|
Name |
Accession |
Description |
Interval |
E-value |
| chaper_GTP_ZigA |
NF038288 |
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ... |
15-406 |
0e+00 |
|
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: 757.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 15 LPVTVLSGFLGAGKTTLMNHVLNNREGRRVAVIVNDMSEVNIDADLIREGGADLSRTEETLVEMTNGCICCTLRDDLLNE 94
Cdd:NF038288 1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGASLSRTEEKLVEMSNGCICCTLREDLLVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 95 VRRLAEDGRFDYLLIESTGISEPLPVAATFDFRSEEGDSLSDVARLDTMVTVVDAANLLRDYASADFLRDRGESLGEEDE 174
Cdd:NF038288 81 VRRLAREGRFDYLVIESTGISEPLPVAETFTFADEDGVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEEDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 175 RSLVNLLVEQIEFADVVILNKVDVATPEALDAARKIVRALNPDAELIETSQSRVALDRVLDTGRFDFDKAQEHPLWFKEL 254
Cdd:NF038288 161 RTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 255 YGfaDHTPESEQYGVRSFTYRARQPFHPRKFFDFVNADWPG-VIRAKGHFWLATRPDWVGELSQTGALVKHEAMGFWWVS 333
Cdd:NF038288 241 RG--EHTPETEEYGISSFVYRARRPFHPQRFYDFLHSEWPGkVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMWWAA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496228965 334 VPKERWPDDPEWRRHIARAWDAVYGDRRQEIVFIGAHMDEAEIRRRLDDCLLGDADaFTLDFDLWEGLEDPFP 406
Cdd:NF038288 319 VPRERWPQDEESLAAIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEE-MAAGPEAWATLPDPFP 390
|
|
| YejR |
COG0523 |
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ... |
12-388 |
2.33e-152 |
|
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];
Pssm-ID: 440289 [Multi-domain] Cd Length: 318 Bit Score: 433.44 E-value: 2.33e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 12 DPRLPVTVLSGFLGAGKTTLMNHVLNNREGRRVAVIVNDMSEVNIDADLIREggadlsrTEETLVEMTNGCICCTLRDDL 91
Cdd:COG0523 1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRD-------TDEEIVELSNGCICCTLREDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 92 LNEVRRLAEDGRFDYLLIESTGISEPLPVAATFDFrseeGDSLSDVARLDTMVTVVDAANLLRDYASadflrdrgeslge 171
Cdd:COG0523 74 LPALRRLLRRGRFDRLLIETTGLADPAPVAQTFTF----DPELRDRLRLDGVVTVVDARNLLDDLAD------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 172 edeRSLVNLLVEQIEFADVVILNKVDVATPEALDAARKIVRALNPDAELIETSQSRVALDRVLDTGRFDFDKAQEHPLWF 251
Cdd:COG0523 137 ---RTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 252 KELYGfADHTpeseqYGVRSFTYRARQPFHPRKFFDFVNADWPGVIRAKGHFWLATRPdWVGELSQTGALVKHEAMGFWW 331
Cdd:COG0523 214 EELRD-HEHD-----DGIRSFVFRSDRPFDPERLADFLEELGPGVLRAKGFLWLAGRP-RRLVFQGVGGRLSLEPLGPWP 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 496228965 332 VsvpkerwpddpewrrhiarawdavyGDRRQEIVFIGAHMDEAEIRRRLDDCLLGDA 388
Cdd:COG0523 287 A-------------------------DDRRSRLVFIGRDLDEAALEAALDACLLTDA 318
|
|
| CobW-like |
cd03112 |
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ... |
16-237 |
1.77e-94 |
|
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: 281.72 E-value: 1.77e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 16 PVTVLSGFLGAGKTTLMNHVLNNREGRRVAVIVNDMSEVNIDADLIREGGadlsrTEETLVEMTNGCICCTLRDDLLNEV 95
