|
Name |
Accession |
Description |
Interval |
E-value |
| chaper_GTP_ZigA |
NF038288 |
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ... |
4-392 |
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: 558.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 4 IPVTVLSGYLGSGKTTLLNHILKNREGRRIAVIVNDMSEVNIDKDLVAQGGG-LSRTDEKLVELSNGCICCTLRDDLLRE 82
Cdd:NF038288 1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGAsLSRTEEKLVEMSNGCICCTLREDLLVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 83 VERLVHKGGIDQIVIESTGISEPVPVAQTFSYIDEElGIDLTSICRLDTMVTVVDANRFVNDIRSEDLLADRDESVDDED 162
Cdd:NF038288 81 VRRLAREGRFDYLVIESTGISEPLPVAETFTFADED-GVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 163 ERTIADLLIDQVEFCDVMIINKIDLISDEVLEKLENVLRALQPEAKIIKTVNAKVELSDVLNTQLFDFEKASESAGWIKE 242
Cdd:NF038288 160 ERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 243 LtaggHATHTPETEEYGITSFAYTRRLPFHAKRFHQWLEQ-MPENIVRTKGIVWLAQYNDVACLLSQAGSSCNIHPVTYW 321
Cdd:NF038288 240 L----RGEHTPETEEYGISSFVYRARRPFHPQRFYDFLHSeWPGKVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMW 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488432549 322 VATMSESQQQAILEARQDVVEDWDIEYGDRQTQFVIIGTDLDQEKISRELDACLIHSSEIDED---WRLLDSPY 392
Cdd:NF038288 316 WAAVPRERWPQDEESLAAIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEEMAAGpeaWATLPDPF 389
|
|
| YejR |
COG0523 |
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ... |
1-379 |
3.90e-144 |
|
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];
Pssm-ID: 440289 [Multi-domain] Cd Length: 318 Bit Score: 412.26 E-value: 3.90e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 1 MAKIPVTVLSGYLGSGKTTLLNHILKNREGRRIAVIVNDMSEVNIDKDLVAQggglsrTDEKLVELSNGCICCTLRDDLL 80
Cdd:COG0523 1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRD------TDEEIVELSNGCICCTLREDLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 81 REVERLVHKGGIDQIVIESTGISEPVPVAQTFSYideelGIDLTSICRLDTMVTVVDANRFvndirsedlladrdesVDD 160
Cdd:COG0523 75 PALRRLLRRGRFDRLLIETTGLADPAPVAQTFTF-----DPELRDRLRLDGVVTVVDARNL----------------LDD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 161 EDERTIADLLIDQVEFCDVMIINKIDLISDEVLEKLENVLRALQPEAKIIKTVNAKVELSDVLNTQLFDFEKASESAGWI 240
Cdd:COG0523 134 LADRTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 241 KELTAGGHAthtpeteeYGITSFAYTRRLPFHAKRFHQWLEQMPENIVRTKGIVWLAQyNDVACLLSQAGSSCNIHPVTY 320
Cdd:COG0523 214 EELRDHEHD--------DGIRSFVFRSDRPFDPERLADFLEELGPGVLRAKGFLWLAG-RPRRLVFQGVGGRLSLEPLGP 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 488432549 321 WVAtmsesqqqailearqdvvedwdieyGDRQTQFVIIGTDLDQEKISRELDACLIHSS 379
Cdd:COG0523 285 WPA-------------------------DDRRSRLVFIGRDLDEAALEAALDACLLTDA 318
|
|
| CobW-like |
cd03112 |
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ... |
5-225 |
2.54e-87 |
|
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: 263.23 E-value: 2.54e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 5 PVTVLSGYLGSGKTTLLNHILKNREGRRIAVIVNDMSEVNIDKDLVAQGGGlsrtDEKLVELSNGCICCTLRDDLLREVE 84
