-FPHMTveENIALVPKLLK- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 EPASRRDEIVRAAMTHAGVD--HLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALD----LKY 183
Cdd:cd03295 105 WPKEKIRERADELLALVGLDpaEFADR-YPHeLSGGQQQRVGVARALAA------DPP---LLLMDEPFGALDpitrDQL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 743522756 184 QHQLLAMARALagRNTAVLVVlHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:cd03295 175 QEEFKRLQQEL--GKTIVFVT-HDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
32-230 |
1.09e-24 |
|
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: 97.96 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFG---QTRRgwagNALAHRVGVLPQSSSLsFPFL-CEE-VVAMG 105
Cdd:cd03263 26 YKGEIFGLLGHNGAGKTTTLKMLTGELRpTSGTAYINGysiRTDR----KAARQSLGYCPQFDAL-FDELtVREhLRFYA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 RLpHSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQH 185
Cdd:cd03263 101 RL-KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG------GPS---VLLLDEPTSGLDPASRR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 743522756 186 QLLAMARALaGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADG 230
Cdd:cd03263 171 AIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
32-237 |
2.07e-24 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 98.19 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKC------LTGELEHEGEIHLFGQ--TRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVA 103
Cdd:COG1117 35 PENKVTALIGPSGCGKSTLLRClnrmndLIPGARVEGEILLDGEdiYDPDVDVVELRRRVGMVFQKPNP-FPKSIYDNVA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 104 MG-RLPHSEPASRRDEIVRAAMTHAGV-DHLANRLY-PG--LSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSA 178
Cdd:COG1117 114 YGlRLHGIKSKSELDEIVEESLRKAALwDEVKDRLKkSAlgLSGGQQQRLCIARALAV------EPE---VLLMDEPTSA 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 179 LD----LKYQhQLLamaRALAGRNTaVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:COG1117 185 LDpistAKIE-ELI---LELKKDYT-IVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFT 242
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
32-230 |
6.44e-24 |
|
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: 95.73 E-value: 6.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLSFPFLcEEVVAMGRLPHS 110
Cdd:cd03245 28 RAGEKVAIIGRVGSGKSTLLKLLAGLYKpTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTL-RDNITLGAPLAD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 EpasrrDEIVRAAMThAGVDHLANRlYP------------GLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSA 178
Cdd:cd03245 107 D-----ERILRAAEL-AGVTDFVNK-HPngldlqigergrGLSGGQRQAVALARALLN---------DPPILLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 743522756 179 LDLKYQHQLLAMARALAGRNTaVLVVLHDLNLAArYADRLVMLEQGRLMADG 230
Cdd:cd03245 171 MDMNSEERLKERLRQLLGDKT-LIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
33-234 |
8.51e-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: 97.46 E-value: 8.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFG--------QTRRgwagnalahRVGVLPQSSSLSFPFLCEE-VV 102
Cdd:TIGR01188 18 EGEVFGFLGPNGAGKTTTIRMLTTLLRpTSGTARVAGydvvreprKVRR---------SIGIVPQYASVDEDLTGREnLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 103 AMGRL---PHSEPASRRDEIV-RAAMTHAgvdhlANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSA 178
Cdd:TIGR01188 89 MMGRLyglPKDEAEERAEELLeLFELGEA-----ADRPVGTYSGGMRRRLDIAASLI---------HQPDVLFLDEPTTG 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743522756 179 LDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGE 234
Cdd:TIGR01188 155 LDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
32-206 |
1.06e-23 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 95.42 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH----EGEIHLFGQTRRgwagnalAH----RVGVLPQSSSLSFPFLCEEVV- 102
Cdd:cd03234 31 ESGQVMAILGSSGSGKTTLLDAISGRVEGggttSGQILFNGQPRK-------PDqfqkCVAYVRQDDILLPGLTVRETLt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 103 --AMGRLPHSEPASRRDEIVR-AAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSAL 179
Cdd:cd03234 104 ytAILRLPRKSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLW------DP---KVLILDEPTSGL 174
|
170 180
....*....|....*....|....*..
gi 743522756 180 DLKYQHQLLAMARALAGRNTAVLVVLH 206
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
34-249 |
1.29e-23 |
|
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: 95.48 E-value: 1.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGeLEHEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFL-CEEVVAMG-RLPHSE 111
Cdd:cd03296 28 GELVALLGPSGSGKTTLLRLIAG-LERPDSGTILFGGEDATDVPVQERNVGFVFQHYAL-FRHMtVFDNVAFGlRVKPRS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEI---VRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALDLKYQHQLL 188
Cdd:cd03296 106 ERPPEAEIrakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV------EP---KVLLLDEPFGALDAKVRKELR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743522756 189 AMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVltpeliarlYDYPA 249
Cdd:cd03296 177 RWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV---------YDHPA 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
33-236 |
1.31e-23 |
|
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: 95.37 E-value: 1.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAMGRlphse 111
Cdd:cd03254 28 PGETVAIVGPTGAGKTTLINLLMRFYDPQkGQILIDGIDIRDISRKSLRSMIGVVLQDTFL-FSGTIMENIRLGR----- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAAMThAGVDHLANRLYPG-----------LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALD 180
Cdd:cd03254 102 PNATDEEVIEAAKE-AGAHDFIMKLPNGydtvlgenggnLSQGERQLLAIARAML---------RDPKILILDEATSNID 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 181 LKYQhQLL--AMARALAGRNTavLVVLHDLNlAARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:cd03254 172 TETE-KLIqeALEKLMKGRTS--IIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
32-244 |
2.25e-23 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 2.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQTRRGW-AGNALAHRVGVLPQSSSLSFPFLCEEVVAMGRLP 108
Cdd:COG3845 29 RPGEIHALLGENGAGKSTLMKILYG-LYQpdSGEILIDGKPVRIRsPRDAIALGIGMVHQHFMLVPNLTVAENIVLGLEP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSEPASRRDEI---VRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQH 185
Cdd:COG3845 108 TKGGRLDRKAArarIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALY---------RGARILILDEPTAVLTPQEAD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 743522756 186 QLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVlTPELIARL 244
Cdd:COG3845 179 ELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET-SEEELAEL 236
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
33-236 |
6.95e-23 |
|
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: 97.13 E-value: 6.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAmgRLPHSE 111
Cdd:COG4618 357 PGEVLGVIGPSGSGKSTLARLLVGVWPpTAGSVRLDGADLSQWDREELGRHIGYLPQDVEL-FDGTIAENIA--RFGDAD 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PasrrDEIVRAAMThAGVDHLANRLyP------------GLSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSAL 179
Cdd:COG4618 434 P----EKVVAAAKL-AGVHEMILRL-PdgydtrigeggaRLSGGQRQRIGLARALYG------DP---RLVVLDEPNSNL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 180 DLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARyADRLVMLEQGRLMADGNAGEVL 236
Cdd:COG4618 499 DDEGEAALAAAIRALKARGATVVVITHRPSLLAA-VDKLLVLRDGRVQAFGPRDEVL 554
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
32-230 |
1.41e-22 |
|
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: 91.96 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTrrgwAGNALAHRVGVLPQSSSLsFPFL--CEEVVAMGRL- 107
Cdd:cd03269 24 EKGEIFGLLGPNGAGKTTTIRMILGIILpDSGEVLFDGKP----LDIAARNRIGYLPEERGL-YPKMkvIDQLVYLAQLk 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 --PHSEPASRRDEIVRaamtHAGVDHLANRLYPGLSGGERQRVQFArvlAQIWQAPEepqqarLLLLDEPTSALDLKYQH 185
Cdd:cd03269 99 glKKEEARRRIDEWLE----RLELSEYANKRVEELSKGNQQKVQFI---AAVIHDPE------LLILDEPFSGLDPVNVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 743522756 186 QLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADG 230
Cdd:cd03269 166 LLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
34-258 |
2.60e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 92.88 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQTRRGWAGNALAHRVGVLPQS-SSLSFPFLCEEVVAMGRLPHSE 111
Cdd:PRK13647 31 GSKTALLGPNGAGKSTLLLHLNGiYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDpDDQVFSSTVWDDVAFGPVNMGL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQHQLLAMA 191
Cdd:PRK13647 111 DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAM------DPD---VIVLDEPMAYLDPRGQETLMEIL 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743522756 192 RALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGnAGEVLTPELIARLYD--YP--AQVIHH-PESG 258
Cdd:PRK13647 182 DRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDEDIVEQAGlrLPlvAQIFEDlPELG 252
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
33-234 |
3.70e-22 |
|
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: 91.28 E-value: 3.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAhRVGVLPQSSSLSfPFLC--EEVVAMGRLpH 109
Cdd:cd03265 25 RGEIFGLLGPNGAGKTTTIKMLTTLLKpTSGRATVAGHDVVREPREVRR-RIGIVFQDLSVD-DELTgwENLYIHARL-Y 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 110 SEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALDLKYQHQLLA 189
Cdd:cd03265 102 GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVH------RP---EVLFLDEPTIGLDPQTRAHVWE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 743522756 190 MARAL-AGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGE 234
Cdd:cd03265 173 YIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
32-232 |
1.13e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.84 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCL----TGELEHEGEIHLFGQT--RRGWAGNAL----AHRVGVLPQSSSLSFPFLCEEV 101
Cdd:PRK09984 28 HHGEMVALLGPSGSGKSTLLRHLsgliTGDKSAGSHIELLGRTvqREGRLARDIrksrANTGYIFQQFNLVNRLSVLENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 102 V--AMGRLPHSEPASR---RDEIVRA--AMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDE 174
Cdd:PRK09984 108 LigALGSTPFWRTCFSwftREQKQRAlqALTRVGMVHFAHQRVSTLSGGQQQRVAIARALM---------QQAKVILADE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 743522756 175 PTSALDLKYQHQLLAMARALAGRN-TAVLVVLHDLNLAARYADRLVMLEQGRLMADGNA 232
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNDgITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
9-245 |
1.27e-21 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 89.91 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 9 LSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQT-------RRGWAGnala 80
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGlVKPDSGKILLDGQDitklpmhKRARLG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 81 hrVGVLPQSSSLsFPFLC--EEVVAMGRLpHSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiw 158
Cdd:cd03218 77 --IGYLPQEASI-FRKLTveENILAVLEI-RGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALA--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 159 qapeepQQARLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTP 238
Cdd:cd03218 150 ------TNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAAN 223
|
....*..
gi 743522756 239 ELIARLY 245
Cdd:cd03218 224 ELVRKVY 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
34-249 |
1.32e-21 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 92.06 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQT-------RRGwagnalahrVGVLPQSSSLsFPFL-CEEVVA 103
Cdd:COG3839 29 GEFLVLLGPSGCGKSTLLRMIAG-LEDptSGEILIGGRDvtdlppkDRN---------IAMVFQSYAL-YPHMtVYENIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 104 MG-RLpHSEPASRRDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDL 181
Cdd:COG3839 98 FPlKL-RKVPKAEIDRRVREAAELLGLEDLLDR-KPKqLSGGQRQRVALGRALV---------REPKVFLLDEPLSNLDA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743522756 182 KYQHQLLA-MARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGnagevlTPEliaRLYDYPA 249
Cdd:COG3839 167 KLRVEMRAeIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVG------TPE---ELYDRPA 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-235 |
2.23e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 90.55 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQTRrgwaGNALAHRVGVLPqssslsfpflcEE---------- 100
Cdd:COG4152 25 PKGEIFGLLGPNGAGKTTTIRIILGILAPdSGEVLWDGEPL----DPEDRRRIGYLP-----------EErglypkmkvg 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 101 --VVAMGRLpHSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSA 178
Cdd:COG4152 90 eqLVYLARL-KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH------DPE---LLILDEPFSG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 179 LD------LKyqhQLLamaRALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEV 235
Cdd:COG4152 160 LDpvnvelLK---DVI---RELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
33-232 |
2.72e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.30 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCL-------TGELEHEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPF------LCE 99
Cdd:PRK11124 27 QGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIAGNHFDFSKTPSDKAIRELRRNVGMVFQQYNL-WPHltvqqnLIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 100 EVVAMGRLPHSEPASRRDEIvraaMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSAL 179
Cdd:PRK11124 106 APCRVLGLSKDQALARAEKL----LERLRLKPYADRFPLHLSGGQQQRVAIARALMM------EPQ---VLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 743522756 180 DLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNA 232
Cdd:PRK11124 173 DPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
33-236 |
2.72e-21 |
|
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: 89.21 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAMGRLPHSE 111
Cdd:cd03253 26 AGKKVAIVGPSGSGKSTILRLLFRFYDvSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVL-FNDTIGYNIRYGRPDATD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 pasrrDEIVRAAMThAGVDHLANRLYPG-----------LSGGERQRVQFARVlaqIWQAPeepqqaRLLLLDEPTSALD 180
Cdd:cd03253 105 -----EEVIEAAKA-AQIHDKIMRFPDGydtivgerglkLSGGEKQRVAIARA---ILKNP------PILLLDEATSALD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 181 LKYQHQLL-AMARALAGRNTavLVVLHDLNLAARyADRLVMLEQGRLMADGNAGEVL 236
Cdd:cd03253 170 THTEREIQaALRDVSKGRTT--IVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
32-244 |
3.16e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.07 E-value: 3.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQT---------RRgwagnalahRVGVLPQSSSLSF-PFLCEE 100
Cdd:PRK13635 31 YEGEWVAIVGHNGSGKSTLAKLLNGLLLPEaGTITVGGMVlseetvwdvRR---------QVGMVFQNPDNQFvGATVQD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 101 VVAMGRLPHSEPasrRDEIVR---AAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwQAPEepqqarLLLLDEPTS 177
Cdd:PRK13635 102 DVAFGLENIGVP---REEMVErvdQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA---LQPD------IIILDEATS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 178 ALDLKYQHQLLAMARAL-AGRNTAVLVVLHDLNLAARyADRLVMLEQGRLMADGnagevlTPELIARL 244
Cdd:PRK13635 170 MLDPRGRREVLETVRQLkEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG------TPEEIFKS 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
32-242 |
3.91e-21 |
|
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: 92.05 E-value: 3.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEHEGEIHLFGQ---TRRGWAGNALAHRVGVLPQS--SSLSFPFLCEEVVAMGR 106
Cdd:COG4172 310 RRGETLGLVGESGSGKSTLGLALLRLIPSEGEIRFDGQdldGLSRRALRPLRRRMQVVFQDpfGSLSPRMTVGQIIAEGL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 107 LPHSEPASR--RDEIVRAAMTHAGVDH-LANRlYPG-LSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALDLK 182
Cdd:COG4172 390 RVHGPGLSAaeRRARVAEALEEVGLDPaARHR-YPHeFSGGQRQRIAIARALIL------EP---KLLVLDEPTSALDVS 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 183 YQHQLLAMARAL-AGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVL-------TPELIA 242
Cdd:COG4172 460 VQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFdapqhpyTRALLA 527
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
33-237 |
4.20e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.04 E-value: 4.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLT------------GELEHEGEIHLFGQTRRGwagNALAHRVGVLPQSSSLsFPF--LC 98
Cdd:PRK11264 28 PGEVVAIIGPSGSGKTTLLRCINlleqpeagtirvGDITIDTARSLSQQKGLI---RQLRQHVGFVFQNFNL-FPHrtVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 99 EEVVAMGRLPHSEPASRRDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTS 177
Cdd:PRK11264 104 ENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETS-YPRrLSGGQQQRVAIARALAM------RPE---VILFDEPTS 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 178 ALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:PRK11264 174 ALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFA 233
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
34-243 |
4.45e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 89.52 E-value: 4.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQ----TRRGWAgnALAHRVGVLPQSSSLS-FPFLCEEVVAMGRL 107
Cdd:PRK13636 32 GEVTAILGGNGAGKSTLFQNLNGILKpSSGRILFDGKpidySRKGLM--KLRESVGMVFQDPDNQlFSASVYQDVSFGAV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 PHSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQHQL 187
Cdd:PRK13636 110 NLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVM------EPK---VLVLDEPTAGLDPMGVSEI 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 188 LAMARALA-GRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIAR 243
Cdd:PRK13636 181 MKLLVEMQkELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-229 |
5.29e-21 |
|
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: 88.26 E-value: 5.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 1 MPGSPSPLLSCRGLRLSRGNRlildsldldlhAGSLT---------------ALLGPNGAGKSSLLKCLTGeLEH--EGE 63
Cdd:COG4181 1 MSSSSAPIIELRGLTKTVGTG-----------AGELTilkgisleveagesvAIVGASGSGKSTLLGLLAG-LDRptSGT 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 64 IHLFGQTRRGWAGNALA----HRVGVLPQSSSLsFPFL-CEEVVAmgrLPhSEPASRRD--EIVRAAMTHAGVDHLANRl 136
Cdd:COG4181 69 VRLAGQDLFALDEDARArlraRHVGFVFQSFQL-LPTLtALENVM---LP-LELAGRRDarARARALLERVGLGHRLDH- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 137 YPG-LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQLLAMARAL-AGRNTAVLVVLHDLNLAARy 214
Cdd:COG4181 143 YPAqLSGGEQQRVALARAFA---------TEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAAR- 212
|
250
....*....|....*
gi 743522756 215 ADRLVMLEQGRLMAD 229
Cdd:COG4181 213 CDRVLRLRAGRLVED 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
33-226 |
5.75e-21 |
|
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: 86.89 E-value: 5.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsfpFlceevvamgrlphse 111
Cdd:cd03246 27 PGESLAIIGPSGSGKSTLARLILGLLRpTSGRVRLDGADISQWDPNELGDHVGYLPQDDEL---F--------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIvraamthagvdhlanrlypgLSGGERQRVQFARVLaqiWQAPeepqqaRLLLLDEPTSALDLKYQHQLLAMA 191
Cdd:cd03246 89 SGSIAENI--------------------LSGGQRQRLGLARAL---YGNP------RILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....*
gi 743522756 192 RALAGRNTAVLVVLHDLNLAARyADRLVMLEQGRL 226
Cdd:cd03246 140 AALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
33-236 |
6.65e-21 |
|
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: 88.02 E-value: 6.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQ---TRRGWAGNALAHRVGVLPQ-----SSSLSFpflceEVVA 103
Cdd:cd03258 30 KGEIFGIIGRSGAGKSTLIRCINGlERPTSGSVLVDGTdltLLSGKELRKARRRIGMIFQhfnllSSRTVF-----ENVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 104 mgrLP---HSEPASRRDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSAL 179
Cdd:cd03258 105 ---LPleiAGVPKAEIEERVLELLELVGLEDKADA-YPAqLSGGQKQRVGIARALAN------NP---KVLLCDEATSAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 180 DLKYQHQLLAMARAL-AGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:cd03258 172 DPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
33-230 |
6.92e-21 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 86.60 E-value: 6.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIhLFGQTRRGWAGNALAHRVGVLPQSsslsfpflceevvamgrlPHSE 111
Cdd:cd03247 27 QGEKIALLGRSGSGKSTLLQLLTGDLKpQQGEI-TLDGVPVSDLEKALSSLISVLNQR------------------PYLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAamthagvdhlanrlypgLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQLLA-M 190
Cdd:cd03247 88 DTTLRNNLGRR-----------------FSGGERQRLALARILL---------QDAPIVLLDEPTVGLDPITERQLLSlI 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 743522756 191 ARALagRNTAVLVVLHDLnLAARYADRLVMLEQGRLMADG 230
Cdd:cd03247 142 FEVL--KDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
33-232 |
7.16e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 88.15 E-value: 7.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCL-------TGELEHEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPF------LCE 99
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIAGHQFDFSQKPSEKAIRLLRQKVGMVFQQYNL-WPHltvmenLIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 100 EVVAMGRLPHSEPASRRDEIvraaMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSAL 179
Cdd:COG4161 106 APCKVLGLSKEQAREKAMKL----LARLRLTDKADRFPLHLSGGQQQRVAIARALMM------EPQ---VLLFDEPTAAL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 743522756 180 DLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNA 232
Cdd:COG4161 173 DPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
33-249 |
1.27e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 89.37 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQTRRGWagNALAHRVGVLPQSSSLSFPFLCEEVVAMG--RLP 108
Cdd:PRK10851 27 SGQMVALLGPSGSGKTTLLRIIAG-LEHqtSGHIRFHGTDVSRL--HARDRKVGFVFQHYALFRHMTVFDNIAFGltVLP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSEPASRrdEIVRAAMTH----AGVDHLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKY 183
Cdd:PRK10851 104 RRERPNA--AAIKAKVTQllemVQLAHLADR-YPAqLSGGQKQRVALARALAV------EPQ---ILLLDEPFGALDAQV 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 184 QHQLLAMARALAG--RNTAVLVVlHDLNLAARYADRLVmleqgrLMADGNAGEVLTPELIARlydYPA 249
Cdd:PRK10851 172 RKELRRWLRQLHEelKFTSVFVT-HDQEEAMEVADRVV------VMSQGNIEQAGTPDQVWR---EPA 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
33-236 |
2.77e-20 |
|
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: 86.52 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAMGRlphse 111
Cdd:cd03251 27 AGETVALVGPSGSGKSTLVNLIPRFYDvDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFL-FNDTVAENIAYGR----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAAMThAGVDHLANRLYPG-----------LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALD 180
Cdd:cd03251 101 PGATREEVEEAARA-ANAHEFIMELPEGydtvigergvkLSGGQRQRIAIARALL---------KDPPILILDEATSALD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 181 LKYQHQLL-AMARALAGRNTavLVVLHDLNlAARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:cd03251 171 TESERLVQaALERLMKNRTT--FVIAHRLS-TIENADRIVVLEDGKIVERGTHEELL 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
32-225 |
2.97e-20 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 86.33 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGE-LEHEGEI---HLFGQT-------------RRgwagnalaHRVG-------VLP 87
Cdd:COG4778 35 AAGECVALTGPSGAGKSTLLKCIYGNyLPDSGSIlvrHDGGWVdlaqaspreilalRR--------RTIGyvsqflrVIP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 88 QSSSLsfpflceEVVAMGRLPHSEPASRRDEIVRAAMTHAGVD-HLAnRLYPG-LSGGERQRVQFARVLAQiwqapeepq 165
Cdd:COG4778 107 RVSAL-------DVVAEPLLERGVDREEARARARELLARLNLPeRLW-DLPPAtFSGGEQQRVNIARGFIA--------- 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 166 QARLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGR 225
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
32-226 |
3.09e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLfgqtRRGWagnalahRVGVLPQSSSLSFPFLCEEVVAMGRLPHS 110
Cdd:COG0488 22 NPGDRIGLVGRNGAGKSTLLKILAGELEPdSGEVSI----PKGL-------RIGYLPQEPPLDDDLTVLDTVLDGDAELR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 EPASRRDEI--------------------------------VRAAMTHAGV-DHLANRLYPGLSGGERQRVQFARVLAqi 157
Cdd:COG0488 91 ALEAELEELeaklaepdedlerlaelqeefealggweaearAEEILSGLGFpEEDLDRPVSELSGGWRRRVALARALL-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 158 wqapeepQQARLLLLDEPTSALDL-------KYqhqllamaraLAGRNTAVLVVLHDlnlaaRY-----ADRLVMLEQGR 225
Cdd:COG0488 169 -------SEPDLLLLDEPTNHLDLesiewleEF----------LKNYPGTVLVVSHD-----RYfldrvATRILELDRGK 226
|
.