Cdd:cd03112 1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSG-----GGEEVVELSNGCICCTLKGDLVKAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 96 RRLAED-GRFDYLLIESTGISEPLPVAATFDFRSEegdsLSDVARLDTMVTVVDAANLLRDYASADflrdrgeslgeede 174
Cdd:cd03112 76 EQLLERrGKFDYILIETTGLADPGPIAQTLWSDEE----LESRLRLDGVVTVVDAKNFLKQLDEED-------------- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496228965 175 rsLVNLLVEQIEFADVVILNKVDVATPEALDAARKIVRALNPDAELIETSQSRVALDRVLDTG 237
Cdd:cd03112 138 --VSDLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
|
|
| cobW |
pfam02492 |
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ... |
16-222 |
3.63e-71 |
|
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: 221.36 E-value: 3.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 16 PVTVLSGFLGAGKTTLMNHVL-NNREGRRVAVIVNDMSEVNIDADLIREggadlsrTEETLVEMTNGCICCTLRDDLLNE 94
Cdd:pfam02492 1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETGIDAELLSE-------TGVLIVELSNGCICCTIREDLSMA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 95 VRRLAED-GRFDYLLIESTGISEPLPVAATFDFRseegdSLSDVARLDTMVTVVDAANllrdyasadflrdrgeslgEED 173
Cdd:pfam02492 74 LEALLEReGRLDVIFIETTGLAEPAPVAQTFLSP-----ELRSPVLLDGVITVVDAAN-------------------EAD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496228965 174 ERSLVNLLVEQIEFADVVILNKVDVATPEA-LDAARKIVRALNPDAELIE 222
Cdd:pfam02492 130 GEKIPRKAGDQIAFADLIVLNKTDLAPEVAlLEVLEEDLRRLNPGAPVVP 179
|
|
| CobW |
TIGR02475 |
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ... |
14-380 |
7.90e-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: 7.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 14 RLPVTVLSGFLGAGKTTLMNHVLNNREGRRVAVIVNDMSEVNIDADLIREGGADLSrTEETLVEMTNGCICCTLRDDLLN 93
Cdd:TIGR02475 3 KIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEGC-SEENIVELANGCICCTVADDFIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 94 EVRRL-AEDGRFDYLLIESTGISEPLPVAATFDF---RSEegdslsdvARLDTMVTVVDAANLL-----RDYASADFLRD 164
Cdd:TIGR02475 82 TMTKLlARRQRPDHILIETSGLALPKPLVQAFQWpeiRSR--------VTVDGVVTVVDGPAVAagrfaADPDALDAQRA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 165 RGESLGEEDerSLVNLLVEQIEFADVVILNKVDVATPEALDAARKIVRALNPDA-ELIETSQSRVALDRVLDTG---RFD 240
Cdd:TIGR02475 154 ADDNLDHET--PLEELFEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAvKIVEASHGEVDARVLLGLGaaaEDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 241 FDKAQEHplwfKELYGFADHTPESEQygvrSFTYRARQPFHPRKFFDFVN--ADWPGVIRAKGHFWLATRPdwvgelsqT 318
Cdd:TIGR02475 232 LDNRPSH----HDFEGGEEHDHDEFD----SVVVDLGEVADPAALRQRLErlAEEHDVLRIKGFAAVPGKP--------M 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496228965 319 GALVkhEAMGfwwvsvpkerwpddPEWRRHIARAWDAVYgDRRQEIVFIGAH-MDEAEIRRRL 380
Cdd:TIGR02475 296 RLLV--QGVG--------------QRVDSYYDRPWQAAE-TRQTRLVVIGLHdLDQAAIRAAL 341
|
|
| CobW_C |
smart00833 |
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ... |
269-384 |
2.60e-29 |
|
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: 109.22 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 269 VRSFTYRARQPFHPRKFFDFVNADWPGVIRAKGHFWLATRPDWVGELSQTGALVKHEAMGFWWVSvpkerwpddpewrrh 348
Cdd:smart00833 1 ISSFVYRARRPFHPQRLLAALDELPEGVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPAA--------------- 65
|
90 100 110
....*....|....*....|....*....|....*.
