|
Name |
Accession |
Description |
Interval |
E-value |
| YejR |
COG0523 |
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ... |
7-317 |
9.99e-101 |
|
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];
Pssm-ID: 440289 [Multi-domain] Cd Length: 318 Bit Score: 299.01 E-value: 9.99e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 7 VPVLALAGYLGAGKTTLLNHLLRNSRGVRIGALVNDFGAVNIDAMLVAGQVDAMAGLTNGCICCAVdADEAGEMLGKLAA 86
Cdd:COG0523 4 IPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRDTDEEIVELSNGCICCTL-REDLLPALRRLLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 87 vKPRLDLIVVEASGLAEPAALARTIAMADD--TRYHYAGLVLVVDAV-------ESTRAELGNN-VQVADLVVVNKADQV 156
Cdd:COG0523 83 -RGRFDRLLIETTGLADPAPVAQTFTFDPElrDRLRLDGVVTVVDARnllddlaDRTLHELLVDqIAFADVIVLNKTDLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 157 SDAELEAVRAKITALNDRVPVLPTEFGRVDPELLVDPPQQVPRVAqLSLDELLWETYDHDHHEHatFQSVAFTSDVPLDP 236
Cdd:COG0523 162 DEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAA-LARPGWLEELRDHEHDDG--IRSFVFRSDRPFDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 237 RRFMDLLKNRPAGMYRAKGFVDFgdAGEGRKFVLQLVGGSLRFER-RRWdRGEARRTSLVLIGTDIDEAAALSALQGCAT 315
Cdd:COG0523 239 ERLADFLEELGPGVLRAKGFLWL--AGRPRRLVFQGVGGRLSLEPlGPW-PADDRRSRLVFIGRDLDEAALEAALDACLL 315
|
..
gi 500046712 316 AE 317
Cdd:COG0523 316 TD 317
|
|
| CobW-like |
cd03112 |
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ... |
8-193 |
1.16e-68 |
|
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.
Pssm-ID: 349766 Cd Length: 198 Bit Score: 213.15 E-value: 1.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 8 PVLALAGYLGAGKTTLLNHLLRNSRGVRIGALVNDFGAVNIDAMLVAGQV--DAMAGLTNGCICCAVdADEAGEMLGKLA 85
Cdd:cd03112 1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGggEEVVELSNGCICCTL-KGDLVKALEQLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 86 AVKPRLDLIVVEASGLAEPAALARTIAMADD--TRYHYAGLVLVVDAV--------ESTRAELGNNVQVADLVVVNKADQ 155
Cdd:cd03112 80 ERRGKFDYILIETTGLADPGPIAQTLWSDEEleSRLRLDGVVTVVDAKnflkqldeEDVSDLAVDQIAFADVIVLNKTDL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 500046712 156 VSDAELEAVRAKITALNDRVPVLPTEFGRVDPELLVDP 193
Cdd:cd03112 160 VDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGT 197
|
|
| cobW |
pfam02492 |
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ... |
8-179 |
5.16e-48 |
|
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.
Pssm-ID: 396860 Cd Length: 179 Bit Score: 159.34 E-value: 5.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 8 PVLALAGYLGAGKTTLLNHLLR-NSRGVRIGALVNDFGAVNIDAMLVAGQVDAMAGLTNGCICCAVdADEAGEMLGKLAA 86
Cdd:pfam02492 1 PVTVITGFLGSGKTTLLNHLLKqNRAGLRIAVIVNEFGETGIDAELLSETGVLIVELSNGCICCTI-REDLSMALEALLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 87 VKPRLDLIVVEASGLAEPAALARTIAmADDTRYHYA--GLVLVVDAV-----ESTRAELGNNVQVADLVVVNKADQVSDA 159
Cdd:pfam02492 80 REGRLDVIFIETTGLAEPAPVAQTFL-SPELRSPVLldGVITVVDAAneadgEKIPRKAGDQIAFADLIVLNKTDLAPEV 158
|
170 180
....*....|....*....|.
