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Conserved domains on  [gi|446680320|ref|WP_000757666|]
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MULTISPECIES: GTP-binding protein [Bacillus]

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 ...
5-389 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: 562.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   5 PITVLSGFLGSGKTTLLHHILTNKNNLKVAVIVNDMSEVNIDASLIKKGG--FSRTEEKLVEIQNGCICCTLREDLMIEV 82
Cdd:NF038288   2 PVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGasLSRTEEKLVEMSNGCICCTLREDLLVEV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  83 NRLVENGDIDYIIIESSGISEPIPVAQTFTYTDEVlNIDLTKNCRLDTMVTVVDANRFWDDFADGESLLDRKQAIDENDT 162
Cdd:NF038288  82 RRLAREGRFDYLVIESTGISEPLPVAETFTFADED-GVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEEDE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320 163 REVIDLLIDQIEFANVIILNKIDLLEKEDVIELHHLLKKLNPKAKVLESSFSKVPLQEILNTNLFNYEEASQSAGWIQEL 242
Cdd:NF038288 161 RTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320 243 NsDHHTPETEEYGIKSFVYRRKYPFHPKRLMNWL-EKWPLDVVRAKGFFWLASRNNMIGLLSQAGSSITIQGAGEWIAAL 321
Cdd:NF038288 241 R-GEHTPETEEYGISSFVYRARRPFHPQRFYDFLhSEWPGKVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMWWAAV 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446680320 322 PETERNQMITEEPEVLKNWDKQYGDRITELVFIGIDMNCSLIEQSLDSCLLTEKEMRQD---WNTFIDPIP 389
Cdd:NF038288 320 PRERWPQDEESLAAIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEEMAAGpeaWATLPDPFP 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 ...
5-389 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: 562.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   5 PITVLSGFLGSGKTTLLHHILTNKNNLKVAVIVNDMSEVNIDASLIKKGG--FSRTEEKLVEIQNGCICCTLREDLMIEV 82
Cdd:NF038288   2 PVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGasLSRTEEKLVEMSNGCICCTLREDLLVEV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  83 NRLVENGDIDYIIIESSGISEPIPVAQTFTYTDEVlNIDLTKNCRLDTMVTVVDANRFWDDFADGESLLDRKQAIDENDT 162
Cdd:NF038288  82 RRLAREGRFDYLVIESTGISEPLPVAETFTFADED-GVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEEDE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320 163 REVIDLLIDQIEFANVIILNKIDLLEKEDVIELHHLLKKLNPKAKVLESSFSKVPLQEILNTNLFNYEEASQSAGWIQEL 242
Cdd:NF038288 161 RTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320 243 NsDHHTPETEEYGIKSFVYRRKYPFHPKRLMNWL-EKWPLDVVRAKGFFWLASRNNMIGLLSQAGSSITIQGAGEWIAAL 321
Cdd:NF038288 241 R-GEHTPETEEYGISSFVYRARRPFHPQRFYDFLhSEWPGKVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMWWAAV 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446680320 322 PETERNQMITEEPEVLKNWDKQYGDRITELVFIGIDMNCSLIEQSLDSCLLTEKEMRQD---WNTFIDPIP 389
Cdd:NF038288 320 PRERWPQDEESLAAIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEEMAAGpeaWATLPDPFP 390
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
1-374 1.23e-151

