|
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: 574.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 4 IPVTVLSGYLGSGKTTLLNHILQNREGRRIAVIVNDMSEVNIDKDLVADGGG-LSRTDEKLVELSNGCICCTLRDDLLKE 82
Cdd:NF038288 1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGAsLSRTEEKLVEMSNGCICCTLREDLLVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 83 VERLVKKGGIDQIVIESTGISEPVPVAQTFSYIDDElGIDLTAICRLDTMVTVVDANRFVHDINSEDLLMDRDQSVDETD 162
Cdd:NF038288 81 VRRLAREGRFDYLVIESTGISEPLPVAETFTFADED-GVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 163 ERSIADLLIDQVEFCDVLIINKIDLISEEELAKLEKVLSALQPTAKIIKTTNSEVDLKEVLNTQRFDFEKASESAGWIKE 242
Cdd:NF038288 160 ERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 243 LesggHASHTPETEEYGISSFVYKRRLPFHAKRFNDWLES-MPNNVVRSKGIVWLAQYNHVACLLSQAGSSCNIHPVTYW 321
Cdd:NF038288 240 L----RGEHTPETEEYGISSFVYRARRPFHPQRFYDFLHSeWPGKVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMW 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446985735 322 VASMSEAQQTQILAERQDVAAEWDPEYGDRHTQFVIIGTDLDEGAITKELDACLVNAQEIDAD---WQQFEDPY 392
Cdd:NF038288 316 WAAVPRERWPQDEESLAAIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEEMAAGpeaWATLPDPF 389
|
|
| YejR |
COG0523 |
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ... |
1-379 |
3.07e-149 |
|
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];
Pssm-ID: 440289 [Multi-domain] Cd Length: 318 Bit Score: 424.97 E-value: 3.07e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 1 MAKIPVTVLSGYLGSGKTTLLNHILQNREGRRIAVIVNDMSEVNIDKDLVADggglsrTDEKLVELSNGCICCTLRDDLL 80
Cdd:COG0523 1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRD------TDEEIVELSNGCICCTLREDLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 81 KEVERLVKKGGIDQIVIESTGISEPVPVAQTFSYiddelGIDLTAICRLDTMVTVVDANRFVHDInsedllmdrdqsvde 160
Cdd:COG0523 75 PALRRLLRRGRFDRLLIETTGLADPAPVAQTFTF-----DPELRDRLRLDGVVTVVDARNLLDDL--------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 161 tDERSIADLLIDQVEFCDVLIINKIDLISEEELAKLEKVLSALQPTAKIIKTTNSEVDLKEVLNTQRFDFEKASESAGWI 240
Cdd:COG0523 135 -ADRTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 241 KELESGGHAshtpeteeYGISSFVYKRRLPFHAKRFNDWLESMPNNVVRSKGIVWLAQYNHvACLLSQAGSSCNIHPVTY 320
Cdd:COG0523 214 EELRDHEHD--------DGIRSFVFRSDRPFDPERLADFLEELGPGVLRAKGFLWLAGRPR-RLVFQGVGGRLSLEPLGP 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446985735 321 WVAsmseaqqtqilaerqdvaaewdpeyGDRHTQFVIIGTDLDEGAITKELDACLVNAQ 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 |
1.71e-91 |
|
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: 273.63 E-value: 1.71e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 5 PVTVLSGYLGSGKTTLLNHILQNREGRRIAVIVNDMSEVNIDKDLVADGGGlsrtDEKLVELSNGCICCTLRDDLLKEVE 84
Cdd:cd03112 1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGG----GEEVVELSNGCICCTLKGDLVKALE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 85 RLVKKGG-IDQIVIESTGISEPVPVAQTFSYIDdelgiDLTAICRLDTMVTVVDANRFVHDINSEDLlmdrdqsvdetde 163
Cdd:cd03112 77 QLLERRGkFDYILIETTGLADPGPIAQTLWSDE-----ELESRLRLDGVVTVVDAKNFLKQLDEEDV------------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446985735 164 rsiADLLIDQVEFCDVLIINKIDLISEEELAKLEKVLSALQPTAKIIKTTNSEVDLKEVLNT 225
Cdd:cd03112 139 ---SDLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGT 197
|
|
| cobW |
pfam02492 |
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ... |
5-210 |
4.21e-73 |
|
