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Conserved domains on  [gi|1005325449|ref|WP_061610489|]
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zinc metallochaperone GTPase ZigA [Sorangium cellulosum]

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 ...
5-396 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: 692.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449   5 LPVTVLSGFLGAGKTTLLNHVLANRDALRVAVIVNDMSEVNVDAALVRGGGAALRRVEEKLVEMSNGCICCTLREDLLVE 84
Cdd:NF038288    1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGASLSRTEEKLVEMSNGCICCTLREDLLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  85 VARLAGEGRFDYLLIESTGISEPLPVAETFTFADpATGKGLSELARLDTLVTVVDAQRFLADWTSADELRARRAALDGDD 164
Cdd:NF038288   81 VRRLAREGRFDYLVIESTGISEPLPVAETFTFAD-EDGVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEED 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 165 ERTVADLLVEQVEFANVLVLNKTDLVSEDEVERLRAMLLHLNPGARVIRACRGQVDPREILGTGRFDHEEAARSPGWMRE 244
Cdd:NF038288  160 ERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 245 LRGEHVPETEEYGIESFVYRADRPMHPERLWAFLHGatAWDG-VLRSKGFFWLATRMDTTGAWSQAGGAASFEAAGRWYA 323
Cdd:NF038288  240 LRGEHTPETEEYGISSFVYRARRPFHPQRFYDFLHS--EWPGkVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMWWA 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005325449 324 ALPEEQRPEDEEERAALDAAWNPVWGDRRQEIVFIGVDMARDELTRGLDACLLTQEEMAAGPSGWSRLDDPFP 396
Cdd:NF038288  318 AVPRERWPQDEESLAAIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEEMAAGPEAWATLPDPFP 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 ...
5-396 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: 692.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449   5 LPVTVLSGFLGAGKTTLLNHVLANRDALRVAVIVNDMSEVNVDAALVRGGGAALRRVEEKLVEMSNGCICCTLREDLLVE 84
Cdd:NF038288    1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGASLSRTEEKLVEMSNGCICCTLREDLLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  85 VARLAGEGRFDYLLIESTGISEPLPVAETFTFADpATGKGLSELARLDTLVTVVDAQRFLADWTSADELRARRAALDGDD 164
Cdd:NF038288   81 VRRLAREGRFDYLVIESTGISEPLPVAETFTFAD-EDGVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEED 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 165 ERTVADLLVEQVEFANVLVLNKTDLVSEDEVERLRAMLLHLNPGARVIRACRGQVDPREILGTGRFDHEEAARSPGWMRE 244
Cdd:NF038288  160 ERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 245 LRGEHVPETEEYGIESFVYRADRPMHPERLWAFLHGatAWDG-VLRSKGFFWLATRMDTTGAWSQAGGAASFEAAGRWYA 323
Cdd:NF038288  240 LRGEHTPETEEYGISSFVYRARRPFHPQRFYDFLHS--EWPGkVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMWWA 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005325449 324 ALPEEQRPEDEEERAALDAAWNPVWGDRRQEIVFIGVDMARDELTRGLDACLLTQEEMAAGPSGWSRLDDPFP 396
Cdd:NF038288  318 AVPRERWPQDEESLAAIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEEMAAGPEAWATLPDPFP 390
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
2-377 2.51e-150