Cdd:cd03112 1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGG----GEEVVELSNGCICCTLKGDLVKALE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 85 RLVHKGG-IDQIVIESTGISEPVPVAQTFSYIDEelgidLTSICRLDTMVTVVDANRFVNDIRSEDLladrdesvddede 163
Cdd:cd03112 77 QLLERRGkFDYILIETTGLADPGPIAQTLWSDEE-----LESRLRLDGVVTVVDAKNFLKQLDEEDV------------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488432549 164 rtiADLLIDQVEFCDVMIINKIDLISDEVLEKLENVLRALQPEAKIIKTVNAKVELSDVLNT 225
Cdd:cd03112 139 ---SDLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGT 197
|
|
| cobW |
pfam02492 |
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ... |
5-210 |
1.05e-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: 222.51 E-value: 1.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 5 PVTVLSGYLGSGKTTLLNHILK-NREGRRIAVIVNDMSEVNIDKDLvaqgggLSRTDEKLVELSNGCICCTLRDDLLREV 83
Cdd:pfam02492 1 PVTVITGFLGSGKTTLLNHLLKqNRAGLRIAVIVNEFGETGIDAEL------LSETGVLIVELSNGCICCTIREDLSMAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 84 ERLVHKGG-IDQIVIESTGISEPVPVAQTFSYideelgIDLTSICRLDTMVTVVDANRFvndirsedlladrdesvddED 162
Cdd:pfam02492 75 EALLEREGrLDVIFIETTGLAEPAPVAQTFLS------PELRSPVLLDGVITVVDAANE-------------------AD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488432549 163 ERTIADLLIDQVEFCDVMIINKIDLISDE-VLEKLENVLRALQPEAKII 210
Cdd:pfam02492 130 GEKIPRKAGDQIAFADLIVLNKTDLAPEVaLLEVLEEDLRRLNPGAPVV 178
|
|
| CobW |
TIGR02475 |
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ... |
1-223 |
1.83e-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: 159.91 E-value: 1.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 1 MAKIPVTVLSGYLGSGKTTLLNHILKNREGRRIAVIVNDMSEVNIDKDLVAQGGGLSRTDEKLVELSNGCICCTLRDDLL 80
Cdd:TIGR02475 1 LAKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEGCSEENIVELANGCICCTVADDFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 81 REVERLVHKGG-IDQIVIESTGISEPVPVAQTFSYideelgIDLTSICRLDTMVTVVD-----ANRFVNDIRSEDLLADR 154
Cdd:TIGR02475 81 PTMTKLLARRQrPDHILIETSGLALPKPLVQAFQW------PEIRSRVTVDGVVTVVDgpavaAGRFAADPDALDAQRAA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 155 DESVDDEDerTIADLLIDQVEFCDVMIINKIDLISDEVLEKLENVLRALQPEA-KIIKTVNAKVELSDVL 223
Cdd:TIGR02475 155 DDNLDHET--PLEELFEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAvKIVEASHGEVDARVLL 222
|
|
| PRK11537 |
PRK11537 |
putative GTP-binding protein YjiA; Provisional |
1-373 |
1.11e-32 |
|
putative GTP-binding protein YjiA; Provisional
Pssm-ID: 183183 [Multi-domain] Cd Length: 318 Bit Score: 125.20 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 1 MAKIPVTVLSGYLGSGKTTLLNHILKNREGRRIAVIVNDMSEVNIDKDLVAQGGGLSRTdeklveLSNGCICCT----LR 76
Cdd:PRK11537 1 MNPIAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIGDRATQIKT------LTNGCICCSrsneLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 77 DDLLREVErLVHKGGI--DQIVIESTGISEPVPVAQTFsYIDEELgidltsiCR---LDTMVTVVDAnrfvndIRSEDLL 151
Cdd:PRK11537 75 DALLDLLD-NLDKGNIqfDRLVIECTGMADPGPIIQTF-FSHEVL-------CQrylLDGVIALVDA------VHADEQM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 152 adrdesvddeDERTIADlliDQVEFCDVMIINKIDLISDEvlEKLENVLRALQPEAKIIKTVNAKVELSDVLNTQLFDFE 231