gi 743522756 226 L 226
Cdd:COG0488 227 L 227
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
34-241 |
3.15e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 87.06 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHR--VGVLPQSSSLS-FPFLCEEVVAMG---- 105
Cdd:PRK13639 28 GEMVALLGPNGAGKSTLFLHFNGILKpTSGEVLIKGEPIKYDKKSLLEVRktVGIVFQNPDDQlFAPTVEEDVAFGplnl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 RLPHSEPASRrdeiVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqAPEepqqarLLLLDEPTSALDLKYQH 185
Cdd:PRK13639 108 GLSKEEVEKR----VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM---KPE------IIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 186 QLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT-PELI 241
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSdIETI 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
33-230 |
4.17e-20 |
|
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: 86.23 E-value: 4.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQ---TRRgwagNALAHRVG-VLPQSSSL--------SFPFLce 99
Cdd:cd03267 46 KGEIVGFIGPNGAGKTTTLKILSGLLQpTSGEVRVAGLvpwKRR----KKFLRRIGvVFGQKTQLwwdlpvidSFYLL-- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 100 evVAMGRLPHSEPASRRDEIVRAamthAGVDHLANRLYPGLSGGERQRVQFARVLaqIWqapeEPQqarLLLLDEPTSAL 179
Cdd:cd03267 120 --AAIYDLPPARFKKRLDELSEL----LDLEELLDTPVRQLSLGQRMRAEIAAAL--LH----EPE---ILFLDEPTIGL 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 743522756 180 DLKYQHQLLAMARAL-AGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADG 230
Cdd:cd03267 185 DVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
9-245 |
4.98e-20 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 85.79 E-value: 4.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 9 LSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGWAGNALAHR-VGVL 86
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDaGKILIDGQDITHLPMHERARLgIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 87 PQSSSLsFPFLCEEVVAMGRLPHSE--PASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEP 164
Cdd:TIGR04406 82 PQEASI-FRKLTVEENIMAVLEIRKdlDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALAT------NP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 165 qqaRLLLLDE------PTSALDLKYQhqllamARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTP 238
Cdd:TIGR04406 155 ---KFILLDEpfagvdPIAVGDIKKI------IKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVAN 225
|
....*..
gi 743522756 239 ELIARLY 245
Cdd:TIGR04406 226 EKVRRVY 232
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
34-230 |
6.52e-20 |
|
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: 84.96 E-value: 6.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQtrrGWAGNALA-HRVGVLPQSSSLsFPFLC--EEVVAMGRLP 108
Cdd:cd03268 26 GEIYGFLGPNGAGKTTTMKIILG-LIKpdSGEITFDGK---SYQKNIEAlRRIGALIEAPGF-YPNLTarENLRLLARLL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 hsepaSRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQHQLL 188
Cdd:cd03268 101 -----GIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLG------NPD---LLILDEPTNGLDPDGIKELR 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 743522756 189 AMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADG 230
Cdd:cd03268 167 ELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
33-237 |
7.61e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 85.40 E-value: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRgwaGNALAHR-VGVLPQSSSLsFPFL-CEEVVAMG---- 105
Cdd:PRK10771 24 RGERVAILGPSGAGKSTLLNLIAGFLTpASGSLTLNGQDHT---TTPPSRRpVSMLFQENNL-FSHLtVAQNIGLGlnpg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 -RLPHSEPASRRDeIVRaamtHAGVDHLANRLYPGLSGGERQRVQFARVLaqIWQAPeepqqarLLLLDEPTSALDLKYQ 184
Cdd:PRK10771 100 lKLNAAQREKLHA-IAR----QMGIEDLLARLPGQLSGGQRQRVALARCL--VREQP-------ILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 743522756 185 HQLLAMARAL-AGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:PRK10771 166 QEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-240 |
9.37e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 86.40 E-value: 9.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 5 PSPLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQTRRGWAGNALAhRV 83
Cdd:PRK13537 4 SVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGlTHPDAGSISLCGEPVPSRARHARQ-RV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 84 GVLPQSSSLSFPF-LCEEVVAMGRLpHSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqape 162
Cdd:PRK13537 83 GVVPQFDNLDPDFtVRENLLVFGRY-FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVN------ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 163 EPQqarLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPEL 240
Cdd:PRK13537 156 DPD---VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEI 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
33-226 |
1.14e-19 |
|
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: 84.38 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQTRRGWAGNALAH---RVGVLPQSSSL----------SFPFLC 98
Cdd:cd03292 26 AGEFVFLVGPSGAGKSTLLKLIYKeELPTSGTIRVNGQDVSDLRGRAIPYlrrKIGVVFQDFRLlpdrnvyenvAFALEV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 99 EEVvamgrlPHSEPASRrdeiVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSA 178
Cdd:cd03292 106 TGV------PPREIRKR----VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIV---------NSPTILIADEPTGN 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 743522756 179 LDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRL 226
Cdd:cd03292 167 LDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-249 |
1.37e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.81 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 6 SPLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQTrrgwagnaLAH--- 81
Cdd:PRK11607 17 TPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGfEQPTAGQIMLDGVD--------LSHvpp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 82 ---RVGVLPQSSSLsFPFL-CEEVVAMG----RLPHSEPASRRDEIVraAMTHagVDHLANRLYPGLSGGERQRVQFARV 153
Cdd:PRK11607 89 yqrPINMMFQSYAL-FPHMtVEQNIAFGlkqdKLPKAEIASRVNEML--GLVH--MQEFAKRKPHQLSGGQRQRVALARS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 154 LAqiwqapeepQQARLLLLDEPTSALDLKYQHQL-LAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNa 232
Cdd:PRK11607 164 LA---------KRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE- 233
|
250
....*....|....*..
gi 743522756 233 gevltPELIarlYDYPA 249
Cdd:PRK11607 234 -----PEEI---YEHPT 242
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
32-249 |
1.76e-19 |
|
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: 84.21 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQTrrgwAGNALAHR--VGVLPQSSSLsFPFL-CEEVVAMG-- 105
Cdd:cd03300 24 KEGEFFTLLGPSGCGKTTLLRLIAGfETPTSGEILLDGKD----ITNLPPHKrpVNTVFQNYAL-FPHLtVFENIAFGlr 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 --RLPHSEPASRrdeiVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALDLKY 183
Cdd:cd03300 99 lkKLPKAEIKER----VAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVN------EP---KVLLLDEPLGALDLKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 184 QHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGnagevlTPELIarlYDYPA 249
Cdd:cd03300 166 RKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG------TPEEI---YEEPA 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
35-261 |
2.36e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 84.67 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 35 SLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQ----TRRGWAgnALAHRVGVLPQS-----------SSLSFpflc 98
Cdd:PRK13638 28 PVTGLVGANGCGKSTLFMNLSGLLRpQKGAVLWQGKpldySKRGLL--ALRQQVATVFQDpeqqifytdidSDIAF---- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 99 eEVVAMGrLPHSEPASRRDEivraAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSA 178
Cdd:PRK13638 102 -SLRNLG-VPEAEITRRVDE----ALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVL---------QARYLLLDEPTAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 179 LDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT-PELIARL-YDYPAQVIHHPE 256
Cdd:PRK13638 167 LDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAcTEAMEQAgLTQPWLVKLHTQ 246
|
....*
gi 743522756 257 SGVPM 261
Cdd:PRK13638 247 LGLPL 251
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-230 |
2.68e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 85.65 E-value: 2.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 2 PGSPSPL-LSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNAL 79
Cdd:PRK13536 34 PGSMSTVaIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSpDAGKITVLGVPVPARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 80 AhRVGVLPQSSSLSFPFLCEE-VVAMGRLpHSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiw 158
Cdd:PRK13536 114 A-RIGVVPQFDNLDLEFTVREnLLVFGRY-FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN-- 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743522756 159 qapeEPQqarLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADG 230
Cdd:PRK13536 190 ----DPQ---LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
6-239 |
8.17e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 82.90 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 6 SPLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLT--GELEHE----GEIHLFGQTRRGWAGNAL 79
Cdd:PRK14239 3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtitGSIVYNGHNIYSPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 80 AHR--VGVLPQSSSlSFPFLCEEVVAMG-RLPHSEPASRRDEIVRAAMTHAGV-DHLANRLYP---GLSGGERQRVQFAR 152
Cdd:PRK14239 83 DLRkeIGMVFQQPN-PFPMSIYENVVYGlRLKGIKDKQVLDEAVEKSLKGASIwDEVKDRLHDsalGLSGGQQQRVCIAR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 153 VLAQiwqapeEPqqaRLLLLDEPTSALDLKYQHQLLAMARALAGRNTaVLVVLHDLNLAARYADRLVMLEQGRLMADGNA 232
Cdd:PRK14239 162 VLAT------SP---KIILLDEPTSALDPISAGKIEETLLGLKDDYT-MLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231
|
....*...
gi 743522756 233 GEV-LTPE 239
Cdd:PRK14239 232 KQMfMNPK 239
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
34-226 |
1.09e-18 |
|
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: 81.44 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELEHE---GEIHLFGQTRRGwagNALAHRVGVLPQSSSLsFPFLceevvamgrlphs 110
Cdd:cd03213 35 GELTAIMGPSGAGKSTLLNALAGRRTGLgvsGEVLINGRPLDK---RSFRKIIGYVPQDDIL-HPTL------------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 epasrrdeIVRAAMTHAGvdHLAnrlypGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLAM 190
Cdd:cd03213 98 --------TVRETLMFAA--KLR-----GLSGGERKRVSIALELVS---------NPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 743522756 191 ARALAGRNTAVLVVLHDL-NLAARYADRLVMLEQGRL 226
Cdd:cd03213 154 LRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
36-230 |
1.10e-18 |
|
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: 81.47 E-value: 1.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 36 LTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGwAGNALAHRVGVLPQSSSLSFPFLCEEVVA-MGRLpHSEPA 113
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPpSSGTIRIDGQDVLK-QPQKLRRRIGYLPQEFGVYPNFTVREFLDyIAWL-KGIPS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 114 SRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQHQLLAMARA 193
Cdd:cd03264 105 KEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG------DPS---ILIVDEPTAGLDPEERIRFRNLLSE 175
|
170 180 190
....*....|....*....|....*....|....*..
gi 743522756 194 LaGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADG 230
Cdd:cd03264 176 L-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
33-235 |
1.40e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 83.77 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQT-------------RRgwagnalahRVGVLPQSSSLsFPFL 97
Cdd:PRK11144 23 AQGITAIFGRSGAGKTSLINAISG-LTRpqKGRIVLNGRVlfdaekgiclppeKR---------RIGYVFQDARL-FPHY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 98 CeevvAMGRLPHSEPASRR---DEIVRAAmthaGVDHLANRlYPG-LSGGERQRVQFARVLAqiwQAPEepqqarLLLLD 173
Cdd:PRK11144 92 K----VRGNLRYGMAKSMVaqfDKIVALL----GIEPLLDR-YPGsLSGGEKQRVAIGRALL---TAPE------LLLMD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 174 EPTSALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEV 235
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEV 216
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
33-246 |
2.10e-18 |
|
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: 81.38 E-value: 2.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAMGRlphse 111
Cdd:cd03252 27 PGEVVGIVGRSGSGKSTLTKLIQRFYVPEnGRVLVDGHDLALADPAWLRRQVGVVLQENVL-FNRSIRDNIALAD----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAAM---THA-------GVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDL 181
Cdd:cd03252 101 PGMSMERVIEAAKlagAHDfiselpeGYDTIVGEQGAGLSGGQRQRIAIARALIH---------NPRILIFDEATSALDY 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 182 KYQHQLLA-MARALAGRntAVLVVLHDLNlAARYADRLVMLEQGRLMADGNAGEVLTPE-LIARLYD 246
Cdd:cd03252 172 ESEHAIMRnMHDICAGR--TVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAENgLYAYLYQ 235
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-241 |
2.44e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.81 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGE-LEHEGEIHLFGQTRR-GWAGNALAHRVGVLPQSSSLSFPFLCEEVVAMGRLPH 109
Cdd:PRK11288 28 RAGQVHALMGENGAGKSTLLKILSGNyQPDAGSILIDGQEMRfASTTAALAAGVAIIYQELHLVPEMTVAENLYLGQLPH 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 110 SEPASRRDEIVRAAMthAGVDHLANRLYPG-----LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQ 184
Cdd:PRK11288 108 KGGIVNRRLLNYEAR--EQLEHLGVDIDPDtplkyLSIGQRQMVEIAKALA---------RNARVIAFDEPTSSLSAREI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 185 HQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELI 241
Cdd:PRK11288 177 EQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDRDQL 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
38-226 |
2.90e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 38 ALLGPNGAGKSSLLKCLTGELE-HEGEIHLfGQTRrgwagnalahRVGVLPQSSSlsfpFLCEEvvamgrlphsepASRR 116
Cdd:COG0488 345 GLIGPNGAGKSTLLKLLAGELEpDSGTVKL-GETV----------KIGYFDQHQE----ELDPD------------KTVL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 117 DEIVRAA----MTHAgVDHLANRLYPG---------LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLky 183
Cdd:COG0488 398 DELRDGApggtEQEV-RGYLGRFLFSGddafkpvgvLSGGEKARLALAKLLL---------SPPNVLLLDEPTNHLDI-- 465
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 743522756 184 qHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRL 226
Cdd:COG0488 466 -ETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
6-249 |
4.01e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 82.69 E-value: 4.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 6 SPLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQTRRGWAgnALAHRV 83
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAG-FETpdSGRIMLDGQDITHVP--AENRHV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 84 GVLPQSSSLsFPFL-CEEVVA----MGRLPHSEPASRRDEIVRaaMTHagVDHLANRLYPGLSGGERQRVQFARVLAqiw 158
Cdd:PRK09452 89 NTVFQSYAL-FPHMtVFENVAfglrMQKTPAAEITPRVMEALR--MVQ--LEEFAQRKPHQLSGGQQQRVAIARAVV--- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 159 qapeepQQARLLLLDEPTSALDLK----YQHQLLAMARALagrNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGnage 234
Cdd:PRK09452 161 ------NKPKVLLLDESLSALDYKlrkqMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG---- 227
|
250
....*....|....*
gi 743522756 235 vlTPELIarlYDYPA 249
Cdd:PRK09452 228 --TPREI---YEEPK 237
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
34-237 |
4.50e-18 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 80.94 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRG----WAgnaLAHRVGVLPQSsslsfP---FLC---EEVV 102
Cdd:TIGR04520 28 GEFVAIIGHNGSGKSTLAKLLNGLLLpTSGKVTVDGLDTLDeenlWE---IRKKVGMVFQN-----PdnqFVGatvEDDV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 103 AMG----RLPHSEPASRRDEIVRAAmthaGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSA 178
Cdd:TIGR04520 100 AFGlenlGVPREEMRKRVDEALKLV----GMEDFRDREPHLLSGGQKQRVAIAGVLAM------RP---DIIILDEATSM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 179 LDLKYQHQLLAMARAL-AGRNTAVLVVLHDLNLAARyADRLVMLEQGRLMADGNAGEVLT 237
Cdd:TIGR04520 167 LDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFS 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
34-244 |
5.16e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.38 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGEL----EHEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLSF-PFLCEEVVAMGRLP 108
Cdd:PRK13640 33 GSWTALIGHNGSGKSTISKLINGLLlpddNPNSKITVDGITLTAKTVWDIREKVGIVFQNPDNQFvGATVGDDVAFGLEN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQHQLL 188
Cdd:PRK13640 113 RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAV------EPK---IIILDESTSMLDPAGKEQIL 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 189 AMARALAGRNT-AVLVVLHDLNLAArYADRLVMLEQGRLMADGNAGEVLT-PELIARL 244
Cdd:PRK13640 184 KLIRKLKKKNNlTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSkVEMLKEI 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
36-247 |
5.71e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.85 E-value: 5.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 36 LTALLGPNGAGKSSLLKCLT------GELEHEGEIHLFGQT--RRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAMG-R 106
Cdd:PRK14258 35 VTAIIGPSGCGKSTFLKCLNrmneleSEVRVEGRVEFFNQNiyERRVNLNRLRRQVSMVHPKPNL-FPMSVYDNVAYGvK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 107 LPHSEPASRRDEIVRAAMTHAGV-DHLANRLYPG---LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLK 182
Cdd:PRK14258 114 IVGWRPKLEIDDIVESALKDADLwDEIKHKIHKSaldLSGGQQQRLCIARALA---------VKPKVLLMDEPCFGLDPI 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743522756 183 YQHQLLAMARALAGRNTAVLVVL-HDLNLAARYADRLVMLEQ-----GRLMADGNAGEVLTPELIARLYDY 247
Cdd:PRK14258 185 ASMKVESLIQSLRLRSELTMVIVsHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFNSPHDSRTREY 255
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-237 |
7.37e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 80.91 E-value: 7.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 4 SPSPLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCL------TGELEHEGEIHLFGQTRRGWAGN 77
Cdd:PRK14271 17 AAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkVSGYRYSGDVLLGGRSIFNYRDV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 78 -ALAHRVGVLPQSSSlSFPF-LCEEVVAMGRLPHSEPASRRDEIVRAAMTHAGV-DHLANRLYPG---LSGGERQRVQFA 151
Cdd:PRK14271 97 lEFRRRVGMLFQRPN-PFPMsIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSpfrLSGGQQQLLCLA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 152 RVLAqiwQAPEepqqarLLLLDEPTSALDLKYQHQLLAMARALAGRNTaVLVVLHDLNLAARYADRLVMLEQGRLMADGN 231
Cdd:PRK14271 176 RTLA---VNPE------VLLLDEPTSALDPTTTEKIEEFIRSLADRLT-VIIVTHNLAQAARISDRAALFFDGRLVEEGP 245
|
....*.