gi 500046712 160 ELEAVRAKIT-ALNDRVPVLP 179
Cdd:pfam02492 159 ALLEVLEEDLrRLNPGAPVVP 179
|
|
| CobW |
TIGR02475 |
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ... |
7-310 |
1.17e-45 |
|
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is generally found proximal to the trimeric cobaltochelatase subunit CobN which is essential for vitamin B12 (cobalamin) biosynthesis. The protein contains an P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. A broader CobW family is delineated by two Pfam models which identify the N- and C-terminal domains (pfam02492 and pfam07683). [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 274151 [Multi-domain] Cd Length: 341 Bit Score: 158.37 E-value: 1.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 7 VPVLALAGYLGAGKTTLLNHLLRNSRGVRIGALVNDFGAVNIDAMLVAGQVDA------MAGLTNGCICCAVdADEAGEM 80
Cdd:TIGR02475 4 IPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEgcseenIVELANGCICCTV-ADDFIPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 81 LGKLAAVKPRLDLIVVEASGLAEPAALARTIAMAD-DTRYHYAGLVLVVD--------------AVESTRA--------- 136
Cdd:TIGR02475 83 MTKLLARRQRPDHILIETSGLALPKPLVQAFQWPEiRSRVTVDGVVTVVDgpavaagrfaadpdALDAQRAaddnldhet 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 137 ---ELGNN-VQVADLVVVNKADQVSDAELEAVRAKITA-LNDRVPVLPTEFGRVDPELLVDppqqVPRVAQLSLDELLWE 211
Cdd:TIGR02475 163 pleELFEDqLACADLVILNKADLLDAAGLARVRAEIAAeLPRAVKIVEASHGEVDARVLLG----LGAAAEDDLDNRPSH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 212 TYDHDH--HEHATFQSVAFTSDVPLDPRRFMDLLKN--RPAGMYRAKGFVDFGdaGEGRKFVLQLVGGSL-RFERRRWDR 286
Cdd:TIGR02475 239 HDFEGGeeHDHDEFDSVVVDLGEVADPAALRQRLERlaEEHDVLRIKGFAAVP--GKPMRLLVQGVGQRVdSYYDRPWQA 316
|
330 340
....*....|....*....|....*
gi 500046712 287 GEARRTSLVLIGT-DIDEAAALSAL 310
Cdd:TIGR02475 317 AETRQTRLVVIGLhDLDQAAIRAAL 341
|
|
| chaper_GTP_ZigA |
NF038288 |
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ... |
8-313 |
3.92e-40 |
|
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc metallochaperone thought to be important for histidine utilization (HUT), supplying Zn to the histidine ammonia-lyase HutH when required under low-Zn conditions.
Pssm-ID: 468453 [Multi-domain] Cd Length: 390 Bit Score: 144.92 E-value: 3.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 8 PVLALAGYLGAGKTTLLNHLLRNSRGVRIGALVNDFGAVNIDAMLVA-GQVD------AMAGLTNGCICCAVDADEAGEm 80
Cdd:NF038288 2 PVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRnGGASlsrteeKLVEMSNGCICCTLREDLLVE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 81 LGKLAAVKpRLDLIVVEASGLAEPAALARTIAMAD------------DTryhyagLVLVVDAV------EST-----RAE 137
Cdd:NF038288 81 VRRLAREG-RFDYLVIESTGISEPLPVAETFTFADedgvslsdvarlDT------MVTVVDAVnflrdyDSAdslqeRGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 138 -LGN----NV------QV--ADLVVVNKADQVSDAELEAVRAKITALNDRVPVLPTEFGRVDPELLVDP-------PQQV 197
Cdd:NF038288 154 sLGEederTVvdllvdQVefADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTglfdferAAQA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 198 PRVAQLSLDELLWETydhdhhEHATFQSVAFTSDVPLDPRRFMDLLKNRPAG-MYRAKGFV------DFgdAGEgrkfvL 270
Cdd:NF038288 234 PGWLKELRGEHTPET------EEYGISSFVYRARRPFHPQRFYDFLHSEWPGkVLRSKGFFwlasrpDF--AGS-----W 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500046712 271 QLVGGSLRFE----------RRRWDRGEA---------------RRTSLVLIGTDIDEAAALSALQGC 313
Cdd:NF038288 301 SQAGGIARHGpagmwwaavpRERWPQDEEslaairenwdepfgdRRQELVFIGQDMDEAALRAALDAC 368
|
|
| PRK11537 |
PRK11537 |
