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Conserved domains on  [gi|1835040000|gb|QJD84786|]
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GTP-binding protein [Cohnella herbarum]

Protein Classification

chaper_GTP_ZigA superfamily-containing protein( domain architecture ID 1904169)

chaper_GTP_ZigA superfamily-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
chaper_GTP_ZigA super family cl45739
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
23-409 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.


The actual alignment was detected with superfamily member NF038288:

Pssm-ID: 468453 [Multi-domain]  Cd Length: 390  Bit Score: 604.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  23 LPVTVLSGYLGAGKTTILNHVLNNRQGLKVAVIVNDLGDVNIDAALIKDGGG-LSRTDEKLVEMSNGCICCTLREDLLHE 101
Cdd:NF038288    1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGAsLSRTEEKLVEMSNGCICCTLREDLLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 102 VERLACENRFDYILIESTGVGEPIPVAQTFSYIDEEhGIDLTKFCRLDCMVTVVDAYRFWSDFSSGERLMDRKQEIGEND 181
Cdd:NF038288   81 VRRLAREGRFDYLVIESTGISEPLPVAETFTFADED-GVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEED 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 182 TREVVDLLIDQIEFCDVLILNKCDRVGDKELAELETVLRSLQPRAKIIRSEFGRVEASDILNTGLFDFDEASRSAGWMQE 261
Cdd:NF038288  160 ERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 262 MAKEhHVPETEEYGISSFVYERIRPFHPERLMRWM-SEWPAEVVRAKGIIWLATRNNMAQNFSQAGPSIQFGPAGYWVAS 340
Cdd:NF038288  240 LRGE-HTPETEEYGISSFVYRARRPFHPQRFYDFLhSEWPGKVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMWWAA 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835040000 341 LPQHEMEDivreDPD----ISKYWDPVYGDRVNKIVFIGLEMDRQGLVAELDDCLLTDEEI--GME-WSAFPDDFP 409
Cdd:NF038288  319 VPRERWPQ----DEEslaaIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEEMaaGPEaWATLPDPFP 390
 
Name Accession Description Interval E-value
chaper_GTP_ZigA NF038288
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
23-409 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: 604.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  23 LPVTVLSGYLGAGKTTILNHVLNNRQGLKVAVIVNDLGDVNIDAALIKDGGG-LSRTDEKLVEMSNGCICCTLREDLLHE 101
Cdd:NF038288    1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGAsLSRTEEKLVEMSNGCICCTLREDLLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 102 VERLACENRFDYILIESTGVGEPIPVAQTFSYIDEEhGIDLTKFCRLDCMVTVVDAYRFWSDFSSGERLMDRKQEIGEND 181
Cdd:NF038288   81 VRRLAREGRFDYLVIESTGISEPLPVAETFTFADED-GVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEED 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 182 TREVVDLLIDQIEFCDVLILNKCDRVGDKELAELETVLRSLQPRAKIIRSEFGRVEASDILNTGLFDFDEASRSAGWMQE 261
Cdd:NF038288  160 ERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 262 MAKEhHVPETEEYGISSFVYERIRPFHPERLMRWM-SEWPAEVVRAKGIIWLATRNNMAQNFSQAGPSIQFGPAGYWVAS 340
Cdd:NF038288  240 LRGE-HTPETEEYGISSFVYRARRPFHPQRFYDFLhSEWPGKVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMWWAA 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835040000 341 LPQHEMEDivreDPD----ISKYWDPVYGDRVNKIVFIGLEMDRQGLVAELDDCLLTDEEI--GME-WSAFPDDFP 409
Cdd:NF038288  319 VPRERWPQ----DEEslaaIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEEMaaGPEaWATLPDPFP 390
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
20-395 2.39e-156

Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 443.84  E-value: 2.39e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  20 PNKLPVTVLSGYLGAGKTTILNHVLNNRQGLKVAVIVNDLGDVNIDAALIKDggglsrTDEKLVEMSNGCICCTLREDLL 99
Cdd:COG0523     1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRD------TDEEIVELSNGCICCTLREDLL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 100 HEVERLACENRFDYILIESTGVGEPIPVAQTFSyideeHGIDLTKFCRLDCMVTVVDAYRFWSDFssgerlmdrkqeige 179
Cdd:COG0523    75 PALRRLLRRGRFDRLLIETTGLADPAPVAQTFT-----FDPELRDRLRLDGVVTVVDARNLLDDL--------------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 180 nDTREVVDLLIDQIEFCDVLILNKCDRVGDKELAELETVLRSLQPRAKIIRSEFGRVEASDILNTGLFDFDEASRSAGWM 259
Cdd:COG0523   135 -ADRTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWL 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 260 QEMAKEHHVpeteeYGISSFVYERIRPFHPERLMRWMSEWPAEVVRAKGIIWLATRnNMAQNFSQAGPSIQFGPAGYWVA 339
Cdd:COG0523   214 EELRDHEHD-----DGIRSFVFRSDRPFDPERLADFLEELGPGVLRAKGFLWLAGR-PRRLVFQGVGGRLSLEPLGPWPA 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1835040000 340 slpqhemedivredpdiskywdpvyGDRVNKIVFIGLEMDRQGLVAELDDCLLTDE 395
Cdd:COG0523   288 -------------------------DDRRSRLVFIGRDLDEAALEAALDACLLTDA 318
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
24-245 3.64e-90