Cdd:PRK11537 140 ----------NQFTIAQ---SQVGYADRILLTKTDVAGEA--EKLRERLARINARAPVYTVVHGDIDLSLLFNTNGFMLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 232 kasesagwiKELTAGGHATHTPETEEYGITS----FAYTRRLPFHAKRFHQWLEQMPENIVRTKGIVWLAqyNDVACLLS 307
Cdd:PRK11537 205 ---------ENVVSTKPRFHFIADKQNDISSivveLDYPVDISEVSRVMENLLLESADKLLRYKGMLWID--GEPNRLLF 273
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488432549 308 QAgsscnihpvtywvatmsesqQQAILEArqdvveDWDIEYGD--RQTQFVIIGTDLDQEKISRELDA 373
Cdd:PRK11537 274 QG--------------------VQRLYSA------DWDRPWGDetPHSTLVFIGIQLPEEEIRAAFAG 315
|
|
| CobW_C |
smart00833 |
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ... |
260-375 |
1.01e-30 |
|
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: 113.08 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 260 ITSFAYTRRLPFHAKRFHQWLEQMPENIVRTKGIVWLAQYNDVACLLSQAGSSCNIHPVTYWVATmsesqqqailearqd 339
Cdd:smart00833 1 ISSFVYRARRPFHPQRLLAALDELPEGVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPAA--------------- 65
|
90 100 110
....*....|....*....|....*....|....*.
gi 488432549 340 vvedwdieyGDRQTQFVIIGTDLDQEKISRELDACL 375
Cdd:smart00833 66 ---------GDRRTRLVFIGRDLDEEAIRAALDACL 92
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| chaper_GTP_ZigA |
NF038288 |
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ... |
4-392 |
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: 558.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 4 IPVTVLSGYLGSGKTTLLNHILKNREGRRIAVIVNDMSEVNIDKDLVAQGGG-LSRTDEKLVELSNGCICCTLRDDLLRE 82
Cdd:NF038288 1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGAsLSRTEEKLVEMSNGCICCTLREDLLVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 83 VERLVHKGGIDQIVIESTGISEPVPVAQTFSYIDEElGIDLTSICRLDTMVTVVDANRFVNDIRSEDLLADRDESVDDED 162
Cdd:NF038288 81 VRRLAREGRFDYLVIESTGISEPLPVAETFTFADED-GVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 163 ERTIADLLIDQVEFCDVMIINKIDLISDEVLEKLENVLRALQPEAKIIKTVNAKVELSDVLNTQLFDFEKASESAGWIKE 242
Cdd:NF038288 160 ERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 243 LtaggHATHTPETEEYGITSFAYTRRLPFHAKRFHQWLEQ-MPENIVRTKGIVWLAQYNDVACLLSQAGSSCNIHPVTYW 321
Cdd:NF038288 240 L----RGEHTPETEEYGISSFVYRARRPFHPQRFYDFLHSeWPGKVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMW 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488432549 322 VATMSESQQQAILEARQDVVEDWDIEYGDRQTQFVIIGTDLDQEKISRELDACLIHSSEIDED---WRLLDSPY 392
Cdd:NF038288 316 WAAVPRERWPQDEESLAAIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEEMAAGpeaWATLPDPF 389
|
|
| YejR |
COG0523 |
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ... |
1-379 |
3.90e-144 |
|
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];
Pssm-ID: 440289 [Multi-domain] Cd Length: 318 Bit Score: 412.26 E-value: 3.90e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 1 MAKIPVTVLSGYLGSGKTTLLNHILKNREGRRIAVIVNDMSEVNIDKDLVAQggglsrTDEKLVELSNGCICCTLRDDLL 80