gi 496228965 349 iarawdavyGDRRQEIVFIGAHMDEAEIRRRLDDCL 384
Cdd:smart00833 66 ---------GDRRTRLVFIGRDLDEEAIRAALDACL 92
|
|
| PRK11537 |
PRK11537 |
putative GTP-binding protein YjiA; Provisional |
15-239 |
7.67e-26 |
|
putative GTP-binding protein YjiA; Provisional
Pssm-ID: 183183 [Multi-domain] Cd Length: 318 Bit Score: 106.33 E-value: 7.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 15 LPVTVLSGFLGAGKTTLMNHVLNNREGRRVAVIVNDMSEVNIDADLIreggADLSRTEETLvemTNGCICCT----LRD- 89
Cdd:PRK11537 4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLI----GDRATQIKTL---TNGCICCSrsneLEDa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 90 --DLLNEVRRlaEDGRFDYLLIESTGISEPLPVAATFdFRSEegdSLSDVARLDTMVTVVDAANllrdyasADFLRDRge 167
Cdd:PRK11537 77 llDLLDNLDK--GNIQFDRLVIECTGMADPGPIIQTF-FSHE---VLCQRYLLDGVIALVDAVH-------ADEQMNQ-- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496228965 168 slgeederslVNLLVEQIEFADVVILNKVDVAtPEAlDAARKIVRALNPDAELIETSQSRVALDRVLDTGRF 239
Cdd:PRK11537 142 ----------FTIAQSQVGYADRILLTKTDVA-GEA-EKLRERLARINARAPVYTVVHGDIDLSLLFNTNGF 201
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| chaper_GTP_ZigA |
NF038288 |
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ... |
15-406 |
0e+00 |
|
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: 757.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 15 LPVTVLSGFLGAGKTTLMNHVLNNREGRRVAVIVNDMSEVNIDADLIREGGADLSRTEETLVEMTNGCICCTLRDDLLNE 94
Cdd:NF038288 1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGASLSRTEEKLVEMSNGCICCTLREDLLVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 95 VRRLAEDGRFDYLLIESTGISEPLPVAATFDFRSEEGDSLSDVARLDTMVTVVDAANLLRDYASADFLRDRGESLGEEDE 174
Cdd:NF038288 81 VRRLAREGRFDYLVIESTGISEPLPVAETFTFADEDGVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEEDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 175 RSLVNLLVEQIEFADVVILNKVDVATPEALDAARKIVRALNPDAELIETSQSRVALDRVLDTGRFDFDKAQEHPLWFKEL 254
Cdd:NF038288 161 RTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 255 YGfaDHTPESEQYGVRSFTYRARQPFHPRKFFDFVNADWPG-VIRAKGHFWLATRPDWVGELSQTGALVKHEAMGFWWVS 333
Cdd:NF038288 241 RG--EHTPETEEYGISSFVYRARRPFHPQRFYDFLHSEWPGkVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMWWAA 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496228965 334 VPKERWPDDPEWRRHIARAWDAVYGDRRQEIVFIGAHMDEAEIRRRLDDCLLGDADaFTLDFDLWEGLEDPFP 406
Cdd:NF038288 319 VPRERWPQDEESLAAIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEE-MAAGPEAWATLPDPFP 390
|
|
| YejR |
COG0523 |
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ... |
12-388 |
2.33e-152 |
|
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];
Pssm-ID: 440289 [Multi-domain] Cd Length: 318 Bit Score: 433.44 E-value: 2.33e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 12 DPRLPVTVLSGFLGAGKTTLMNHVLNNREGRRVAVIVNDMSEVNIDADLIREggadlsrTEETLVEMTNGCICCTLRDDL 91
Cdd:COG0523 1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRD-------TDEEIVELSNGCICCTLREDL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 92 LNEVRRLAEDGRFDYLLIESTGISEPLPVAATFDFrseeGDSLSDVARLDTMVTVVDAANLLRDYASadflrdrgeslge 171
Cdd:COG0523 74 LPALRRLLRRGRFDRLLIETTGLADPAPVAQTFTF----DPELRDRLRLDGVVTVVDARNLLDDLAD------------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 172 edeRSLVNLLVEQIEFADVVILNKVDVATPEALDAARKIVRALNPDAELIETSQSRVALDRVLDTGRFDFDKAQEHPLWF 251
Cdd:COG0523 137 ---RTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 252 KELYGfADHTpeseqYGVRSFTYRARQPFHPRKFFDFVNADWPGVIRAKGHFWLATRPdWVGELSQTGALVKHEAMGFWW 331
Cdd:COG0523 214 EELRD-HEHD-----DGIRSFVFRSDRPFDPERLADFLEELGPGVLRAKGFLWLAGRP-RRLVFQGVGGRLSLEPLGPWP 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 496228965 332 VsvpkerwpddpewrrhiarawdavyGDRRQEIVFIGAHMDEAEIRRRLDDCLLGDA 388