gi 743522756 232 AGEVLT 237
Cdd:PRK14271 246 TEQLFS 251
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
32-227 |
9.55e-18 |
|
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: 79.22 E-value: 9.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQTRRGWAGNalaHR-VGVLPQSSSLsFPFL-CEEVVAMGRLP 108
Cdd:cd03301 24 ADGEFVVLLGPSGCGKTTTLRMIAGlEEPTSGRIYIGGRDVTDLPPK---DRdIAMVFQNYAL-YPHMtVYDNIAFGLKL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQHQLL 188
Cdd:cd03301 100 RKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVR------EPK---VFLMDEPLSNLDAKLRVQMR 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 743522756 189 AMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLM 227
Cdd:cd03301 171 AELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
34-230 |
1.08e-17 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 79.33 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELEHEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLC--EEVVAMGRLPHSE 111
Cdd:cd03266 31 GEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGL-YDRLTarENLEYFAGLYGLK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAAMThAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQHQLLAMA 191
Cdd:cd03266 110 GDELTARLEELADR-LGMEELLDRRVGGFSTGMRQKVAIARALVH------DPP---VLLLDEPTTGLDVMATRALREFI 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 743522756 192 RALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADG 230
Cdd:cd03266 180 RQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
32-225 |
2.10e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKS----SLLKCL--------TGELEHEGE--IHLFGQTRRGWAGNalahRVGVLPQSSSLSFPFL 97
Cdd:PRK15134 33 EAGETLALVGESGSGKSvtalSILRLLpsppvvypSGDIRFHGEslLHASEQTLRGVRGN----KIAMIFQEPMVSLNPL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 98 ------CEEVVAMGRLPHSEPAsrRDEIVRAaMTHAGVDHLANRL--YP-GLSGGERQRVQFARVLAQiwqapeepqQAR 168
Cdd:PRK15134 109 htlekqLYEVLSLHRGMRREAA--RGEILNC-LDRVGIRQAAKRLtdYPhQLSGGERQRVMIAMALLT---------RPE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 169 LLLLDEPTSALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGR 225
Cdd:PRK15134 177 LLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
32-237 |
2.34e-17 |
|
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: 79.22 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNAL----AHRVGVLPQSSSLsFPFLCE-EVVAMG 105
Cdd:cd03294 48 REGEIFVIMGLSGSGKSTLLRCINRLIEpTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFAL-LPHRTVlENVAFG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 RLPHSEPASRRDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAqiwQAPEepqqarLLLLDEPTSALD---- 180
Cdd:cd03294 127 LEVQGVPRAEREERAAEALELVGLEGWEHK-YPDeLSGGMQQRVGLARALA---VDPD------ILLMDEAFSALDplir 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 181 LKYQHQLLAMARALagRNTAVLVVlHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:cd03294 197 REMQDELLRLQAEL--QKTIVFIT-HDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
38-243 |
2.62e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.08 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 38 ALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLS-FPFLCEEVVAMGR----LPHSE 111
Cdd:PRK13652 34 AVIGPNGAGKSTLFRHFNGILKpTSGSVLIRGEPITKENIREVRKFVGLVFQNPDDQiFSPTVEQDIAFGPinlgLDEET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAamthAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQHQLLAMA 191
Cdd:PRK13652 114 VAHRVSSALHM----LGLEELRDRVPHHLSGGEKKRVAIAGVIAM------EPQ---VLVLDEPTAGLDPQGVKELIDFL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 743522756 192 RALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT-PELIAR 243
Cdd:PRK13652 181 NDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLqPDLLAR 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
33-244 |
2.68e-17 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 81.02 E-value: 2.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEH---EGEIHLFGQ---------TRRgwAGNALAHR-VGVLPQSSSLSFPFLCE 99
Cdd:TIGR02633 26 PGECVGLCGENGAGKSTLMKILSGVYPHgtwDGEIYWSGSplkasnirdTER--AGIVIIHQeLTLVPELSVAENIFLGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 100 EVVAMGRLPHSEPASRRDEivrAAMTHAGVDHLANRLYPG-LSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSA 178
Cdd:TIGR02633 104 EITLPGGRMAYNAMYLRAK---NLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNK---------QARLLILDEPSSS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743522756 179 LDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARL 244
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDIITMM 237
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
38-225 |
2.86e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 75.95 E-value: 2.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 38 ALLGPNGAGKSSLLKCLTGELE-HEGEIHlfgqtrrgWAGNAlahRVGVLPQssslsfpflceevvamgrlphsepasrr 116
Cdd:cd03221 30 GLVGRNGAGKSTLLKLIAGELEpDEGIVT--------WGSTV---KIGYFEQ---------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 117 deivraamthagvdhlanrlypgLSGGERQRVQFARVLaqiWQAPEepqqarLLLLDEPTSALDLKYQHQLlamARALAG 196
Cdd:cd03221 71 -----------------------LSGGEKMRLALAKLL---LENPN------LLLLDEPTNHLDLESIEAL---EEALKE 115
|
170 180
....*....|....*....|....*....
gi 743522756 197 RNTAVLVVLHDLNLAARYADRLVMLEQGR 225
Cdd:cd03221 116 YPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
33-208 |
3.42e-17 |
|
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: 80.48 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAMGRlphsE 111
Cdd:TIGR02868 360 PGERVAILGPSGSGKSTLLATLAGLLDpLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHL-FDTTVRENLRLAR----P 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASrrDEIVRAAMTHAGVDHLANRLYPGL-----------SGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALD 180
Cdd:TIGR02868 435 DAT--DEELWAALERVGLADWLRALPDGLdtvlgeggarlSGGERQRLALARALLA---------DAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*...
gi 743522756 181 LKYQHQLLAMARAlAGRNTAVLVVLHDL 208
Cdd:TIGR02868 504 AETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
32-237 |
3.99e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 80.52 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEHEGEIHLFGQTRRGWAGNAL---AHRVGVLPQ--SSSLSFPFLCEEVVAMGR 106
Cdd:PRK15134 310 RPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQdpNSSLNPRLNVLQIIEEGL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 107 LPHSEP--ASRRDEIVRAAMTHAGVDHLANRLYPG-LSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKY 183
Cdd:PRK15134 390 RVHQPTlsAAQREQQVIAVMEEVGLDPETRHRYPAeFSGGQRQRIAIARALIL---------KPSLIILDEPTSSLDKTV 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 743522756 184 QHQLLAMARALAGRNT-AVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:PRK15134 461 QAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
34-229 |
4.38e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.93 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQTRRGWAGNALA----HRVGVLPQSSSLSFPFLCEEVVAMGRLP 108
Cdd:PRK11629 35 GEMMAIVGSSGSGKSTLLHLLGGlDTPTSGDVIFNGQPMSKLSSAAKAelrnQKLGFIYQFHHLLPDFTALENVAMPLLI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALDLKYQHQLL 188
Cdd:PRK11629 115 GKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN------NP---RLVLADEPTGNLDARNADSIF 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 743522756 189 AMARALAGRN-TAVLVVLHDLNLAARYADRLVMlEQGRLMAD 229
Cdd:PRK11629 186 QLLGELNRLQgTAFLVVTHDLQLAKRMSRQLEM-RDGRLTAE 226
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
32-237 |
5.33e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.19 E-value: 5.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQ-----TRRGWAgnALAHRVGVLPQSSSLSF-------PFLC 98
Cdd:PRK10419 36 KSGETVALLGRSGCGKSTLARLLVGlESPSQGNVSWRGEplaklNRAQRK--AFRRDIQMVFQDSISAVnprktvrEIIR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 99 EEVVAMGRLPHSEPASRRDEIVRAAMTHAGvdhLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSA 178
Cdd:PRK10419 114 EPLRHLLSLDKAERLARASEMLRAVDLDDS---VLDKRPPQLSGGQLQRVCLARALAV------EPK---LLILDEAVSN 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 179 LDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:PRK10419 182 LDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT 241
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
34-235 |
6.90e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.14 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGN----ALAHRVGVLPQssslsFP--FLCEEVV---- 102
Cdd:PRK13634 33 GSYVAIIGHTGSGKSTLLQHLNGLLQpTSGTVTIGERVITAGKKNkklkPLRKKVGIVFQ-----FPehQLFEETVekdi 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 103 AMGRLPHSEPASRRDEIVRAAMTHAGVDH-LANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDL 181
Cdd:PRK13634 108 CFGPMNFGVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAM------EPE---VLVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 743522756 182 KYQHQLLAMARAL-AGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEV 235
Cdd:PRK13634 179 KGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
41-225 |
1.02e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 79.08 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 41 GPNGAGKSSLLKCLTGELEH-EGEIHLfgqtrrgwagNALAhRVGVLPQSsslsfPFLceevvAMGRL------PHSePA 113
Cdd:COG4178 396 GPSGSGKSTLLRAIAGLWPYgSGRIAR----------PAGA-RVLFLPQR-----PYL-----PLGTLreallyPAT-AE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 114 SRRDEIVRAAMTHAGVDHLANRLYPG------LSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQL 187
Cdd:COG4178 454 AFSDAELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLH---------KPDWLFLDEATSALDEENEAAL 524
|
170 180 190
....*....|....*....|....*....|....*...
gi 743522756 188 LAMARAlAGRNTAVLVVLHDLNLAARYADRLVMLEQGR 225
Cdd:COG4178 525 YQLLRE-ELPGTTVISVGHRSTLAAFHDRVLELTGDGS 561
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
38-236 |
1.41e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.66 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 38 ALLGPNGAGKSSLLKCLTGELE-HEGEIhlfgqTRRGWAGNALAHRVGVLPQSSSLsfpflcEEVVAMGRL---PHSEPA 113
Cdd:COG1134 56 GIIGRNGAGKSTLLKLIAGILEpTSGRV-----EVNGRVSALLELGAGFHPELTGR------ENIYLNGRLlglSRKEID 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 114 SRRDEIVRaamtHAGV-DHLAN--RLYpglSGGERQRVQFArVLAQIwqapeEPQqarLLLLDEPTSALDLKYQHQLLAM 190
Cdd:COG1134 125 EKFDEIVE----FAELgDFIDQpvKTY---SSGMRARLAFA-VATAV-----DPD---ILLVDEVLAVGDAAFQKKCLAR 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 743522756 191 ARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:COG1134 189 IRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVI 234
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
32-231 |
1.42e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 77.82 E-value: 1.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELeH--EGEIHLFGQT---RRgwagNALAHRVG-VLPQSSSL--------SFPFL 97
Cdd:COG4586 46 EPGEIVGFIGPNGAGKSTTIKMLTGIL-VptSGEVRVLGYVpfkRR----KEFARRIGvVFGQRSQLwwdlpaidSFRLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 98 ceevVAMGRLPHSEPASRRDEIVraamTHAGVDHLANRlyP--GLSGGERQRVQFARVLaqIWQaPEepqqarLLLLDEP 175
Cdd:COG4586 121 ----KAIYRIPDAEYKKRLDELV----ELLDLGELLDT--PvrQLSLGQRMRCELAAAL--LHR-PK------ILFLDEP 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 176 TSALDLKYQHQLLAMARAL-AGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGN 231
Cdd:COG4586 182 TIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
33-245 |
1.65e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.47 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEHE-GEI----------HLFGQTRRGwagnalahrVGVLPQSSSLsFPFLC--E 99
Cdd:PRK10895 28 SGEIVGLLGPNGAGKTTTFYMVVGIVPRDaGNIiiddedisllPLHARARRG---------IGYLPQEASI-FRRLSvyD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 100 EVVAMGRLPHSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSAL 179
Cdd:PRK10895 98 NLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA---------ANPKFILLDEPFAGV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743522756 180 DLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLY 245
Cdd:PRK10895 169 DPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVY 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
38-239 |
1.78e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.42 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 38 ALLGPNGAGKSSLLKC------LTGELEHEGEIHLFGQTRRGWAGNALAHR--VGVLPQSSSlSFPFLC-EEVVAMGRLP 108
Cdd:PRK14267 34 ALMGPSGCGKSTLLRTfnrlleLNEEARVEGEVRLFGRNIYSPDVDPIEVRreVGMVFQYPN-PFPHLTiYDNVAIGVKL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSEPASRR--DEIVRAAMTHAGV-DHLANRL--YPG-LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLK 182
Cdd:PRK14267 113 NGLVKSKKelDERVEWALKKAALwDEVKDRLndYPSnLSGGQRQRLVIARALA---------MKPKILLMDEPTANIDPV 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 183 YQHQLLAMARALAGRNTAVLVVlHDLNLAARYADRLVMLEQGRLMADGNAGEVL-TPE 239
Cdd:PRK14267 184 GTAKIEELLFELKKEYTIVLVT-HSPAQAARVSDYVAFLYLGKLIEVGPTRKVFeNPE 240
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
33-239 |
1.82e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 78.71 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQ-----SSSLsfpflcEEVVAMGr 106
Cdd:PRK11160 365 AGEKVALLGRTGCGKSTLLQLLTRAWDpQQGEILLNGQPIADYSEAALRQAISVVSQrvhlfSATL------RDNLLLA- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 107 lphSEPASrrDEIVRAAMTHAGVDHLAN-----RLYPG-----LSGGERQRVQFARVLAQiwQAPeepqqarLLLLDEPT 176
Cdd:PRK11160 438 ---APNAS--DEALIEVLQQVGLEKLLEddkglNAWLGeggrqLSGGEQRRLGIARALLH--DAP-------LLLLDEPT 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 177 SALDLKYQHQLLAMARALAgRNTAVLVVLHDLNLAARYaDRLVMLEQGRLMADGNAGEVLTPE 239
Cdd:PRK11160 504 EGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQ 564
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
34-225 |
2.00e-16 |
|
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: 75.20 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGqtrrgwagnalahRVGVLPQSsslsfPFL----CEEVVAMGRlP 108
Cdd:cd03250 31 GELVAIVGPVGSGKSSLLSALLGELEkLSGSVSVPG-------------SIAYVSQE-----PWIqngtIRENILFGK-P 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSEPasRRDEIVRAA-------------MTHAGVDHLAnrlypgLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEP 175
Cdd:cd03250 92 FDEE--RYEKVIKACalepdleilpdgdLTEIGEKGIN------LSGGQKQRISLARAVY---------SDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 743522756 176 TSALDLK-----YQHQLLAMaraLAGRNTAVLVVlHDLNLaARYADRLVMLEQGR 225
Cdd:cd03250 155 LSAVDAHvgrhiFENCILGL---LLNNKTRILVT-HQLQL-LPHADQIVVLDNGR 204
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
33-245 |
2.04e-16 |
|
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: 78.22 E-value: 2.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGWAGNALAHRVGVLPQSSslsfpFLCEEVVAmGRLPHSE 111
Cdd:TIGR02203 357 PGETVALVGRSGSGKSTLVNLIPRFYEPDsGQILLDGHDLADYTLASLRRQVALVSQDV-----VLFNDTIA-NNIAYGR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAAMTHAGVDHLANRLYPG-----------LSGGERQRVQFARvlAQIWQAPeepqqarLLLLDEPTSALD 180
Cdd:TIGR02203 431 TEQADRAEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIAR--ALLKDAP-------ILILDEATSALD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 181 LKYQHQL-LAMARALAGRNTavLVVLHDLNlAARYADRLVMLEQGRLMADGNAGEVLTPE-LIARLY 245
Cdd:TIGR02203 502 NESERLVqAALERLMQGRTT--LVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLARNgLYAQLH 565
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
33-244 |
2.21e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 78.05 E-value: 2.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEH---EGEIHLFGQTRRGW-------AGNALAHR-VGVLPQSSSLSFPFLCEEV 101
Cdd:PRK13549 30 AGEIVSLCGENGAGKSTLMKVLSGVYPHgtyEGEIIFEGEELQASnirdterAGIAIIHQeLALVKELSVLENIFLGNEI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 102 VAMGRLPHSEPASRRDEIVRaamtHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDL 181
Cdd:PRK13549 110 TPGGIMDYDAMYLRAQKLLA----QLKLDINPATPVGNLGLGQQQLVEIAKALNK---------QARLLILDEPTASLTE 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 182 KYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARL 244
Cdd:PRK13549 177 SETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIITMM 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-237 |
2.46e-16 |
|
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: 78.19 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 4 SPSPLLSCRGLRLSRGNRLILDSLDL----DLHAGSLTALLGPNGAGKS----SLLKCLTGELEH-EGEIHLFGQ----- 69
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGTVEAVKgvsfDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHpSGSILFDGQdllgl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 70 ---TRRGWAGNalahRVGVLPQ--SSSLSFPFLCEEVVAMGRLPHsEPASRRD--EIVRAAMTHAGVDHLANRL--YP-G 139
Cdd:COG4172 82 serELRRIRGN----RIAMIFQepMTSLNPLHTIGKQIAEVLRLH-RGLSGAAarARALELLERVGIPDPERRLdaYPhQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 140 LSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALDLKYQHQLLAMARAL-AGRNTAVLVVLHDLNLAARYADRL 218
Cdd:COG4172 157 LSGGQRQRVMIAMALAN------EP---DLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRV 227
|
250
....*....|....*....
gi 743522756 219 VMLEQGRLMADGNAGEVLT 237
Cdd:COG4172 228 AVMRQGEIVEQGPTAELFA 246
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
7-245 |
2.69e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.18 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 7 PLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAhRVGV 85
Cdd:PRK11300 4 PLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKpTGGTILLRGQHIEGLPGHQIA-RMGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 86 LP--QSSSL--SFPFLCEEVVAMGRlpHSE----------PASRRDEivRAAMTHA-------GVDHLANRLYPGLSGGE 144
Cdd:PRK11300 83 VRtfQHVRLfrEMTVIENLLVAQHQ--QLKtglfsgllktPAFRRAE--SEALDRAatwlervGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 145 RQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQ 223
Cdd:PRK11300 159 QRRLEIARCMVT---------QPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQ 229
|
250 260
....*....|....*....|..
gi 743522756 224 GRLMADGNAGEVLTPELIARLY 245
Cdd:PRK11300 230 GTPLANGTPEEIRNNPDVIKAY 251
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
34-235 |
2.79e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 76.62 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQ--TRRGWAGNALAHRVGVLPQssslsFP--FLCEEVV----AM 104
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKpTSGKIIIDGVdiTDKKVKLSDIRKKVGLVFQ-----YPeyQLFEETIekdiAF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 105 G--RLPHSEpasrrDEI---VRAAMTHAGVDH--LANRLYPGLSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTS 177
Cdd:PRK13637 108 GpiNLGLSE-----EEIenrVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAIAGVVAM------EP---KILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 743522756 178 ALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEV 235
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREV 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
32-237 |
2.96e-16 |
|
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: 2.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH----EGEIHLFGQ--------TRRGWAGNalahRVGVLPQSSSLSF-PF-- 96
Cdd:COG0444 29 RRGETLGLVGESGSGKSTLARAILGLLPPpgitSGEILFDGEdllklsekELRKIRGR----EIQMIFQDPMTSLnPVmt 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 97 ----LCEEVVAMGRLPHSEpasrRDEIVRAAMTHAGVDHLANRL--YPG-LSGGERQRVQFARVLAqiwqapEEPqqaRL 169
Cdd:COG0444 105 vgdqIAEPLRIHGGLSKAE----ARERAIELLERVGLPDPERRLdrYPHeLSGGMRQRVMIARALA------LEP---KL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 170 LLLDEPTSALDLKYQHQLLAMARAL-AGRNTAVLVVLHDLNLAARYADR-LVMLeQGRLMADGNAGEVLT 237
Cdd:COG0444 172 LIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLGVVAEIADRvAVMY-AGRIVEEGPVEELFE 240
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
32-245 |
4.53e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.07 E-value: 4.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQ--T-----RRGWAGnalahrVGVLPQSSS----LSfpflCE 99
Cdd:COG1137 27 NQGEIVGLLGPNGAGKTTTFYMIVGLVKPdSGRIFLDGEdiThlpmhKRARLG------IGYLPQEASifrkLT----VE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 100 E----VVAMGRLPHSEpasrRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDE- 174
Cdd:COG1137 97 DnilaVLELRKLSKKE----REERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT------NP---KFILLDEp 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743522756 175 -----PTSALDLKyqhqllAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLY 245
Cdd:COG1137 164 fagvdPIAVADIQ------KIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVY 233
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
32-252 |
4.69e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.19 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEHEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAMGRlphse 111
Cdd:PRK11174 374 PAGQRIALVGPSGAGKTSLLNALLGFLPYQGSLKINGIELRELDPESWRKHLSWVGQNPQL-PHGTLRDNVLLGN----- 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 pASRRDEIVRAAMTHAGVDHLANRL-----YP------GLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALD 180
Cdd:PRK11174 448 -PDASDEQLQQALENAWVSEFLPLLpqgldTPigdqaaGLSVGQAQRLALARALL---------QPCQLLLLDEPTASLD 517
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743522756 181 LKYQHQLLamaRAL--AGRNTAVLVVLHDLNLAARYaDRLVMLEQGRLMADGNAGE-VLTPELIARLYDYPAQVI 252
Cdd:PRK11174 518 AHSEQLVM---QALnaASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAElSQAGGLFATLLAHRQEEI 588
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
33-237 |
5.79e-16 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 76.27 E-value: 5.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQ---TRRGWAGNALAHRVGVLPQSSSL----------SFPFL 97
Cdd:COG1135 30 KGEIFGIIGYSGAGKSTLIRCINL-LERptSGSVLVDGVdltALSERELRAARRKIGMIFQHFNLlssrtvaenvALPLE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 98 CEEVvamgrlphsePASRRDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPT 176
Cdd:COG1135 109 IAGV----------PKAEIRKRVAELLELVGLSDKADA-YPSqLSGGQKQRVGIARALAN------NPK---VLLCDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743522756 177 SALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:COG1135 169 SALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFA 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-237 |
6.35e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 74.95 E-value: 6.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 9 LSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELEH------EGEIHLFGQTRRGWAGNALAHR 82
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearvSGEVYLDGQDIFKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 83 VGVLPQSSSlSFPFLC-EEVVAMGRLPHSEPASRRD--EIVRAAMTHAGV-DHLANRL-YPG--LSGGERQRVQFARVLA 155
Cdd:PRK14247 84 VQMVFQIPN-PIPNLSiFENVALGLKLNRLVKSKKElqERVRWALEKAQLwDEVKDRLdAPAgkLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 156 qiwqapeepQQARLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVlHDLNLAARYADRLVMLEQGRLMADGNAGEV 235
Cdd:PRK14247 163 ---------FQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVT-HFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
..