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: 270.93  E-value: 3.64e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  24 PVTVLSGYLGAGKTTILNHVLNNRQGLKVAVIVNDLGDVNIDAALIKDGGGlsrtDEKLVEMSNGCICCTLREDLLHEVE 103
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGG----GEEVVELSNGCICCTLKGDLVKALE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 104 RLA-CENRFDYILIESTGVGEPIPVAQTFSYIDEehgidLTKFCRLDCMVTVVDAYRFWSDFssgerlmdrkqeigenDT 182
Cdd:cd03112    77 QLLeRRGKFDYILIETTGLADPGPIAQTLWSDEE-----LESRLRLDGVVTVVDAKNFLKQL----------------DE 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835040000 183 REVVDLLIDQIEFCDVLILNKCDRVGDKELAELETVLRSLQPRAKIIRSEFGRVEASDILNTG 245
Cdd:cd03112   136 EDVSDLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
24-230 4.01e-69

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: 216.74  E-value: 4.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  24 PVTVLSGYLGAGKTTILNHVL-NNRQGLKVAVIVNDLGDVNIDAALikdgggLSRTDEKLVEMSNGCICCTLREDLLHEV 102
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETGIDAEL------LSETGVLIVELSNGCICCTIREDLSMAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 103 ERLA-CENRFDYILIESTGVGEPIPVAQTFSYideehgIDLTKFCRLDCMVTVVDAYRfwsdfssgerlmdrkqeigEND 181
Cdd:pfam02492  75 EALLeREGRLDVIFIETTGLAEPAPVAQTFLS------PELRSPVLLDGVITVVDAAN-------------------EAD 129
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1835040000 182 TREVVDLLIDQIEFCDVLILNKCDRVGDKELAE-LETVLRSLQPRAKIIR 230
Cdd:pfam02492 130 GEKIPRKAGDQIAFADLIVLNKTDLAPEVALLEvLEEDLRRLNPGAPVVP 179
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
22-310 6.40e-40

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: 145.66  E-value: 6.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  22 KLPVTVLSGYLGAGKTTILNHVLNNRQGLKVAVIVNDLGDVNIDAALIKDGGGLSRTDEKLVEMSNGCICCTLREDLLHE 101
Cdd:TIGR02475   3 KIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEGCSEENIVELANGCICCTVADDFIPT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 102 VERL-ACENRFDYILIESTGVGEPIPVAQTFSYIDEEHGidltkfCRLDCMVTVVD-----AYRFWSDFSSGERLMDRKQ 175
Cdd:TIGR02475  83 MTKLlARRQRPDHILIETSGLALPKPLVQAFQWPEIRSR------VTVDGVVTVVDgpavaAGRFAADPDALDAQRAADD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 176 EIGENDTREvvDLLIDQIEFCDVLILNKCDRVGDKELAELETVLRSLQPRA-KIIRSEFGRVEASDILNTGL-FDFDEAS 253
Cdd:TIGR02475 157 NLDHETPLE--ELFEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAvKIVEASHGEVDARVLLGLGAaAEDDLDN 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835040000 254 RSAGWMQEMAKEHhvpETEEygISSFVYERIRPFHPERLMRWMSEWPAE--VVRAKGII 310
Cdd:TIGR02475 235 RPSHHDFEGGEEH---DHDE--FDSVVVDLGEVADPAALRQRLERLAEEhdVLRIKGFA 288
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
276-391 2.74e-32

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: 117.31  E-value: 2.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  276 ISSFVYERIRPFHPERLMRWMSEWPAEVVRAKGIIWLATRNNMAQNFSQAGPSIQFGPAGYWVASlpqhemedivredpd 355
Cdd:smart00833   1 ISSFVYRARRPFHPQRLLAALDELPEGVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPAA--------------- 65
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1835040000  356 iskywdpvyGDRVNKIVFIGLEMDRQGLVAELDDCL 391
Cdd:smart00833  66 ---------GDRRTRLVFIGRDLDEEAIRAALDACL 92
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
23-313 4.91e-31