Cdd:COG0523 287 A-------------------------DDRRSRLVFIGRDLDEAALEAALDACLLTDA 318
|
|
| CobW-like |
cd03112 |
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ... |
16-237 |
1.77e-94 |
|
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: 281.72 E-value: 1.77e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 16 PVTVLSGFLGAGKTTLMNHVLNNREGRRVAVIVNDMSEVNIDADLIREGGadlsrTEETLVEMTNGCICCTLRDDLLNEV 95
Cdd:cd03112 1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSG-----GGEEVVELSNGCICCTLKGDLVKAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 96 RRLAED-GRFDYLLIESTGISEPLPVAATFDFRSEegdsLSDVARLDTMVTVVDAANLLRDYASADflrdrgeslgeede 174
Cdd:cd03112 76 EQLLERrGKFDYILIETTGLADPGPIAQTLWSDEE----LESRLRLDGVVTVVDAKNFLKQLDEED-------------- 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496228965 175 rsLVNLLVEQIEFADVVILNKVDVATPEALDAARKIVRALNPDAELIETSQSRVALDRVLDTG 237
Cdd:cd03112 138 --VSDLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
|
|
| cobW |
pfam02492 |
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ... |
16-222 |
3.63e-71 |
|
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: 221.36 E-value: 3.63e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 16 PVTVLSGFLGAGKTTLMNHVL-NNREGRRVAVIVNDMSEVNIDADLIREggadlsrTEETLVEMTNGCICCTLRDDLLNE 94
Cdd:pfam02492 1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETGIDAELLSE-------TGVLIVELSNGCICCTIREDLSMA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 95 VRRLAED-GRFDYLLIESTGISEPLPVAATFDFRseegdSLSDVARLDTMVTVVDAANllrdyasadflrdrgeslgEED 173
Cdd:pfam02492 74 LEALLEReGRLDVIFIETTGLAEPAPVAQTFLSP-----ELRSPVLLDGVITVVDAAN-------------------EAD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 496228965 174 ERSLVNLLVEQIEFADVVILNKVDVATPEA-LDAARKIVRALNPDAELIE 222
Cdd:pfam02492 130 GEKIPRKAGDQIAFADLIVLNKTDLAPEVAlLEVLEEDLRRLNPGAPVVP 179
|
|
| CobW |
TIGR02475 |
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ... |
14-380 |
7.90e-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: 7.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 14 RLPVTVLSGFLGAGKTTLMNHVLNNREGRRVAVIVNDMSEVNIDADLIREGGADLSrTEETLVEMTNGCICCTLRDDLLN 93
Cdd:TIGR02475 3 KIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEGC-SEENIVELANGCICCTVADDFIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 94 EVRRL-AEDGRFDYLLIESTGISEPLPVAATFDF---RSEegdslsdvARLDTMVTVVDAANLL-----RDYASADFLRD 164
Cdd:TIGR02475 82 TMTKLlARRQRPDHILIETSGLALPKPLVQAFQWpeiRSR--------VTVDGVVTVVDGPAVAagrfaADPDALDAQRA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 165 RGESLGEEDerSLVNLLVEQIEFADVVILNKVDVATPEALDAARKIVRALNPDA-ELIETSQSRVALDRVLDTG---RFD 240
Cdd:TIGR02475 154 ADDNLDHET--PLEELFEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAvKIVEASHGEVDARVLLGLGaaaEDD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 241 FDKAQEHplwfKELYGFADHTPESEQygvrSFTYRARQPFHPRKFFDFVN--ADWPGVIRAKGHFWLATRPdwvgelsqT 318
Cdd:TIGR02475 232 LDNRPSH----HDFEGGEEHDHDEFD----SVVVDLGEVADPAALRQRLErlAEEHDVLRIKGFAAVPGKP--------M 295
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496228965 319 GALVkhEAMGfwwvsvpkerwpddPEWRRHIARAWDAVYgDRRQEIVFIGAH-MDEAEIRRRL 380
Cdd:TIGR02475 296 RLLV--QGVG--------------QRVDSYYDRPWQAAE-TRQTRLVVIGLHdLDQAAIRAAL 341
|
|
| CobW_C |
smart00833 |
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ... |
269-384 |
2.60e-29 |
|
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: 109.22 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 269 VRSFTYRARQPFHPRKFFDFVNADWPGVIRAKGHFWLATRPDWVGELSQTGALVKHEAMGFWWVSvpkerwpddpewrrh 348
Cdd:smart00833 1 ISSFVYRARRPFHPQRLLAALDELPEGVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPAA--------------- 65
|
90 100 110
....*....|....*....|....*....|....*.