gi 743522756 236 LT 237
Cdd:PRK14247 233 FT 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
32-247 |
1.00e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.62 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQTRRGWAGN-------------ALAHRVGVLPQSSSL-SFPF 96
Cdd:PRK10619 29 NAGDVISIIGSSGSGKSTFLRCINFlEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrLLRTRLTMVFQHFNLwSHMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 97 LCEEVV-AMGRLPHSEPASRRDEIVRAaMTHAGVDHLANRLYP-GLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDE 174
Cdd:PRK10619 109 VLENVMeAPIQVLGLSKQEARERAVKY-LAKVGIDERAQGKYPvHLSGGQQQRVSIARALAM------EPE---VLLFDE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 175 PTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLYDY 247
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQF 251
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
39-229 |
3.37e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.20 E-value: 3.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 39 LLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQ------SSSLSFpflcEE--VVAMGR--- 106
Cdd:COG1101 37 VIGSNGAGKSTLLNAIAGSLPpDSGSILIDGKDVTKLPEYKRAKYIGRVFQdpmmgtAPSMTI----EEnlALAYRRgkr 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 107 --LPHSEPASRRDEIV-RAAMTHAGvdhLANRLYP--G-LSGGERQRVQFarVLAQIwqapeepQQARLLLLDEPTSALD 180
Cdd:COG1101 113 rgLRRGLTKKRRELFReLLATLGLG---LENRLDTkvGlLSGGQRQALSL--LMATL-------TKPKLLLLDEHTAALD 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 743522756 181 LKYQHQLLAMARAL-AGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMAD 229
Cdd:COG1101 181 PKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILD 230
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
32-226 |
3.80e-15 |
|
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: 72.50 E-value: 3.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAMGrLPhS 110
Cdd:cd03248 38 HPGEVTALVGPSGSGKSTVVALLENFYQPQgGQVLLDGKPISQYEHKYLHSKVSLVGQEPVL-FARSLQDNIAYG-LQ-S 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 EPASRRDEIVRAAMTHAGVDHLANRLYPG-------LSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKY 183
Cdd:cd03248 115 CSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIR------NPQ---VLILDEATSALDAES 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 743522756 184 QHQLlamARALAG--RNTAVLVVLHDLNLAARyADRLVMLEQGRL 226
Cdd:cd03248 186 EQQV---QQALYDwpERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
34-255 |
4.22e-15 |
|
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: 72.50 E-value: 4.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQ--TRRGwagnalAHRVGVLpQSSSLsFPFLC--EEV-VAMGRL 107
Cdd:TIGR01184 11 GEFISLIGHSGCGKSTLLNLISGlAQPTSGGVILEGKqiTEPG------PDRMVVF-QNYSL-LPWLTvrENIaLAVDRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 PHSEPASRRDEIVRAAMTHAGVDHLANRlYPG-LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDL----K 182
Cdd:TIGR01184 83 LPDLSKSERRAIVEEHIALVGLTEAADK-RPGqLSGGMKQRVAIARALS---------IRPKVLLLDEPFGALDAltrgN 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 183 YQHQLLAMARalAGRNTAVLVVlHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLydypaQVIHHP 255
Cdd:TIGR01184 153 LQEELMQIWE--EHRVTVLMVT-HDVDEALLLSDRVVMLTNGPAANIGQILEVPFPRPRDRL-----EVVEDP 217
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
7-211 |
5.22e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 71.44 E-value: 5.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 7 PLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQ----TRRGWAGNALAH 81
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAaGTIKLDGGdiddPDVAEACHYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 82 RVGVLPQSS---SLSF--PFLceevvamgrlphsepaSRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLA- 155
Cdd:PRK13539 81 RNAMKPALTvaeNLEFwaAFL----------------GGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVs 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 743522756 156 --QIWqapeepqqarllLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLH-DLNLA 211
Cdd:PRK13539 145 nrPIW------------ILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHiPLGLP 191
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
39-222 |
5.23e-15 |
|
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: 72.44 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 39 LLGPNGAGKSSLLKCLTGELE-HEGEIhlfgqtrrGWAGNALAHRvgvlPQSSSLSFP-----FLCEEVVAMGRLPHSep 112
Cdd:cd03237 30 ILGPNGIGKTTFIKMLAGVLKpDEGDI--------EIELDTVSYK----PQYIKADYEgtvrdLLSSITKDFYTHPYF-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 113 asrRDEIvraaMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKyqhQLLAMAR 192
Cdd:cd03237 96 ---KTEI----AKPLQIEQILDREVPELSGGELQRVAIAACLS---------KDADIYLLDEPSAYLDVE---QRLMASK 156
|
170 180 190
....*....|....*....|....*....|....*
gi 743522756 193 -----ALAGRNTAvLVVLHDLNLAARYADRLVMLE 222
Cdd:cd03237 157 virrfAENNEKTA-FVVEHDIIMIDYLADRLIVFE 190
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-222 |
6.52e-15 |
|
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: 74.05 E-value: 6.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLfgqtrrgwagnalAHRVGVLPQSSSLSFPFLCEEVVAMGRLPHS 110
Cdd:COG1245 364 REGEVLGIVGPNGIGKTTFAKILAGVLKpDEGEVDE-------------DLKISYKPQYISPDYDGTVEEFLRSANTDDF 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 EPASRRDEIVRaamtHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKyqhQLLAM 190
Cdd:COG1245 431 GSSYYKTEIIK----PLGLEKLLDKNVKDLSGGELQRVAIAACLS---------RDADLYLLDEPSAHLDVE---QRLAV 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 743522756 191 ARAL----AGRNTAVLVVLHDLNLAARYADRLVMLE 222
Cdd:COG1245 495 AKAIrrfaENRGKTAMVVDHDIYLIDYISDRLMVFE 530
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
33-225 |
7.29e-15 |
|
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: 71.80 E-value: 7.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCltgeLEH-----EGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsfpFLC--EEVVAMG 105
Cdd:cd03249 28 PGKTVALVGSSGCGKSTVVSL----LERfydptSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVL---FDGtiAENIRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 RlpHSEPASRRDEIVRAAMTHAGVDHLANRLYP--G-----LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSA 178
Cdd:cd03249 101 K--PDATDEEVEEAAKKANIHDFIMSLPDGYDTlvGergsqLSGGQKQRIAIARALL---------RNPKILLLDEATSA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 743522756 179 LDLKYQHQLL-AMARALAGRNTavLVVLHDLNlAARYADRLVMLEQGR 225
Cdd:cd03249 170 LDAESEKLVQeALDRAMKGRTT--IVIAHRLS-TIRNADLIAVLQNGQ 214
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
34-244 |
7.46e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 72.33 E-value: 7.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLSFPFL-CEEVVAMGRLPHSE 111
Cdd:PRK13632 35 GEYVAILGHNGSGKSTISKILTGLLKpQSGEIKIDGITISKENLKEIRKKIGIIFQNPDNQFIGAtVEDDIAFGLENKKV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQHQLLAMA 191
Cdd:PRK13632 115 PPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL------NPE---IIIFDESTSMLDPKGKREIKKIM 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 743522756 192 RALAGRNTAVLV-VLHDLNLAARyADRLVMLEQGRLMADGNAGEVLTPELIARL 244
Cdd:PRK13632 186 VDLRKTRKKTLIsITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNKEILEK 238
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
33-236 |
7.60e-15 |
|
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: 73.70 E-value: 7.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAMGRlphse 111
Cdd:COG5265 383 AGKTVAIVGPSGAGKSTLARLLFRFYDvTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVL-FNDTIAYNIAYGR----- 456
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAAmTHAGVDHLANRLYPG-----------LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALD 180
Cdd:COG5265 457 PDASEEEVEAAA-RAAQIHDFIESLPDGydtrvgerglkLSGGEKQRVAIARTLL---------KNPPILIFDEATSALD 526
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743522756 181 LKYQHQLLAMARALAgRNTAVLVVLHDLNLAARyADRLVMLEQGRLMADGNAGEVL 236
Cdd:COG5265 527 SRTERAIQAALREVA-RGRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAELL 580
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
9-211 |
2.28e-14 |
|
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: 69.69 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 9 LSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHL----FGQTRRGWAGNA--LAH 81
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDsGEVRWngtpLAEQRDEPHENIlyLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 82 RVGVLPQSSSL-SFPFLCEEVVAMGRLPHsepasrrdeivrAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqa 160
Cdd:TIGR01189 81 LPGLKPELSALeNLHFWAAIHGGAQRTIE------------DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLS---- 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 743522756 161 peepqQARLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLH-DLNLA 211
Cdd:TIGR01189 145 -----RRPLWILDEPTTALDKAGVALLAGLLRAHLARGGIVLLTTHqDLGLV 191
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
33-235 |
2.70e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 70.55 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLSF-PFLCEEVVAMGRLPHS 110
Cdd:PRK13648 34 KGQWTSIVGHNGSGKSTIAKLMIGiEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDNQFvGSIVKYDVAFGLENHA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 EPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwQAPEepqqarLLLLDEPTSALDLKYQHQLLAM 190
Cdd:PRK13648 114 VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLA---LNPS------VIILDEATSMLDPDARQNLLDL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 743522756 191 ARAL-AGRNTAVLVVLHDLNLAARyADRLVMLEQGRLMADGNAGEV 235
Cdd:PRK13648 185 VRKVkSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
32-221 |
4.83e-14 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 69.89 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAgnalAHRvGVLPQSSSLsFPFL-CEEVVAMGRLPH 109
Cdd:COG4525 31 ESGEFVVALGASGCGKTTLLNLIAGFLApSSGEITLDGVPVTGPG----ADR-GVVFQKDAL-LPWLnVLDNVAFGLRLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 110 SEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALDL----KYQH 185
Cdd:COG4525 105 GVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA------DP---RFLLMDEPFGALDAltreQMQE 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 743522756 186 QLLamaRALAGRNTAVLVVLHDLNLAARYADRLVML 221
Cdd:COG4525 176 LLL---DVWQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
34-236 |
6.20e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 70.15 E-value: 6.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHL----FGQTRRGWAGNALAHRVGVL---PQSSSLSFPFLCEevVAMG 105
Cdd:PRK13643 32 GSYTALIGHTGSGKSTLLQHLNGLLQpTEGKVTVgdivVSSTSKQKEIKPVRKKVGVVfqfPESQLFEETVLKD--VAFG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 RLPHSEPASRRDEIVRAAMTHAGVDHLANRLYP-GLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQ 184
Cdd:PRK13643 110 PQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAM------EPE---VLVLDEPTAGLDPKAR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 743522756 185 HQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:PRK13643 181 IEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-236 |
1.51e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.41 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 4 SPSPLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIH--LFGQTRRGWAGNALA 80
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLApDAGEVHyrMRDGQLRDLYALSEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 81 HRV-------GVLPQSSSLSfpfLCEEVVAMGRLphSEP----ASRRDEIVRAAMTH--AGVDHLANRL--YPG-LSGGE 144
Cdd:PRK11701 82 ERRrllrtewGFVHQHPRDG---LRMQVSAGGNI--GERlmavGARHYGDIRATAGDwlERVEIDAARIddLPTtFSGGM 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 145 RQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQ 223
Cdd:PRK11701 157 QQRLQIARNLVT---------HPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQ 227
|
250
....*....|...
gi 743522756 224 GRLMADGNAGEVL 236
Cdd:PRK11701 228 GRVVESGLTDQVL 240
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-223 |
1.56e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 68.22 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 6 SPLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTrrgwagnalahRVG 84
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIKRNGKL-----------RIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 85 VLPQSSSLSfPFLCEEVVAMGRLphsEPASRRDEIVrAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeep 164
Cdd:PRK09544 71 YVPQKLYLD-TTLPLTVNRFLRL---RPGTKKEDIL-PALKRVQAGHLIDAPMQKLSGGETQRVLLARALL--------- 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 165 QQARLLLLDEPTSALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQ 223
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH 196
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
33-235 |
1.72e-13 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 69.92 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAMGRlphsE 111
Cdd:TIGR01192 360 AGQTVAIVGPTGAGKTTLINLLQRVYDPTvGQILIDGIDINTVTRESLRKSIATVFQDAGL-FNRSIRENIRLGR----E 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRrDEIVRAAMTHAGVDHLANRLY----------PGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDL 181
Cdd:TIGR01192 435 GATD-EEVYEAAKAAAAHDFILKRSNgydtlvgergNRLSGGERQRLAIARAIL---------KNAPILVLDEATSALDV 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 743522756 182 KYQHQLLAMARALAgRNTAVLVVLHDLNlAARYADRLVMLEQGRLMADGNAGEV 235
Cdd:TIGR01192 505 ETEARVKNAIDALR-KNRTTFIIAHRLS-TVRNADLVLFLDQGRLIEKGSFQEL 556
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-241 |
1.88e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.43 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRrgwagNALAHR------VGVLPQSSSLSFPFLCEEVVAMGR 106
Cdd:PRK09700 31 GEIHALLGENGAGKSTLMKVLSGIHEpTKGTITINNINY-----NKLDHKlaaqlgIGIIYQELSVIDELTVLENLYIGR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 107 LPHSE----PASRRDEI-VRAAMT--HAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSAL 179
Cdd:PRK09700 106 HLTKKvcgvNIIDWREMrVRAAMMllRVGLKVDLDEKVANLSISHKQMLEIAKTLM---------LDAKVIIMDEPTSSL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 743522756 180 DLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELI 241
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIV 238
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-237 |
2.40e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 67.76 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 35 SLTALLGPNGAGKSSLLKCLT-------GELEHEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSlSFPFLC-EEVVAMGR 106
Cdd:PRK14246 37 SIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN-PFPHLSiYDNIAYPL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 107 LPHSEPASRR-DEIVRAAMTHAGV-----DHLaNRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALD 180
Cdd:PRK14246 116 KSHGIKEKREiKKIVEECLRKVGLwkevyDRL-NSPASQLSGGQQQRLTIARALA---------LKPKVLLMDEPTSMID 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 181 LKYQHQLLAMARALAgRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:PRK14246 186 IVNSQAIEKLITELK-NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
34-235 |
2.86e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 67.85 E-value: 2.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQTRRGWAGN----ALAHRVGVLPQssslsFP--FLCEEVV---- 102
Cdd:PRK13649 33 GSYTAFIGHTGSGKSTIMQLLNGlHVPTQGSVRVDDTLITSTSKNkdikQIRKKVGLVFQ-----FPesQLFEETVlkdv 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 103 AMGrlPHSEPASRRD--EIVRAAMTHAGVDH-LANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSAL 179
Cdd:PRK13649 108 AFG--PQNFGVSQEEaeALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAM------EPK---ILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743522756 180 DLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEV 235
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
32-231 |
3.46e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.98 E-value: 3.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLtgelEH-----EGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAMGr 106
Cdd:TIGR00958 505 HPGEVVALVGPSGSGKSTVAALL----QNlyqptGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVL-FSGSVRENIAYG- 578
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 107 LPHSEpasrrDEIVRAAMTHAGVDHLANRLYPG-----------LSGGERQRVQFARVLAQiwqapeepqQARLLLLDEP 175
Cdd:TIGR00958 579 LTDTP-----DEEIMAAAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRIAIARALVR---------KPRVLILDEA 644
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743522756 176 TSALDLKYQhQLLAMARALAGRntAVLVVLHDLNLAARyADRLVMLEQGRLMADGN 231
Cdd:TIGR00958 645 TSALDAECE-QLLQESRSRASR--TVLLIAHRLSTVER-ADQILVLKKGSVVEMGT 696
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
33-224 |
3.89e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 67.42 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGWAgnalAHRvGVLPQSSSLsFPFL-CEEVVAMGRLPHS 110
Cdd:PRK11248 26 SGELLVVLGPSGCGKTTLLNLIAGFVPYQhGSITLDGKPVEGPG----AER-GVVFQNEGL-LPWRnVQDNVAFGLQLAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 EPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALD--LKYQHQLL 188
Cdd:PRK11248 100 VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALA---------ANPQLLLLDEPFGALDafTREQMQTL 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 743522756 189 aMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQG 224
Cdd:PRK11248 171 -LLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
34-206 |
3.91e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.54 E-value: 3.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGE----LEHEGEIHLFGQTRRGWAgnalAHRVGVLPQSSSLSFPFLCEE----VVAMG 105
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRspkgVKGSGSVLLNGMPIDAKE----MRAISAYVQQDDLFIPTLTVRehlmFQAHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 RLPHSEPASRRDEIVRAAMTHAGVDHLANRL------YPGLSGGERQRVQFArvlAQIWQAPeepqqaRLLLLDEPTSAL 179
Cdd:TIGR00955 127 RMPRRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFA---SELLTDP------PLLFCDEPTSGL 197
|
170 180
....*....|....*....|....*..
gi 743522756 180 DLKYQHQLLAMARALAGRNTAVLVVLH 206
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
33-236 |
5.39e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.12 E-value: 5.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsfpFlcEEVVAMGRLPHSE 111
Cdd:PRK11176 368 AGKTVALVGRSGSGKSTIANLLTRFYDiDEGEILLDGHDLRDYTLASLRNQVALVSQNVHL---F--NDTIANNIAYART 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAA-MTHA---------GVDHLANRLYPGLSGGERQRVQFARVLAQiwQAPeepqqarLLLLDEPTSALDL 181
Cdd:PRK11176 443 EQYSREQIEEAArMAYAmdfinkmdnGLDTVIGENGVLLSGGQRQRIAIARALLR--DSP-------ILILDEATSALDT 513
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 182 KYQHqllAMARALA--GRNTAVLVVLHDLNLAARyADRLVMLEQGRLMADGNAGEVL 236
Cdd:PRK11176 514 ESER---AIQAALDelQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELL 566
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
34-249 |
5.94e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 67.44 E-value: 5.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQ--TRRgwagnALAHR-VGVLPQSSSLsFPFLC-EEVVAMGRL 107
Cdd:PRK11432 32 GTMVTLLGPSGCGKTTVLRLVAG-LEKptEGQIFIDGEdvTHR-----SIQQRdICMVFQSYAL-FPHMSlGENVGYGLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 PHSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQL 187
Cdd:PRK11432 105 MLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALI---------LKPKVLLFDEPLSNLDANLRRSM 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 188 LAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEvltpeliarLYDYPA 249
Cdd:PRK11432 176 REKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE---------LYRQPA 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-242 |
8.04e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 8.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 4 SPSPLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQtRRGWAGNALAHR 82
Cdd:PRK15439 7 TAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGiVPPDSGTLEIGGN-PCARLTPAKAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 83 VGV--LPQSSSLsFPFL-CEEVVAMGRLPHSEPASRRDEIVRAAMTHAGVDHLANrlypGLSGGERQRVQFARVLAqiwq 159
Cdd:PRK15439 86 LGIylVPQEPLL-FPNLsVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSAG----SLEVADRQIVEILRGLM---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 160 apeepQQARLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPE 239
Cdd:PRK15439 157 -----RDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
...
gi 743522756 240 LIA 242
Cdd:PRK15439 232 IIQ 234
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
33-243 |
8.57e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.68 E-value: 8.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFLCEEVVAMGRlphse 111
Cdd:PRK13657 360 PGQTVAIVGPTGAGKSTLINLLQRVFDpQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGL-FNRSIEDNIRVGR----- 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAAMTHAGVDHLANRlyPG------------LSGGERQRVQFARVLAQiwQAPeepqqarLLLLDEPTSAL 179
Cdd:PRK13657 434 PDATDEEMRAAAERAQAHDFIERK--PDgydtvvgergrqLSGGERQRLAIARALLK--DPP-------ILILDEATSAL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743522756 180 DLKYQHQL-LAMARALAGRNTavLVVLHDLNlAARYADRLVMLEQGRLMADGNAGevltpELIAR 243
Cdd:PRK13657 503 DVETEAKVkAALDELMKGRTT--FIIAHRLS-TVRNADRILVFDNGRVVESGSFD-----ELVAR 559
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
135-235 |
8.90e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 8.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 135 RLYPG-LSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAA 212
Cdd:PRK09473 156 KMYPHeFSGGMRQRVMIAMALLC---------RPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVA 226
|
90 100
....*....|....*....|...