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: 225.98 E-value: 4.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 5 PVTVLSGYLGSGKTTLLNHIL-QNREGRRIAVIVNDMSEVNIDKDLVADggglsrTDEKLVELSNGCICCTLRDDLLKEV 83
Cdd:pfam02492 1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETGIDAELLSE------TGVLIVELSNGCICCTIREDLSMAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 84 ERLV-KKGGIDQIVIESTGISEPVPVAQTFSYiddelgIDLTAICRLDTMVTVVDANRfvhdinsedllmdrdqsvdETD 162
Cdd:pfam02492 75 EALLeREGRLDVIFIETTGLAEPAPVAQTFLS------PELRSPVLLDGVITVVDAAN-------------------EAD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446985735 163 ERSIADLLIDQVEFCDVLIINKIDLISEEE-LAKLEKVLSALQPTAKII 210
Cdd:pfam02492 130 GEKIPRKAGDQIAFADLIVLNKTDLAPEVAlLEVLEEDLRRLNPGAPVV 178
|
|
| CobW |
TIGR02475 |
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ... |
1-223 |
9.59e-47 |
|
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: 163.38 E-value: 9.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 1 MAKIPVTVLSGYLGSGKTTLLNHILQNREGRRIAVIVNDMSEVNIDKDLVADGGGLSRTDEKLVELSNGCICCTLRDDLL 80
Cdd:TIGR02475 1 LAKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEGCSEENIVELANGCICCTVADDFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 81 KEVERLV-KKGGIDQIVIESTGISEPVPVAQTFSYiddelgIDLTAICRLDTMVTVVD-----ANRFVHDINSEDLLMDR 154
Cdd:TIGR02475 81 PTMTKLLaRRQRPDHILIETSGLALPKPLVQAFQW------PEIRSRVTVDGVVTVVDgpavaAGRFAADPDALDAQRAA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 155 DQSVDEtdERSIADLLIDQVEFCDVLIINKIDLISEEELAKLEKVLSALQPTA-KIIKTTNSEVDLKEVL 223
Cdd:TIGR02475 155 DDNLDH--ETPLEELFEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAvKIVEASHGEVDARVLL 222
|
|
| PRK11537 |
PRK11537 |
putative GTP-binding protein YjiA; Provisional |
1-373 |
2.60e-35 |
|
putative GTP-binding protein YjiA; Provisional
Pssm-ID: 183183 [Multi-domain] Cd Length: 318 Bit Score: 132.13 E-value: 2.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 1 MAKIPVTVLSGYLGSGKTTLLNHILQNREGRRIAVIVNDMSEVNIDKDLVADGGGLSRTdeklveLSNGCICCT----LR 76
Cdd:PRK11537 1 MNPIAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIGDRATQIKT------LTNGCICCSrsneLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 77 DDLLKEVErLVKKGGI--DQIVIESTGISEPVPVAQTFsyIDDELgidltaICR---LDTMVTVVDAnrfVHdinsedll 151
Cdd:PRK11537 75 DALLDLLD-NLDKGNIqfDRLVIECTGMADPGPIIQTF--FSHEV------LCQrylLDGVIALVDA---VH-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 152 mdrdqSVDETDERSIADlliDQVEFCDVLIINKIDLISEEElaKLEKVLSALQPTAKIIKTTNSEVDLKEVLNTQRFDFE 231
Cdd:PRK11537 135 -----ADEQMNQFTIAQ---SQVGYADRILLTKTDVAGEAE--KLRERLARINARAPVYTVVHGDIDLSLLFNTNGFMLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 232 kasesagwiKELESGGHASHTPETEEYGISSFVYKRRLPFHAKRFNDWLESM----PNNVVRSKGIVWLaqynhvaclls 307
Cdd:PRK11537 205 ---------ENVVSTKPRFHFIADKQNDISSIVVELDYPVDISEVSRVMENLllesADKLLRYKGMLWI----------- 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446985735 308 qAGSSCNIHpvtywvasmseAQQTQILaerqdVAAEWDPEYGD--RHTQFVIIGTDLDEGAITKELDA 373
Cdd:PRK11537 265 -DGEPNRLL-----------FQGVQRL-----YSADWDRPWGDetPHSTLVFIGIQLPEEEIRAAFAG 315
|
|
| CobW_C |
smart00833 |
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ... |
260-375 |
7.91e-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: 110.38 E-value: 7.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 260 ISSFVYKRRLPFHAKRFNDWLESMPNNVVRSKGIVWLAQYNHVACLLSQAGSSCNIHPVTYWVASmseaqqtqilaerqd 339
Cdd:smart00833 1 ISSFVYRARRPFHPQRLLAALDELPEGVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPAA--------------- 65
|
90 100 110
....*....|....*....|....*....|....*.