Cdd:COG0523 1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRD------TDEEIVELSNGCICCTLREDLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 81 REVERLVHKGGIDQIVIESTGISEPVPVAQTFSYideelGIDLTSICRLDTMVTVVDANRFvndirsedlladrdesVDD 160
Cdd:COG0523 75 PALRRLLRRGRFDRLLIETTGLADPAPVAQTFTF-----DPELRDRLRLDGVVTVVDARNL----------------LDD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 161 EDERTIADLLIDQVEFCDVMIINKIDLISDEVLEKLENVLRALQPEAKIIKTVNAKVELSDVLNTQLFDFEKASESAGWI 240
Cdd:COG0523 134 LADRTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 241 KELTAGGHAthtpeteeYGITSFAYTRRLPFHAKRFHQWLEQMPENIVRTKGIVWLAQyNDVACLLSQAGSSCNIHPVTY 320
Cdd:COG0523 214 EELRDHEHD--------DGIRSFVFRSDRPFDPERLADFLEELGPGVLRAKGFLWLAG-RPRRLVFQGVGGRLSLEPLGP 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 488432549 321 WVAtmsesqqqailearqdvvedwdieyGDRQTQFVIIGTDLDQEKISRELDACLIHSS 379
Cdd:COG0523 285 WPA-------------------------DDRRSRLVFIGRDLDEAALEAALDACLLTDA 318
|
|
| CobW-like |
cd03112 |
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ... |
5-225 |
2.54e-87 |
|
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: 263.23 E-value: 2.54e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 5 PVTVLSGYLGSGKTTLLNHILKNREGRRIAVIVNDMSEVNIDKDLVAQGGGlsrtDEKLVELSNGCICCTLRDDLLREVE 84
Cdd:cd03112 1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGG----GEEVVELSNGCICCTLKGDLVKALE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 85 RLVHKGG-IDQIVIESTGISEPVPVAQTFSYIDEelgidLTSICRLDTMVTVVDANRFVNDIRSEDLladrdesvddede 163
Cdd:cd03112 77 QLLERRGkFDYILIETTGLADPGPIAQTLWSDEE-----LESRLRLDGVVTVVDAKNFLKQLDEEDV------------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488432549 164 rtiADLLIDQVEFCDVMIINKIDLISDEVLEKLENVLRALQPEAKIIKTVNAKVELSDVLNT 225
Cdd:cd03112 139 ---SDLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGT 197
|
|
| cobW |
pfam02492 |
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ... |
5-210 |
1.05e-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: 222.51 E-value: 1.05e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 5 PVTVLSGYLGSGKTTLLNHILK-NREGRRIAVIVNDMSEVNIDKDLvaqgggLSRTDEKLVELSNGCICCTLRDDLLREV 83
Cdd:pfam02492 1 PVTVITGFLGSGKTTLLNHLLKqNRAGLRIAVIVNEFGETGIDAEL------LSETGVLIVELSNGCICCTIREDLSMAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 84 ERLVHKGG-IDQIVIESTGISEPVPVAQTFSYideelgIDLTSICRLDTMVTVVDANRFvndirsedlladrdesvddED 162
Cdd:pfam02492 75 EALLEREGrLDVIFIETTGLAEPAPVAQTFLS------PELRSPVLLDGVITVVDAANE-------------------AD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 488432549 163 ERTIADLLIDQVEFCDVMIINKIDLISDE-VLEKLENVLRALQPEAKII 210
Cdd:pfam02492 130 GEKIPRKAGDQIAFADLIVLNKTDLAPEVaLLEVLEEDLRRLNPGAPVV 178
|
|
| CobW |
TIGR02475 |
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ... |
1-223 |
1.83e-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: 159.91 E-value: 1.83e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 1 MAKIPVTVLSGYLGSGKTTLLNHILKNREGRRIAVIVNDMSEVNIDKDLVAQGGGLSRTDEKLVELSNGCICCTLRDDLL 80