gi 743522756 213 RYADRLVMLEQGRLMADGNAGEV 235
Cdd:PRK09473 227 GICDKVLVMYAGRTMEYGNARDV 249
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-208 |
9.89e-13 |
|
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: 67.50 E-value: 9.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGEL-----EHEGE------IHLFgqtrrgwAGNAL--------------AHR---VGV 85
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELkpnlgDYDEEpswdevLKRF-------RGTELqdyfkklangeikvAHKpqyVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 86 LPQSSSLSFPFLCEEVVAMGRLphsepasrrDEIVRAAmthaGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepq 165
Cdd:COG1245 172 IPKVFKGTVRELLEKVDERGKL---------DELAEKL----GLENILDRDISELSGGELQRVAIAAALLR--------- 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 743522756 166 QARLLLLDEPTSALDLKyqhQLLAMARA---LAGRNTAVLVVLHDL 208
Cdd:COG1245 230 DADFYFFDEPSSYLDIY---QRLNVARLireLAEEGKYVLVVEHDL 272
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
34-237 |
1.19e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 66.39 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGN----ALAHRVGVLPQ-SSSLSFPFLCEEVVAMGrl 107
Cdd:PRK13641 33 GSFVALVGHTGSGKSTLMQHFNALLKpSSGTITIAGYHITPETGNknlkKLRKKVSLVFQfPEAQLFENTVLKDVEFG-- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 PHSEPASRRDEIVRAA--MTHAGV-DHLANRLYPGLSGGERQRVQFARVLAqiwqapEEPQqarLLLLDEPTSALDLKYQ 184
Cdd:PRK13641 111 PKNFGFSEDEAKEKALkwLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA------YEPE---ILCLDEPAAGLDPEGR 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 743522756 185 HQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:PRK13641 182 KEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
5-226 |
2.54e-12 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 66.35 E-value: 2.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 5 PSPLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNalaHRV 83
Cdd:PRK10636 309 PNPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELApVSGEIGLAKGIKLGYFAQ---HQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 84 GVLPQSSSlsfpflceEVVAMGRLPHSEPASR-RDEIVRAAMTHAGVDHLANRlypgLSGGERQRVqfarVLAQI-WQAP 161
Cdd:PRK10636 386 EFLRADES--------PLQHLARLAPQELEQKlRDYLGGFGFQGDKVTEETRR----FSGGEKARL----VLALIvWQRP 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743522756 162 EepqqarLLLLDEPTSALDLKYQHqllAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRL 226
Cdd:PRK10636 450 N------LLLLDEPTNHLDLDMRQ---ALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
32-226 |
4.16e-12 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 62.83 E-value: 4.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGW-AGNALAHRVGVLPqssslsfpflceevvamgrlph 109
Cdd:cd03215 24 RAGEIVGIAGLVGNGQTELAEALFGLRPPAsGEITLDGKPVTRRsPRDAIRAGIAYVP---------------------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 110 sepASRRDEIVRAAMTHAgvDHLANRLYpgLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLA 189
Cdd:cd03215 82 ---EDRKREGLVLDLSVA--ENIALSSL--LSGGNQQKVVLARWLAR---------DPRVLILDEPTRGVDVGAKAEIYR 145
|
170 180 190
....*....|....*....|....*....|....*..
gi 743522756 190 MARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRL 226
Cdd:cd03215 146 LIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
32-179 |
4.73e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.41 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRR-------GWAGNALAHR-VGVLPQSSSLSFPFLCEEVV 102
Cdd:PRK10762 28 YPGRVMALVGENGAGKSTMMKVLTGIYTRDaGSILYLGKEVTfngpkssQEAGIGIIHQeLNLIPQLTIAENIFLGREFV 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 103 -AMGRLPHSEPASRRDeivrAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSAL 179
Cdd:PRK10762 108 nRFGRIDWKKMYAEAD----KLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLS---------FESKVIIMDEPTDAL 172
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
32-244 |
4.81e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 63.93 E-value: 4.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEHE---GEIHLFGQ-------TRRGWAGNALA--HRV---GVlpqssSLSFpF 96
Cdd:COG0396 24 KPGEVHAIMGPNGSGKSTLAKVLMGHPKYEvtsGSILLDGEdilelspDERARAGIFLAfqYPVeipGV-----SVSN-F 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 97 LCEEVVAMGRLPHSEPASRRDeiVRAAMTHAGVDH-LANR-LYPGLSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDE 174
Cdd:COG0396 98 LRTALNARRGEELSAREFLKL--LKEKMKELGLDEdFLDRyVNEGFSGGEKKRNEILQMLLL------EP---KLAILDE 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743522756 175 PTSALD---LKyqhqllAMAR---ALAGRNTAVLVVLHD---LNLAAryADRLVMLEQGRLMADGnagevlTPELIARL 244
Cdd:COG0396 167 TDSGLDidaLR------IVAEgvnKLRSPDRGILIITHYqriLDYIK--PDFVHVLVDGRIVKSG------GKELALEL 231
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
32-232 |
5.39e-12 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 65.52 E-value: 5.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLtGELEH--EGEIHLFGQTRRGWAGNALA----HRVGVLPQSSSLSFPFLCEEVVAMG 105
Cdd:PRK10535 32 YAGEMVAIVGASGSGKSTLMNIL-GCLDKptSGTYRVAGQDVATLDADALAqlrrEHFGFIFQRYHLLSHLTAAQNVEVP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 RLPHSEPASRRDEIVRAAMTHAGvdhLANRLY--PG-LSGGERQRVQFARVLAQIWQapeepqqarLLLLDEPTSALDLK 182
Cdd:PRK10535 111 AVYAGLERKQRLLRAQELLQRLG---LEDRVEyqPSqLSGGQQQRVSIARALMNGGQ---------VILADEPTGALDSH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 743522756 183 YQHQLLAMARALAGRNTAVLVVLHDLNLAARyADRLVMLEQGRLMADGNA 232
Cdd:PRK10535 179 SGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPA 227
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
34-245 |
7.12e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 63.36 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGW-AGNALAHRVGVLPQSSSLSFPFLCEEVVAMGRLPhse 111
Cdd:PRK11614 31 GEIVTLIGANGAGKTTLLGTLCGDPRaTSGRIVFDGKDITDWqTAKIMREAVAIVPEGRRVFSRMTVEENLAMGGFF--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 pASRRDEIVRAAMTHAGVDHLANRLYP---GLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLL 188
Cdd:PRK11614 108 -AERDQFQERIKWVYELFPRLHERRIQragTMSGGEQQMLAIGRALMS---------QPRLLLLDEPSLGLAPIIIQQIF 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 189 AMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARLY 245
Cdd:PRK11614 178 DTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAY 234
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
34-249 |
1.08e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.90 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIhLFGQTR--------RGwagnalahrVGVLPQSSSLsFPFL-CEEVV 102
Cdd:PRK11000 29 GEFVVFVGPSGCGKSTLLRMIAG-LEDitSGDL-FIGEKRmndvppaeRG---------VGMVFQSYAL-YPHLsVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 103 AMGRLPHSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLK 182
Cdd:PRK11000 97 SFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV---------AEPSVFLLDEPLSNLDAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 183 YQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEvltpeliarLYDYPA 249
Cdd:PRK11000 168 LRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLE---------LYHYPA 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
38-226 |
1.08e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 62.87 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 38 ALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQ--TRRGWAGNAL--AHRVGVLPQSSSLSFPFLCEEVVAMGRLPHSEP 112
Cdd:PRK10584 40 ALIGESGSGKSTLLAILAGlDDGSSGEVSLVGQplHQMDEEARAKlrAKHVGFVFQSFMLIPTLNALENVELPALLRGES 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 113 ASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQ----LL 188
Cdd:PRK10584 120 SRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFN---------GRPDVLFADEPTGNLDRQTGDKiadlLF 190
|
170 180 190
....*....|....*....|....*....|....*...
gi 743522756 189 AMARALAgrnTAVLVVLHDLNLAARyADRLVMLEQGRL 226
Cdd:PRK10584 191 SLNREHG---TTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-208 |
1.16e-11 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 63.15 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGEL-----EHEGEIHlFGQTRRGWAGNALAH----------RVGVLPQSSSL---SFP 95
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLkpnlgKFDDPPD-WDEILDEFRGSELQNyftkllegdvKVIVKPQYVDLipkAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 96 FLCEEVvamgrLPHSEPASRRDEIVRAAmthaGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEP 175
Cdd:cd03236 105 GKVGEL-----LKKKDERGKLDELVDQL----ELRHVLDRNIDQLSGGELQRVAIAAALAR---------DADFYFFDEP 166
|
170 180 190
....*....|....*....|....*....|....*.
gi 743522756 176 TSALDLKyqhQLLAMARALAGRNT---AVLVVLHDL 208
Cdd:cd03236 167 SSYLDIK---QRLNAARLIRELAEddnYVLVVEHDL 199
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-229 |
1.70e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.77 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 2 PGSPsplLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGeLEHEGEIHLFgqtrrgwAGNALAH 81
Cdd:PRK11247 9 QGTP---LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAG-LETPSAGELL-------AGTAPLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 82 RVG-----------VLPQSSSLsfpflceEVVAMGRLPHSEPASRRdeivraAMTHAGVDHLANRLYPGLSGGERQRVQF 150
Cdd:PRK11247 78 EARedtrlmfqdarLLPWKKVI-------DNVGLGLKGQWRDAALQ------ALAAVGLADRANEWPAALSGGQKQRVAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 151 ARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMAD 229
Cdd:PRK11247 145 ARALIH---------RPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
40-222 |
1.75e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 40 LGPNGAGKSSLLKCLTGELE-HEGEIhlfgqtrrgwagnALAHRVGVLPQSSSLSFPFLCEEVVAM--GRLpHSEPAsrR 116
Cdd:PRK13409 371 VGPNGIGKTTFAKLLAGVLKpDEGEV-------------DPELKISYKPQYIKPDYDGTVEDLLRSitDDL-GSSYY--K 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 117 DEIVRAAmthaGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKyqhQLLAMARAL-- 194
Cdd:PRK13409 435 SEIIKPL----QLERLLDKNVKDLSGGELQRVAIAACLS---------RDADLYLLDEPSAHLDVE---QRLAVAKAIrr 498
|
170 180 190
....*....|....*....|....*....|
gi 743522756 195 --AGRNTAVLVVLHDLNLAARYADRLVMLE 222
Cdd:PRK13409 499 iaEEREATALVVDHDIYMIDYISDRLMVFE 528
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
33-181 |
1.81e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.76 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHlfgqtrrgWAGNAlahRVGVLPQSSSLSFP-------FLC------ 98
Cdd:PRK15064 344 AGERLAIIGENGVGKTTLLRTLVGELEPdSGTVK--------WSENA---NIGYYAQDHAYDFEndltlfdWMSqwrqeg 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 99 --EEVV--AMGRLPHSEpasrrDEIVRAAMThagvdhlanrlypgLSGGERQRVQFARVLAqiwqapeepQQARLLLLDE 174
Cdd:PRK15064 413 ddEQAVrgTLGRLLFSQ-----DDIKKSVKV--------------LSGGEKGRMLFGKLMM---------QKPNVLVMDE 464
|
....*..
gi 743522756 175 PTSALDL 181
Cdd:PRK15064 465 PTNHMDM 471
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
34-208 |
3.87e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGEL-----EHEGE------IHLFgqtrrgwAGNAL--------------AHR---VGV 85
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELipnlgDYEEEpswdevLKRF-------RGTELqnyfkklyngeikvVHKpqyVDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 86 LPQSSSLSFPFLCEEVVAMGRLphsepasrrDEIVRAAmthaGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQ 165
Cdd:PRK13409 172 IPKVFKGKVRELLKKVDERGKL---------DEVVERL----GLENILDRDISELSGGELQRVAIAAALL---------R 229
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 743522756 166 QARLLLLDEPTSALDLKyqhQLLAMARA---LAgRNTAVLVVLHDL 208
Cdd:PRK13409 230 DADFYFFDEPTSYLDIR---QRLNVARLireLA-EGKYVLVVEHDL 271
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
9-220 |
3.93e-11 |
|
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: 60.58 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 9 LSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHL----FGQTRRGWAGNAL--AH 81
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPpLAGRVLLnggpLDFQRDSIARGLLylGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 82 RVGVLPQSSSL-SFPFLCeevvamgrlphsepASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqa 160
Cdd:cd03231 81 APGIKTTLSVLeNLRFWH--------------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLL----- 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743522756 161 peepQQARLLLLDEPTSALDLKYQHQLL-AMARALAGRNTAVLVVLHDLNLAARYADRLVM 220
Cdd:cd03231 142 ----SGRPLWILDEPTTALDKAGVARFAeAMAGHCARGGMVVLTTHQDLGLSEAGARELDL 198
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
34-236 |
4.08e-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: 62.51 E-value: 4.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHL------FGQTRRGWAGNALAHR-VGVLPQSSSLsFP---FLCEEVV 102
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGVLEpTSGEVNVrvgdewVDMTKPGPDGRGRAKRyIGILHQEYDL-YPhrtVLDNLTE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 103 AMG-RLPhSEPASRRDEIV--RAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSAL 179
Cdd:TIGR03269 389 AIGlELP-DELARMKAVITlkMVGFDEEKAEEILDKYPDELSEGERHRVALAQVLIK------EP---RIVILDEPTGTM 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743522756 180 D----LKYQHQLLAMARALagrNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:TIGR03269 459 DpitkVDVTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
32-230 |
4.65e-11 |
|
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: 61.01 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIhlfgqTRRGWAGNALAHRVGVLPQSSSLsfpflcEEVVAMGRL--- 107
Cdd:cd03220 46 PRGERIGLIGRNGAGKSTLLRLLAGIYPpDSGTV-----TVRGRVSSLLGLGGGFNPELTGR------ENIYLNGRLlgl 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 PHSEPASRRDEIVraamTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQL 187
Cdd:cd03220 115 SRKEIDEKIDEII----EFSELGDFIDLPVKTYSSGMKARLAFAIATA---------LEPDILLIDEVLAVGDAAFQEKC 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 743522756 188 LAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADG 230
Cdd:cd03220 182 QRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
34-243 |
5.59e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 61.29 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQ---TRRGWAgnaLAHRVGVLPQSSSLSF-PFLCEEVVAMGR-- 106
Cdd:PRK13650 33 GEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDGDlltEENVWD---IRHKIGMVFQNPDNQFvGATVEDDVAFGLen 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 107 --LPHSEPASRRDEivraAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQ 184
Cdd:PRK13650 110 kgIPHEEMKERVNE----ALELVGMQDFKEREPARLSGGQKQRVAIAGAVAM------RPK---IIILDEATSMLDPEGR 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743522756 185 HQLLAMARALAGR-NTAVLVVLHDLNLAArYADRLVMLEQGRLMAdgnageVLTP-ELIAR 243
Cdd:PRK13650 177 LELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVES------TSTPrELFSR 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
34-236 |
6.16e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 61.26 E-value: 6.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQtrRGWAGNA--LAHRVGVLPQSSSLSF-PFLCEEVVAMGR--- 106
Cdd:PRK13642 33 GEWVSIIGQNGSGKSTTARLIDGLFEEfEGKVKIDGE--LLTAENVwnLRRKIGMVFQNPDNQFvGATVEDDVAFGMenq 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 107 -LPHSEPASRRDEivraAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwQAPEepqqarLLLLDEPTSALDLKYQH 185
Cdd:PRK13642 111 gIPREEMIKRVDE----ALLAVNMLDFKTREPARLSGGQKQRVAVAGIIA---LRPE------IIILDESTSMLDPTGRQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 743522756 186 QLLAMARALAGR-NTAVLVVLHDLNLAARyADRLVMLEQGRLMADGNAGEVL 236
Cdd:PRK13642 178 EIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
34-236 |
7.20e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.82 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELEHEGEIHLFGQTRRGWAGNALaHRVGVLPQSSSLsFPFLC--EEVV--AMGRLPH 109
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQIL-KRTGFVTQDDIL-YPHLTvrETLVfcSLLRLPK 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 110 SepASRRDEIVRA-------AMTHAGVDHLANRLYPGLSGGERQRVQFARvlaqiwqapEEPQQARLLLLDEPTSALDLK 182
Cdd:PLN03211 172 S--LTKQEKILVAesviselGLTKCENTIIGNSFIRGISGGERKRVSIAH---------EMLINPSLLILDEPTSGLDAT 240
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 743522756 183 YQHQLLAMARALAGRNTAVLVVLHD-LNLAARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:PLN03211 241 AAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGKGSDAM 295
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
38-255 |
1.00e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 60.90 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 38 ALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQTRRGWAGNAL-AHRVGVL-----PQSS---------SLSFPFLCEE 100
Cdd:COG4608 48 GLVGESGCGKSTLGRLLLR-LEEptSGEILFDGQDITGLSGRELrPLRRRMQmvfqdPYASlnprmtvgdIIAEPLRIHG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 101 VVamgrlphsePASRRDEIVRAAMTHAGV--DHlANRlYPG-LSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTS 177
Cdd:COG4608 127 LA---------SKAERRERVAELLELVGLrpEH-ADR-YPHeFSGGQRQRIGIARALAL------NP---KLIVCDEPVS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 178 ALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADR-LVM-LeqGRLMADGNAGEvltpeliarLYDYPAqvihH 254
Cdd:COG4608 187 ALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRvAVMyL--GKIVEIAPRDE---------LYARPL----H 251
|
.
