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Conserved domains on  [gi|1635513800]
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Chain B, DNA damage-inducible protein

Protein Classification

cyanamide hydratase( domain architecture ID 10799147)

cyanamide hydratase is involved in the detoxification and/or utilization of cyanamide, a toxic nitrile compound distributed widely in the environment

CATH:  3.30.70.1370
EC:  4.2.1.69
Gene Ontology:  GO:0008270|GO:0018890|GO:0018820
SCOP:  3000943

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
cyanamide_fam TIGR03401
HD domain protein, cyanamide hydratase family; Members of this protein family are known, so ...
10-232 5.24e-134

HD domain protein, cyanamide hydratase family; Members of this protein family are known, so far, in the Ascomycota, a branch of the Fungi, and contain an HD domain (pfam01966), found typically in various metal-dependent phosphohydrolases. The only characterized member of this family, from the soil fungus Myrothecium verrucaria, is cyanamide hydratase (EC 4.2.1.69), a zinc-containing homohexamer that adds water to the fertilizer cyanamide (NCNH2), a nitrile compound, to produce urea (NH2-CO-NH2). Homologs are likely to be nitrile hydratases.


:

Pssm-ID: 188314  Cd Length: 228  Bit Score: 375.98  E-value: 5.24e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635513800  10 SQYGFVRVPREVEKAI---PVVNAPRPRAVVPPP--NSETARLVREYAAKELTAPVLNHSLRVFQYSVAIIRDQFPAWDL 84
Cdd:TIGR03401   1 SKYGFTAVPRDAKAAIstvPKVKPPPAQSVEDTPlpDTPLVKFAQEYAKARLPPETYNHSLRVYYYGLAIARDQFPEWDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635513800  85 DQEVLYVTCLLHDIATTDKNMRATKMSFEYYGGILSRELVFNATGGNQDYADAVTEAIIRHQDLTGTGYITTLGLILQIA 164
Cdd:TIGR03401  81 SDETWFLTCLLHDIGTTDENMTATKMSFEFYGGILALDVLKEQTGANQDQAEAVAEAIIRHQDLGVDGTITTLGQLLQLA 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1635513800 165 VTLDNVGSNTDLIHIDTVSAINEQFPRLHWLSCFATVVDTENSRKPWGHTSSLGDDFSKKVICNTFGY 232
Cdd:TIGR03401 161 TIFDNVGANTDLVHPDTVDAVNEAYPRHGWSSCFASTIRKENELKPWCHTTALGDDFPKKVLANTLMY 228
 
Name Accession Description Interval E-value
cyanamide_fam TIGR03401
HD domain protein, cyanamide hydratase family; Members of this protein family are known, so ...
10-232 5.24e-134

HD domain protein, cyanamide hydratase family; Members of this protein family are known, so far, in the Ascomycota, a branch of the Fungi, and contain an HD domain (pfam01966), found typically in various metal-dependent phosphohydrolases. The only characterized member of this family, from the soil fungus Myrothecium verrucaria, is cyanamide hydratase (EC 4.2.1.69), a zinc-containing homohexamer that adds water to the fertilizer cyanamide (NCNH2), a nitrile compound, to produce urea (NH2-CO-NH2). Homologs are likely to be nitrile hydratases.


Pssm-ID: 188314  Cd Length: 228  Bit Score: 375.98  E-value: 5.24e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635513800  10 SQYGFVRVPREVEKAI---PVVNAPRPRAVVPPP--NSETARLVREYAAKELTAPVLNHSLRVFQYSVAIIRDQFPAWDL 84
Cdd:TIGR03401   1 SKYGFTAVPRDAKAAIstvPKVKPPPAQSVEDTPlpDTPLVKFAQEYAKARLPPETYNHSLRVYYYGLAIARDQFPEWDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635513800  85 DQEVLYVTCLLHDIATTDKNMRATKMSFEYYGGILSRELVFNATGGNQDYADAVTEAIIRHQDLTGTGYITTLGLILQIA 164
Cdd:TIGR03401  81 SDETWFLTCLLHDIGTTDENMTATKMSFEFYGGILALDVLKEQTGANQDQAEAVAEAIIRHQDLGVDGTITTLGQLLQLA 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1635513800 165 VTLDNVGSNTDLIHIDTVSAINEQFPRLHWLSCFATVVDTENSRKPWGHTSSLGDDFSKKVICNTFGY 232
Cdd:TIGR03401 161 TIFDNVGANTDLVHPDTVDAVNEAYPRHGWSSCFASTIRKENELKPWCHTTALGDDFPKKVLANTLMY 228
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
43-171 2.65e-08

HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only];


Pssm-ID: 441028 [Multi-domain]  Cd Length: 191  Bit Score: 52.21  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635513800  43 ETARLVREYAaKELTAPVLNHSLRVFQYSVAIIRDQfpawDLDQEVLYVTCLLHDIATTDKNMRatKMSFEYYGGILSRE 122
Cdd:COG1418     3 ELIKLVKYLR-TSYGQHDLQHSLRVAKLAGLIAAEE----GADVEVAKRAALLHDIGKAKDHEV--EGSHAEIGAELARK 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1635513800 123 LvFNATGGNQDYADAVTEAIIRHQDLTGTGYITTLGLILQIAVTLDNVG 171
Cdd:COG1418    76 Y-LESLGFPEEEIEAVVHAIEAHSFSGGIEPESLEAKIVQDADRLDALG 123
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
59-164 2.84e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 51.19  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635513800  59 PVLNHSLRVFQYSvAIIRDQFPAWDLDQEVLYVTCLLHDIATTDKNMRATKMSFE------YYGGILSRELVFnatGGNQ 132
Cdd:cd00077     2 HRFEHSLRVAQLA-RRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAITEEESElekdhaIVGAEILRELLL---EEVI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1635513800 133 DYADAVTEAIIR--HQDLTGTGY--------ITTLGLILQIA 164
Cdd:cd00077    78 KLIDELILAVDAshHERLDGLGYpdglkgeeITLEARIVKLA 119
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
59-164 1.09e-07

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 49.22  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635513800   59 PVLNHSLRVFQYSVAIIRDQFpawDLDQEVLYVTCLLHDIATTDKNMRATKMSFEYYG-GILSRELVFNaTGGNQDYADA 137
Cdd:smart00471   4 HVFEHSLRVAQLAAALAEELG---LLDIELLLLAALLHDIGKPGTPDSFLVKTSVLEDhHFIGAEILLE-EEEPRILEEI 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1635513800  138 VTEAIIRHQDLTGTGY---ITTLGLILQIA 164
Cdd:smart00471  80 LRTAILSHHERPDGLRgepITLEARIVKVA 109
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
60-164 6.69e-06

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 43.76  E-value: 6.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635513800  60 VLNHSLRVFQYSVAIIRDqfpAWDLDQEVLYVTCLLHDIA---TTDKNMRATKM-SFEYYGGILSRELvfnatgGNQDYA 135
Cdd:pfam01966   1 RLEHSLRVALLARELAEE---LGELDRELLLLAALLHDIGkgpFGDEKPEFEIFlGHAVVGAEILREL------EKRLGL 71
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1635513800 136 DAVTEAIIRHQDLTGTGY----ITTLGLILQIA 164
Cdd:pfam01966  72 EDVLKLILEHHESWEGAGypeeISLEARIVKLA 104
 
Name Accession Description Interval E-value
cyanamide_fam TIGR03401
HD domain protein, cyanamide hydratase family; Members of this protein family are known, so ...
10-232 5.24e-134

HD domain protein, cyanamide hydratase family; Members of this protein family are known, so far, in the Ascomycota, a branch of the Fungi, and contain an HD domain (pfam01966), found typically in various metal-dependent phosphohydrolases. The only characterized member of this family, from the soil fungus Myrothecium verrucaria, is cyanamide hydratase (EC 4.2.1.69), a zinc-containing homohexamer that adds water to the fertilizer cyanamide (NCNH2), a nitrile compound, to produce urea (NH2-CO-NH2). Homologs are likely to be nitrile hydratases.