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 428.44  E-value: 2.51e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449   2 TPKLPVTVLSGFLGAGKTTLLNHVLANRDALRVAVIVNDMSEVNVDAALVRGggaalrrVEEKLVEMSNGCICCTLREDL 81
Cdd:COG0523     1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRD-------TDEEIVELSNGCICCTLREDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  82 LVEVARLAGEGRFDYLLIESTGISEPLPVAETFTFADPatgkgLSELARLDTLVTVVDAQRFLADWtsadelrarraald 161
Cdd:COG0523    74 LPALRRLLRRGRFDRLLIETTGLADPAPVAQTFTFDPE-----LRDRLRLDGVVTVVDARNLLDDL-------------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 162 gdDERTVADLLVEQVEFANVLVLNKTDLVSEDEVERLRAMLLHLNPGARVIRACRGQVDPREILGTGRFDHEEAARSPGW 241
Cdd:COG0523   135 --ADRTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGW 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 242 MRELRGEHvpetEEYGIESFVYRADRPMHPERLWAFLHgaTAWDGVLRSKGFFWLATRmDTTGAWSQAGGAASFEAAGRW 321
Cdd:COG0523   213 LEELRDHE----HDDGIRSFVFRSDRPFDPERLADFLE--ELGPGVLRAKGFLWLAGR-PRRLVFQGVGGRLSLEPLGPW 285
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1005325449 322 YAalpeeqrpedeeeraaldaawnpvwGDRRQEIVFIGVDMARDELTRGLDACLLT 377
Cdd:COG0523   286 PA-------------------------DDRRSRLVFIGRDLDEAALEAALDACLLT 316
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
6-228 5.78e-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: 272.86  E-value: 5.78e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449   6 PVTVLSGFLGAGKTTLLNHVLANRDALRVAVIVNDMSEVNVDAALVRGGGAalrrvEEKLVEMSNGCICCTLREDLLVEV 85
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGG-----GEEVVELSNGCICCTLKGDLVKAL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  86 ARLAGE-GRFDYLLIESTGISEPLPVAETFTFADpatgkGLSELARLDTLVTVVDAQRFLADWTSADelrarraaldgdd 164
Cdd:cd03112    76 EQLLERrGKFDYILIETTGLADPGPIAQTLWSDE-----ELESRLRLDGVVTVVDAKNFLKQLDEED------------- 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005325449 165 ertVADLLVEQVEFANVLVLNKTDLVSEDEVERLRAMLLHLNPGARVIRACRGQVDPREILGTG 228
Cdd:cd03112   138 ---VSDLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
6-213 2.16e-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: 217.12  E-value: 2.16e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449   6 PVTVLSGFLGAGKTTLLNHVLA-NRDALRVAVIVNDMSEVNVDAALVRGGGAalrrveeKLVEMSNGCICCTLREDLLVE 84
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLKqNRAGLRIAVIVNEFGETGIDAELLSETGV-------LIVELSNGCICCTIREDLSMA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  85 VARLAG-EGRFDYLLIESTGISEPLPVAETFTFADpatgkgLSELARLDTLVTVVDAQRFladwtsadelrarraaldgD 163
Cdd:pfam02492  74 LEALLErEGRLDVIFIETTGLAEPAPVAQTFLSPE------LRSPVLLDGVITVVDAANE-------------------A 128
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1005325449 164 DERTVADLLVEQVEFANVLVLNKTDLVSEDE-VERLRAMLLHLNPGARVIR 213
Cdd:pfam02492 129 DGEKIPRKAGDQIAFADLIVLNKTDLAPEVAlLEVLEEDLRRLNPGAPVVP 179
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
4-293 1.03e-43

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: 155.68  E-value: 1.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449   4 KLPVTVLSGFLGAGKTTLLNHVLANRDALRVAVIVNDMSEVNVDAALVRGGGAALRRvEEKLVEMSNGCICCTLREDLLV 83
Cdd:TIGR02475   3 KIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEGCS-EENIVELANGCICCTVADDFIP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  84 EVARL-AGEGRFDYLLIESTGISEPLPVAETFTFADpatgkgLSELARLDTLVTVVD-----AQRFLADWTSADELRARR 157
Cdd:TIGR02475  82 TMTKLlARRQRPDHILIETSGLALPKPLVQAFQWPE------IRSRVTVDGVVTVVDgpavaAGRFAADPDALDAQRAAD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 158 AALDGDDerTVADLLVEQVEFANVLVLNKTDLVSEDEVERLRAMLL-HLNPGARVIRACRGQVDPREILGTGRFDHEEAA 236
Cdd:TIGR02475 156 DNLDHET--PLEELFEDQLACADLVILNKADLLDAAGLARVRAEIAaELPRAVKIVEASHGEVDARVLLGLGAAAEDDLD 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1005325449 237 RSPGWMRELRGEhvpETEEYGIESFVYRADRPMHPERLWAFLHGATAWDGVLRSKGF 293
Cdd:TIGR02475 234 NRPSHHDFEGGE---EHDHDEFDSVVVDLGEVADPAALRQRLERLAEEHDVLRIKGF 287
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
1-373 1.24e-35