putative GTP-binding protein YjiA; Provisional |
7-310 |
1.79e-26 |
|
putative GTP-binding protein YjiA; Provisional
Pssm-ID: 183183 [Multi-domain] Cd Length: 318 Bit Score: 106.71 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 7 VPVLALAGYLGAGKTTLLNHLLRNSRGVRIGALVNDFGAVNIDAMLVAGQVDAMAGLTNGCICCAVD---ADEAGEMLGK 83
Cdd:PRK11537 4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIGDRATQIKTLTNGCICCSRSnelEDALLDLLDN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 84 LAAVKPRLDLIVVEASGLAEPAALARTIaMADDT---RYHYAGLVLVVDAVES-------TRAElgNNVQVADLVVVNKA 153
Cdd:PRK11537 84 LDKGNIQFDRLVIECTGMADPGPIIQTF-FSHEVlcqRYLLDGVIALVDAVHAdeqmnqfTIAQ--SQVGYADRILLTKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 154 DQVSDAelEAVRAKITALNDRVPVLPTEFGRVDPELLVDppqqvprVAQLSLDELLWETYDHDH---HEHATFQSVAFTS 230
Cdd:PRK11537 161 DVAGEA--EKLRERLARINARAPVYTVVHGDIDLSLLFN-------TNGFMLEENVVSTKPRFHfiaDKQNDISSIVVEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 231 DVPLD---PRRFMD-LLKNRPAGMYRAKGFVDFgdAGEGRKFVLQlvgGSLRFERRRWDR---GEARRTSLVLIGTDIDE 303
Cdd:PRK11537 232 DYPVDiseVSRVMEnLLLESADKLLRYKGMLWI--DGEPNRLLFQ---GVQRLYSADWDRpwgDETPHSTLVFIGIQLPE 306
|
330
....*....|
gi 500046712 304 A---AALSAL 310
Cdd:PRK11537 307 EeirAAFAGL 316
|
|
| CobW_C |
smart00833 |
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ... |
223-313 |
2.43e-19 |
|
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal to the trimeric cobaltochelatase subunit CobN, which is essential for vitamin B12 (cobalamin) biosynthesis. They contain a P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. CobW might be involved in cobalt reduction leading to cobalt(I) corrinoids. This entry represents the C-terminal domain found in CobW, as well as in P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression.
Pssm-ID: 214844 [Multi-domain] Cd Length: 92 Bit Score: 81.49 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 223 FQSVAFTSDVPLDPRRFMDLLKNRPAGMYRAKGFVDFGDaGEGRKFVLQLVGGSLRFER-RRWDRGEARRTSLVLIGTDI 301
Cdd:smart00833 1 ISSFVYRARRPFHPQRLLAALDELPEGVLRAKGFFWLAS-RPDLPGVLSQAGGRLRIEPaGAWPAAGDRRTRLVFIGRDL 79
|
90
....*....|..
gi 500046712 302 DEAAALSALQGC 313
Cdd:smart00833 80 DEEAIRAALDAC 91
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| YejR |
COG0523 |
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ... |
7-317 |
9.99e-101 |
|
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];
Pssm-ID: 440289 [Multi-domain] Cd Length: 318 Bit Score: 299.01 E-value: 9.99e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 7 VPVLALAGYLGAGKTTLLNHLLRNSRGVRIGALVNDFGAVNIDAMLVAGQVDAMAGLTNGCICCAVdADEAGEMLGKLAA 86
Cdd:COG0523 4 IPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRDTDEEIVELSNGCICCTL-REDLLPALRRLLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 87 vKPRLDLIVVEASGLAEPAALARTIAMADD--TRYHYAGLVLVVDAV-------ESTRAELGNN-VQVADLVVVNKADQV 156
Cdd:COG0523 83 -RGRFDRLLIETTGLADPAPVAQTFTFDPElrDRLRLDGVVTVVDARnllddlaDRTLHELLVDqIAFADVIVLNKTDLV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 157 SDAELEAVRAKITALNDRVPVLPTEFGRVDPELLVDPPQQVPRVAqLSLDELLWETYDHDHHEHatFQSVAFTSDVPLDP 236
Cdd:COG0523 162 DEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAA-LARPGWLEELRDHEHDDG--IRSFVFRSDRPFDP 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 237 RRFMDLLKNRPAGMYRAKGFVDFgdAGEGRKFVLQLVGGSLRFER-RRWdRGEARRTSLVLIGTDIDEAAALSALQGCAT 315
Cdd:COG0523 239 ERLADFLEELGPGVLRAKGFLWL--AGRPRRLVFQGVGGRLSLEPlGPW-PADDRRSRLVFIGRDLDEAALEAALDACLL 315
|
..