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 120.96  E-value: 4.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  23 LPVTVLSGYLGAGKTTILNHVLNNRQGLKVAVIVNDLGDVNIDAALIKDGGGLSRTdeklveMSNGCICCTLRE------ 96
Cdd:PRK11537    4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIGDRATQIKT------LTNGCICCSRSNeledal 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  97 -DLLHEVERlaCENRFDYILIESTGVGEPIPVAQTFSyideEHGIDLTKFCrLDCMVTVVDAYRfwsdfssGERLMDRkQ 175
Cdd:PRK11537   78 lDLLDNLDK--GNIQFDRLVIECTGMADPGPIIQTFF----SHEVLCQRYL-LDGVIALVDAVH-------ADEQMNQ-F 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 176 EIGENdtrevvdllidQIEFCDVLILNKCDRVGDKElaELETVLRSLQPRAKIIRSEFGRVEASDILNTGLFDFDEASRS 255
Cdd:PRK11537  143 TIAQS-----------QVGYADRILLTKTDVAGEAE--KLRERLARINARAPVYTVVHGDIDLSLLFNTNGFMLEENVVS 209
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835040000 256 AgwmqeMAKEHHVPETEEyGISSFVYERIRPFHPERLMRWMSEWPAE----VVRAKGIIWLA 313
Cdd:PRK11537  210 T-----KPRFHFIADKQN-DISSIVVELDYPVDISEVSRVMENLLLEsadkLLRYKGMLWID 265
 
Name Accession Description Interval E-value
chaper_GTP_ZigA NF038288
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
23-409 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: 604.46  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  23 LPVTVLSGYLGAGKTTILNHVLNNRQGLKVAVIVNDLGDVNIDAALIKDGGG-LSRTDEKLVEMSNGCICCTLREDLLHE 101
Cdd:NF038288    1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGAsLSRTEEKLVEMSNGCICCTLREDLLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 102 VERLACENRFDYILIESTGVGEPIPVAQTFSYIDEEhGIDLTKFCRLDCMVTVVDAYRFWSDFSSGERLMDRKQEIGEND 181
Cdd:NF038288   81 VRRLAREGRFDYLVIESTGISEPLPVAETFTFADED-GVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEED 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 182 TREVVDLLIDQIEFCDVLILNKCDRVGDKELAELETVLRSLQPRAKIIRSEFGRVEASDILNTGLFDFDEASRSAGWMQE 261
Cdd:NF038288  160 ERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 262 MAKEhHVPETEEYGISSFVYERIRPFHPERLMRWM-SEWPAEVVRAKGIIWLATRNNMAQNFSQAGPSIQFGPAGYWVAS 340
Cdd:NF038288  240 LRGE-HTPETEEYGISSFVYRARRPFHPQRFYDFLhSEWPGKVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMWWAA 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835040000 341 LPQHEMEDivreDPD----ISKYWDPVYGDRVNKIVFIGLEMDRQGLVAELDDCLLTDEEI--GME-WSAFPDDFP 409
Cdd:NF038288  319 VPRERWPQ----DEEslaaIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEEMaaGPEaWATLPDPFP 390
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
20-395 2.39e-156

Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction only];


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 443.84  E-value: 2.39e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  20 PNKLPVTVLSGYLGAGKTTILNHVLNNRQGLKVAVIVNDLGDVNIDAALIKDggglsrTDEKLVEMSNGCICCTLREDLL 99
Cdd:COG0523     1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRD------TDEEIVELSNGCICCTLREDLL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 100 HEVERLACENRFDYILIESTGVGEPIPVAQTFSyideeHGIDLTKFCRLDCMVTVVDAYRFWSDFssgerlmdrkqeige 179
Cdd:COG0523    75 PALRRLLRRGRFDRLLIETTGLADPAPVAQTFT-----FDPELRDRLRLDGVVTVVDARNLLDDL--------------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 180 nDTREVVDLLIDQIEFCDVLILNKCDRVGDKELAELETVLRSLQPRAKIIRSEFGRVEASDILNTGLFDFDEASRSAGWM 259
Cdd:COG0523   135 -ADRTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWL 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 260 QEMAKEHHVpeteeYGISSFVYERIRPFHPERLMRWMSEWPAEVVRAKGIIWLATRnNMAQNFSQAGPSIQFGPAGYWVA 339
Cdd:COG0523   214 EELRDHEHD-----DGIRSFVFRSDRPFDPERLADFLEELGPGVLRAKGFLWLAGR-PRRLVFQGVGGRLSLEPLGPWPA 287
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1835040000 340 slpqhemedivredpdiskywdpvyGDRVNKIVFIGLEMDRQGLVAELDDCLLTDE 395
Cdd:COG0523   288 -------------------------DDRRSRLVFIGRDLDEAALEAALDACLLTDA 318
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
24-245 3.64e-90