gi 743522756 255 P 255
Cdd:COG4608 252 P 252
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
34-234 |
1.76e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 59.12 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQ--TR-RGWAGNALAHRVGVLPQSSSLSFPFLCEEVVAMGRL-- 107
Cdd:PRK10908 28 GEMAFLTGHSGAGKSTLLKLICGiERPSAGKIWFSGHdiTRlKNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIia 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 -PHSEPASRRdeiVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQ 186
Cdd:PRK10908 108 gASGDDIRRR---VSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV---------NKPAVLLADEPTGNLDDALSEG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 743522756 187 LLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRlMADGNAGE 234
Cdd:PRK10908 176 ILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH-LHGGVGGE 222
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
114-235 |
1.91e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.14 E-value: 1.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 114 SRRDEIVRAA--MTHAGVDHLANRL--YP-GLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLL 188
Cdd:PRK11022 123 NKKTRRQRAIdlLNQVGIPDPASRLdvYPhQLSGGMSQRVMIAMAIAC---------RPKLLIADEPTTALDVTIQAQII 193
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 743522756 189 AMARALAGR-NTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEV 235
Cdd:PRK11022 194 ELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
36-216 |
2.23e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 59.41 E-value: 2.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 36 LTALLGPNGAGKSSLLKC------LTGELEHEGEIHLFGQTRrgWAGN----ALAHRVGVLPQSSSlSFPFLCEEVVAMG 105
Cdd:PRK14243 38 ITAFIGPSGCGKSTILRCfnrlndLIPGFRVEGKVTFHGKNL--YAPDvdpvEVRRRIGMVFQKPN-PFPKSIYDNIAYG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 RLPHSEPASRrDEIVRAAMTHAGV-DHLANRLYP---GLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALD- 180
Cdd:PRK14243 115 ARINGYKGDM-DELVERSLRQAALwDEVKDKLKQsglSLSGGQQQRLCIARAIA---------VQPEVILMDEPCSALDp 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 743522756 181 ---LKYQ---HQLlamaralaGRNTAVLVVLHDLNLAARYAD 216
Cdd:PRK14243 185 istLRIEelmHEL--------KEQYTIIIVTHNMQQAARVSD 218
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
39-214 |
2.82e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 39 LLGPNGAGKSSLLKCLTG-ELEHEGEIHLfgqtrrgwagnALAHRVGVLPQSsslsfPFLCE-----EVVAMG------- 105
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGvDKEFEGEARP-----------APGIKVGYLPQE-----PQLDPektvrENVEEGvaevkaa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 --RL-----PHSEPASRRDEI------VRAAMTHAGVDHL---------ANRLYPG------LSGGERQRVQFARVLAqi 157
Cdd:PRK11819 102 ldRFneiyaAYAEPDADFDALaaeqgeLQEIIDAADAWDLdsqleiamdALRCPPWdakvtkLSGGERRRVALCRLLL-- 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 158 wQAPEepqqarLLLLDEPTSALD------LKyQHqllamaraLAGRNTAVLVVLHDlnlaaRY 214
Cdd:PRK11819 180 -EKPD------MLLLDEPTNHLDaesvawLE-QF--------LHDYPGTVVAVTHD-----RY 221
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
32-230 |
2.86e-10 |
|
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: 58.81 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEHE---GEIHLFGQT-------RRGWAGNALAHRVGV-LPQSSSLSfpFLCEE 100
Cdd:TIGR01978 24 KKGEIHAIMGPNGSGKSTLSKTIAGHPSYEvtsGTILFKGQDllelepdERARAGLFLAFQYPEeIPGVSNLE--FLRSA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 101 VVAMGRLPHSEPASRRD--EIVRAAMTHAGVD-HLANR-LYPGLSGGERQRvqfarvlAQIWQ-APEEPqqaRLLLLDEP 175
Cdd:TIGR01978 102 LNARRSARGEEPLDLLDfeKLLKEKLALLDMDeEFLNRsVNEGFSGGEKKR-------NEILQmALLEP---KLAILDEI 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 176 TSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLaARY--ADRLVMLEQGRLMADG 230
Cdd:TIGR01978 172 DSGLDIDALKIVAEGINRLREPDRSFLIITHYQRL-LNYikPDYVHVLLDGRIVKSG 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
44-244 |
3.12e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.03 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 44 GAGKSSLLKCLTGELE-HEGEIHLFGQT-RRGWAGNALAHRVG-----------VLPQSSS--LSFPFLcEEVVAMGRLP 108
Cdd:COG1129 288 GAGRTELARALFGADPaDSGEIRLDGKPvRIRSPRDAIRAGIAyvpedrkgeglVLDLSIRenITLASL-DRLSRGGLLD 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSepasRRDEIVRAAMT-----HAGVDHLANRLypglSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDL-- 181
Cdd:COG1129 367 RR----RERALAEEYIKrlrikTPSPEQPVGNL----SGGNQQKVVLAKWLAT---------DPKVLILDEPTRGIDVga 429
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743522756 182 KYQ-HQLLamaRALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEvLTPELIARL 244
Cdd:COG1129 430 KAEiYRLI---RELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREE-ATEEAIMAA 489
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
34-235 |
3.61e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.56 E-value: 3.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSslLKCLT-------GELEHEGEIHLFGQTrrgWAGNALAHR-VGVLPQSSSLSFPFL-------C 98
Cdd:PRK10418 29 GRVLALVGGSGSGKS--LTCAAalgilpaGVRQTAGRVLLDGKP---VAPCALRGRkIATIMQNPRSAFNPLhtmhthaR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 99 EEVVAMGRLPhsepasrRDEIVRAAMTHAGVDHLAN--RLYP-GLSGGERQRVQFArvLAQIWQAPeepqqarLLLLDEP 175
Cdd:PRK10418 104 ETCLALGKPA-------DDATLTAALEAVGLENAARvlKLYPfEMSGGMLQRMMIA--LALLCEAP-------FIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743522756 176 TSALDLKYQHQLLAM-ARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEV 235
Cdd:PRK10418 168 TTDLDVVAQARILDLlESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-236 |
4.11e-10 |
|
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: 59.96 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQTRRGWAGNALAHRVGVLPQSsslsfPFLCEEVVAMGRLPHS 110
Cdd:TIGR00957 1310 HGGEKVGIVGRTGAGKSSLTLGLFRINESaEGEIIIDGLNIAKIGLHDLRFKITIIPQD-----PVLFSGSLRMNLDPFS 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 epaSRRDEIVRAA--MTH---------AGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSAL 179
Cdd:TIGR00957 1385 ---QYSDEEVWWAleLAHlktfvsalpDKLDHECAEGGENLSVGQRQLVCLARALL---------RKTKILVLDEATAAV 1452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 180 DLKYQHQLLAMARAlAGRNTAVLVVLHDLNLAARYAdRLVMLEQGRLMADGNAGEVL 236
Cdd:TIGR00957 1453 DLETDNLIQSTIRT-QFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLL 1507
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
32-245 |
4.59e-10 |
|
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: 57.54 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEHE---GEIHLFGQ-------TRRGWAGnalahrVGVLPQSSslsfpflcEEV 101
Cdd:cd03217 24 KKGEVHALMGPNGSGKSTLAKTIMGHPKYEvteGEILFKGEditdlppEERARLG------IFLAFQYP--------PEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 102 vamgrlphsePASRRDEIVRaamthaGVDHlanrlypGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDL 181
Cdd:cd03217 90 ----------PGVKNADFLR------YVNE-------GFSGGEKKRNEILQLLL---------LEPDLAILDEPDSGLDI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743522756 182 KYQHQLLAMARALAGRNTAVLVVLHDLNLAARY-ADRLVMLEQGRLMADGnagevlTPELIARLY 245
Cdd:cd03217 138 DALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG------DKELALEIE 196
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
34-236 |
4.87e-10 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 59.28 E-value: 4.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAH----RVGVLPQSSSLSFPFLCEEVVAMGRLP 108
Cdd:PRK10070 54 GEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHMTVLDNTAFGMEL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQLL 188
Cdd:PRK10070 134 AGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALA---------INPDILLMDEAFSALDPLIRTEMQ 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 743522756 189 -AMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVL 236
Cdd:PRK10070 205 dELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-237 |
5.24e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEH-----EGEIHLFGQTR-------RG---WAGNALAHrVGVLPQSSSLSFPFL 97
Cdd:TIGR00956 86 PGELTVVLGRPGSGCSTLLKTIASNTDGfhigvEGVITYDGITPeeikkhyRGdvvYNAETDVH-FPHLTVGETLDFAAR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 98 CeevvamgRLPHSEP-----ASRRDEIVRAAMTHAGVDH-----LANRLYPGLSGGERQRVQFARVLAqiwqapeepQQA 167
Cdd:TIGR00956 165 C-------KTPQNRPdgvsrEEYAKHIADVYMATYGLSHtrntkVGNDFVRGVSGGERKRVSIAEASL---------GGA 228
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 168 RLLLLDEPTSALD----LKYQHQLLAMARALagrNTAVLVVLHDlnlAARYA----DRLVMLEQGRLMADGNAGEVLT 237
Cdd:TIGR00956 229 KIQCWDNATRGLDsataLEFIRALKTSANIL---DTTPLVAIYQ---CSQDAyelfDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
39-214 |
6.94e-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: 58.79 E-value: 6.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 39 LLGPNGAGKSSLLKCLTG-ELEHEGEihlfgqtrrgwAGNALAHRVGVLPQSSSLSFPFLCEEVVAMGrLPHSEPASRRD 117
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGvDKDFNGE-----------ARPQPGIKVGYLPQEPQLDPTKTVRENVEEG-VAEIKDALDRF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 118 EIVRAAMTH--AGVDHLAN----------------------------RLYPG------LSGGERQRVQFARVLAqiwQAP 161
Cdd:TIGR03719 104 NEISAKYAEpdADFDKLAAeqaelqeiidaadawdldsqleiamdalRCPPWdadvtkLSGGERRRVALCRLLL---SKP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 743522756 162 EepqqarLLLLDEPTSALDLKyqhQLLAMARALAGRNTAVLVVLHDlnlaaRY 214
Cdd:TIGR03719 181 D------MLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHD-----RY 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
139-236 |
7.14e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.17 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 139 GLSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRL 218
Cdd:PRK13651 165 ELSGGQKRRVALAGILAM------EP---DFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRT 235
|
90
....*....|....*...
gi 743522756 219 VMLEQGRLMADGNAGEVL 236
Cdd:PRK13651 236 IFFKDGKIIKDGDTYDIL 253
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-226 |
7.38e-10 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.10 E-value: 7.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 35 SLTALLGPNGAGKSSLLKCLTGELehegeihlfgQTRRGWAGNALAHRVGVLPQSSSLSFPFLCEEVVAMGRLPHSEPAS 114
Cdd:PLN03073 536 SRIAMVGPNGIGKSTILKLISGEL----------QPSSGTVFRSAKVRMAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQ 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 115 RrdeiVRAAMTHAGVD-HLANRLYPGLSGGERQRVQFARVlaqIWQAPEepqqarLLLLDEPTSALDLKyqhQLLAMARA 193
Cdd:PLN03073 606 K----LRAHLGSFGVTgNLALQPMYTLSGGQKSRVAFAKI---TFKKPH------ILLLDEPSNHLDLD---AVEALIQG 669
|
170 180 190
....*....|....*....|....*....|...
gi 743522756 194 LAGRNTAVLVVLHDLNLAARYADRLVMLEQGRL 226
Cdd:PLN03073 670 LVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
34-231 |
7.41e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.96 E-value: 7.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSsslsfPFLCEEVV----AMGRlp 108
Cdd:PRK10789 341 GQMLGICGPTGSGKSTLLSLIQRHFDvSEGDIRFHDIPLTKLQLDSWRSRLAVVSQT-----PFLFSDTVanniALGR-- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 hsePASRRDEIVRAAmthagvdHLAN------RLYPG-----------LSGGERQRVQFARVLAqiwqapeepQQARLLL 171
Cdd:PRK10789 414 ---PDATQQEIEHVA-------RLASvhddilRLPQGydtevgergvmLSGGQKQRISIARALL---------LNAEILI 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 172 LDEPTSALDLKYQHQLLAMARALaGRNTAVLVVLHDLNlAARYADRLVMLEQGRLMADGN 231
Cdd:PRK10789 475 LDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGN 532
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
34-180 |
1.15e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.80 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQT----RRGWAGNAlAHRVGVLpQSSSLSFPFLCEEVVAMGRLP 108
Cdd:TIGR00957 664 GALVAVVGQVGCGKSSLLSALLAEMDKvEGHVHMKGSVayvpQQAWIQND-SLRENIL-FGKALNEKYYQQVLEACALLP 741
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743522756 109 HSE--PASRRDEIvraamTHAGVDhlanrlypgLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALD 180
Cdd:TIGR00957 742 DLEilPSGDRTEI-----GEKGVN---------LSGGQKQRVSLARAVY---------SNADIYLFDDPLSAVD 792
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
140-231 |
1.22e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 57.48 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 140 LSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQHQLLAMARALA-GRNTAVLVVLHDLNLAARYADRL 218
Cdd:PRK13646 146 MSGGQMRKIAIVSILAM------NPD---IIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEV 216
|
90
....*....|...
gi 743522756 219 VMLEQGRLMADGN 231
Cdd:PRK13646 217 IVMKEGSIVSQTS 229
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
6-221 |
1.23e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 57.03 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 6 SPLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVG 84
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISpTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 85 VLPQSSSL---------SFPFLCeevvamgRLPHSEPASRRDEIVRAAMThagvDHLANRLYPGLSGGERQRVQFARVLA 155
Cdd:PRK10247 85 YCAQTPTLfgdtvydnlIFPWQI-------RNQQPDPAIFLDDLERFALP----DTILTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 156 QIwqapeepqqARLLLLDEPTSALDLKYQHQLLAMARALA-GRNTAVLVVLHDLNlAARYADRLVML 221
Cdd:PRK10247 154 FM---------PKVLLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHDKD-EINHADKVITL 210
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-224 |
2.31e-09 |
|
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: 55.71 E-value: 2.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELEH---EGEIHLFGQTRrgwaGNALAHRVGVLPQsSSLSFPFLceevvamgrlphs 110
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAGRKTAgviTGEILINGRPL----DKNFQRSTGYVEQ-QDVHSPNL------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 epasrrdeIVRAAMTHagvdHLANRlypGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQHQLLAM 190
Cdd:cd03232 95 --------TVREALRF----SALLR---GLSVEQRKRLTIGVELAA------KPS---ILFLDEPTSGLDSQAAYNIVRF 150
|
170 180 190
....*....|....*....|....*....|....*
gi 743522756 191 ARALAGRNTAVLVVLHDLNLAA-RYADRLVMLEQG 224
Cdd:cd03232 151 LKKLADSGQAILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
33-237 |
2.82e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 56.73 E-value: 2.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGeLEH--EGEIHLFGQ--TRRGWAGNALAHR-VGVLPQ-----SSSLSFpflceEVV 102
Cdd:PRK11153 30 AGEIFGVIGASGAGKSTLIRCINL-LERptSGRVLVDGQdlTALSEKELRKARRqIGMIFQhfnllSSRTVF-----DNV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 103 AM----GRLPHSEPASRRDE---IVraamthaGVDHLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPQqarLLLLDE 174
Cdd:PRK11153 104 ALplelAGTPKAEIKARVTElleLV-------GLSDKADR-YPAqLSGGQKQRVAIARALAS------NPK---VLLCDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 175 PTSALDLKYQHQLLAMaraLAGRN-----TAVLVVlHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:PRK11153 167 ATSALDPATTRSILEL---LKDINrelglTIVLIT-HEMDVVKRICDRVAVIDAGRLVEQGTVSEVFS 230
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
36-230 |
3.36e-09 |
|
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: 57.33 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 36 LTALLGPNGAGKSSLLKCLTGELEHEGEIHLFGQTRRGWAGNALAHRVGVLPQSSSLsFPFL--CEEVVAMGRLPHSEPA 113
Cdd:TIGR01257 958 ITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNIL-FHHLtvAEHILFYAQLKGRSWE 1036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 114 SRRDEIvRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQLL-AMAR 192
Cdd:TIGR01257 1037 EAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFV---------GDAKVVVLDEPTSGVDPYSRRSIWdLLLK 1106
|
170 180 190
....*....|....*....|....*....|....*...
gi 743522756 193 ALAGRntAVLVVLHDLNLAARYADRLVMLEQGRLMADG 230
Cdd:TIGR01257 1107 YRSGR--TIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
139-241 |
4.25e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 56.01 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 139 GLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRL 218
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAI---------QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEV 246
|
90 100
....*....|....*....|...
gi 743522756 219 VMLEQGRLMADGNAGEVLTPELI 241
Cdd:PRK13631 247 IVMDKGKILKTGTPYEIFTDQHI 269
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-181 |
5.79e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 5.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 2 PGSPSPLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQ----TRRGWAG 76
Cdd:PRK13543 5 LHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVEsGQIQIDGKtatrGDRSRFM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 77 NALAHRVGVLPQSSSL-SFPFLCEevvAMGRLPHSEPASrrdeivraAMTHAGVDHLANRLYPGLSGGERQRVQfarvLA 155
Cdd:PRK13543 85 AYLGHLPGLKADLSTLeNLHFLCG---LHGRRAKQMPGS--------ALAIVGLAGYEDTLVRQLSAGQKKRLA----LA 149
|
170 180
....*....|....*....|....*.
gi 743522756 156 QIWQAPeepqqARLLLLDEPTSALDL 181
Cdd:PRK13543 150 RLWLSP-----APLWLLDEPYANLDL 170
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
40-243 |
7.43e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 7.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 40 LGPNGAGKSSLLKCLTGELE-HEGEIHLFGQ--------TRRgwagnalahRVGVLPQSSSLSfpflcEEV------VAM 104
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPaSEGEAWLFGQpvdagdiaTRR---------RVGYMSQAFSLY-----GELtvrqnlELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 105 GRLPHSePASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFArvlAQIWQAPEepqqarLLLLDEPTS-----AL 179
Cdd:NF033858 364 ARLFHL-PAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLA---VAVIHKPE------LLILDEPTSgvdpvAR 433
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 180 DLKYQHqLLAMARalaGRNTAVLVVLHDLNLAARyADRLvmleqgRLMadgNAGEVL---TP-ELIAR 243
Cdd:NF033858 434 DMFWRL-LIELSR---EDGVTIFISTHFMNEAER-CDRI------SLM---HAGRVLasdTPaALVAA 487
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
39-194 |
7.87e-09 |
|
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: 53.70 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 39 LLGPNGAGKSSLLKCL-------TGELE-HEGEIHLFgqtrrgwagnalahrvgvLPQSsslsfPFLCEevvamGRLphs 110
Cdd:cd03223 32 ITGPSGTGKSSLFRALaglwpwgSGRIGmPEGEDLLF------------------LPQR-----PYLPL-----GTL--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 epasrRDEIVraamthagvdhlanrlYP---GLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQL 187
Cdd:cd03223 81 -----REQLI----------------YPwddVLSGGEQQRLAFARLLL---------HKPKFVFLDEATSALDEESEDRL 130
|
....*..
gi 743522756 188 LAMARAL 194
Cdd:cd03223 131 YQLLKEL 137
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
32-219 |
8.08e-09 |
|
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: 53.52 E-value: 8.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLtgelehegeihlfgqtrrGWAgnalahrvgvlpqssslsfpflceEVVAMGRLPHSE 111
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTILDAI------------------GLA------------------------LGGAQSATRRRS 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAAMTHAGVDHlanrlypGLSGGERQRVQFARVLAQiwqapEEPQQARLLLLDEPTSALDLKYQHQLLAMA 191
Cdd:cd03227 57 GVKAGCIVAAVSAELIFTRL-------QLSGGEKELSALALILAL-----ASLKPRPLYILDEIDRGLDPRDGQALAEAI 124
|
170 180
....*....|....*....|....*...
gi 743522756 192 RALAGRNTAVLVVLHDLNLAARyADRLV 219
Cdd:cd03227 125 LEHLVKGAQVIVITHLPELAEL-ADKLI 151
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
32-225 |
9.39e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 9.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH---EGEIHLFGQTRRgWAGNALAHRVGV------LPQSSSLSFP---FLCE 99
Cdd:NF040905 25 REGEIHALCGENGAGKSTLMKVLSGVYPHgsyEGEILFDGEVCR-FKDIRDSEALGIviihqeLALIPYLSIAeniFLGN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 100 EVVAMGRLPHSEPASRRDEIvraaMTHAGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSAL 179
Cdd:NF040905 104 ERAKRGVIDWNETNRRAREL----LAKVGLDESPDTLVTDIGVGKQQLVEIAKALS---------KDVKLLILDEPTAAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 743522756 180 DLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGR 225
Cdd:NF040905 171 NEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
34-242 |
1.42e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQ-TRRGWAGNALAHRVGVLPQSSSLSFPFLCEEVVAMGRLPHSE 111
Cdd:PRK10982 24 HSIHALMGENGAGKSTLLKCLFGIYQkDSGSILFQGKeIDFKSSKEALENGISMVHQELNLVLQRSVMDNMWLGRYPTKG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEIVRAamTHAGVDHLANRLYP-----GLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQ 186
Cdd:PRK10982 104 MFVDQDKMYRD--TKAIFDELDIDIDPrakvaTLSVSQMQMIEIAKAFS---------YNAKIVIMDEPTSSLTEKEVNH 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 743522756 187 LLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIA 242
Cdd:PRK10982 173 LFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIA 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
44-244 |
1.48e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 55.03 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 44 GAGKSSLLKCLTGELEHE-GEIHLFGQTRRGW-AGNALAHRVGVLPQ---------SSSLSfpflceEVVAMGRLpHSEP 112
Cdd:COG3845 294 GNGQSELAEALAGLRPPAsGSIRLDGEDITGLsPRERRRLGVAYIPEdrlgrglvpDMSVA------ENLILGRY-RRPP 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 113 ASRRDEIVRAAMthagvDHLANRL-------YPG-------LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSA 178
Cdd:COG3845 367 FSRGGFLDRKAI-----RAFAEELieefdvrTPGpdtparsLSGGNQQKVILARELS---------RDPKLLIAAQPTRG 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 743522756 179 LDLK---YQHQLLAMARAlagRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVlTPELIARL 244
Cdd:COG3845 433 LDVGaieFIHQRLLELRD---AGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA-TREEIGLL 497
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
34-235 |
1.83e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 54.98 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELEHEGEIHLfgqTRRGwagnalahRVGVLPQSSSLsFPFLCEEVVAMGRlpHSEPA 113
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAMLGELSHAETSSV---VIRG--------SVAYVPQVSWI-FNATVRENILFGS--DFESE 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 114 SRRDEIVRAAMTHaGVDhlanrLYPG------------LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDL 181
Cdd:PLN03232 709 RYWRAIDVTALQH-DLD-----LLPGrdlteigergvnISGGQKQRVSMARAVY---------SNSDIYIFDDPLSALDA 773
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 743522756 182 KYQHQLL--AMARALAGRnTAVLVV--LHDLNLaaryADRLVMLEQGRLMADGNAGEV 235
Cdd:PLN03232 774 HVAHQVFdsCMKDELKGK-TRVLVTnqLHFLPL----MDRIILVSEGMIKEEGTFAEL 826
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
34-237 |
3.35e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 53.07 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAG-NALAHRVGVLPQSSSLSF-PFLCEEVVAMGR---- 106
Cdd:PRK13644 28 GEYIGIIGKNGSGKSTLALHLNGLLRpQKGKVLVSGIDTGDFSKlQGIRKLVGIVFQNPETQFvGRTVEEDLAFGPenlc 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 107 LPHSEPASRRDEivraAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQHQ 186
Cdd:PRK13644 108 LPPIEIRKRVDR----ALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTM------EPE---CLIFDEVTSMLDPDSGIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 743522756 187 LLAMARALAGRNTAVLVVLHDLNlAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:PRK13644 175 VLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
34-224 |
3.41e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 3.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELEH---EGEIHLFG--------QTRRGWAGNALAHrvgvLPQSS---SLSFPflce 99
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNgrpldssfQRSIGYVQQQDLH----LPTSTvreSLRFS---- 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 100 evvAMGRLPHSEPASRRDEIVRAAMTHAGVDHLANRLY----PGLSGGERQRVQFARVLAQiwqapeepQQARLLLLDEP 175
Cdd:TIGR00956 861 ---AYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVA--------KPKLLLFLDEP 929
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 743522756 176 TSALDLKYQHQLLAMARALAGRNTAVLVVLH--DLNLAARYaDRLVMLEQG 224
Cdd:TIGR00956 930 TSGLDSQTAWSICKLMRKLADHGQAILCTIHqpSAILFEEF-DRLLLLQKG 979
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
32-229 |
3.42e-08 |
|
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: 3.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELE--HEGEIHLFGQ---TRRgwAGNALAHRVGVLPQ------------------ 88
Cdd:TIGR02633 284 RRGEILGVAGLVGAGRTELVQALFGAYPgkFEGNVFINGKpvdIRN--PAQAIRAGIAMVPEdrkrhgivpilgvgknit 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 89 -SSSLSFPFLceevvamGRLPhsepASRRDEIVRAAMTHAGVDHLANRL-YPGLSGGERQRVQFARVLAQiwqapeepqQ 166
Cdd:TIGR02633 362 lSVLKSFCFK-------MRID----AAAELQIIGSAIQRLKVKTASPFLpIGRLSGGNQQKAVLAKMLLT---------N 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 167 ARLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMAD 229
Cdd:TIGR02633 422 PRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
8-235 |
3.59e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 52.85 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 8 LLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGWAGNAL---AHRV 83
Cdd:PRK11831 7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDhGEILFDGENIPAMSRSRLytvRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 84 GVLPQSSSLSFPFLCEEVVAMGRLPHSE-PASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFARVLAQiwqape 162
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDNVAYPLREHTQlPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIAL------ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 743522756 163 EPQqarLLLLDEPTSALDLKYQHQLLAMARALagrNTAV----LVVLHDLNLAARYADRLVMLEQGRLMADGNAGEV 235
Cdd:PRK11831 161 EPD---LIMFDEPFVGQDPITMGVLVKLISEL---NSALgvtcVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
137-237 |
3.88e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 53.37 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 137 YP-GLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLamaRALAG----RNTAVLVVLHDLNLA 211
Cdd:COG4170 155 YPhELTEGECQKVMIAMAIAN---------QPRLLIADEPTNAMESTTQAQIF---RLLARlnqlQGTSILLISHDLESI 222
|
90 100
....*....|....*....|....*.