gi 496228965 349 iarawdavyGDRRQEIVFIGAHMDEAEIRRRLDDCL 384
Cdd:smart00833 66 ---------GDRRTRLVFIGRDLDEEAIRAALDACL 92
|
|
| PRK11537 |
PRK11537 |
putative GTP-binding protein YjiA; Provisional |
15-239 |
7.67e-26 |
|
putative GTP-binding protein YjiA; Provisional
Pssm-ID: 183183 [Multi-domain] Cd Length: 318 Bit Score: 106.33 E-value: 7.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 15 LPVTVLSGFLGAGKTTLMNHVLNNREGRRVAVIVNDMSEVNIDADLIreggADLSRTEETLvemTNGCICCT----LRD- 89
Cdd:PRK11537 4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLI----GDRATQIKTL---TNGCICCSrsneLEDa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 90 --DLLNEVRRlaEDGRFDYLLIESTGISEPLPVAATFdFRSEegdSLSDVARLDTMVTVVDAANllrdyasADFLRDRge 167
Cdd:PRK11537 77 llDLLDNLDK--GNIQFDRLVIECTGMADPGPIIQTF-FSHE---VLCQRYLLDGVIALVDAVH-------ADEQMNQ-- 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496228965 168 slgeederslVNLLVEQIEFADVVILNKVDVAtPEAlDAARKIVRALNPDAELIETSQSRVALDRVLDTGRF 239
Cdd:PRK11537 142 ----------FTIAQSQVGYADRILLTKTDVA-GEA-EKLRERLARINARAPVYTVVHGDIDLSLLFNTNGF 201
|
|
| CobW_C |
pfam07683 |
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ... |
269-384 |
3.21e-23 |
|
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: 3.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 269 VRSFTYRARQPFHPRKFFDFVNAD--WPGVIRAKGHFWLATRPDWVgELSQTGALVKHEAMGFWWVsvpkerwpddpewr 346
Cdd:pfam07683 1 ISSFVFRADRPFDPERLEAWLEDLllPEGILRAKGILWLAGRPRPL-VFQGVGGRLSLEPAGRWWP-------------- 65
|
90 100 110
....*....|....*....|....*....|....*...
gi 496228965 347 rhiarawdavYGDRRQEIVFIGAHMDEAEIRRRLDDCL 384
Cdd:pfam07683 66 ----------DEDRRSRLVFIGRDLDREALRAALDACL 93
|
|
| YjiA |
COG2403 |
Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion ... |
141-232 |
7.93e-09 |
|
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: 57.15 E-value: 7.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 141 DTMVTVVDAanllrdyasadfLRDRGESL---GEederslVNLLVeqiefADVVILNKVDVATPEALDAARKIVRALNPD 217
Cdd:COG2403 235 DLHIVVADP------------HRPGHELSyypGE------VNLRM-----ADVVVINKVDTADPEDIETVRENIRKVNPK 291
|
90
....*....|....*
gi 496228965 218 AELIETSqSRVALDR 232
Cdd:COG2403 292 AEIIEAA-SPVTVDD 305
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
25-224 |
1.52e-08 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 54.30 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 25 GAGKTTLMNHVLNN-REGRRVAVIVNDMsEVNIDADLIREGGAdlsRTEEtlVEmTNGciCCTLrDDLLNE--VRRLAED 101
Cdd:COG0378 23 GSGKTTLLEKTIRAlKDRLRIAVIEGDI-YTTEDAERLRAAGV---PVVQ--IN-TGG--CCHL-DASMVLeaLEELDLP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 102 GrFDYLLIESTGIseplPVAATFdfrSEEGDSLSdvarldtmVTVVDAA---NLLRDYASAdflrdrgeslgeederslv 178
Cdd:COG0378 93 D-LDLLFIENVGN----LVCPAF---FPLGEDLK--------VVVLSVTegdDKPRKYPPM------------------- 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 496228965 179 nllveqIEFADVVILNKVDVAtPEA---LDAARKIVRALNPDAELIETS 224
Cdd:COG0378 138 ------FTAADLLVINKIDLA-PYVgfdLEVMEEDARRVNPGAPIFEVS 179
|
|
| HypB |