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 133.29  E-value: 1.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449   1 MTPkLPVTVLSGFLGAGKTTLLNHVLANRDALRVAVIVNDMSEVNVDAALVrgGGAALRrveekLVEMSNGCICCTLRE- 79
Cdd:PRK11537    1 MNP-IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLI--GDRATQ-----IKTLTNGCICCSRSNe 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  80 ------DLLVEVARlaGEGRFDYLLIESTGISEPLPVAETFtFADPAtgkgLSELARLDTLVTVVDAqrfladwTSADEL 153
Cdd:PRK11537   73 ledallDLLDNLDK--GNIQFDRLVIECTGMADPGPIIQTF-FSHEV----LCQRYLLDGVIALVDA-------VHADEQ 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 154 RarraaldgdDERTVADllvEQVEFANVLVLNKTDLVSEDevERLRAMLLHLNPGARVIRACRGQVDPREILGTGRFDHE 233
Cdd:PRK11537  139 M---------NQFTIAQ---SQVGYADRILLTKTDVAGEA--EKLRERLARINARAPVYTVVHGDIDLSLLFNTNGFMLE 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 234 EAARSPgwmrELRGEHVPETEEyGIESFVYRADRPMHPERLWAFLHG--ATAWDGVLRSKGFFWLA---TRMdttgawsq 308
Cdd:PRK11537  205 ENVVST----KPRFHFIADKQN-DISSIVVELDYPVDISEVSRVMENllLESADKLLRYKGMLWIDgepNRL-------- 271
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005325449 309 aggaaSFEAAGRWYAalpeeqrpedeeeraaldAAWNPVWGD--RRQEIVFIGVDMARDELTRGLDA 373
Cdd:PRK11537  272 -----LFQGVQRLYS------------------ADWDRPWGDetPHSTLVFIGIQLPEEEIRAAFAG 315
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
258-375 8.58e-31

Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal to the trimeric cobaltochelatase subunit CobN, which is essential for vitamin B12 (cobalamin) biosynthesis. They contain a P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. CobW might be involved in cobalt reduction leading to cobalt(I) corrinoids. This entry represents the C-terminal domain found in CobW, as well as in P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression.


Pssm-ID: 214844 [Multi-domain]  Cd Length: 92  Bit Score: 113.46  E-value: 8.58e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  258 IESFVYRADRPMHPERLWAFLHgaTAWDGVLRSKGFFWLATRMDTTGAWSQAGGAASFEAAGRWYAAlpeeqrpedeeer 337
Cdd:smart00833   1 ISSFVYRARRPFHPQRLLAALD--ELPEGVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPAA------------- 65
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1005325449  338 aaldaawnpvwGDRRQEIVFIGVDMARDELTRGLDACL 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 ...
5-396 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: 692.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449   5 LPVTVLSGFLGAGKTTLLNHVLANRDALRVAVIVNDMSEVNVDAALVRGGGAALRRVEEKLVEMSNGCICCTLREDLLVE 84
Cdd:NF038288    1 LPVTVLSGFLGAGKTTLLNHILNNREGRRVAVIVNDMSEVNIDAALVRNGGASLSRTEEKLVEMSNGCICCTLREDLLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  85 VARLAGEGRFDYLLIESTGISEPLPVAETFTFADpATGKGLSELARLDTLVTVVDAQRFLADWTSADELRARRAALDGDD 164
Cdd:NF038288   81 VRRLAREGRFDYLVIESTGISEPLPVAETFTFAD-EDGVSLSDVARLDTMVTVVDAVNFLRDYDSADSLQERGESLGEED 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 165 ERTVADLLVEQVEFANVLVLNKTDLVSEDEVERLRAMLLHLNPGARVIRACRGQVDPREILGTGRFDHEEAARSPGWMRE 244
Cdd:NF038288  160 ERTVVDLLVDQVEFADVILLNKTDLVSEAELERLTAILRSLNPRARIVPISFGQVPLDKVLNTGLFDFERAAQAPGWLKE 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 245 LRGEHVPETEEYGIESFVYRADRPMHPERLWAFLHGatAWDG-VLRSKGFFWLATRMDTTGAWSQAGGAASFEAAGRWYA 323
Cdd:NF038288  240 LRGEHTPETEEYGISSFVYRARRPFHPQRFYDFLHS--EWPGkVLRSKGFFWLASRPDFAGSWSQAGGIARHGPAGMWWA 317
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005325449 324 ALPEEQRPEDEEERAALDAAWNPVWGDRRQEIVFIGVDMARDELTRGLDACLLTQEEMAAGPSGWSRLDDPFP 396
Cdd:NF038288  318 AVPRERWPQDEESLAAIRENWDEPFGDRRQELVFIGQDMDEAALRAALDACLLTDEEMAAGPEAWATLPDPFP 390
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
2-377 2.51e-150