gi 500046712 316 AE 317
Cdd:COG0523 316 TD 317
|
|
| CobW-like |
cd03112 |
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ... |
8-193 |
1.16e-68 |
|
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino acid sequence of YjiA protein in E. coli contains several conserved motifs that characterizes it as a P-loop GTPase. YijA gene is among the genes significantly induced in response to DNA-damage caused by mitomycin. YijA gene is a homologue of the CobW gene which encodes the cobalamin synthesis protein/P47K.
Pssm-ID: 349766 Cd Length: 198 Bit Score: 213.15 E-value: 1.16e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 8 PVLALAGYLGAGKTTLLNHLLRNSRGVRIGALVNDFGAVNIDAMLVAGQV--DAMAGLTNGCICCAVdADEAGEMLGKLA 85
Cdd:cd03112 1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGggEEVVELSNGCICCTL-KGDLVKALEQLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 86 AVKPRLDLIVVEASGLAEPAALARTIAMADD--TRYHYAGLVLVVDAV--------ESTRAELGNNVQVADLVVVNKADQ 155
Cdd:cd03112 80 ERRGKFDYILIETTGLADPGPIAQTLWSDEEleSRLRLDGVVTVVDAKnflkqldeEDVSDLAVDQIAFADVIVLNKTDL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 500046712 156 VSDAELEAVRAKITALNDRVPVLPTEFGRVDPELLVDP 193
Cdd:cd03112 160 VDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGT 197
|
|
| cobW |
pfam02492 |
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ... |
8-179 |
5.16e-48 |
|
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase expression / formation protein, and UreG a urease accessory protein. Both these proteins contain a P-loop nucleotide binding motif. HypB has GTPase activity and is a guanine nucleotide binding protein. It is not known whether UreG binds GTP or some other nucleotide. Both enzymes are involved in nickel binding. HypB can store nickel and is required for nickel dependent hydrogenase expression. UreG is required for functional incorporation of the urease nickel metallocenter. GTP hydrolysis may required by these proteins for nickel incorporation into other nickel proteins. This family of domains also contains P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression, and the cobW gene product, which may be involved in cobalamin biosynthesis in Pseudomonas denitrificans.
Pssm-ID: 396860 Cd Length: 179 Bit Score: 159.34 E-value: 5.16e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 8 PVLALAGYLGAGKTTLLNHLLR-NSRGVRIGALVNDFGAVNIDAMLVAGQVDAMAGLTNGCICCAVdADEAGEMLGKLAA 86
Cdd:pfam02492 1 PVTVITGFLGSGKTTLLNHLLKqNRAGLRIAVIVNEFGETGIDAELLSETGVLIVELSNGCICCTI-REDLSMALEALLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 87 VKPRLDLIVVEASGLAEPAALARTIAmADDTRYHYA--GLVLVVDAV-----ESTRAELGNNVQVADLVVVNKADQVSDA 159
Cdd:pfam02492 80 REGRLDVIFIETTGLAEPAPVAQTFL-SPELRSPVLldGVITVVDAAneadgEKIPRKAGDQIAFADLIVLNKTDLAPEV 158
|
170 180
....*....|....*....|.