gi 446985735 340 vaaewdpeyGDRHTQFVIIGTDLDEGAITKELDACL 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: 574.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 4 IPVTVLSGYLGSGKTTLLNHILQNREGRRIAVIVNDMSEVNIDKDLVADGGG-LSRTDEKLVELSNGCICCTLRDDLLKE 82
Cdd:NF038288 1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGAsLSRTEEKLVEMSNGCICCTLREDLLVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 83 VERLVKKGGIDQIVIESTGISEPVPVAQTFSYIDDElGIDLTAICRLDTMVTVVDANRFVHDINSEDLLMDRDQSVDETD 162
Cdd:NF038288 81 VRRLAREGRFDYLVIESTGISEPLPVAETFTFADED-GVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEED 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 163 ERSIADLLIDQVEFCDVLIINKIDLISEEELAKLEKVLSALQPTAKIIKTTNSEVDLKEVLNTQRFDFEKASESAGWIKE 242
Cdd:NF038288 160 ERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 243 LesggHASHTPETEEYGISSFVYKRRLPFHAKRFNDWLES-MPNNVVRSKGIVWLAQYNHVACLLSQAGSSCNIHPVTYW 321
Cdd:NF038288 240 L----RGEHTPETEEYGISSFVYRARRPFHPQRFYDFLHSeWPGKVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMW 315
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446985735 322 VASMSEAQQTQILAERQDVAAEWDPEYGDRHTQFVIIGTDLDEGAITKELDACLVNAQEIDAD---WQQFEDPY 392
Cdd:NF038288 316 WAAVPRERWPQDEESLAAIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEEMAAGpeaWATLPDPF 389
|
|
| YejR |
COG0523 |
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ... |
1-379 |
3.07e-149 |
|
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];
Pssm-ID: 440289 [Multi-domain] Cd Length: 318 Bit Score: 424.97 E-value: 3.07e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 1 MAKIPVTVLSGYLGSGKTTLLNHILQNREGRRIAVIVNDMSEVNIDKDLVADggglsrTDEKLVELSNGCICCTLRDDLL 80
Cdd:COG0523 1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRD------TDEEIVELSNGCICCTLREDLL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 81 KEVERLVKKGGIDQIVIESTGISEPVPVAQTFSYiddelGIDLTAICRLDTMVTVVDANRFVHDInsedllmdrdqsvde 160
Cdd:COG0523 75 PALRRLLRRGRFDRLLIETTGLADPAPVAQTFTF-----DPELRDRLRLDGVVTVVDARNLLDDL--------------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 161 tDERSIADLLIDQVEFCDVLIINKIDLISEEELAKLEKVLSALQPTAKIIKTTNSEVDLKEVLNTQRFDFEKASESAGWI 240
Cdd:COG0523 135 -ADRTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 241 KELESGGHAshtpeteeYGISSFVYKRRLPFHAKRFNDWLESMPNNVVRSKGIVWLAQYNHvACLLSQAGSSCNIHPVTY 320
Cdd:COG0523 214 EELRDHEHD--------DGIRSFVFRSDRPFDPERLADFLEELGPGVLRAKGFLWLAGRPR-RLVFQGVGGRLSLEPLGP 284
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446985735 321 WVAsmseaqqtqilaerqdvaaewdpeyGDRHTQFVIIGTDLDEGAITKELDACLVNAQ 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 |
1.71e-91 |
|
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: 273.63 E-value: 1.71e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 5 PVTVLSGYLGSGKTTLLNHILQNREGRRIAVIVNDMSEVNIDKDLVADGGGlsrtDEKLVELSNGCICCTLRDDLLKEVE 84
Cdd:cd03112 1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGG----GEEVVELSNGCICCTLKGDLVKALE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 85 RLVKKGG-IDQIVIESTGISEPVPVAQTFSYIDdelgiDLTAICRLDTMVTVVDANRFVHDINSEDLlmdrdqsvdetde 163
Cdd:cd03112 77 QLLERRGkFDYILIETTGLADPGPIAQTLWSDE-----ELESRLRLDGVVTVVDAKNFLKQLDEEDV------------- 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446985735 164 rsiADLLIDQVEFCDVLIINKIDLISEEELAKLEKVLSALQPTAKIIKTTNSEVDLKEVLNT 225
Cdd:cd03112 139 ---SDLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGT 197
|
|
| cobW |
pfam02492 |
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ... |
5-210 |
4.21e-73 |
|