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: 270.93  E-value: 3.64e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  24 PVTVLSGYLGAGKTTILNHVLNNRQGLKVAVIVNDLGDVNIDAALIKDGGGlsrtDEKLVEMSNGCICCTLREDLLHEVE 103
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGG----GEEVVELSNGCICCTLKGDLVKALE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 104 RLA-CENRFDYILIESTGVGEPIPVAQTFSYIDEehgidLTKFCRLDCMVTVVDAYRFWSDFssgerlmdrkqeigenDT 182
Cdd:cd03112    77 QLLeRRGKFDYILIETTGLADPGPIAQTLWSDEE-----LESRLRLDGVVTVVDAKNFLKQL----------------DE 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835040000 183 REVVDLLIDQIEFCDVLILNKCDRVGDKELAELETVLRSLQPRAKIIRSEFGRVEASDILNTG 245
Cdd:cd03112   136 EDVSDLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
24-230 4.01e-69

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: 216.74  E-value: 4.01e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  24 PVTVLSGYLGAGKTTILNHVL-NNRQGLKVAVIVNDLGDVNIDAALikdgggLSRTDEKLVEMSNGCICCTLREDLLHEV 102
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETGIDAEL------LSETGVLIVELSNGCICCTIREDLSMAL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 103 ERLA-CENRFDYILIESTGVGEPIPVAQTFSYideehgIDLTKFCRLDCMVTVVDAYRfwsdfssgerlmdrkqeigEND 181
Cdd:pfam02492  75 EALLeREGRLDVIFIETTGLAEPAPVAQTFLS------PELRSPVLLDGVITVVDAAN-------------------EAD 129
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1835040000 182 TREVVDLLIDQIEFCDVLILNKCDRVGDKELAE-LETVLRSLQPRAKIIR 230
Cdd:pfam02492 130 GEKIPRKAGDQIAFADLIVLNKTDLAPEVALLEvLEEDLRRLNPGAPVVP 179
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
22-310 6.40e-40

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: 145.66  E-value: 6.40e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  22 KLPVTVLSGYLGAGKTTILNHVLNNRQGLKVAVIVNDLGDVNIDAALIKDGGGLSRTDEKLVEMSNGCICCTLREDLLHE 101
Cdd:TIGR02475   3 KIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEGCSEENIVELANGCICCTVADDFIPT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 102 VERL-ACENRFDYILIESTGVGEPIPVAQTFSYIDEEHGidltkfCRLDCMVTVVD-----AYRFWSDFSSGERLMDRKQ 175
Cdd:TIGR02475  83 MTKLlARRQRPDHILIETSGLALPKPLVQAFQWPEIRSR------VTVDGVVTVVDgpavaAGRFAADPDALDAQRAADD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 176 EIGENDTREvvDLLIDQIEFCDVLILNKCDRVGDKELAELETVLRSLQPRA-KIIRSEFGRVEASDILNTGL-FDFDEAS 253
Cdd:TIGR02475 157 NLDHETPLE--ELFEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAvKIVEASHGEVDARVLLGLGAaAEDDLDN 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835040000 254 RSAGWMQEMAKEHhvpETEEygISSFVYERIRPFHPERLMRWMSEWPAE--VVRAKGII 310
Cdd:TIGR02475 235 RPSHHDFEGGEEH---DHDE--FDSVVVDLGEVADPAALRQRLERLAEEhdVLRIKGFA 288
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
276-391 2.74e-32

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: 117.31  E-value: 2.74e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  276 ISSFVYERIRPFHPERLMRWMSEWPAEVVRAKGIIWLATRNNMAQNFSQAGPSIQFGPAGYWVASlpqhemedivredpd 355
Cdd:smart00833   1 ISSFVYRARRPFHPQRLLAALDELPEGVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPAA--------------- 65
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1835040000  356 iskywdpvyGDRVNKIVFIGLEMDRQGLVAELDDCL 391
Cdd:smart00833  66 ---------GDRRTRLVFIGRDLDEEAIRAALDACL 92
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
23-313 4.91e-31