cd05390 |
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the ... |
25-224 |
1.22e-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: 51.83 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 25 GAGKTTLMNHVLNN-REGRRVAVIVNDMsEVNIDADLIREGGAdlsrteetLVEMTNGCICCTLRDDLLNE-VRRLAEDG 102
Cdd:cd05390 31 GSGKTTLLERTIDAlKDELKIAVIEGDL-ETDNDAERIRATGV--------PAIQINTGGACHLDADMVARaLHDLDLDE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 103 rFDYLLIESTGisePLPVAATFDfrseegdsLSDVARldtmVTVVdaanllrdyasadflrdrgeSLGEEDERSLVNLLV 182
Cdd:cd05390 102 -LDLLFIENVG---NLVCPAEFD--------LGEHKN----VVLL--------------------SVTEGDDKPLKYPLM 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 496228965 183 EQIefADVVILNKVDVAtpEALD----AARKIVRALNPDAELIETS 224
Cdd:cd05390 146 FQV--ADVVLINKIDLL--PYFDfdveKAKEDIKKLNPNAPIIEVS 187
|
|
| MobB |
cd03116 |
molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace ... |
20-135 |
1.45e-04 |
|
molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace element in the form of molybdenum cofactor (Moco) which is associated with the metabolism of nitrogen, carbon and sulfur by redox active enzymes. In Escherichia coli, the synthesis of Moco involves genes from several loci: moa, mob, mod, moe and mog. The mob locus contains mobA and mobB genes. MobB catalyzes the attachment of the guanine dinucleotide to molybdopterin.
Pssm-ID: 349770 [Multi-domain] Cd Length: 157 Bit Score: 41.86 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 20 LSGFLGAGKTTLMNHVLN--NREGRRVAVIVNDMSEVNI-----DADLIREGGADlsrteETLVEmTNGCI----CCTLR 88
Cdd:cd03116 5 VVGKSGSGKTTLIEKLIPelKARGLRVAVIKHTHHGFDIdtpgkDSYRHRQAGAD-----AVLVS-SPNRLalihERPEW 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 496228965 89 DDLLNEVRRLAEDgrFDYLLIEstGI-SEPLPVAATfdFRSEEGDSLS 135
Cdd:cd03116 79 ELTLLELLARFSD--VDLVLVE--GFkKEPIPKIEV--FREEEGKPLL 120
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
25-163 |
5.47e-04 |
|
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: 40.05 E-value: 5.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 25 GAGKTTLMNHVLNNREGRRVAVIVndmsevnIDADLIREGGADLSRTEETLVEMTNGcicctLRDDLLNEVRRLAEDGRF 104
Cdd:smart00382 12 GSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLDQLLLIIVGGKKASG-----SGELRLRLALALARKLKP 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 496228965 105 DYLLIEStgISEPLPVAATFDFRSEEGDSLSDVARLDTMVTVVDAANLLRDYASADFLR 163
Cdd:smart00382 80 DVLILDE--ITSLLDAEQEALLLLLEELRLLLLLKSEKNLTVILTTNDEKDLGPALLRR 136
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
143-236 |
2.86e-03 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 39.20 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496228965 143 MVTVVDAAnlLRDyasAD---FLRDRGESLGEEDERslvnlLVEQIEFAD---VVILNKVDVATPEALDAARKIVRALNP 216
Cdd:COG1159 72 MNKAAWSA--LED---VDvilFVVDATEKIGEGDEF-----ILELLKKLKtpvILVINKIDLVKKEELLPLLAEYSELLD 141
|
90 100
....*....|....*....|.
gi 496228965 217 DAELIETS-QSRVALDRVLDT 236
Cdd:COG1159 142 FAEIVPISaLKGDNVDELLDE 162
|
|
| |
