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Conserved domains on  [gi|530390018|ref|XP_005251574|]
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zinc-regulated GTPase metalloprotein activator 1A isoform X3 [Homo sapiens]

Protein Classification

GTP-binding protein( domain architecture ID 10123105)

GTP-binding protein similar to GTPase YjiA, a GTP dependent regulatory protein, and CobW, which is involved in the synthesis of cobalamin

Gene Ontology:  GO:0005525|GO:0003924
PubMed:  11916378

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
 43-236 1.79e-95

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: 277.87  E-value: 1.79e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018  43 PVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSaLEKSLAVSQGGelYEEWLELRNGCLCCSVKDSGLRAIEN 122
Cdd:cd03112    1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVG-IDAALLADSGG--GEEVVELSNGCICCTLKGDLVKALEQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018 123 LMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEEKpdgLINEATRQVALADAILI 202
Cdd:cd03112   78 LLERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEED---VSDLAVDQIAFADVIVL 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530390018 203 NKTDLVPEEDVKKLRTTIRSINGLGQILETQRSR 236
Cdd:cd03112  155 NKTDLVDEEELEALRARIRALNPGAKIVETTYGR 188
 
Name Accession Description Interval E-value
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
 43-236 1.79e-95

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: 277.87  E-value: 1.79e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018  43 PVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSaLEKSLAVSQGGelYEEWLELRNGCLCCSVKDSGLRAIEN 122
Cdd:cd03112    1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVG-IDAALLADSGG--GEEVVELSNGCICCTLKGDLVKALEQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018 123 LMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEEKpdgLINEATRQVALADAILI 202
Cdd:cd03112   78 LLERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEED---VSDLAVDQIAFADVIVL 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530390018 203 NKTDLVPEEDVKKLRTTIRSINGLGQILETQRSR 236
Cdd:cd03112  155 NKTDLVDEEELEALRARIRALNPGAKIVETTYGR 188
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
 40-236 1.76e-71

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 220.81  E-value: 1.76e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGE---GSALekslaVSQGGelyEEWLELRNGCLCCSVKDSG 116
Cdd:COG0523    2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEvgiDAAL-----VRDTD---EEIVELSNGCICCTLREDL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018 117 LRAIENLMqKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEekpDGLINEATRQVAL 196
Cdd:COG0523   74 LPALRRLL-RRGRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLAD---RTLHELLVDQIAF 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530390018 197 ADAILINKTDLVPEEDVKKLRTTIRSINGLGQILETQRSR 236
Cdd:COG0523  150 ADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGE 189
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
 43-231 4.05e-60

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: 187.46  E-value: 4.05e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018   43 PVTIITGYLGAGKTTLLNYIL-TEQHSKRVAVILNEFGEGSaLEKSLAVSQGgelyEEWLELRNGCLCCSVKDSGLRAIE 121
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETG-IDAELLSETG----VLIVELSNGCICCTIREDLSMALE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018  122 NLMQKKGKFDYILLETTGLADPGAVASMFWVDaELGSDIYLDGIITIVDSkyglKHLTEEKPdgLINEATRQVALADAIL 201
Cdd:pfam02492  76 ALLEREGRLDVIFIETTGLAEPAPVAQTFLSP-ELRSPVLLDGVITVVDA----ANEADGEK--IPRKAGDQIAFADLIV 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 530390018  202 INKTDLVPEE-DVKKLRTTIRSINGLGQILE 231
Cdd:pfam02492 149 LNKTDLAPEVaLLEVLEEDLRRLNPGAPVVP 179
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
 40-236 1.24e-36

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: 131.79  E-value: 1.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018   40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGE----GSALeKSLAVSQGGElyEEWLELRNGCLCCSVKDS 115
Cdd:TIGR02475   2 AKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDlgidGEIL-KACGIEGCSE--ENIVELANGCICCTVADD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018  116 GLRAIENLMQKKGKFDYILLETTGLADPGAVASMF-WvdAELGSDIYLDGIITIVDSKYGLKHLTEEKPDGLinEATR-- 192
Cdd:TIGR02475  79 FIPTMTKLLARRQRPDHILIETSGLALPKPLVQAFqW--PEIRSRVTVDGVVTVVDGPAVAAGRFAADPDAL--DAQRaa 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530390018  193 ----------------QVALADAILINKTDLVPEEDVKKLRTTIRS-INGLGQILETQRSR 236
Cdd:TIGR02475 155 ddnldhetpleelfedQLACADLVILNKADLLDAAGLARVRAEIAAeLPRAVKIVEASHGE 215
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
 42-224 6.28e-36