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 431.13  E-value: 1.23e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   1 MKKVPITVLSGFLGSGKTTLLHHILTNKNNLKVAVIVNDMSEVNIDASLIKkggfsRTEEKLVEIQNGCICCTLREDLMI 80
Cdd:COG0523    1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVR-----DTDEEIVELSNGCICCTLREDLLP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  81 EVNRLVENGDIDYIIIESSGISEPIPVAQTFTYtdevlNIDLTKNCRLDTMVTVVDANRFWDDFADgeslldrkqaiden 160
Cdd:COG0523   76 ALRRLLRRGRFDRLLIETTGLADPAPVAQTFTF-----DPELRDRLRLDGVVTVVDARNLLDDLAD-------------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320 161 dtREVIDLLIDQIEFANVIILNKIDLLEKEDVIELHHLLKKLNPKAKVLESSFSKVPLQEILNTNLFNYEEASQSAGWIQ 240
Cdd:COG0523  137 --RTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLE 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320 241 ELNSDHHTpeteeYGIKSFVYRRKYPFHPKRLMNWLEKWPLDVVRAKGFFWLASRnNMIGLLSQAGSSITIQGAGEWIAa 320
Cdd:COG0523  215 ELRDHEHD-----DGIRSFVFRSDRPFDPERLADFLEELGPGVLRAKGFLWLAGR-PRRLVFQGVGGRLSLEPLGPWPA- 287
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446680320 321 lpeternqmiteepevlknwdkqyGDRITELVFIGIDMNCSLIEQSLDSCLLTE 374
Cdd:COG0523  288 ------------------------DDRRSRLVFIGRDLDEAALEAALDACLLTD 317
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
5-225 2.20e-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: 270.55  E-value: 2.20e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   5 PITVLSGFLGSGKTTLLHHILTNKNNLKVAVIVNDMSEVNIDASLIKKGGfsrTEEKLVEIQNGCICCTLREDLMIEVNR 84
Cdd:cd03112    1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSG---GGEEVVELSNGCICCTLKGDLVKALEQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  85 LVEN-GDIDYIIIESSGISEPIPVAQTFTYTDEvlnidLTKNCRLDTMVTVVDANRFWDDFADGeslldrkqaidendtr 163
Cdd:cd03112   78 LLERrGKFDYILIETTGLADPGPIAQTLWSDEE-----LESRLRLDGVVTVVDAKNFLKQLDEE---------------- 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446680320 164 EVIDLLIDQIEFANVIILNKIDLLEKEDVIELHHLLKKLNPKAKVLESSFSKVPLQEILNTN 225
Cdd:cd03112  137 DVSDLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
5-210 2.05e-67

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: 211.34  E-value: 2.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320    5 PITVLSGFLGSGKTTLLHHIL-TNKNNLKVAVIVNDMSEVNIDASLIKKggfsrTEEKLVEIQNGCICCTLREDLMIEVN 83
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETGIDAELLSE-----TGVLIVELSNGCICCTIREDLSMALE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   84 RLVEN-GDIDYIIIESSGISEPIPVAQTFTYTdevlniDLTKNCRLDTMVTVVDANRfwddfadgeslldrkqaidENDT 162
Cdd:pfam02492  76 ALLEReGRLDVIFIETTGLAEPAPVAQTFLSP------ELRSPVLLDGVITVVDAAN-------------------EADG 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 446680320  163 REVIDLLIDQIEFANVIILNKIDLLEKEDVIE-LHHLLKKLNPKAKVLE 210
Cdd:pfam02492 131 EKIPRKAGDQIAFADLIVLNKTDLAPEVALLEvLEEDLRRLNPGAPVVP 179
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
3-333 1.78e-44

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: 157.22  E-value: 1.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320    3 KVPITVLSGFLGSGKTTLLHHILTNKNNLKVAVIVNDMSEVNIDASLIKKGGFSR-TEEKLVEIQNGCICCTLREDLMIE 81
Cdd:TIGR02475   3 KIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEGcSEENIVELANGCICCTVADDFIPT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   82 VNRLVE-NGDIDYIIIESSGISEPIPVAQTFTYTdevlniDLTKNCRLDTMVTVVD-----ANRFWDDFADgeslLDRKQ 155
Cdd:TIGR02475  83 MTKLLArRQRPDHILIETSGLALPKPLVQAFQWP------EIRSRVTVDGVVTVVDgpavaAGRFAADPDA----LDAQR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  156 AIDENDTRE--VIDLLIDQIEFANVIILNKIDLLEKEDVIELHHLLKKLNPKA-KVLESSFSKVPLQEILNTNLfnyeea 232
Cdd:TIGR02475 153 AADDNLDHEtpLEELFEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAvKIVEASHGEVDARVLLGLGA------ 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  233 sQSAGWIQELNSDHHTPETEEYG---IKSFVYRRKYPFHPKRLMNWLEKW--PLDVVRAKGFfwLASRNNMIGLLSQA-G 306
Cdd:TIGR02475 227 -AAEDDLDNRPSHHDFEGGEEHDhdeFDSVVVDLGEVADPAALRQRLERLaeEHDVLRIKGF--AAVPGKPMRLLVQGvG 303
                         330       340
                  ....*....|....*....|....*..
gi 446680320  307 SSITIQGAGEWIAALPETERNQMITEE 333
Cdd:TIGR02475 304 QRVDSYYDRPWQAAETRQTRLVVIGLH 330
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
256-371 1.04e-34