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: 225.98 E-value: 4.21e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 5 PVTVLSGYLGSGKTTLLNHIL-QNREGRRIAVIVNDMSEVNIDKDLVADggglsrTDEKLVELSNGCICCTLRDDLLKEV 83
Cdd:pfam02492 1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETGIDAELLSE------TGVLIVELSNGCICCTIREDLSMAL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 84 ERLV-KKGGIDQIVIESTGISEPVPVAQTFSYiddelgIDLTAICRLDTMVTVVDANRfvhdinsedllmdrdqsvdETD 162
Cdd:pfam02492 75 EALLeREGRLDVIFIETTGLAEPAPVAQTFLS------PELRSPVLLDGVITVVDAAN-------------------EAD 129
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446985735 163 ERSIADLLIDQVEFCDVLIINKIDLISEEE-LAKLEKVLSALQPTAKII 210
Cdd:pfam02492 130 GEKIPRKAGDQIAFADLIVLNKTDLAPEVAlLEVLEEDLRRLNPGAPVV 178
|
|
| CobW |
TIGR02475 |
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ... |
1-223 |
9.59e-47 |
|
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: 163.38 E-value: 9.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 1 MAKIPVTVLSGYLGSGKTTLLNHILQNREGRRIAVIVNDMSEVNIDKDLVADGGGLSRTDEKLVELSNGCICCTLRDDLL 80
Cdd:TIGR02475 1 LAKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEGCSEENIVELANGCICCTVADDFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 81 KEVERLV-KKGGIDQIVIESTGISEPVPVAQTFSYiddelgIDLTAICRLDTMVTVVD-----ANRFVHDINSEDLLMDR 154
Cdd:TIGR02475 81 PTMTKLLaRRQRPDHILIETSGLALPKPLVQAFQW------PEIRSRVTVDGVVTVVDgpavaAGRFAADPDALDAQRAA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 155 DQSVDEtdERSIADLLIDQVEFCDVLIINKIDLISEEELAKLEKVLSALQPTA-KIIKTTNSEVDLKEVL 223
Cdd:TIGR02475 155 DDNLDH--ETPLEELFEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAvKIVEASHGEVDARVLL 222
|
|
| PRK11537 |
PRK11537 |
putative GTP-binding protein YjiA; Provisional |
1-373 |
2.60e-35 |
|
putative GTP-binding protein YjiA; Provisional
Pssm-ID: 183183 [Multi-domain] Cd Length: 318 Bit Score: 132.13 E-value: 2.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 1 MAKIPVTVLSGYLGSGKTTLLNHILQNREGRRIAVIVNDMSEVNIDKDLVADGGGLSRTdeklveLSNGCICCT----LR 76
Cdd:PRK11537 1 MNPIAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIGDRATQIKT------LTNGCICCSrsneLE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 77 DDLLKEVErLVKKGGI--DQIVIESTGISEPVPVAQTFsyIDDELgidltaICR---LDTMVTVVDAnrfVHdinsedll 151
Cdd:PRK11537 75 DALLDLLD-NLDKGNIqfDRLVIECTGMADPGPIIQTF--FSHEV------LCQrylLDGVIALVDA---VH-------- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 152 mdrdqSVDETDERSIADlliDQVEFCDVLIINKIDLISEEElaKLEKVLSALQPTAKIIKTTNSEVDLKEVLNTQRFDFE 231
Cdd:PRK11537 135 -----ADEQMNQFTIAQ---SQVGYADRILLTKTDVAGEAE--KLRERLARINARAPVYTVVHGDIDLSLLFNTNGFMLE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 232 kasesagwiKELESGGHASHTPETEEYGISSFVYKRRLPFHAKRFNDWLESM----PNNVVRSKGIVWLaqynhvaclls 307
Cdd:PRK11537 205 ---------ENVVSTKPRFHFIADKQNDISSIVVELDYPVDISEVSRVMENLllesADKLLRYKGMLWI----------- 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446985735 308 qAGSSCNIHpvtywvasmseAQQTQILaerqdVAAEWDPEYGD--RHTQFVIIGTDLDEGAITKELDA 373
Cdd:PRK11537 265 -DGEPNRLL-----------FQGVQRL-----YSADWDRPWGDetPHSTLVFIGIQLPEEEIRAAFAG 315
|
|
| CobW_C |
smart00833 |
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ... |
260-375 |
7.91e-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: 110.38 E-value: 7.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 260 ISSFVYKRRLPFHAKRFNDWLESMPNNVVRSKGIVWLAQYNHVACLLSQAGSSCNIHPVTYWVASmseaqqtqilaerqd 339
Cdd:smart00833 1 ISSFVYRARRPFHPQRLLAALDELPEGVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPAA--------------- 65
|
90 100 110
....*....|....*....|....*....|....*.