gi 500046712 160 ELEAVRAKIT-ALNDRVPVLP 179
Cdd:pfam02492 159 ALLEVLEEDLrRLNPGAPVVP 179
|
|
| CobW |
TIGR02475 |
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ... |
7-310 |
1.17e-45 |
|
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is generally found proximal to the trimeric cobaltochelatase subunit CobN which is essential for vitamin B12 (cobalamin) biosynthesis. The protein contains an P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. A broader CobW family is delineated by two Pfam models which identify the N- and C-terminal domains (pfam02492 and pfam07683). [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 274151 [Multi-domain] Cd Length: 341 Bit Score: 158.37 E-value: 1.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 7 VPVLALAGYLGAGKTTLLNHLLRNSRGVRIGALVNDFGAVNIDAMLVAGQVDA------MAGLTNGCICCAVdADEAGEM 80
Cdd:TIGR02475 4 IPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEgcseenIVELANGCICCTV-ADDFIPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 81 LGKLAAVKPRLDLIVVEASGLAEPAALARTIAMAD-DTRYHYAGLVLVVD--------------AVESTRA--------- 136
Cdd:TIGR02475 83 MTKLLARRQRPDHILIETSGLALPKPLVQAFQWPEiRSRVTVDGVVTVVDgpavaagrfaadpdALDAQRAaddnldhet 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 137 ---ELGNN-VQVADLVVVNKADQVSDAELEAVRAKITA-LNDRVPVLPTEFGRVDPELLVDppqqVPRVAQLSLDELLWE 211
Cdd:TIGR02475 163 pleELFEDqLACADLVILNKADLLDAAGLARVRAEIAAeLPRAVKIVEASHGEVDARVLLG----LGAAAEDDLDNRPSH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 212 TYDHDH--HEHATFQSVAFTSDVPLDPRRFMDLLKN--RPAGMYRAKGFVDFGdaGEGRKFVLQLVGGSL-RFERRRWDR 286
Cdd:TIGR02475 239 HDFEGGeeHDHDEFDSVVVDLGEVADPAALRQRLERlaEEHDVLRIKGFAAVP--GKPMRLLVQGVGQRVdSYYDRPWQA 316
|
330 340
....*....|....*....|....*
gi 500046712 287 GEARRTSLVLIGT-DIDEAAALSAL 310
Cdd:TIGR02475 317 AETRQTRLVVIGLhDLDQAAIRAAL 341
|
|
| chaper_GTP_ZigA |
NF038288 |
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ... |
8-313 |
3.92e-40 |
|
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc metallochaperone thought to be important for histidine utilization (HUT), supplying Zn to the histidine ammonia-lyase HutH when required under low-Zn conditions.
Pssm-ID: 468453 [Multi-domain] Cd Length: 390 Bit Score: 144.92 E-value: 3.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 8 PVLALAGYLGAGKTTLLNHLLRNSRGVRIGALVNDFGAVNIDAMLVA-GQVD------AMAGLTNGCICCAVDADEAGEm 80
Cdd:NF038288 2 PVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRnGGASlsrteeKLVEMSNGCICCTLREDLLVE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 81 LGKLAAVKpRLDLIVVEASGLAEPAALARTIAMAD------------DTryhyagLVLVVDAV------EST-----RAE 137
Cdd:NF038288 81 VRRLAREG-RFDYLVIESTGISEPLPVAETFTFADedgvslsdvarlDT------MVTVVDAVnflrdyDSAdslqeRGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 138 -LGN----NV------QV--ADLVVVNKADQVSDAELEAVRAKITALNDRVPVLPTEFGRVDPELLVDP-------PQQV 197
Cdd:NF038288 154 sLGEederTVvdllvdQVefADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTglfdferAAQA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 198 PRVAQLSLDELLWETydhdhhEHATFQSVAFTSDVPLDPRRFMDLLKNRPAG-MYRAKGFV------DFgdAGEgrkfvL 270
Cdd:NF038288 234 PGWLKELRGEHTPET------EEYGISSFVYRARRPFHPQRFYDFLHSEWPGkVLRSKGFFwlasrpDF--AGS-----W 300