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: 123.48  E-value: 1.04e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   256 IKSFVYRRKYPFHPKRLMNWLEKWPLDVVRAKGFFWLASRNNMIGLLSQAGSSITIQGAGEWIAAlpeternqmiteepe 335
Cdd:smart00833   1 ISSFVYRARRPFHPQRLLAALDELPEGVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPAA--------------- 65
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 446680320   336 vlknwdkqyGDRITELVFIGIDMNCSLIEQSLDSCL 371
Cdd:smart00833  66 ---------GDRRTRLVFIGRDLDEEAIRAALDACL 92
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
1-358 4.39e-31

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 120.58  E-value: 4.39e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   1 MKKVPITVLSGFLGSGKTTLLHHILTNKNNLKVAVIVNDMSEVNIDASLIkkgGFSRTEEKlvEIQNGCICCTLR---ED 77
Cdd:PRK11537   1 MNPIAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLI---GDRATQIK--TLTNGCICCSRSnelED 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  78 LMIEVNRLVENGDI--DYIIIESSGISEPIPVAQTFtYTDEVLnidltknCR---LDTMVTVVDAnrfwddfADGESLLD 152
Cdd:PRK11537  76 ALLDLLDNLDKGNIqfDRLVIECTGMADPGPIIQTF-FSHEVL-------CQrylLDGVIALVDA-------VHADEQMN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320 153 R---KQAidendtrevidllidQIEFANVIILNKIDLleKEDVIELHHLLKKLNPKAKVLESSFSKVPLQEILNTNLFNY 229
Cdd:PRK11537 141 QftiAQS---------------QVGYADRILLTKTDV--AGEAEKLRERLARINARAPVYTVVHGDIDLSLLFNTNGFML 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320 230 EEASQSAgwiqeLNSDHHTPETEEyGIKSFVYRRKYPF---HPKRLM-NWLEKWPLDVVRAKGFFWLASRNNMigLLsqa 305
Cdd:PRK11537 204 EENVVST-----KPRFHFIADKQN-DISSIVVELDYPVdisEVSRVMeNLLLESADKLLRYKGMLWIDGEPNR--LL--- 272
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446680320 306 gssitIQGAGEWIAAlpeternqmiteepevlkNWDKQYGD--RITELVFIGIDM 358
Cdd:PRK11537 273 -----FQGVQRLYSA------------------DWDRPWGDetPHSTLVFIGIQL 304
 
Name Accession Description Interval E-value
chaper_GTP_ZigA NF038288
zinc metallochaperone GTPase ZigA; The GTPase ZigA (Zur-induced GTPase A) is a zinc ...
5-389 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: 562.48  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   5 PITVLSGFLGSGKTTLLHHILTNKNNLKVAVIVNDMSEVNIDASLIKKGG--FSRTEEKLVEIQNGCICCTLREDLMIEV 82
Cdd:NF038288   2 PVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGasLSRTEEKLVEMSNGCICCTLREDLLVEV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  83 NRLVENGDIDYIIIESSGISEPIPVAQTFTYTDEVlNIDLTKNCRLDTMVTVVDANRFWDDFADGESLLDRKQAIDENDT 162
Cdd:NF038288  82 RRLAREGRFDYLVIESTGISEPLPVAETFTFADED-GVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEEDE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320 163 REVIDLLIDQIEFANVIILNKIDLLEKEDVIELHHLLKKLNPKAKVLESSFSKVPLQEILNTNLFNYEEASQSAGWIQEL 242
Cdd:NF038288 161 RTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKEL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320 243 NsDHHTPETEEYGIKSFVYRRKYPFHPKRLMNWL-EKWPLDVVRAKGFFWLASRNNMIGLLSQAGSSITIQGAGEWIAAL 321
Cdd:NF038288 241 R-GEHTPETEEYGISSFVYRARRPFHPQRFYDFLhSEWPGKVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMWWAAV 319
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446680320 322 PETERNQMITEEPEVLKNWDKQYGDRITELVFIGIDMNCSLIEQSLDSCLLTEKEMRQD---WNTFIDPIP 389
Cdd:NF038288 320 PRERWPQDEESLAAIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEEMAAGpeaWATLPDPFP 390
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
1-374 1.23e-151