Cdd:TIGR02475 1 LAKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEGCSEENIVELANGCICCTVADDFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 81 REVERLVHKGG-IDQIVIESTGISEPVPVAQTFSYideelgIDLTSICRLDTMVTVVD-----ANRFVNDIRSEDLLADR 154
Cdd:TIGR02475 81 PTMTKLLARRQrPDHILIETSGLALPKPLVQAFQW------PEIRSRVTVDGVVTVVDgpavaAGRFAADPDALDAQRAA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 155 DESVDDEDerTIADLLIDQVEFCDVMIINKIDLISDEVLEKLENVLRALQPEA-KIIKTVNAKVELSDVL 223
Cdd:TIGR02475 155 DDNLDHET--PLEELFEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAvKIVEASHGEVDARVLL 222
|
|
| PRK11537 |
PRK11537 |
putative GTP-binding protein YjiA; Provisional |
1-373 |
1.11e-32 |
|
putative GTP-binding protein YjiA; Provisional
Pssm-ID: 183183 [Multi-domain] Cd Length: 318 Bit Score: 125.20 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 1 MAKIPVTVLSGYLGSGKTTLLNHILKNREGRRIAVIVNDMSEVNIDKDLVAQGGGLSRTdeklveLSNGCICCT----LR 76
Cdd:PRK11537 1 MNPIAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIGDRATQIKT------LTNGCICCSrsneLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 77 DDLLREVErLVHKGGI--DQIVIESTGISEPVPVAQTFsYIDEELgidltsiCR---LDTMVTVVDAnrfvndIRSEDLL 151
Cdd:PRK11537 75 DALLDLLD-NLDKGNIqfDRLVIECTGMADPGPIIQTF-FSHEVL-------CQrylLDGVIALVDA------VHADEQM 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 152 adrdesvddeDERTIADlliDQVEFCDVMIINKIDLISDEvlEKLENVLRALQPEAKIIKTVNAKVELSDVLNTQLFDFE 231
Cdd:PRK11537 140 ----------NQFTIAQ---SQVGYADRILLTKTDVAGEA--EKLRERLARINARAPVYTVVHGDIDLSLLFNTNGFMLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 232 kasesagwiKELTAGGHATHTPETEEYGITS----FAYTRRLPFHAKRFHQWLEQMPENIVRTKGIVWLAqyNDVACLLS 307
Cdd:PRK11537 205 ---------ENVVSTKPRFHFIADKQNDISSivveLDYPVDISEVSRVMENLLLESADKLLRYKGMLWID--GEPNRLLF 273
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488432549 308 QAgsscnihpvtywvatmsesqQQAILEArqdvveDWDIEYGD--RQTQFVIIGTDLDQEKISRELDA 373
Cdd:PRK11537 274 QG--------------------VQRLYSA------DWDRPWGDetPHSTLVFIGIQLPEEEIRAAFAG 315
|
|
| CobW_C |
smart00833 |
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ... |
260-375 |
1.01e-30 |
|
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: 113.08 E-value: 1.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 260 ITSFAYTRRLPFHAKRFHQWLEQMPENIVRTKGIVWLAQYNDVACLLSQAGSSCNIHPVTYWVATmsesqqqailearqd 339
Cdd:smart00833 1 ISSFVYRARRPFHPQRLLAALDELPEGVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPAA--------------- 65
|
90 100 110
....*....|....*....|....*....|....*.
gi 488432549 340 vvedwdieyGDRQTQFVIIGTDLDQEKISRELDACL 375
Cdd:smart00833 66 ---------GDRRTRLVFIGRDLDEEAIRAALDACL 92
|
|
| CobW_C |
pfam07683 |
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ... |
260-375 |
7.88e-21 |
|
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: 86.14 E-value: 7.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 260 ITSFAYTRRLPFHAKRFHQWLE--QMPENIVRTKGIVWLAQyNDVACLLSQAGSSCNIHPVTYWvatmsesqqqailear 337
Cdd:pfam07683 1 ISSFVFRADRPFDPERLEAWLEdlLLPEGILRAKGILWLAG-RPRPLVFQGVGGRLSLEPAGRW---------------- 63
|
90 100 110
....*....|....*....|....*....|....*...