gi 743522756 212 ARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:COG4170 223 SQWADTITVLYCGQTVESGPTEQILK 248
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
33-210 |
5.77e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.87 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQT----RRGWAGNA--LAHRVGVlpqssslsFPFLCEEVVAMG 105
Cdd:PRK13540 26 AGGLLHLKGSNGAGKTTLLKLIAGLLNPEkGEILFERQSikkdLCTYQKQLcfVGHRSGI--------NPYLTLRENCLY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 106 RLPHSEPASRRDEIVRAamthAGVDHLANrlYPG--LSGGERQRVQFARvlaqIWQApeepqQARLLLLDEPTSALDLKY 183
Cdd:PRK13540 98 DIHFSPGAVGITELCRL----FSLEHLID--YPCglLSSGQKRQVALLR----LWMS-----KAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|....*...
gi 743522756 184 QHQLLAMARALAGRNTAVLVVLH-DLNL 210
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSHqDLPL 190
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
34-222 |
6.34e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.03 E-value: 6.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELEHEGEihlfgqtRRGWAGNalahRVGVLPQssslsfpflceevvamgrlphsepa 113
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGD-------NDEWDGI----TPVYKPQ------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 114 srrdeivraamthagvdhlanrlYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKyqhQLLAMARA 193
Cdd:cd03222 69 -----------------------YIDLSGGELQRVAIAAALL---------RNATFYLFDEPSAYLDIE---QRLNAARA 113
|
170 180 190
....*....|....*....|....*....|....
gi 743522756 194 L-----AGRNTAvLVVLHDLNLAARYADRLVMLE 222
Cdd:cd03222 114 IrrlseEGKKTA-LVVEHDLAVLDYLSDRIHVFE 146
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
32-219 |
6.39e-08 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 51.89 E-value: 6.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTgelehegeIHLFGQTRRgwAGNALAHRVGVLP--QSSSLSFPF-LCEEVVAMGRLP 108
Cdd:cd03279 26 DNNGLFLICGPTGAGKSTILDAIT--------YALYGKTPR--YGRQENLRSVFAPgeDTAEVSFTFqLGGKKYRVERSR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSEpasrRDEIVRAAMTHAG-VDHLANRLYPGLSGGERQRVQFARVLA---QIWQAPEEPQQArlLLLDEPTSALDLKYQ 184
Cdd:cd03279 96 GLD----YDQFTRIVLLPQGeFDRFLARPVSTLSGGETFLASLSLALAlseVLQNRGGARLEA--LFIDEGFGTLDPEAL 169
|
170 180 190
....*....|....*....|....*....|....*
gi 743522756 185 HQLLAMARALAGRNTAVLVVLHDLNLAARYADRLV 219
Cdd:cd03279 170 EAVATALELIRTENRMVGVISHVEELKERIPQRLE 204
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
99-237 |
7.85e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.43 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 99 EEVVAMGR---LPHSEPASRRDEIV-RAAMTHAgvdhlANRLYPGLSGGERQRVQFArvlAQIWQAPEepqqarLLLLDE 174
Cdd:NF000106 105 ENLYMIGR*ldLSRKDARARADELLeRFSLTEA-----AGRAAAKYSGGMRRRLDLA---ASMIGRPA------VLYLDE 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 175 PTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
112-261 |
7.90e-08 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.40 E-value: 7.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 112 PASRRDEI---VRAAMTHAGV-DHLANRlYPG-LSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALDLKYQHQ 186
Cdd:PRK15079 130 PKLSRQEVkdrVKAMMLKVGLlPNLINR-YPHeFSGGQCQRIGIARALIL------EP---KLIICDEPVSALDVSIQAQ 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 187 LLAMARALAGRNTAVLV-VLHDLNLAARYADR-LVMLEqgrlmadGNAGEVLTPEliaRLYDYPaqviHHPE-----SGV 259
Cdd:PRK15079 200 VVNLLQQLQREMGLSLIfIAHDLAVVKHISDRvLVMYL-------GHAVELGTYD---EVYHNP----LHPYtkalmSAV 265
|
..
gi 743522756 260 PM 261
Cdd:PRK15079 266 PI 267
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
32-239 |
8.37e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFGQTRRgWAGNALAHRVGVLpqssslsfpfLC-EEVVAMGRLPH 109
Cdd:PRK11288 277 RAGEIVGLFGLVGAGRSELMKLLYGaTRRTAGQVYLDGKPID-IRSPRDAIRAGIM----------LCpEDRKAEGIIPV 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 110 sepASRRDEI---VRAAMTHAGV-----------DHLANRL---YPG-------LSGGERQRVQFARVLAQiwqapeepq 165
Cdd:PRK11288 346 ---HSVADNInisARRHHLRAGClinnrweaenaDRFIRSLnikTPSreqlimnLSGGNQQKAILGRWLSE--------- 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743522756 166 QARLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLmadgnAGEVLTPE 239
Cdd:PRK11288 414 DMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI-----AGELAREQ 482
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
34-224 |
9.78e-08 |
|
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: 51.18 E-value: 9.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHlFGQTRRGWAGNALAHRVGVLPQSSSLSFPFL----CEEVVAMGRlP 108
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQTlEGKVH-WSNKNESEPSFEATRSRNRYSVAYAAQKPWLlnatVEENITFGS-P 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 HSEpaSRRDEIVRAAMTHAGVDHL--ANRLYPG-----LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDL 181
Cdd:cd03290 105 FNK--QRYKAVTDACSLQPDIDLLpfGDQTEIGerginLSGGQRQRICVARALY---------QNTNIVFLDDPFSALDI 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 743522756 182 KYQHQLL--AMARALAGRNTAVLVVLHDLNLAArYADRLVMLEQG 224
Cdd:cd03290 174 HLSDHLMqeGILKFLQDDKRTLVLVTHKLQYLP-HADWIIAMKDG 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
137-235 |
1.29e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.17 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 137 YP-GLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARY 214
Cdd:PRK10261 165 YPhQLSGGMRQRVMIAMALSC---------RPAVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEI 235
|
90 100
....*....|....*....|.
gi 743522756 215 ADRLVMLEQGRLMADGNAGEV 235
Cdd:PRK10261 236 ADRVLVMYQGEAVETGSVEQI 256
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
113-235 |
1.36e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.50 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 113 ASRRDEIVRAAMTHAGV--DHlANRlYPGL-SGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLL- 188
Cdd:PRK11308 127 AAERREKALAMMAKVGLrpEH-YDR-YPHMfSGGQRQRIAIARALML---------DPDVVVADEPVSALDVSVQAQVLn 195
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 743522756 189 AMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEV 235
Cdd:PRK11308 196 LMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-207 |
1.60e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 38 ALLGPNGAGKSSLLKCLTGELEHE-GEIHL--------FGQtrrgwagnalaHRVGVLPQSSslsfpflCEEVVAMGrlp 108
Cdd:PRK11147 349 ALIGPNGCGKTTLLKLMLGQLQADsGRIHCgtklevayFDQ-----------HRAELDPEKT-------VMDNLAEG--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 109 hsepasRRDEIVRAAMTHAgVDHLANRLYP---------GLSGGERQRVQFARVLAQiwqaPeepqqARLLLLDEPTSAL 179
Cdd:PRK11147 408 ------KQEVMVNGRPRHV-LGYLQDFLFHpkramtpvkALSGGERNRLLLARLFLK----P-----SNLLILDEPTNDL 471
|
170 180
....*....|....*....|....*...
gi 743522756 180 DLKYQHQLLAMaraLAGRNTAVLVVLHD 207
Cdd:PRK11147 472 DVETLELLEEL---LDSYQGTVLLVSHD 496
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
34-244 |
1.72e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.09 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIhlfgqtrrgWAGNALAHrvgvLPQSsslsfPFLCEEVVAMGRLPHSEP 112
Cdd:PTZ00243 686 GKLTVVLGATGSGKSTLLQSLLSQFEiSEGRV---------WAERSIAY----VPQQ-----AWIMNATVRGNILFFDEE 747
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 113 -ASRRDEIVRAAMTHAGVDHLANRLYP-------GLSGGERQRVQFAR-VLAqiwqapeepqQARLLLLDEPTSALDLKY 183
Cdd:PTZ00243 748 dAARLADAVRVSQLEADLAQLGGGLETeigekgvNLSGGQKARVSLARaVYA----------NRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 184 QHQLL--AMARALAGRnTAVLVVlHDLNLAARyADRLVMLEQGRLMADGNAGEVLTPELIARL 244
Cdd:PTZ00243 818 GERVVeeCFLGALAGK-TRVLAT-HQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTSLYATL 877
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
135-237 |
1.73e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.34 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 135 RLYP-GLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLAM-ARALAGRNTAVLVVLHDLNLAA 212
Cdd:PRK15093 153 RSFPyELTEGECQKVMIAIALAN---------QPRLLIADEPTNAMEPTTQAQIFRLlTRLNQNNNTTILLISHDLQMLS 223
|
90 100
....*....|....*....|....*
gi 743522756 213 RYADRLVMLEQGRLMADGNAGEVLT 237
Cdd:PRK15093 224 QWADKINVLYCGQTVETAPSKELVT 248
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
33-225 |
1.94e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 50.34 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEH----EGEIHL-------FGQTRRGWA--GNALAHRVGVLPQSSSLSFPFLCe 99
Cdd:cd03233 32 PGEMVLVLGRPGSGCSTLLKALANRTEGnvsvEGDIHYngipykeFAEKYPGEIiyVSEEDVHFPTLTVRETLDFALRC- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 100 evvamgrlphsepasRRDEIVRaamthagvdhlanrlypGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSAL 179
Cdd:cd03233 111 ---------------KGNEFVR-----------------GISGGERKRVSIAEALV---------SRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 743522756 180 D----LKYQHQLLAMARALagRNTAVLVVLHDLNLAARYADRLVMLEQGR 225
Cdd:cd03233 150 DsstaLEILKCIRTMADVL--KTTTFVSLYQASDEIYDLFDKVLVLYEGR 197
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
139-244 |
1.94e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.59 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 139 GLSGGERQRVQFARVLAQiwqAPeepqqaRLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRL 218
Cdd:PRK15439 403 TLSGGNQQKVLIAKCLEA---SP------QLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRV 473
|
90 100
....*....|....*....|....*.
gi 743522756 219 VMLEQGRLmADGNAGEVLTPELIARL 244
Cdd:PRK15439 474 LVMHQGEI-SGALTGAAINVDTIMRL 498
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
34-235 |
2.07e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 50.86 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGEL-EHEGEIHLFG----QTRRGWAgnaLAHRVGVLPQSSSLSF-PFLCEEVVAMGR- 106
Cdd:PRK13633 36 GEFLVILGRNGSGKSTIAKHMNALLiPSEGKVYVDGldtsDEENLWD---IRNKAGMVFQNPDNQIvATIVEEDVAFGPe 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 107 ---LPHSEPASRRDEIVRAamthagVDHLANRLYPG--LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDL 181
Cdd:PRK13633 113 nlgIPPEEIRERVDESLKK------VGMYEYRRHAPhlLSGGQKQRVAIAGILA---------MRPECIIFDEPTAMLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 743522756 182 KYQHQLLAMARALAGR-NTAVLVVLHDLNLAARyADRLVMLEQGRLMADGNAGEV 235
Cdd:PRK13633 178 SGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
124-235 |
2.10e-07 |
|
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: 51.34 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 124 MTHAGVDhlanrlypgLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLV 203
Cdd:TIGR03269 162 ITHIARD---------LSGGEKQRVVLARQLAK------EPF---LFLADEPTGTLDPQTAKLVHNALEEAVKASGISMV 223
|
90 100 110
....*....|....*....|....*....|...
gi 743522756 204 VL-HDLNLAARYADRLVMLEQGRLMADGNAGEV 235
Cdd:TIGR03269 224 LTsHWPEVIEDLSDKAIWLENGEIKEEGTPDEV 256
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
8-212 |
2.36e-07 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.80 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 8 LLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRG----------Wag 76
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARpDAGEVLWQGEPIRRqrdeyhqdllY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 77 naLAHRVGVLPQSSSL-SFPFLCeevvamgrlPHSEPASrrDEIVRAAMTH---AGVDHLANRLypgLSGGERQRVQFAR 152
Cdd:PRK13538 79 --LGHQPGIKTELTALeNLRFYQ---------RLHGPGD--DEALWEALAQvglAGFEDVPVRQ---LSAGQQRRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743522756 153 vlaqIWQApeepqQARLLLLDEPTSALDLKYQHQLLA-MARALAGRNTAVLVVLHDLNLAA 212
Cdd:PRK13538 143 ----LWLT-----RAPLWILDEPFTAIDKQGVARLEAlLAQHAEQGGMVILTTHQDLPVAS 194
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
32-231 |
3.06e-07 |
|
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: 49.80 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGELEH-EGEIHLFGQTRRGWAGNALAHRVGVLPQSsslsfPFLCEEVVAMGRLPHS 110
Cdd:cd03244 28 KPGEKVGIVGRTGSGKSSLLLALFRLVELsSGSILIDGVDISKIGLHDLRSRISIIPQD-----PVLFSGTIRSNLDPFG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 EPAsrrDEIVRAAMTHAGVDHLANRLYPGL-----------SGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSAL 179
Cdd:cd03244 103 EYS---DEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALL---------RKSKILVLDEATASV 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 743522756 180 DLKYQHQLLAMARAlAGRNTAVLVVLHDLNLAARYaDRLVMLEQGRLMADGN 231
Cdd:cd03244 171 DPETDALIQKTIRE-AFKDCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDS 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
33-226 |
3.36e-07 |
|
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: 49.72 E-value: 3.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQssslsfpflcEEVVAMGRL---- 107
Cdd:cd03369 33 AGEKIGIVGRTGAGKSTLILALFRFLEaEEGKIEIDGIDISTIPLEDLRSSLTIIPQ----------DPTLFSGTIrsnl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 108 -PHSEpasRRDEIVRAAM--THAGVDhlanrlypgLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQ 184
Cdd:cd03369 103 dPFDE---YSDEEIYGALrvSEGGLN---------LSQGQRQLLCLARALL---------KRPRVLVLDEATASIDYATD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 743522756 185 HQLLAMARALAgRNTAVLVVLHDLNLAARYaDRLVMLEQGRL 226
Cdd:cd03369 162 ALIQKTIREEF-TNSTILTIAHRLRTIIDY-DKILVMDAGEV 201
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
140-251 |
3.86e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 50.01 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 140 LSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLAM-ARALAGRNTAVLVVLHDLNLAARYADRL 218
Cdd:PRK13645 151 LSGGQKRRVALAGIIAM---------DGNTLVLDEPTGGLDPKGEEDFINLfERLNKEYKKRIIMVTHNMDQVLRIADEV 221
|
90 100 110
....*....|....*....|....*....|....
gi 743522756 219 VMLEQGRLMADGNAGEVLT-PELIARLYDYPAQV 251
Cdd:PRK13645 222 IVMHEGKVISIGSPFEIFSnQELLTKIEIDPPKL 255
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
34-224 |
4.06e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.68 E-value: 4.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGqtrrgwagnalahRVGVLPQSSSLsFPFLCEEVVAMGrLPHSEp 112
Cdd:TIGR01271 452 GQLLAVAGSTGSGKSSLLMMIMGELEpSEGKIKHSG-------------RISFSPQTSWI-MPGTIKDNIIFG-LSYDE- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 113 aSRRDEIVRAAMTHAGVDHLANR----LYPG---LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQH 185
Cdd:TIGR01271 516 -YRYTSVIKACQLEEDIALFPEKdktvLGEGgitLSGGQRARISLARAVY---------KDADLYLLDSPFTHLDVVTEK 585
|
170 180 190
....*....|....*....|....*....|....*....
gi 743522756 186 QLLAMARALAGRNTAVLVVLHDLNLAARyADRLVMLEQG 224
Cdd:TIGR01271 586 EIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEG 623
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
33-207 |
4.15e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 50.70 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHL--------FGQTRRGWAGNalaHRVGvlpqssslsfpflceEVVA 103
Cdd:TIGR03719 347 PGGIVGVIGPNGAGKSTLFRMITGqEQPDSGTIEIgetvklayVDQSRDALDPN---KTVW---------------EEIS 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 104 MG----RLPHSEPASRRdeiVRAAMTHAGVDHlaNRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSAL 179
Cdd:TIGR03719 409 GGldiiKLGKREIPSRA---YVGRFNFKGSDQ--QKKVGQLSGGERNRVHLAKTLK---------SGGNVLLLDEPTNDL 474
|
170 180
....*....|....*....|....*...
gi 743522756 180 DLkyqHQLLAMARALAGRNTAVLVVLHD 207
Cdd:TIGR03719 475 DV---ETLRALEEALLNFAGCAVVISHD 499
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
140-249 |
4.88e-07 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 49.84 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 140 LSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSALDLKYQHQLLAMARALAGR-NTAVLVVLHDLNLAARYADRL 218
Cdd:PRK11650 135 LSGGQRQRVAMGRAIVR------EPA---VFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRV 205
|
90 100 110
....*....|....*....|....*....|.
gi 743522756 219 VMLEQGRLMADGNAGEVltpeliarlYDYPA 249
Cdd:PRK11650 206 VVMNGGVAEQIGTPVEV---------YEKPA 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
34-180 |
5.07e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.19 E-value: 5.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELehegeihlfgqtrrgwagnalahrvgvlpqssslsfpfLCEEVVAMGRLPHSEPA 113
Cdd:COG2401 56 GEIVLIVGASGSGKSTLLRLLAGAL--------------------------------------KGTPVAGCVDVPDNQFG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 114 SRR---DEIVRAAMTHAGVDHLAN----------RLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALD 180
Cdd:COG2401 98 REAsliDAIGRKGDFKDAVELLNAvglsdavlwlRRFKELSTGQKFRFRLALLLA---------ERPKLLVIDEFCSHLD 168
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-224 |
1.21e-06 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 49.63 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 2 PGSPSPLLS--CRGLRlsrgnrlildsldldlhAGSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNa 78
Cdd:TIGR01257 1948 SGTSSPAVDrlCVGVR-----------------PGECFGLLGVNGAGKTTTFKMLTGDTTvTSGDATVAGKSILTNISD- 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 79 LAHRVGVLPQSSSLSFPFLCEEVVAMGRLPHSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQRVQFArvLAQIW 158
Cdd:TIGR01257 2010 VHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTA--IALIG 2087
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743522756 159 QAPeepqqarLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQG 224
Cdd:TIGR01257 2088 CPP-------LVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
34-224 |
2.27e-06 |
|
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: 47.93 E-value: 2.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGqtrrgwagnalahRVGVLPQSSSLsFPFLCEEVVAMGrLPHSEp 112
Cdd:cd03291 63 GEMLAITGSTGSGKTSLLMLILGELEpSEGKIKHSG-------------RISFSSQFSWI-MPGTIKENIIFG-VSYDE- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 113 aSRRDEIVRAAMTHAGVDHLANR----LYPG---LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQH 185
Cdd:cd03291 127 -YRYKSVVKACQLEEDITKFPEKdntvLGEGgitLSGGQRARISLARAVY---------KDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 743522756 186 QLL-AMARALAGRNTAVLVVLHDLNLaaRYADRLVMLEQG 224
Cdd:cd03291 197 EIFeSCVCKLMANKTRILVTSKMEHL--KKADKILILHEG 234
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
39-239 |
3.07e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 3.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 39 LLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGWAGNALAHRVGVLPQSsslsfPFLCEEVVAMGRLPHSEpasRRD 117
Cdd:PLN03232 1267 VVGRTGAGKSSMLNALFRIVELEkGRIMIDDCDVAKFGLTDLRRVLSIIPQS-----PVLFSGTVRFNIDPFSE---HND 1338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 118 EIVRAAMTHAGVDHLANRLYPGL-----------SGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQ 186
Cdd:PLN03232 1339 ADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALL---------RRSKILVLDEATASVDVRTDSL 1409
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 743522756 187 LLAMARAlAGRNTAVLVVLHDLNLAARyADRLVMLEQGRLMADGNAGEVLTPE 239
Cdd:PLN03232 1410 IQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
33-180 |
5.14e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.60 E-value: 5.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEHEGEIHLFGQTRRGWAGNALAHRVGVLPQSSslsfpFLCEEVVAMGRLPHSEP 112
Cdd:TIGR01271 1244 GGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKV-----FIFSGTFRKNLDPYEQW 1318
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 743522756 113 ASRR-----DEIVRAAMTHAGVDHLANRLYPG---LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALD 180
Cdd:TIGR01271 1319 SDEEiwkvaEEVGLKSVIEQFPDKLDFVLVDGgyvLSNGHKQLMCLARSIL---------SKAKILLLDEPSAHLD 1385
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
134-236 |
7.49e-06 |
|
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: 45.01 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 134 NRLYPGLSGGERQRVQFARVLAQiwqapeePQQARLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLaAR 213
Cdd:cd03238 82 GQKLSTLSGGELQRVKLASELFS-------EPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDV-LS 153
|
90 100
....*....|....*....|...