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 431.13  E-value: 1.23e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   1 MKKVPITVLSGFLGSGKTTLLHHILTNKNNLKVAVIVNDMSEVNIDASLIKkggfsRTEEKLVEIQNGCICCTLREDLMI 80
Cdd:COG0523    1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVR-----DTDEEIVELSNGCICCTLREDLLP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  81 EVNRLVENGDIDYIIIESSGISEPIPVAQTFTYtdevlNIDLTKNCRLDTMVTVVDANRFWDDFADgeslldrkqaiden 160
Cdd:COG0523   76 ALRRLLRRGRFDRLLIETTGLADPAPVAQTFTF-----DPELRDRLRLDGVVTVVDARNLLDDLAD-------------- 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320 161 dtREVIDLLIDQIEFANVIILNKIDLLEKEDVIELHHLLKKLNPKAKVLESSFSKVPLQEILNTNLFNYEEASQSAGWIQ 240
Cdd:COG0523  137 --RTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGWLE 214
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320 241 ELNSDHHTpeteeYGIKSFVYRRKYPFHPKRLMNWLEKWPLDVVRAKGFFWLASRnNMIGLLSQAGSSITIQGAGEWIAa 320
Cdd:COG0523  215 ELRDHEHD-----DGIRSFVFRSDRPFDPERLADFLEELGPGVLRAKGFLWLAGR-PRRLVFQGVGGRLSLEPLGPWPA- 287
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446680320 321 lpeternqmiteepevlknwdkqyGDRITELVFIGIDMNCSLIEQSLDSCLLTE 374
Cdd:COG0523  288 ------------------------DDRRSRLVFIGRDLDEAALEAALDACLLTD 317
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
5-225 2.20e-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: 270.55  E-value: 2.20e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   5 PITVLSGFLGSGKTTLLHHILTNKNNLKVAVIVNDMSEVNIDASLIKKGGfsrTEEKLVEIQNGCICCTLREDLMIEVNR 84
Cdd:cd03112    1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSG---GGEEVVELSNGCICCTLKGDLVKALEQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  85 LVEN-GDIDYIIIESSGISEPIPVAQTFTYTDEvlnidLTKNCRLDTMVTVVDANRFWDDFADGeslldrkqaidendtr 163
Cdd:cd03112   78 LLERrGKFDYILIETTGLADPGPIAQTLWSDEE-----LESRLRLDGVVTVVDAKNFLKQLDEE---------------- 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446680320 164 EVIDLLIDQIEFANVIILNKIDLLEKEDVIELHHLLKKLNPKAKVLESSFSKVPLQEILNTN 225
Cdd:cd03112  137 DVSDLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
5-210 2.05e-67

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: 211.34  E-value: 2.05e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320    5 PITVLSGFLGSGKTTLLHHIL-TNKNNLKVAVIVNDMSEVNIDASLIKKggfsrTEEKLVEIQNGCICCTLREDLMIEVN 83
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETGIDAELLSE-----TGVLIVELSNGCICCTIREDLSMALE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   84 RLVEN-GDIDYIIIESSGISEPIPVAQTFTYTdevlniDLTKNCRLDTMVTVVDANRfwddfadgeslldrkqaidENDT 162
Cdd:pfam02492  76 ALLEReGRLDVIFIETTGLAEPAPVAQTFLSP------ELRSPVLLDGVITVVDAAN-------------------EADG 130
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 446680320  163 REVIDLLIDQIEFANVIILNKIDLLEKEDVIE-LHHLLKKLNPKAKVLE 210
Cdd:pfam02492 131 EKIPRKAGDQIAFADLIVLNKTDLAPEVALLEvLEEDLRRLNPGAPVVP 179
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
3-333 1.78e-44

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: 157.22  E-value: 1.78e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320    3 KVPITVLSGFLGSGKTTLLHHILTNKNNLKVAVIVNDMSEVNIDASLIKKGGFSR-TEEKLVEIQNGCICCTLREDLMIE 81
Cdd:TIGR02475   3 KIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEGcSEENIVELANGCICCTVADDFIPT 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   82 VNRLVE-NGDIDYIIIESSGISEPIPVAQTFTYTdevlniDLTKNCRLDTMVTVVD-----ANRFWDDFADgeslLDRKQ 155
Cdd:TIGR02475  83 MTKLLArRQRPDHILIETSGLALPKPLVQAFQWP------EIRSRVTVDGVVTVVDgpavaAGRFAADPDA----LDAQR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  156 AIDENDTRE--VIDLLIDQIEFANVIILNKIDLLEKEDVIELHHLLKKLNPKA-KVLESSFSKVPLQEILNTNLfnyeea 232
Cdd:TIGR02475 153 AADDNLDHEtpLEELFEDQLACADLVILNKADLLDAAGLARVRAEIAAELPRAvKIVEASHGEVDARVLLGLGA------ 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  233 sQSAGWIQELNSDHHTPETEEYG---IKSFVYRRKYPFHPKRLMNWLEKW--PLDVVRAKGFfwLASRNNMIGLLSQA-G 306
Cdd:TIGR02475 227 -AAEDDLDNRPSHHDFEGGEEHDhdeFDSVVVDLGEVADPAALRQRLERLaeEHDVLRIKGF--AAVPGKPMRLLVQGvG 303
                         330       340
                  ....*....|....*....|....*..
gi 446680320  307 SSITIQGAGEWIAALPETERNQMITEE 333
Cdd:TIGR02475 304 QRVDSYYDRPWQAAETRQTRLVVIGLH 330
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
256-371 1.04e-34