gi 488432549 338 qdvvedWdiEYGDRQTQFVIIGTDLDQEKISRELDACL 375
Cdd:pfam07683 64 ------W--PDEDRRSRLVFIGRDLDREALRAALDACL 93
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
14-216 |
4.35e-05 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 43.90 E-value: 4.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 14 GSGKTTLLNHILKN-REGRRIAVIVNDMsEVNIDKDLvaqgggLSRTDEKLVELSNGCICCTLRDDLLREVERLVHKGgI 92
Cdd:COG0378 23 GSGKTTLLEKTIRAlKDRLRIAVIEGDI-YTTEDAER------LRAAGVPVVQINTGGCCHLDASMVLEALEELDLPD-L 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 93 DQIVIESTGisepVPVAQTFSyideELGIDLTsICRLDT------------MVTvvdanrfvndirsedlladrdesvdd 160
Cdd:COG0378 95 DLLFIENVG----NLVCPAFF----PLGEDLK-VVVLSVtegddkprkyppMFT-------------------------- 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 488432549 161 edertiadllidqveFCDVMIINKIDLIS--DEVLEKLENVLRALQPEAKIIkTVNAK 216
Cdd:COG0378 140 ---------------AADLLVINKIDLAPyvGFDLEVMEEDARRVNPGAPIF-EVSAK 181
|
|
| shulin_C20orf194-like |
cd22936 |
Tetrahymena thermophila shulin, human uncharacterized protein C20orf194, and similar proteins; ... |
3-374 |
4.59e-05 |
|
Tetrahymena thermophila shulin, human uncharacterized protein C20orf194, and similar proteins; This family contains Tetrahymena thermophila shulin, human uncharacterized protein C20orf194, and similar proteins. Shulin is a negative regulator of the ciliary outer dynein arm (ODA). It binds newly synthesized ODAs, locks the dynein motors together by shutting off motor activity, and facilitates the delivery of ODAs from the cytoplasm to their final position in the cilia. ODAs, together with inner dynein arms (IDAs), are arrayed along a microtubule-based structure called the axoneme and drive the movement of cilia. Human C20orf194 interacts with the small GTPase Arf-like 3 (ARL3) and may act as its effector. The rs6051702 single nucleotide polymorphism (SNP) within the C20orf194 gene is associated with inosine triphosphatase (ITPA) functional gene polymorphisms that were found to influence RBV-induced hemoglobin (Hb)-decline during treatment of chronic hepatitis C patients with pegylated interferon (PEG-IFN) plus ribavirin (RBV).
Pssm-ID: 438574 [Multi-domain] Cd Length: 1092 Bit Score: 45.80 E-value: 4.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 3 KIPVTVLSGYLGSGKTTLLNHILK-NREGRRIAVIVNDMSEVNIDKDLVAQGgglsrtdeklvELSngcicctlrddLLR 81
Cdd:cd22936 689 KIVITIVTGIPGSGKEKLAANLVSlAKEDNRWHVLRQDLRESSAFDDKSLQK-----------QLS-----------SVL 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 82 EVERLVHKGGIDQIVIESTGISEPVPVAQTFSYideelGIDLTSICRLDTMVTVVDANRFVNDirsedlladrdesvdde 161
Cdd:cd22936 747 SSQRRQAARKRPRILVVVPGYTDDVVIAAALHP-----DPEVSGSFKIGAVTTCVNPLNFFME----------------- 804
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 162 DERTIADLLIDQVE---FCDVMIINKIDlISDEVLEKLENVLRALQPEAKIIktvnaKVELSDVLNTQLFDFeKASESAG 238
Cdd:cd22936 805 HNRNTFPKLLDQLAqgwVTNVVFTSTTD-NQDPELEEVQKLLRAVNPDAAFI-----LALKGNVTRGEDAEL-ILSENSF 877
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 239 WIKELTAGGHAtHTP----ETEEYGITSFAYTR-RLPFhakrfhqwleQMPENIVRTKGIVWLA----------QYNDVA 303
Cdd:cd22936 878 SSPEMNRARRL-LYPgwseGLFSSGPLVPKMIQvTLPF----------SRDRPLERDLFILRLKalksslkpspFTGNIY 946
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488432549 304 CLLSQAGSSCNIHPVTYWVATMSesqqqAILEARQDVVEDWDIEYGDRQTQFVIIGTDLDQEKISRELDAC 374
Cdd:cd22936 947 CIEGTVKFTDEEEKIEVLNNTLS-----NNLRLVPVPTPPSPNDETPQELGLVFTGCNLNEEKLKELLRQC 1012
|
|
| HypB |
cd05390 |
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the ... |
177-216 |
1.77e-03 |
|
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: 39.50 E-value: 1.77e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 488432549 177 CDVMIINKIDLIS--DEVLEKLENVLRALQPEAKIIkTVNAK 216
Cdd:cd05390 149 ADVVLINKIDLLPyfDFDVEKAKEDIKKLNPNAPII-EVSAK 189
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
150-210 |
2.76e-03 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 39.26 E-value: 2.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488432549 150 LLADRDESVDDEDERtIADLLIDQVEFCdVMIINKIDLISD-EVLEKLENVLRALQPEAKII 210
Cdd:PRK00089 90 FVVDADEKIGPGDEF-ILEKLKKVKTPV-ILVLNKIDLVKDkEELLPLLEELSELMDFAEIV 149
|
|
| YjiA |
COG2403 |
Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion ... |
177-212 |
3.72e-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: 39.44 E-value: 3.72e-03
10 20 30
....*....|....*....|....*....|....*.