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 120.96  E-value: 4.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  23 LPVTVLSGYLGAGKTTILNHVLNNRQGLKVAVIVNDLGDVNIDAALIKDGGGLSRTdeklveMSNGCICCTLRE------ 96
Cdd:PRK11537    4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLIGDRATQIKT------LTNGCICCSRSNeledal 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  97 -DLLHEVERlaCENRFDYILIESTGVGEPIPVAQTFSyideEHGIDLTKFCrLDCMVTVVDAYRfwsdfssGERLMDRkQ 175
Cdd:PRK11537   78 lDLLDNLDK--GNIQFDRLVIECTGMADPGPIIQTFF----SHEVLCQRYL-LDGVIALVDAVH-------ADEQMNQ-F 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 176 EIGENdtrevvdllidQIEFCDVLILNKCDRVGDKElaELETVLRSLQPRAKIIRSEFGRVEASDILNTGLFDFDEASRS 255
Cdd:PRK11537  143 TIAQS-----------QVGYADRILLTKTDVAGEAE--KLRERLARINARAPVYTVVHGDIDLSLLFNTNGFMLEENVVS 209
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835040000 256 AgwmqeMAKEHHVPETEEyGISSFVYERIRPFHPERLMRWMSEWPAE----VVRAKGIIWLA 313
Cdd:PRK11537  210 T-----KPRFHFIADKQN-DISSIVVELDYPVDISEVSRVMENLLLEsadkLLRYKGMLWID 265
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
276-391 3.02e-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: 3.02e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000 276 ISSFVYERIRPFHPERLMRWMSE--WPAEVVRAKGIIWLATRNnMAQNFSQAGPSIQFGPAGYWvaslpqhemedivred 353
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDllLPEGILRAKGILWLAGRP-RPLVFQGVGGRLSLEPAGRW---------------- 63
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1835040000 354 pdiskywdPVYGDRVNKIVFIGLEMDRQGLVAELDDCL 391
Cdd:pfam07683  64 --------WPDEDRRSRLVFIGRDLDREALRAALDACL 93
shulin_C20orf194-like cd22936
Tetrahymena thermophila shulin, human uncharacterized protein C20orf194, and similar proteins; ...
19-262 9.75e-06

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: 48.12  E-value: 9.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000   19 KPNKLPVTVLSGYLGAGKTTIlnhvlnnrqglkVAVIVNdLGDVNIDAALIK-DGGGLSRTDEKLVEMSNgcicctlreD 97
Cdd:cd22936    686 SKDKIVITIVTGIPGSGKEKL------------AANLVS-LAKEDNRWHVLRqDLRESSAFDDKSLQKQL---------S 743
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000   98 LLHEVERLACENRFDYILIESTGVGEPIPVAQTFSyideeHGIDLTKFCRLDCMVTVVDAYRFWsdfssgerlmdrkqei 177
Cdd:cd22936    744 SVLSSQRRQAARKRPRILVVVPGYTDDVVIAAALH-----PDPEVSGSFKIGAVTTCVNPLNFF---------------- 802
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  178 gENDTREVVDLLIDQIE---FCDVLILNkCDRVGDKELAELETVLRSLQPRAKIIRSEFGRVE----ASDILNTGLFDFD 250
Cdd:cd22936    803 -MEHNRNTFPKLLDQLAqgwVTNVVFTS-TTDNQDPELEEVQKLLRAVNPDAAFILALKGNVTrgedAELILSENSFSSP 880
                          250
                   ....*....|....*..
gi 1835040000  251 EASRS-----AGWMQEM 262
Cdd:cd22936    881 EMNRArrllyPGWSEGL 897
HypB cd05390
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the ...
33-120 5.82e-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: 37.96  E-value: 5.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835040000  33 GAGKTTILNHVLNN-RQGLKVAVIVNDLgDVNIDAALIKDGGGlsrtdeKLVEMSNGCIcCTLREDLLHE-VERLAcENR 110
Cdd:cd05390    31 GSGKTTLLERTIDAlKDELKIAVIEGDL-ETDNDAERIRATGV------PAIQINTGGA-CHLDADMVARaLHDLD-LDE 101
                          90
                  ....*....|
gi 1835040000 111 FDYILIESTG 120
Cdd:cd05390   102 LDLLFIENVG 111
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
24-54 6.23e-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: 38.80  E-value: 6.23e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1835040000  24 PVTVLSGYLGAGKTTILNHVLNN--RQGLKVAV 54
Cdd:COG0507   141 RVSVLTGGAGTGKTTTLRALLAAleALGLRVAL 173
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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