Pssm-ID: 188314  Cd Length: 228  Bit Score: 375.98  E-value: 5.24e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635513800  10 SQYGFVRVPREVEKAI---PVVNAPRPRAVVPPP--NSETARLVREYAAKELTAPVLNHSLRVFQYSVAIIRDQFPAWDL 84
Cdd:TIGR03401   1 SKYGFTAVPRDAKAAIstvPKVKPPPAQSVEDTPlpDTPLVKFAQEYAKARLPPETYNHSLRVYYYGLAIARDQFPEWDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635513800  85 DQEVLYVTCLLHDIATTDKNMRATKMSFEYYGGILSRELVFNATGGNQDYADAVTEAIIRHQDLTGTGYITTLGLILQIA 164
Cdd:TIGR03401  81 SDETWFLTCLLHDIGTTDENMTATKMSFEFYGGILALDVLKEQTGANQDQAEAVAEAIIRHQDLGVDGTITTLGQLLQLA 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1635513800 165 VTLDNVGSNTDLIHIDTVSAINEQFPRLHWLSCFATVVDTENSRKPWGHTSSLGDDFSKKVICNTFGY 232
Cdd:TIGR03401 161 TIFDNVGANTDLVHPDTVDAVNEAYPRHGWSSCFASTIRKENELKPWCHTTALGDDFPKKVLANTLMY 228
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
43-171 2.65e-08

HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal structure and biogenesis, General function prediction only];


Pssm-ID: 441028 [Multi-domain]  Cd Length: 191  Bit Score: 52.21  E-value: 2.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635513800  43 ETARLVREYAaKELTAPVLNHSLRVFQYSVAIIRDQfpawDLDQEVLYVTCLLHDIATTDKNMRatKMSFEYYGGILSRE 122
Cdd:COG1418     3 ELIKLVKYLR-TSYGQHDLQHSLRVAKLAGLIAAEE----GADVEVAKRAALLHDIGKAKDHEV--EGSHAEIGAELARK 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1635513800 123 LvFNATGGNQDYADAVTEAIIRHQDLTGTGYITTLGLILQIAVTLDNVG 171
Cdd:COG1418    76 Y-LESLGFPEEEIEAVVHAIEAHSFSGGIEPESLEAKIVQDADRLDALG 123
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
59-164 2.84e-08

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 51.19  E-value: 2.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635513800  59 PVLNHSLRVFQYSvAIIRDQFPAWDLDQEVLYVTCLLHDIATTDKNMRATKMSFE------YYGGILSRELVFnatGGNQ 132
Cdd:cd00077     2 HRFEHSLRVAQLA-RRLAEELGLSEEDIELLRLAALLHDIGKPGTPDAITEEESElekdhaIVGAEILRELLL---EEVI 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1635513800 133 DYADAVTEAIIR--HQDLTGTGY--------ITTLGLILQIA 164
Cdd:cd00077    78 KLIDELILAVDAshHERLDGLGYpdglkgeeITLEARIVKLA 119
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
59-164 1.09e-07

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 49.22  E-value: 1.09e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635513800   59 PVLNHSLRVFQYSVAIIRDQFpawDLDQEVLYVTCLLHDIATTDKNMRATKMSFEYYG-GILSRELVFNaTGGNQDYADA 137
Cdd:smart00471   4 HVFEHSLRVAQLAAALAEELG---LLDIELLLLAALLHDIGKPGTPDSFLVKTSVLEDhHFIGAEILLE-EEEPRILEEI 79
                           90       100       110
                   ....*....|....*....|....*....|
gi 1635513800  138 VTEAIIRHQDLTGTGY---ITTLGLILQIA 164
Cdd:smart00471  80 LRTAILSHHERPDGLRgepITLEARIVKVA 109
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
60-164 6.69e-06

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 43.76  E-value: 6.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1635513800  60 VLNHSLRVFQYSVAIIRDqfpAWDLDQEVLYVTCLLHDIA---TTDKNMRATKM-SFEYYGGILSRELvfnatgGNQDYA 135
Cdd:pfam01966   1 RLEHSLRVALLARELAEE---LGELDRELLLLAALLHDIGkgpFGDEKPEFEIFlGHAVVGAEILREL------EKRLGL 71
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1635513800 136 DAVTEAIIRHQDLTGTGY----ITTLGLILQIA 164
Cdd:pfam01966  72 EDVLKLILEHHESWEGAGypeeISLEARIVKLA 104
 
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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