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 428.44  E-value: 2.51e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449   2 TPKLPVTVLSGFLGAGKTTLLNHVLANRDALRVAVIVNDMSEVNVDAALVRGggaalrrVEEKLVEMSNGCICCTLREDL 81
Cdd:COG0523     1 DKRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEVGIDAALVRD-------TDEEIVELSNGCICCTLREDL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  82 LVEVARLAGEGRFDYLLIESTGISEPLPVAETFTFADPatgkgLSELARLDTLVTVVDAQRFLADWtsadelrarraald 161
Cdd:COG0523    74 LPALRRLLRRGRFDRLLIETTGLADPAPVAQTFTFDPE-----LRDRLRLDGVVTVVDARNLLDDL-------------- 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 162 gdDERTVADLLVEQVEFANVLVLNKTDLVSEDEVERLRAMLLHLNPGARVIRACRGQVDPREILGTGRFDHEEAARSPGW 241
Cdd:COG0523   135 --ADRTLHELLVDQIAFADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGEVDPALLLDLGLFDLEAALARPGW 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 242 MRELRGEHvpetEEYGIESFVYRADRPMHPERLWAFLHgaTAWDGVLRSKGFFWLATRmDTTGAWSQAGGAASFEAAGRW 321
Cdd:COG0523   213 LEELRDHE----HDDGIRSFVFRSDRPFDPERLADFLE--ELGPGVLRAKGFLWLAGR-PRRLVFQGVGGRLSLEPLGPW 285
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1005325449 322 YAalpeeqrpedeeeraaldaawnpvwGDRRQEIVFIGVDMARDELTRGLDACLLT 377
Cdd:COG0523   286 PA-------------------------DDRRSRLVFIGRDLDEAALEAALDACLLT 316
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
6-228 5.78e-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: 272.86  E-value: 5.78e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449   6 PVTVLSGFLGAGKTTLLNHVLANRDALRVAVIVNDMSEVNVDAALVRGGGAalrrvEEKLVEMSNGCICCTLREDLLVEV 85
Cdd:cd03112     1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVGIDAALLADSGG-----GEEVVELSNGCICCTLKGDLVKAL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  86 ARLAGE-GRFDYLLIESTGISEPLPVAETFTFADpatgkGLSELARLDTLVTVVDAQRFLADWTSADelrarraaldgdd 164
Cdd:cd03112    76 EQLLERrGKFDYILIETTGLADPGPIAQTLWSDE-----ELESRLRLDGVVTVVDAKNFLKQLDEED------------- 137
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005325449 165 ertVADLLVEQVEFANVLVLNKTDLVSEDEVERLRAMLLHLNPGARVIRACRGQVDPREILGTG 228
Cdd:cd03112   138 ---VSDLAVDQIAFADVIVLNKTDLVDEEELEALRARIRALNPGAKIVETTYGRVDLEELLGTG 198
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
6-213 2.16e-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: 217.12  E-value: 2.16e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449   6 PVTVLSGFLGAGKTTLLNHVLA-NRDALRVAVIVNDMSEVNVDAALVRGGGAalrrveeKLVEMSNGCICCTLREDLLVE 84
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLKqNRAGLRIAVIVNEFGETGIDAELLSETGV-------LIVELSNGCICCTIREDLSMA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  85 VARLAG-EGRFDYLLIESTGISEPLPVAETFTFADpatgkgLSELARLDTLVTVVDAQRFladwtsadelrarraaldgD 163
Cdd:pfam02492  74 LEALLErEGRLDVIFIETTGLAEPAPVAQTFLSPE------LRSPVLLDGVITVVDAANE-------------------A 128
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1005325449 164 DERTVADLLVEQVEFANVLVLNKTDLVSEDE-VERLRAMLLHLNPGARVIR 213
Cdd:pfam02492 129 DGEKIPRKAGDQIAFADLIVLNKTDLAPEVAlLEVLEEDLRRLNPGAPVVP 179
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
4-293 1.03e-43