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 129.44  E-value: 6.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018  42 IPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSALEKSLavsqgGELYEEWLELRNGCLCCS----VKDSGL 117
Cdd:PRK11537   4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLI-----GDRATQIKTLTNGCICCSrsneLEDALL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018 118 RAIENLMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEekpdglINEATRQVALA 197
Cdd:PRK11537  79 DLLDNLDKGNIQFDRLVIECTGMADPGPIIQTFFSHEVLCQRYLLDGVIALVDAVHADEQMNQ------FTIAQSQVGYA 152

                        170       180
                 ....*....|....*....|....*..
gi 530390018 198 DAILINKTDLVPEEDvkKLRTTIRSIN 224
Cdd:PRK11537 153 DRILLTKTDVAGEAE--KLRERLARIN 177
 
Name Accession Description Interval E-value
CobW-like cd03112
cobalamin synthesis protein CobW; The function of this protein family is unknown. The amino ...
 43-236 1.79e-95

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: 277.87  E-value: 1.79e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018  43 PVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSaLEKSLAVSQGGelYEEWLELRNGCLCCSVKDSGLRAIEN 122
Cdd:cd03112    1 PVTLLTGFLGAGKTTLLNHILSEQHGKRIAVIVNEFGEVG-IDAALLADSGG--GEEVVELSNGCICCTLKGDLVKALEQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018 123 LMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEEKpdgLINEATRQVALADAILI 202
Cdd:cd03112   78 LLERRGKFDYILIETTGLADPGPIAQTLWSDEELESRLRLDGVVTVVDAKNFLKQLDEED---VSDLAVDQIAFADVIVL 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 530390018 203 NKTDLVPEEDVKKLRTTIRSINGLGQILETQRSR 236
Cdd:cd03112  155 NKTDLVDEEELEALRARIRALNPGAKIVETTYGR 188
YejR COG0523
Zinc metallochaperone YeiR/ZagA and related GTPases, G3E family [General function prediction ...
 40-236 1.76e-71

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


Pssm-ID: 440289 [Multi-domain]  Cd Length: 318  Bit Score: 220.81  E-value: 1.76e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018  40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGE---GSALekslaVSQGGelyEEWLELRNGCLCCSVKDSG 116
Cdd:COG0523    2 KRIPVTVLTGFLGAGKTTLLNHLLANPEGRRIAVIVNEFGEvgiDAAL-----VRDTD---EEIVELSNGCICCTLREDL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018 117 LRAIENLMqKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEekpDGLINEATRQVAL 196
Cdd:COG0523   74 LPALRRLL-RRGRFDRLLIETTGLADPAPVAQTFTFDPELRDRLRLDGVVTVVDARNLLDDLAD---RTLHELLVDQIAF 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530390018 197 ADAILINKTDLVPEEDVKKLRTTIRSINGLGQILETQRSR 236
Cdd:COG0523  150 ADVIVLNKTDLVDEEELAALEARLRALNPGAPIVRTSHGE 189
cobW pfam02492
CobW/HypB/UreG, nucleotide-binding domain; This domain is found in HypB, a hydrogenase ...
 43-231 4.05e-60

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: 187.46  E-value: 4.05e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018   43 PVTIITGYLGAGKTTLLNYIL-TEQHSKRVAVILNEFGEGSaLEKSLAVSQGgelyEEWLELRNGCLCCSVKDSGLRAIE 121
Cdd:pfam02492   1 PVTVITGFLGSGKTTLLNHLLkQNRAGLRIAVIVNEFGETG-IDAELLSETG----VLIVELSNGCICCTIREDLSMALE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018  122 NLMQKKGKFDYILLETTGLADPGAVASMFWVDaELGSDIYLDGIITIVDSkyglKHLTEEKPdgLINEATRQVALADAIL 201
Cdd:pfam02492  76 ALLEREGRLDVIFIETTGLAEPAPVAQTFLSP-ELRSPVLLDGVITVVDA----ANEADGEK--IPRKAGDQIAFADLIV 148

                         170       180       190
                  ....*....|....*....|....*....|.
gi 530390018  202 INKTDLVPEE-DVKKLRTTIRSINGLGQILE 231
Cdd:pfam02492 149 LNKTDLAPEVaLLEVLEEDLRRLNPGAPVVP 179
CobW TIGR02475
cobalamin biosynthesis protein CobW; The family of proteins identified by this model is ...
 40-236 1.24e-36