gi 446985735 340 vaaewdpeyGDRHTQFVIIGTDLDEGAITKELDACL 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 |
5.21e-22 |
|
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: 89.60 E-value: 5.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 260 ISSFVYKRRLPFHAKRFNDWLE--SMPNNVVRSKGIVWLAQYNHvACLLSQAGSSCNIHPvtywvasmseaqqtqilaer 337
Cdd:pfam07683 1 ISSFVFRADRPFDPERLEAWLEdlLLPEGILRAKGILWLAGRPR-PLVFQGVGGRLSLEP-------------------- 59
|
90 100 110
....*....|....*....|....*....|....*...
gi 446985735 338 qdvAAEWDPeYGDRHTQFVIIGTDLDEGAITKELDACL 375
Cdd:pfam07683 60 ---AGRWWP-DEDRRSRLVFIGRDLDREALRAALDACL 93
|
|
| RAD55 |
COG0467 |
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms]; |
6-99 |
1.27e-04 |
|
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
Pssm-ID: 440235 [Multi-domain] Cd Length: 221 Bit Score: 42.98 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 6 VTVLSGYLGSGKTTLLNHILQN--REGRRIAVI---------VNDMSEVNIDKDLVADGGGLS----RTDEKLVELsngc 70
Cdd:COG0467 22 STLLSGPPGTGKTTLALQFLAEglRRGEKGLYVsfeespeqlLRRAESLGLDLEEYIESGLLRiidlSPEELGLDL---- 97
|
90 100
....*....|....*....|....*....
gi 446985735 71 icctlrDDLLKEVERLVKKGGIDQIVIES 99
Cdd:COG0467 98 ------EELLARLREAVEEFGAKRVVIDS 120
|
|
| Era |
COG1159 |
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis]; |
150-223 |
3.82e-04 |
|
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440773 [Multi-domain] Cd Length: 290 Bit Score: 41.90 E-value: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 150 LLMDRDQSVDETDERsIADLLIDQ---VefcdVLIINKIDLISEEELAKLEKVLSALQPTAKIIK---TTNSEVD-LKEV 222
Cdd:COG1159 88 FVVDATEKIGEGDEF-ILELLKKLktpV----ILVINKIDLVKKEELLPLLAEYSELLDFAEIVPisaLKGDNVDeLLDE 162
|
.