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: 155.68  E-value: 1.03e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449   4 KLPVTVLSGFLGAGKTTLLNHVLANRDALRVAVIVNDMSEVNVDAALVRGGGAALRRvEEKLVEMSNGCICCTLREDLLV 83
Cdd:TIGR02475   3 KIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDLGIDGEILKACGIEGCS-EENIVELANGCICCTVADDFIP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  84 EVARL-AGEGRFDYLLIESTGISEPLPVAETFTFADpatgkgLSELARLDTLVTVVD-----AQRFLADWTSADELRARR 157
Cdd:TIGR02475  82 TMTKLlARRQRPDHILIETSGLALPKPLVQAFQWPE------IRSRVTVDGVVTVVDgpavaAGRFAADPDALDAQRAAD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 158 AALDGDDerTVADLLVEQVEFANVLVLNKTDLVSEDEVERLRAMLL-HLNPGARVIRACRGQVDPREILGTGRFDHEEAA 236
Cdd:TIGR02475 156 DNLDHET--PLEELFEDQLACADLVILNKADLLDAAGLARVRAEIAaELPRAVKIVEASHGEVDARVLLGLGAAAEDDLD 233
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1005325449 237 RSPGWMRELRGEhvpETEEYGIESFVYRADRPMHPERLWAFLHGATAWDGVLRSKGF 293
Cdd:TIGR02475 234 NRPSHHDFEGGE---EHDHDEFDSVVVDLGEVADPAALRQRLERLAEEHDVLRIKGF 287
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
1-373 1.24e-35

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 133.29  E-value: 1.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449   1 MTPkLPVTVLSGFLGAGKTTLLNHVLANRDALRVAVIVNDMSEVNVDAALVrgGGAALRrveekLVEMSNGCICCTLRE- 79
Cdd:PRK11537    1 MNP-IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLI--GDRATQ-----IKTLTNGCICCSRSNe 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  80 ------DLLVEVARlaGEGRFDYLLIESTGISEPLPVAETFtFADPAtgkgLSELARLDTLVTVVDAqrfladwTSADEL 153
Cdd:PRK11537   73 ledallDLLDNLDK--GNIQFDRLVIECTGMADPGPIIQTF-FSHEV----LCQRYLLDGVIALVDA-------VHADEQ 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 154 RarraaldgdDERTVADllvEQVEFANVLVLNKTDLVSEDevERLRAMLLHLNPGARVIRACRGQVDPREILGTGRFDHE 233
Cdd:PRK11537  139 M---------NQFTIAQ---SQVGYADRILLTKTDVAGEA--EKLRERLARINARAPVYTVVHGDIDLSLLFNTNGFMLE 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 234 EAARSPgwmrELRGEHVPETEEyGIESFVYRADRPMHPERLWAFLHG--ATAWDGVLRSKGFFWLA---TRMdttgawsq 308
Cdd:PRK11537  205 ENVVST----KPRFHFIADKQN-DISSIVVELDYPVDISEVSRVMENllLESADKLLRYKGMLWIDgepNRL-------- 271
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005325449 309 aggaaSFEAAGRWYAalpeeqrpedeeeraaldAAWNPVWGD--RRQEIVFIGVDMARDELTRGLDA 373
Cdd:PRK11537  272 -----LFQGVQRLYS------------------ADWDRPWGDetPHSTLVFIGIQLPEEEIRAAFAG 315
CobW_C smart00833
Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal ...
258-375 8.58e-31

Cobalamin synthesis protein cobW C-terminal domain; CobW proteins are generally found proximal to the trimeric cobaltochelatase subunit CobN, which is essential for vitamin B12 (cobalamin) biosynthesis. They contain a P-loop nucleotide-binding loop in the N-terminal domain and a histidine-rich region in the C-terminal portion suggesting a role in metal binding, possibly as an intermediary between the cobalt transport and chelation systems. CobW might be involved in cobalt reduction leading to cobalt(I) corrinoids. This entry represents the C-terminal domain found in CobW, as well as in P47K, a Pseudomonas chlororaphis protein needed for nitrile hydratase expression.