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: 123.48  E-value: 1.04e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   256 IKSFVYRRKYPFHPKRLMNWLEKWPLDVVRAKGFFWLASRNNMIGLLSQAGSSITIQGAGEWIAAlpeternqmiteepe 335
Cdd:smart00833   1 ISSFVYRARRPFHPQRLLAALDELPEGVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPAA--------------- 65
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 446680320   336 vlknwdkqyGDRITELVFIGIDMNCSLIEQSLDSCL 371
Cdd:smart00833  66 ---------GDRRTRLVFIGRDLDEEAIRAALDACL 92
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
1-358 4.39e-31

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 120.58  E-value: 4.39e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   1 MKKVPITVLSGFLGSGKTTLLHHILTNKNNLKVAVIVNDMSEVNIDASLIkkgGFSRTEEKlvEIQNGCICCTLR---ED 77
Cdd:PRK11537   1 MNPIAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLI---GDRATQIK--TLTNGCICCSRSnelED 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  78 LMIEVNRLVENGDI--DYIIIESSGISEPIPVAQTFtYTDEVLnidltknCR---LDTMVTVVDAnrfwddfADGESLLD 152
Cdd:PRK11537  76 ALLDLLDNLDKGNIqfDRLVIECTGMADPGPIIQTF-FSHEVL-------CQrylLDGVIALVDA-------VHADEQMN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320 153 R---KQAidendtrevidllidQIEFANVIILNKIDLleKEDVIELHHLLKKLNPKAKVLESSFSKVPLQEILNTNLFNY 229
Cdd:PRK11537 141 QftiAQS---------------QVGYADRILLTKTDV--AGEAEKLRERLARINARAPVYTVVHGDIDLSLLFNTNGFML 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320 230 EEASQSAgwiqeLNSDHHTPETEEyGIKSFVYRRKYPF---HPKRLM-NWLEKWPLDVVRAKGFFWLASRNNMigLLsqa 305
Cdd:PRK11537 204 EENVVST-----KPRFHFIADKQN-DISSIVVELDYPVdisEVSRVMeNLLLESADKLLRYKGMLWIDGEPNR--LL--- 272
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446680320 306 gssitIQGAGEWIAAlpeternqmiteepevlkNWDKQYGD--RITELVFIGIDM 358
Cdd:PRK11537 273 -----FQGVQRLYSA------------------DWDRPWGDetPHSTLVFIGIQL 304
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
256-371 4.46e-24

Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of putative metal chaperones that can be separated into up to 15 subgroups. In addition to known roles in cobalamin biosynthesis and the activation of the Fe-type nitrile hydratase, this family is also known to be involved in the response to zinc limitation. The CobW subgroup involved in cobalamin synthesis represents only a small sub-fraction of the family.


Pssm-ID: 462228 [Multi-domain]  Cd Length: 93  Bit Score: 95.00  E-value: 4.46e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  256 IKSFVYRRKYPFHPKRLMNWLEK--WPLDVVRAKGFFWLASRNnMIGLLSQAGSSITIQGAGEWiaalpeternqmitee 333
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDllLPEGILRAKGILWLAGRP-RPLVFQGVGGRLSLEPAGRW---------------- 63
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 446680320  334 pevlknWDkqYGDRITELVFIGIDMNCSLIEQSLDSCL 371
Cdd:pfam07683  64 ------WP--DEDRRSRLVFIGRDLDREALRAALDACL 93
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
14-212 8.85e-07

Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 48.90  E-value: 8.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  14 GSGKTTLLHHILTN-KNNLKVAVIVNDMsEVNIDASLIKKGGFsrteeKLVEIQNGCICCTlrEDLMIE--VNRLvENGD 90
Cdd:COG0378   23 GSGKTTLLEKTIRAlKDRLRIAVIEGDI-YTTEDAERLRAAGV-----PVVQINTGGCCHL--DASMVLeaLEEL-DLPD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  91 IDYIIIESSGisepIPVAQTFTYTDEVLNidltkncrldtmVTVVDAnrfwddfADGEsllD--RKQAidendtrevidl 168
Cdd:COG0378   94 LDLLFIENVG----NLVCPAFFPLGEDLK------------VVVLSV-------TEGD---DkpRKYP------------ 135
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446680320 169 liDQIEFANVIILNKIDLLE---------KEDVielhhllKKLNPKAKVLESS 212
Cdd:COG0378  136 --PMFTAADLLVINKIDLAPyvgfdlevmEEDA-------RRVNPGAPIFEVS 179
HypB cd05390
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the ...
14-212 4.19e-04

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: 41.04  E-value: 4.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  14 GSGKTTLLHHILTN-KNNLKVAVIVNDMsEVNIDASLIKKGGFsrteeKLVEIQNGCIcCTLREDLMIEVNRLVENGDID 92
Cdd:cd05390   31 GSGKTTLLERTIDAlKDELKIAVIEGDL-ETDNDAERIRATGV-----PAIQINTGGA-CHLDADMVARALHDLDLDELD 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320  93 YIIIESSGisepipvaqtftytdevlNIdltkncrldtmvtVVDAnrfwdDFADGEsllDRKQAI---DENDTREVIDLL 169
Cdd:cd05390  104 LLFIENVG------------------NL-------------VCPA-----EFDLGE---HKNVVLlsvTEGDDKPLKYPL 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 446680320 170 IDQIefANVIILNKIDLLEKE--DVIELHHLLKKLNPKAKVLESS 212
Cdd:cd05390  145 MFQV--ADVVLINKIDLLPYFdfDVEKAKEDIKKLNPNAPIIEVS 187
shulin_C20orf194-like cd22936
Tetrahymena thermophila shulin, human uncharacterized protein C20orf194, and similar proteins; ...
1-209 4.66e-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: 42.34  E-value: 4.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320    1 MKKVPITVLSGFLGSGKTTLlhhiltnknnlkVAVIVNdMSEVNIDASLIKK--GGFSRTEEKLVEIQngcicctLREDL 78
Cdd:cd22936   687 KDKIVITIVTGIPGSGKEKL------------AANLVS-LAKEDNRWHVLRQdlRESSAFDDKSLQKQ-------LSSVL 746
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   79 MIEVNRLVENGDIdyIIIESSGISEPIPVAQTFTYTDEVlnidlTKNCRLDTMVTVVDANRFWddfadgeslldrkqaid 158
Cdd:cd22936   747 SSQRRQAARKRPR--ILVVVPGYTDDVVIAAALHPDPEV-----SGSFKIGAVTTCVNPLNFF----------------- 802
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 446680320  159 ENDTREVIDLLIDQIE---FANVIILNKIDLlEKEDVIELHHLLKKLNPKAKVL 209
Cdd:cd22936   803 MEHNRNTFPKLLDQLAqgwVTNVVFTSTTDN-QDPELEEVQKLLRAVNPDAAFI 855
RAD55 COG0467
RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];
6-98 3.04e-03

RecA-superfamily ATPase, KaiC/GvpD/RAD55 family [Signal transduction mechanisms];


Pssm-ID: 440235 [Multi-domain]  Cd Length: 221  Bit Score: 38.74  E-value: 3.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446680320   6 ITVLSGFLGSGKTTLLHHILTN--KNNLKVAVI---------VNDMSEVNID-ASLIKKGGFS----RTEEKLVEIqngc 69
Cdd:COG0467   22 STLLSGPPGTGKTTLALQFLAEglRRGEKGLYVsfeespeqlLRRAESLGLDlEEYIESGLLRiidlSPEELGLDL---- 97
                         90       100
                 ....*....|....*....|....*....
gi 446680320  70 icctlrEDLMIEVNRLVENGDIDYIIIES 98
Cdd:COG0467   98 ------EELLARLREAVEEFGAKRVVIDS 120
YjiA COG2403
Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion ...
176-210 8.75e-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: 8.75e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 446680320 176 ANVIILNKIDLLEKEDVIELHHLLKKLNPKAKVLE 210
Cdd:COG2403  262 ADVVVINKVDTADPEDIETVRENIRKVNPKAEIIE 296
 
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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