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 500046712 271 QLVGGSLRFE----------RRRWDRGEA---------------RRTSLVLIGTDIDEAAALSALQGC 313
Cdd:NF038288 301 SQAGGIARHGpagmwwaavpRERWPQDEEslaairenwdepfgdRRQELVFIGQDMDEAALRAALDAC 368
|
|
| PRK11537 |
PRK11537 |
putative GTP-binding protein YjiA; Provisional |
7-310 |
1.79e-26 |
|
putative GTP-binding protein YjiA; Provisional
Pssm-ID: 183183 [Multi-domain] Cd Length: 318 Bit Score: 106.71 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 7 VPVLALAGYLGAGKTTLLNHLLRNSRGVRIGALVNDFGAVNIDAMLVAGQVDAMAGLTNGCICCAVD---ADEAGEMLGK 83
Cdd:PRK11537 4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIGDRATQIKTLTNGCICCSRSnelEDALLDLLDN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 84 LAAVKPRLDLIVVEASGLAEPAALARTIaMADDT---RYHYAGLVLVVDAVES-------TRAElgNNVQVADLVVVNKA 153
Cdd:PRK11537 84 LDKGNIQFDRLVIECTGMADPGPIIQTF-FSHEVlcqRYLLDGVIALVDAVHAdeqmnqfTIAQ--SQVGYADRILLTKT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 154 DQVSDAelEAVRAKITALNDRVPVLPTEFGRVDPELLVDppqqvprVAQLSLDELLWETYDHDH---HEHATFQSVAFTS 230
Cdd:PRK11537 161 DVAGEA--EKLRERLARINARAPVYTVVHGDIDLSLLFN-------TNGFMLEENVVSTKPRFHfiaDKQNDISSIVVEL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 231 DVPLD---PRRFMD-LLKNRPAGMYRAKGFVDFgdAGEGRKFVLQlvgGSLRFERRRWDR---GEARRTSLVLIGTDIDE 303
Cdd:PRK11537 232 DYPVDiseVSRVMEnLLLESADKLLRYKGMLWI--DGEPNRLLFQ---GVQRLYSADWDRpwgDETPHSTLVFIGIQLPE 306
|
330
....*....|
gi 500046712 304 A---AALSAL 310
Cdd:PRK11537 307 EeirAAFAGL 316
|
|
| CobW_C |
pfam07683 |
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ... |
223-313 |
9.29e-24 |
|
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of putative metal chaperones that can be separated into up to 15 subgroups. In addition to known roles in cobalamin biosynthesis and the activation of the Fe-type nitrile hydratase, this family is also known to be involved in the response to zinc limitation. The CobW subgroup involved in cobalamin synthesis represents only a small sub-fraction of the family.
Pssm-ID: 462228 [Multi-domain] Cd Length: 93 Bit Score: 93.07 E-value: 9.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 223 FQSVAFTSDVPLDPRRFMDLLKN--RPAGMYRAKGFVDFgdAGEGRKFVLQLVGGSLRFER-RRWDRGEARRTSLVLIGT 299
Cdd:pfam07683 1 ISSFVFRADRPFDPERLEAWLEDllLPEGILRAKGILWL--AGRPRPLVFQGVGGRLSLEPaGRWWPDEDRRSRLVFIGR 78
|
90
....*....|....
gi 500046712 300 DIDEAAALSALQGC 313
Cdd:pfam07683 79 DLDREALRAALDAC 92
|
|
| CobW_C |
smart00833 |
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ... |
223-313 |
2.43e-19 |
|
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal to the trimeric cobaltochelatase subunit CobN, which is essential for vitamin B12 (cobalamin) biosynthesis. They contain a P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. CobW might be involved in cobalt reduction leading to cobalt(I) corrinoids. This entry represents the C-terminal domain found in CobW, as well as in P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression.
Pssm-ID: 214844 [Multi-domain] Cd Length: 92 Bit Score: 81.49 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 223 FQSVAFTSDVPLDPRRFMDLLKNRPAGMYRAKGFVDFGDaGEGRKFVLQLVGGSLRFER-RRWDRGEARRTSLVLIGTDI 301
Cdd:smart00833 1 ISSFVYRARRPFHPQRLLAALDELPEGVLRAKGFFWLAS-RPDLPGVLSQAGGRLRIEPaGAWPAAGDRRTRLVFIGRDL 79
|
90
....*....|..