Pssm-ID: 214844 [Multi-domain]  Cd Length: 92  Bit Score: 113.46  E-value: 8.58e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  258 IESFVYRADRPMHPERLWAFLHgaTAWDGVLRSKGFFWLATRMDTTGAWSQAGGAASFEAAGRWYAAlpeeqrpedeeer 337
Cdd:smart00833   1 ISSFVYRARRPFHPQRLLAALD--ELPEGVLRAKGFFWLASRPDLPGVLSQAGGRLRIEPAGAWPAA------------- 65
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1005325449  338 aaldaawnpvwGDRRQEIVFIGVDMARDELTRGLDACL 375
Cdd:smart00833  66 -----------GDRRTRLVFIGRDLDEEAIRAALDACL 92
CobW_C pfam07683
Cobalamin synthesis protein cobW C-terminal domain; This is a large and diverse family of ...
258-375 1.58e-25

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: 99.23  E-value: 1.58e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449 258 IESFVYRADRPMHPERLWAFLHGATAWDGVLRSKGFFWLATRmDTTGAWSQAGGAASFEAAGRWyaalpeeqrpedeeer 337
Cdd:pfam07683   1 ISSFVFRADRPFDPERLEAWLEDLLLPEGILRAKGILWLAGR-PRPLVFQGVGGRLSLEPAGRW---------------- 63
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1005325449 338 aaldaawnPVWGDRRQEIVFIGVDMARDELTRGLDACL 375
Cdd:pfam07683  64 --------WPDEDRRSRLVFIGRDLDREALRAALDACL 93
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
15-213 6.81e-05

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


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 43.51  E-value: 6.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  15 GAGKTTLLNHVLAN-RDALRVAVIVNDMsEVNVDAALVRGGGAALRRVEeklvemSNGciCCTLREDLLVEVARLAGEGR 93
Cdd:COG0378    23 GSGKTTLLEKTIRAlKDRLRIAVIEGDI-YTTEDAERLRAAGVPVVQIN------TGG--CCHLDASMVLEALEELDLPD 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  94 FDYLLIESTGIseplPVAetFTFADpatgkgLSELARldtlVTVVDaqrfladwtsadelrarraALDGDDE-RTVADLL 172
Cdd:COG0378    94 LDLLFIENVGN----LVC--PAFFP------LGEDLK----VVVLS-------------------VTEGDDKpRKYPPMF 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1005325449 173 veqvEFANVLVLNKTDLVS--EDEVERLRAMLLHLNPGARVIR 213
Cdd:COG0378   139 ----TAADLLVINKIDLAPyvGFDLEVMEEDARRVNPGAPIFE 177
HypB cd05390
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the ...
15-103 4.07e-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: 41.43  E-value: 4.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005325449  15 GAGKTTLLNHVLAN-RDALRVAVIVNDMsEVNVDAALVRGGGAalrrveeKLVEMSNGCIcCTLREDLLVEVARLAGEGR 93
Cdd:cd05390    31 GSGKTTLLERTIDAlKDELKIAVIEGDL-ETDNDAERIRATGV-------PAIQINTGGA-CHLDADMVARALHDLDLDE 101
                          90
                  ....*....|
gi 1005325449  94 FDYLLIESTG 103
Cdd:cd05390   102 LDLLFIENVG 111
YjiA COG2403
Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion ...
179-214 8.54e-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: 38.28  E-value: 8.54e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1005325449 179 ANVLVLNKTDLVSEDEVERLRAMLLHLNPGARVIRA 214
Cdd:COG2403   262 ADVVVINKVDTADPEDIETVRENIRKVNPKAEIIEA 297
 
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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