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: 131.79  E-value: 1.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018   40 AKIPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGE----GSALeKSLAVSQGGElyEEWLELRNGCLCCSVKDS 115
Cdd:TIGR02475   2 AKIPVTIVTGFLGAGKTTLIRHLLQNAAGRRIAVIVNEFGDlgidGEIL-KACGIEGCSE--ENIVELANGCICCTVADD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018  116 GLRAIENLMQKKGKFDYILLETTGLADPGAVASMF-WvdAELGSDIYLDGIITIVDSKYGLKHLTEEKPDGLinEATR-- 192
Cdd:TIGR02475  79 FIPTMTKLLARRQRPDHILIETSGLALPKPLVQAFqW--PEIRSRVTVDGVVTVVDGPAVAAGRFAADPDAL--DAQRaa 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530390018  193 ----------------QVALADAILINKTDLVPEEDVKKLRTTIRS-INGLGQILETQRSR 236
Cdd:TIGR02475 155 ddnldhetpleelfedQLACADLVILNKADLLDAAGLARVRAEIAAeLPRAVKIVEASHGE 215
PRK11537 PRK11537
putative GTP-binding protein YjiA; Provisional
 42-224 6.28e-36

putative GTP-binding protein YjiA; Provisional


Pssm-ID: 183183 [Multi-domain]  Cd Length: 318  Bit Score: 129.44  E-value: 6.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018  42 IPVTIITGYLGAGKTTLLNYILTEQHSKRVAVILNEFGEGSALEKSLavsqgGELYEEWLELRNGCLCCS----VKDSGL 117
Cdd:PRK11537   4 IAVTLLTGFLGAGKTTLLRHILNEQHGYKIAVIENEFGEVSVDDQLI-----GDRATQIKTLTNGCICCSrsneLEDALL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530390018 118 RAIENLMQKKGKFDYILLETTGLADPGAVASMFWVDAELGSDIYLDGIITIVDSKYGLKHLTEekpdglINEATRQVALA 197
Cdd:PRK11537  79 DLLDNLDKGNIQFDRLVIECTGMADPGPIIQTFFSHEVLCQRYLLDGVIALVDAVHADEQMNQ------FTIAQSQVGYA 152

                        170       180
                 ....*....|....*....|....*..
gi 530390018 198 DAILINKTDLVPEEDvkKLRTTIRSIN 224
Cdd:PRK11537 153 DRILLTKTDVAGEAE--KLRERLARIN 177
YjiA COG2403
Zn/Ni/Co-binding GTPase YjiA, predicted metallochaperone, CobW/Nha3/YciC family [Inorganic ion ...
 196-232 3.26e-04

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: 41.36  E-value: 3.26e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 530390018 196 LADAILINKTDLVPEEDVKKLRTTIRSINGLGQILET 232
Cdd:COG2403  261 MADVVVINKVDTADPEDIETVRENIRKVNPKAEIIEA 297
RecD COG0507
ATPase/5#-3# helicase helicase subunit RecD of the DNA repair enzyme RecBCD (exonuclease V) ...
 43-73 1.41e-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: 39.57  E-value: 1.41e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 530390018  43 PVTIITGYLGAGKTTLLNYIL--TEQHSKRVAV 73
Cdd:COG0507  141 RVSVLTGGAGTGKTTTLRALLaaLEALGLRVAL 173
HypB cd05390
nickel incorporation protein HypB; HypB is one of numerous accessory proteins required for the ...
 197-232 3.36e-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: 37.58  E-value: 3.36e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 530390018 197 ADAILINKTDLVP--EEDVKKLRTTIRSINGLGQILET 232
Cdd:cd05390  149 ADVVLINKIDLLPyfDFDVEKAKEDIKKLNPNAPIIEV 186
HypB COG0378
Hydrogenase/urease maturation factor HypB, Ni2+-binding GTPase [Posttranslational modification, ...
 194-232 3.42e-03

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


Pssm-ID: 440147 [Multi-domain]  Cd Length: 200  Bit Score: 37.35  E-value: 3.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 530390018 194 VALADAILINKTDLVP--EEDVKKLRTTIRSINGLGQILET 232
Cdd:COG0378  138 FTAADLLVINKIDLAPyvGFDLEVMEEDARRVNPGAPIFEV 178
DEXSc_RecD-like cd17933
DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1. ...
 43-73 7.92e-03

DEXS-box helicase domain of RecD and similar proteins; RecD is a member of the RecBCD (EC 3.1.11.5, Exonuclease V) complex. It is the alpha chain of the complex and functions as a 3'-5' helicase. The RecBCD enzyme is both a helicase that unwinds, or separates the strands of DNA, and a nuclease that makes single-stranded nicks in DNA. RecD is a member of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350691 [Multi-domain]  Cd Length: 155  Bit Score: 35.99  E-value: 7.92e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 530390018  43 PVTIITGYLGAGKTTLLNYILT--EQHSKRVAV 73
Cdd:cd17933   13 RVSVLTGGAGTGKTTTLKALLAalEAEGKRVVL 45
 
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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