gi 500046712 302 DEAAALSALQGC 313
Cdd:smart00833 80 DEEAIRAALDAC 91
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
7-180 |
3.83e-10 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 58.53 E-value: 3.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 7 VPVLALAGYLGAGKTTLLNHLLRNSRG-VRIGALVNDFgAVNIDA-MLVAGQVDAMAGLTNGciCCAVDADEAGEMLGKL 84
Cdd:COG0378 13 VLAVNLMGSPGSGKTTLLEKTIRALKDrLRIAVIEGDI-YTTEDAeRLRAAGVPVVQINTGG--CCHLDASMVLEALEEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 85 AavKPRLDLIVVEASG--LAePAALartiamadDTRYHYAglVLVVDAVEstraelGNNV--------QVADLVVVNKAD 154
Cdd:COG0378 90 D--LPDLDLLFIENVGnlVC-PAFF--------PLGEDLK--VVVLSVTE------GDDKprkyppmfTAADLLVINKID 150
|
170 180
....*....|....*....|....*...
gi 500046712 155 QVS--DAELEAVRAKITALNDRVPVLPT 180
Cdd:COG0378 151 LAPyvGFDLEVMEEDARRVNPGAPIFEV 178
|
|
| HypB |
cd05390 |
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the ... |
9-180 |
1.82e-07 |
|
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the maturation of nickel-dependent hydrogenases, like carbon monoxide dehydrogenase or urease. HypB is a GTP-binding protein and has GTP hyrolase activity. It forms homodimer and is capable of binding two nickel ions and two zinc ions. The active site is located on the dimer interface. Energy from hydrolysis of GTP is used to insert nickels into hydrogenases.
Pssm-ID: 349775 Cd Length: 203 Bit Score: 50.67 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 9 VLALAGYLGAGKTTLLNHLLRNSR-GVRIGALVNDFgAVNIDAMLVAGQ-VDAMAGLTNGciCCAVDADEAGEMLGKLAA 86
Cdd:cd05390 23 ALNLMSSPGSGKTTLLERTIDALKdELKIAVIEGDL-ETDNDAERIRATgVPAIQINTGG--ACHLDADMVARALHDLDL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 87 vkPRLDLIVVEASG-LAEPAALartiamadDTRYHYAGLVLVVDAVESTRAELGNNVQVADLVVVNKADQVS--DAELEA 163
Cdd:cd05390 100 --DELDLLFIENVGnLVCPAEF--------DLGEHKNVVLLSVTEGDDKPLKYPLMFQVADVVLINKIDLLPyfDFDVEK 169
|
170
....*....|....*..
gi 500046712 164 VRAKITALNDRVPVLPT 180
Cdd:cd05390 170 AKEDIKKLNPNAPIIEV 186
|
|
| PRK14491 |
PRK14491 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; ... |
1-97 |
4.92e-05 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobB/MoeA; Provisional
Pssm-ID: 237729 [Multi-domain] Cd Length: 597 Bit Score: 44.99 E-value: 4.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 1 MRTTGSVPVLALAGYLGAGKTTLLNHLLR--NSRGVRIGALVNDFGAVNID---------------AMLVAGQVD-AMAG 62
Cdd:PRK14491 4 FTNPLSIPLLGFCAYSGTGKTTLLEQLIPelNQRGLRLAVIKHAHHNFDVDqpgkdsyrlrkagasQMLVASRVRwALMT 83
|
90 100 110
....*....|....*....|....*....|....*.
gi 500046712 63 LTngciccAVDAD-EAGEMLGKLAAVKprLDLIVVE 97
Cdd:PRK14491 84 ET------PRDGEpELPHLLKQIDADK--VDIVLVE 111
|
|
| PRK10751 |
PRK10751 |
molybdopterin-guanine dinucleotide biosynthesis protein B; Provisional |
7-37 |
8.25e-05 |
|
molybdopterin-guanine dinucleotide biosynthesis protein B; Provisional
Pssm-ID: 236750 [Multi-domain] Cd Length: 173 Bit Score: 42.76 E-value: 8.25e-05
10 20 30
....*....|....*....|....*....|....
gi 500046712 7 VPVLALAGYLGAGKTTLLNHL---LRNsRGVRIG 37
Cdd:PRK10751 6 IPLLAIAAWSGTGKTTLLKKLipaLCA-RGIRPG 38
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
7-49 |
1.97e-04 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 441369 [Multi-domain] Cd Length: 162 Bit Score: 41.32 E-value: 1.97e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 500046712 7 VPVLALAGYLGAGKTTLLNHLLR--NSRGVRIGALVNDFGAVNID 49
Cdd:COG1763 1 MPVLGIVGYSGSGKTTLLEKLIPelKARGLRVGTIKHAHHDFDID 45
|
|
| MobB |
pfam03205 |
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop. |
9-97 |
3.47e-04 |
|
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.