gi 446985735 223 L 223
Cdd:COG1159 163 I 163
|
|
| shulin_C20orf194-like |
cd22936 |
Tetrahymena thermophila shulin, human uncharacterized protein C20orf194, and similar proteins; ... |
3-223 |
4.29e-04 |
|
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: 42.72 E-value: 4.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 3 KIPVTVLSGYLGSGKTTLLNhILQNREGRRIAVIVndmsevnidkdLVADGGGLSRTDEKLVELSngcicctLRDDLLKE 82
Cdd:cd22936 689 KIVITIVTGIPGSGKEKLAA-NLVSLAKEDNRWHV-----------LRQDLRESSAFDDKSLQKQ-------LSSVLSSQ 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 83 VERLVKKGgiDQIVIESTGISEPVPVAQTFSYiddelGIDLTAICRLDTMVTVVDANRFVhdinsedllmdrdqsvdETD 162
Cdd:cd22936 750 RRQAARKR--PRILVVVPGYTDDVVIAAALHP-----DPEVSGSFKIGAVTTCVNPLNFF-----------------MEH 805
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446985735 163 ERSIADLLIDQVE---FCDVLIINKIDlISEEELAKLEKVLSALQPTAKIIKTTNSEV----DLKEVL 223
Cdd:cd22936 806 NRNTFPKLLDQLAqgwVTNVVFTSTTD-NQDPELEEVQKLLRAVNPDAAFILALKGNVtrgeDAELIL 872
|
|
| HypB |
COG0378 |
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ... |
14-212 |
5.48e-04 |
|
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440147 [Multi-domain] Cd Length: 200 Bit Score: 40.81 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 14 GSGKTTLLNHILQN-REGRRIAVIVNDMsEVNIDKDLvadgggLSRTDEKLVELSNGCICCTLRDDLLKEVERLvKKGGI 92
Cdd:COG0378 23 GSGKTTLLEKTIRAlKDRLRIAVIEGDI-YTTEDAER------LRAAGVPVVQINTGGCCHLDASMVLEALEEL-DLPDL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 93 DQIVIESTGisepVPVAQTFSyiddELGIDLTaicrldtmVTVVdanrfvhdinsedllmdrdqSVDETDE--RSIADLL 170
Cdd:COG0378 95 DLLFIENVG----NLVCPAFF----PLGEDLK--------VVVL--------------------SVTEGDDkpRKYPPMF 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446985735 171 idqvEFCDVLIINKIDLIS--EEELAKLEKVLSALQPTAKIIKT 212
Cdd:COG0378 139 ----TAADLLVINKIDLAPyvGFDLEVMEEDARRVNPGAPIFEV 178
|
|
| era |
PRK00089 |
GTPase Era; Reviewed |
150-223 |
2.71e-03 |
|
GTPase Era; Reviewed
Pssm-ID: 234624 [Multi-domain] Cd Length: 292 Bit Score: 39.26 E-value: 2.71e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446985735 150 LLMDRDQSVDETDERsIADLLIDQVEFCdVLIINKIDLISE-EELAKLEKVLSALQPTAKIIK---TTNSEVD-LKEVL 223
Cdd:PRK00089 90 FVVDADEKIGPGDEF-ILEKLKKVKTPV-ILVLNKIDLVKDkEELLPLLEELSELMDFAEIVPisaLKGDNVDeLLDVI 166
|
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
5-97 |
3.01e-03 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 38.84 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 5 PVTVLSGYLGSGKTTLLNHILQNREGRRIAVI-VNDMSEVNIDKdlVADGGGLSRTDEKLVEL--SNGCICCTLRDDLLK 81
Cdd:pfam01637 21 LIYVIYGPEGCGKTALLRESIENLLDLGYYVIyYDPLRRYFISK--LDRFEEVRRLAEALGIAvpKAELEESKLAFLAIE 98
|
90
....*....|....*.
gi 446985735 82 EVERLVKKGGIDQIVI 97
Cdd:pfam01637 99 LLLEALKRRGKKIAII 114
|
|
| RecD |
COG0507 |
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ... |
5-35 |
6.91e-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: 6.91e-03
10 20 30
....*....|....*....|....*....|...
gi 446985735 5 PVTVLSGYLGSGKTTLLNHILQN--REGRRIAV 35
Cdd:COG0507 141 RVSVLTGGAGTGKTTTLRALLAAleALGLRVAL 173
|
|
| YjiA |
COG2403 |
Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion ... |
130-217 |
9.81e-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: 37.89 E-value: 9.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446985735 130 DTMVTVVDANRFVHDINSE----DLLMdrdqsvdetdersiadllidqvefCDVLIINKIDLISEEELAKLEKVLSALQP 205
Cdd:COG2403 235 DLHIVVADPHRPGHELSYYpgevNLRM------------------------ADVVVINKVDTADPEDIETVRENIRKVNP 290
|
90
....*....|..
gi 446985735 206 TAKIIKtTNSEV 217
Cdd:COG2403 291 KAEIIE-AASPV 301
|
|
| |