gi 488432549 177 CDVMIINKIDLISDEVLEKLENVLRALQPEAKIIKT 212
Cdd:COG2403 262 ADVVVINKVDTADPEDIETVRENIRKVNPKAEIIEA 297
|
|
| Era |
cd04163 |
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ... |
150-227 |
3.79e-03 |
|
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.
Pssm-ID: 206726 [Multi-domain] Cd Length: 168 Bit Score: 37.83 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 150 LLADRDESVDDEDERtIADLLIDQVEFCdVMIINKIDLISD-EVLEKLENVLRALQPEAKII----KTVNAKVELSDVLN 224
Cdd:cd04163 88 FVVDASEWIGEGDEF-ILELLKKSKTPV-ILVLNKIDLVKDkEDLLPLLEKLKELHPFAEIFpisaLKGENVDELLEYIV 165
|
...
gi 488432549 225 TQL 227
Cdd:cd04163 166 EYL 168
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
6-99 |
4.37e-03 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 38.36 E-value: 4.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488432549 6 VTVLSGYLGSGKTTLLNHILKN--REGRRIAVI---------VNDMSEVNIDKDLVAQGGGLS----RTDEKLVELsngc 70
Cdd:COG0467 22 STLLSGPPGTGKTTLALQFLAEglRRGEKGLYVsfeespeqlLRRAESLGLDLEEYIESGLLRiidlSPEELGLDL---- 97
|
90 100
....*....|....*....|....*....
gi 488432549 71 icctlrDDLLREVERLVHKGGIDQIVIES 99
Cdd:COG0467 98 ------EELLARLREAVEEFGAKRVVIDS 120
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
150-210 |
4.62e-03 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 38.43 E-value: 4.62e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488432549 150 LLADRDESVDDEDERtIADLLIDQ---VefcdVMIINKIDLISDEVLEKLENVLRALQPEAKII 210
Cdd:COG1159 88 FVVDATEKIGEGDEF-ILELLKKLktpV----ILVINKIDLVKKEELLPLLAEYSELLDFAEIV 146
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
5-35 |
6.55e-03 |
|
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) [Replication, recombination and repair];
Pssm-ID: 440273 [Multi-domain] Cd Length: 514 Bit Score: 38.42 E-value: 6.55e-03
10 20 30
....*....|....*....|....*....|...
gi 488432549 5 PVTVLSGYLGSGKTTLLNHILKN--REGRRIAV 35
Cdd:COG0507 141 RVSVLTGGAGTGKTTTLRALLAAleALGLRVAL 173
|
|
| MobB |
cd03116 |
molybdopterin-guanine dinucleotide biosynthesis protein B; Molybdenum is an essential trace ... |
9-47 |
7.85e-03 |
|
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: 36.85 E-value: 7.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 488432549 9 LSGYLGSGKTTLLNHILK--NREGRRIAVIVNDMSEVNIDK 47
Cdd:cd03116 5 VVGKSGSGKTTLIEKLIPelKARGLRVAVIKHTHHGFDIDT 45
|
|
| |