Pssm-ID: 427196 [Multi-domain] Cd Length: 133 Bit Score: 39.84 E-value: 3.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 9 VLALAGYLGAGKTTLLNHLLR--NSRGVRIGALVNDFGAVNID---------------AMLVAGQvDAMAGLTNgcicca 71
Cdd:pfam03205 1 ILGIVGWSGSGKTTLLEKLIPelKARGLRVGTIKHAHHGFDIDkpgkdswrhrkagasEVLVASP-GRWALMHE------ 73
|
90 100
....*....|....*....|....*.
gi 500046712 72 vDADEAGEMLGKLAAVKPRLDLIVVE 97
Cdd:pfam03205 74 -LRDEPEPSLEELLARLSPVDLVLVE 98
|
|
| PRK14489 |
PRK14489 |
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ... |
2-49 |
1.99e-03 |
|
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional
Pssm-ID: 237727 [Multi-domain] Cd Length: 366 Bit Score: 39.74 E-value: 1.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 500046712 2 RTTGSVPVLALAGYLGAGKTTLLNHLLR--NSRGVRIGALVNDFGAVNID 49
Cdd:PRK14489 200 TTTGAPPLLGVVGYSGTGKTTLLEKLIPelIARGYRIGLIKHSHHRVDID 249
|
|
| YjiA |
COG2403 |
Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion ... |
141-197 |
3.71e-03 |
|
Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion transport and metabolism];
Pssm-ID: 441959 Cd Length: 441 Bit Score: 38.67 E-value: 3.71e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 500046712 141 NVQVADLVVVNKADQVSDAELEAVRAKITALNDRVPVLptefgRVDPELLVDPPQQV 197
Cdd:COG2403 258 NLRMADVVVINKVDTADPEDIETVRENIRKVNPKAEII-----EAASPVTVDDPELI 309
|
|
| GTP_EFTU |
pfam00009 |
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ... |
10-180 |
3.99e-03 |
|
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.
Pssm-ID: 425418 [Multi-domain] Cd Length: 187 Bit Score: 37.89 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 10 LALAGYLGAGKTTLLNHLLRNSRGVRIGALVNDFGAVNIDAMlvagqvdamagltngciccavDADEAGEMLGKLAAV-- 87
Cdd:pfam00009 6 IGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGEAGLDNL---------------------PEERERGITIKSAAVsf 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 500046712 88 ---KPRLDLI--------VVEASglaepaalaRTIAMADdtryhyaGLVLVVDAVES----TR--AELGNNVQVADLVVV 150
Cdd:pfam00009 65 etkDYLINLIdtpghvdfVKEVI---------RGLAQAD-------GAILVVDAVEGvmpqTRehLRLARQLGVPIIVFI 128
|
170 180 190
....*....|....*....|....*....|....*...
gi 500046712 151 NKADQVSDAELEAVRAKITAL--------NDRVPVLPT 180
Cdd:pfam00009 129 NKMDRVDGAELEEVVEEVSREllekygedGEFVPVVPG 166
|
|
| HflX |
cd01878 |
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment ... |
2-27 |
8.43e-03 |
|
HflX GTPase family; HflX subfamily. A distinct conserved domain with a glycine-rich segment N-terminal of the GTPase domain characterizes the HflX subfamily. The E. coli HflX has been implicated in the control of the lambda cII repressor proteolysis, but the actual biological functions of these GTPases remain unclear. HflX is widespread, but not universally represented in all three superkingdoms.
Pssm-ID: 206666 [Multi-domain] Cd Length: 204 Bit Score: 37.05 E-value: 8.43e-03
10 20
....*....|....*....|....*.
gi 500046712 2 RTTGSVPVLALAGYLGAGKTTLLNHL 27
Cdd:cd01878 36 RKRSGVPTVALVGYTNAGKSTLFNAL 61
|
|
| |