gi 743522756 214 YADRLVMLEQGrlmADGNAGEVL 236
Cdd:cd03238 154 SADWIIDFGPG---SGKSGGKVV 173
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
33-230 |
8.91e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 46.65 E-value: 8.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEHEGEIHLfgqTRRGwagnalahRVGVLPQSSSLsFPFLCEEVVAMGrLPHSep 112
Cdd:PLN03130 642 VGSLVAIVGSTGEGKTSLISAMLGELPPRSDASV---VIRG--------TVAYVPQVSWI-FNATVRDNILFG-SPFD-- 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 113 ASRRDEIVRAAMTHAGVDhlanrLYPG------------LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALD 180
Cdd:PLN03130 707 PERYERAIDVTALQHDLD-----LLPGgdlteigergvnISGGQKQRVSMARAVY---------SNSDVYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 743522756 181 LKYQHQLL--AMARALAGRnTAVLVV--LHDLNlaarYADRLVMLEQGRLMADG 230
Cdd:PLN03130 773 AHVGRQVFdkCIKDELRGK-TRVLVTnqLHFLS----QVDRIILVHEGMIKEEG 821
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
102-210 |
1.17e-05 |
|
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: 45.84 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 102 VAMGRLPHSEPASRRDEIVRAAMTHAGVDHLANRLYPGLSGGERQrvqFARVLAQIWQAPEEPqqaRLLLLDEPTSALDL 181
Cdd:pfam13304 199 LSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKR---LLALLAALLSALPKG---GLLLIDEPESGLHP 272
|
90 100
....*....|....*....|....*....
gi 743522756 182 KYQHQLLAMARALAGRNTAVLVVLHDLNL 210
Cdd:pfam13304 273 KLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
34-225 |
1.56e-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: 43.90 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLtgelehegeihlfgqtrrgwAGNALAHRVGVLpqssslsfpflceeVVAMGRLPHSEPA 113
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARAL--------------------ARELGPPGGGVI--------------YIDGEDILEEVLD 47
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 114 SRRDEIVraamthagvdhlaNRLYPGLSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLAMARA 193
Cdd:smart00382 48 QLLLIIV-------------GGKKASGSGELRLRLALALARKL---------KPDVLILDEITSLLDAEQEALLLLLEEL 105
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 743522756 194 LAG------RNTAVLVVLHDLN-----LAARYADRLVMLEQGR 225
Cdd:smart00382 106 RLLlllkseKNLTVILTTNDEKdlgpaLLRRRFDRRIVLLLIL 148
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
140-207 |
2.00e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.49 E-value: 2.00e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743522756 140 LSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLkyqHQLLAMARAL---AGrntAVLVVLHD 207
Cdd:PRK11819 446 LSGGERNRLHLAKTLK---------QGGNVLLLDEPTNDLDV---ETLRALEEALlefPG---CAVVISHD 501
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
124-230 |
2.38e-05 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 44.17 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 124 MTHAGVDHLA-NRLYPGLSGGERQRVqfaRVLAQIwqapEEPQQARLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVL 202
Cdd:cd03270 121 LVDVGLGYLTlSRSAPTLSGGEAQRI---RLATQI----GSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVL 193
|
90 100 110
....*....|....*....|....*....|....
gi 743522756 203 VVLHDLNLaARYADRLVML------EQGRLMADG 230
Cdd:cd03270 194 VVEHDEDT-IRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
32-260 |
2.85e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 2.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 32 HAGSLTALLGPNGAGKSSLLKCLTGEL-EHEGEIHlfGQTRRGW--AGNALAHRVGVLPQSSS---LS-----FPFLCEE 100
Cdd:PRK10938 27 NAGDSWAFVGANGSGKSALARALAGELpLLSGERQ--SQFSHITrlSFEQLQKLVSDEWQRNNtdmLSpgeddTGRTTAE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 101 VVAMGrlpHSEPAsrrdeivRAAMTHA--GVDHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarLLLLDEPTSA 178
Cdd:PRK10938 105 IIQDE---VKDPA-------RCEQLAQqfGITALLDRRFKYLSTGETRKTLLCQALMS------EPD---LLILDEPFDG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 179 LDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIARL-YDYPAQVIHHPES 257
Cdd:PRK10938 166 LDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQLaHSEQLEGVQLPEP 245
|
...
gi 743522756 258 GVP 260
Cdd:PRK10938 246 DEP 248
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
39-226 |
3.40e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.56 E-value: 3.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 39 LLGPNGAGKSSLLKCLTGE-LEHEGEIhLFGQ----TR------RGWAGN-------ALAHRVGVLPQSSSLSfpflcee 100
Cdd:PRK11147 34 LVGRNGAGKSTLMKILNGEvLLDDGRI-IYEQdlivARlqqdppRNVEGTvydfvaeGIEEQAEYLKRYHDIS------- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 101 vvamgRLPHSEPASR---RDEIVRAAMTHAGVDHLANR---------LYP-----GLSGGERQRVQFARVLAQiwqapeE 163
Cdd:PRK11147 106 -----HLVETDPSEKnlnELAKLQEQLDHHNLWQLENRinevlaqlgLDPdaalsSLSGGWLRKAALGRALVS------N 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 743522756 164 PqqaRLLLLDEPTSALDLKYQHQLLAMARALAGrntAVLVVLHDLNLAARYADRLVMLEQGRL 226
Cdd:PRK11147 175 P---DVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFISHDRSFIRNMATRIVDLDRGKL 231
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
8-231 |
3.50e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.01 E-value: 3.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 8 LLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELEHE---GEIHLFGQ-------TRRGWAGN 77
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtgGTVEFKGKdllelspEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 78 ALAHRVGVLPQSSSLSFpFLCEEVVAMGRLPHSEPASRRD--EIV--RAAMTHAGVDHLANRLYPGLSGGERQRvqfarv 153
Cdd:PRK09580 81 FMAFQYPVEIPGVSNQF-FLQTALNAVRSYRGQEPLDRFDfqDLMeeKIALLKMPEDLLTRSVNVGFSGGEKKR------ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 154 lAQIWQ-APEEPQqarLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLN-LAARYADRLVMLEQGRLMADGN 231
Cdd:PRK09580 154 -NDILQmAVLEPE---LCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRiLDYIKPDYVHVLYQGRIVKSGD 229
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
34-243 |
5.50e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 44.00 E-value: 5.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTG-ELEHEGEIHLFG--------------------QTRR--GWAGN-ALAHRVGVLPQS 89
Cdd:PRK09700 289 GEILGFAGLVGSGRTELMNCLFGvDKRAGGEIRLNGkdisprspldavkkgmayitESRRdnGFFPNfSIAQNMAISRSL 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 90 SSLSFPFlceevvAMGRLPHSEPAsRRDEIVRAAMTHAGvdHLANRLYPGLSGGERQRVQFARVLAQiwqapeEPQqarL 169
Cdd:PRK09700 369 KDGGYKG------AMGLFHEVDEQ-RTAENQRELLALKC--HSVNQNITELSGGNQQKVLISKWLCC------CPE---V 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 743522756 170 LLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGRLMADGNAGEVLTPELIAR 243
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMA 504
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
6-247 |
5.61e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.48 E-value: 5.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 6 SPLLSCRGLRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGeleH------EGEIHLFGQ-------TRR 72
Cdd:CHL00131 5 KPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG---HpaykilEGDILFKGEsildlepEER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 73 GWAGNALAHRVGV-LPQSSSLSFPFL-CEEVVAMGRLPHSEPASRRdEIVRAAMTHAGVD-HLANR-LYPGLSGGERQR- 147
Cdd:CHL00131 82 AHLGIFLAFQYPIeIPGVSNADFLRLaYNSKRKFQGLPELDPLEFL-EIINEKLKLVGMDpSFLSRnVNEGFSGGEKKRn 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 148 --VQFARVlaqiwqapeEPQqarLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLaARY--ADRLVMLEQ 223
Cdd:CHL00131 161 eiLQMALL---------DSE---LAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRL-LDYikPDYVHVMQN 227
|
250 260
....*....|....*....|....
gi 743522756 224 GRLMADGNAGevLTPELIARLYDY 247
Cdd:CHL00131 228 GKIIKTGDAE--LAKELEKKGYDW 249
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
138-221 |
6.76e-05 |
|
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: 42.99 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 138 PGLSGGERQRVQFARVLAQiwqapeePQQAR-LLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLaARYAD 216
Cdd:cd03271 168 TTLSGGEAQRIKLAKELSK-------RSTGKtLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDV-IKCAD 239
|
....*
gi 743522756 217 RLVML 221
Cdd:cd03271 240 WIIDL 244
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-224 |
6.77e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 140 LSGGERQRVQFARVLaqiWQAPEEPQqarLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLaARYADRLV 219
Cdd:PRK00635 1700 LSLSEKIAIKIAKFL---YLPPKHPT---LFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPAL-LKQADYLI 1772
|
....*
gi 743522756 220 MLEQG 224
Cdd:PRK00635 1773 EMGPG 1777
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
35-236 |
8.74e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 43.55 E-value: 8.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 35 SLTALLGPNGAGKSSLLKCLTGELE-HEGEIHLFGQTRRGWAGNALAHRVGVLPQSSS-LSFPFLCEevVAMGRLPHSEP 112
Cdd:PRK10790 368 GFVALVGHTGSGKSTLASLLMGYYPlTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVvLADTFLAN--VTLGRDISEEQ 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 113 ASRRDEIVR-AAMTHAGVDHLANRLYP---GLSGGERQRVQFARVLAqiwQAPeepqqaRLLLLDEPTSALDLKYQhQLL 188
Cdd:PRK10790 446 VWQALETVQlAELARSLPDGLYTPLGEqgnNLSVGQKQLLALARVLV---QTP------QILILDEATANIDSGTE-QAI 515
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 743522756 189 AMARALAGRNTAVLVVLHDLNLAARyADRLVMLEQGRLMADGNAGEVL 236
Cdd:PRK10790 516 QQALAAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLL 562
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
33-237 |
9.29e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.57 E-value: 9.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTG--ELEhEGEIHLFG---QTRRgwAGNALAHRVGVLPQS------SSLSfpfLCEEV 101
Cdd:NF033858 26 AGCMVGLIGPDGVGKSSLLSLIAGarKIQ-QGRVEVLGgdmADAR--HRRAVCPRIAYMPQGlgknlyPTLS---VFENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 102 VAMGRLPHSEPASRRDEIvrAAMTHA-GVDHLANRLYPGLSGGERQRvqfarvL----AQIwqapEEPQqarLLLLDEPT 176
Cdd:NF033858 100 DFFGRLFGQDAAERRRRI--DELLRAtGLAPFADRPAGKLSGGMKQK------LglccALI----HDPD---LLILDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 743522756 177 SALD-LKYQH--QLLAMARalAGR-NTAVLVVLHDLNLAARYaDRLVMLEQGRLMADGNAGEVLT 237
Cdd:NF033858 165 TGVDpLSRRQfwELIDRIR--AERpGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
140-221 |
1.26e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.09 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 140 LSGGERQRVQFARVLAQiwqapeepqQARLLLLDEPTSALDLKYQHQLLAMARALAG-RNTAVLVVLHDLNlAARYADRL 218
Cdd:PTZ00265 580 LSGGQKQRISIARAIIR---------NPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHRLS-TIRYANTI 649
|
...
gi 743522756 219 VML 221
Cdd:PTZ00265 650 FVL 652
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
140-243 |
1.55e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.71 E-value: 1.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 140 LSGGERQRVQFARVLAqiwqapeEPQQAR-LLLLDEPTSAL---DLkyqHQLLAMARAL--AGrNTaVLVVLHDLNLaAR 213
Cdd:COG0178 827 LSGGEAQRVKLASELS-------KRSTGKtLYILDEPTTGLhfhDI---RKLLEVLHRLvdKG-NT-VVVIEHNLDV-IK 893
|
90 100 110
....*....|....*....|....*....|....*
gi 743522756 214 YADRLVML--EQGrlmADGnaGEVL---TPELIAR 243
Cdd:COG0178 894 TADWIIDLgpEGG---DGG--GEIVaegTPEEVAK 923
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
140-229 |
1.79e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 140 LSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLNLAARYADRLV 219
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLL------NP---KILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVL 476
|
90
....*....|
gi 743522756 220 MLEQGRLMAD 229
Cdd:PRK13549 477 VMHEGKLKGD 486
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-216 |
2.07e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.44 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 36 LTALLGPNGAGKSSLLKCLtgelehegEIHLFGQTRRGWAGNA-LAHRVGVLPQSSSLSFPFlceeVVAMGRLPHsepAS 114
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAL--------KYALTGELPPNSKGGAhDPKLIREGEVRAQVKLAF----ENANGKKYT---IT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 115 RRDEIVR-AAMTHAG------VDHLANrlypgLSGGERQ------RVQFARVLaqiwqapeePQQARLLLLDEPTSALD- 180
Cdd:cd03240 89 RSLAILEnVIFCHQGesnwplLDMRGR-----CSGGEKVlasliiRLALAETF---------GSNCGILALDEPTTNLDe 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 743522756 181 --LKYQ-HQLLAMARALAGRNtaVLVVLHDLNLaARYAD 216
Cdd:cd03240 155 enIEESlAEIIEERKSQKNFQ--LIVITHDEEL-VDAAD 190
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-227 |
5.85e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.92 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 14 LRLSRGNRLILDSLDLDLHAGSLTALLGPNGAGKSSLLKCLTGELEHEGEIHLFGQTrrgWagnALAHrvgVLPQSSSLS 93
Cdd:PRK10636 7 LQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN---W---QLAW---VNQETPALP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 94 FPFLceEVVAMG----RLPHSE--PASRRDEIVRAAMTHAGVDHL--------ANRLYPGL--------------SGGER 145
Cdd:PRK10636 78 QPAL--EYVIDGdreyRQLEAQlhDANERNDGHAIATIHGKLDAIdawtirsrAASLLHGLgfsneqlerpvsdfSGGWR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 146 QRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKyqhQLLAMARALAGRNTAVLVVLHDLNLAARYADRLVMLEQGR 225
Cdd:PRK10636 156 MRLNLAQALI---------CRSDLLLLDEPTNHLDLD---AVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQS 223
|
..
gi 743522756 226 LM 227
Cdd:PRK10636 224 LF 225
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
128-193 |
7.32e-04 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 37.60 E-value: 7.32e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 128 GVDHLANRLYPGLSGGERQR----VQFARVLAQIWQAPEEPQQARLLLLDEPTSALDLKYQHQLLAMARA 193
Cdd:pfam13558 21 GSEVETYRRSGGLSGGEKQLlaylPLAAALAAQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-208 |
8.02e-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: 40.77 E-value: 8.02e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 743522756 138 PGLSGGERQRVQFARVLaqiwQAPEEPQQarLLLLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDL 208
Cdd:TIGR00630 828 TTLSGGEAQRIKLAKEL----SKRSTGRT--LYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNL 892
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-221 |
8.29e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.58 E-value: 8.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 123 AMTHAGVDHLA-NRLYPGLSGGERQRVQFARVLAqiwqAPEEPQQarLLLLDEPTSALDLKYQHQLLAMARALAGRNTAV 201
Cdd:PRK00635 792 ALCSLGLDYLPlGRPLSSLSGGEIQRLKLAYELL----APSKKPT--LYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTV 865
|
90 100
....*....|....*....|
gi 743522756 202 LVVLHDLNLaARYADRLVML 221
Cdd:PRK00635 866 VIIEHNMHV-VKVADYVLEL 884
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
39-239 |
1.34e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 40.11 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 39 LLGPNGAGKSSLLKCLTGELEHE-GEIHLFGQTRRGWAGNALAHRVGVLPQSsslsfPFLCEEVVAMGRLP---HS---- 110
Cdd:PLN03130 1270 IVGRTGAGKSSMLNALFRIVELErGRILIDGCDISKFGLMDLRKVLGIIPQA-----PVLFSGTVRFNLDPfneHNdadl 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 ----EPASRRDEIVRAAMthaGVDHLANRLYPGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTSALDLKYQHQ 186
Cdd:PLN03130 1345 weslERAHLKDVIRRNSL---GLDAEVSEAGENFSVGQRQLLSLARALL---------RRSKILVLDEATAAVDVRTDAL 1412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 743522756 187 LLAMARAlAGRNTAVLVVLHDLNLAARyADRLVMLEQGRLMadgnagEVLTPE 239
Cdd:PLN03130 1413 IQKTIRE-EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVV------EFDTPE 1457
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
111-180 |
1.47e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 40.01 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 111 EPASRRDeiVRAAMTHAGVDHLANRL----------Y-PGLSGGERQRVQFARVLAQiwqapeEPqqaRLLLLDEPTSAL 179
Cdd:PTZ00265 1321 EDATRED--VKRACKFAAIDEFIESLpnkydtnvgpYgKSLSGGQKQRIAIARALLR------EP---KILLLDEATSSL 1389
|
.
gi 743522756 180 D 180
Cdd:PTZ00265 1390 D 1390
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
33-64 |
1.62e-03 |
|
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: 38.29 E-value: 1.62e-03
10 20 30
....*....|....*....|....*....|...
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEHE-GEI 64
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNALLPELDLRtGEI 137
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
36-54 |
1.67e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.30 E-value: 1.67e-03
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
34-180 |
2.18e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.44 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLTGELEH---EGEIHLFGQTRR--------GWAGNALAHRVGVLPQSSSLSFPFLceevv 102
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGgyiEGDIRISGFPKKqetfarisGYCEQNDIHSPQVTVRESLIYSAFL----- 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 103 amgRLPHSEPASRRDEIVRAAMTHAGVDHLANRLY-----PGLSGGERQRVQFARVLAqiwqapeepQQARLLLLDEPTS 177
Cdd:PLN03140 981 ---RLPKEVSKEEKMMFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELV---------ANPSIIFMDEPTS 1048
|
...
gi 743522756 178 ALD 180
Cdd:PLN03140 1049 GLD 1051
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
36-55 |
2.50e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.86 E-value: 2.50e-03
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
33-64 |
2.65e-03 |
|
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: 38.15 E-value: 2.65e-03
10 20 30
....*....|....*....|....*....|...
gi 743522756 33 AGSLTALLGPNGAGKSSLLKCLTGELEHE-GEI 64
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLPELVLAtGEI 116
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
36-54 |
3.47e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 38.06 E-value: 3.47e-03
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
128-236 |
3.54e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 38.46 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 128 GVDHLA-NRLYPGLSGGERQRVQFArvlAQIwqapeepqQARLL----LLDEPTSALDLKYQHQLLAMARALAGRNTAVL 202
Cdd:TIGR00630 476 GLDYLSlSRAAGTLSGGEAQRIRLA---TQI--------GSGLTgvlyVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLI 544
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 743522756 203 VVLHDLNlAARYADRLVML------EQGRLMADGNAGEVL 236
Cdd:TIGR00630 545 VVEHDED-TIRAADYVIDIgpgageHGGEVVASGTPEEIL 583
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
39-73 |
4.27e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 38.07 E-value: 4.27e-03
10 20 30
....*....|....*....|....*....|....*....
gi 743522756 39 LLGPNGAGKSSLLKCLTGelEH----EGEIHLFGQtRRG 73
Cdd:PRK10938 291 IVGPNGAGKSTLLSLITG--DHpqgySNDLTLFGR-RRG 326
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
34-85 |
4.45e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 37.99 E-value: 4.45e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 743522756 34 GSLTALLGPNGAGKSSLLKCLtgelehegeiHLFGQTRRGWAGNALAHRVGV 85
Cdd:COG4637 21 GPLTVLIGANGSGKSNLLDAL----------RFLSDAARGGLQDALARRGGL 62
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
134-239 |
6.31e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.89 E-value: 6.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 743522756 134 NRLYPGLSGGERQRVQFARVLAqiwqapeepqqARLL----LLDEPTSALDLKYQHQLLAMARALAGRNTAVLVVLHDLN 209
Cdd:PRK00635 471 ERALATLSGGEQERTALAKHLG-----------AELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQ 539
|
90 100 110
....*....|....*....|....*....|...
gi 743522756 210 LAArYADRLVMLEQGrlmADGNAGEVL---TPE 239
Cdd:PRK00635 540 MIS-LADRIIDIGPG---AGIFGGEVLfngSPR 568
|
|
| |
