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Conserved domains on  [gi|735999655|gb|AJA43377|]
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HNH endonuclease [Mycobacterium phage Sbash]

Protein Classification

HNH endonuclease( domain architecture ID 10003646)

HNH endonuclease contains an HNH endonuclease signature motif and may catalyze the hydrolysis of DNA

Gene Ontology:  GO:0004519|GO:0003676|GO:0008270
PubMed:  28211904

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
McrA COG1403
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
5-61 1.13e-22

5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];


:

Pssm-ID: 441013 [Multi-domain]  Cd Length: 64  Bit Score: 88.12  E-value: 1.13e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 735999655   5 KRLRFEILRRDNHACRYCGRSAPEVKLTIDHVVPESLGGPDDPSNLVAACADCNGGK 61
Cdd:COG1403    8 PALRRAVLKRDNGRCQYCGRPFSGDALEVDHIIPRSRGGTDTWENLVLLCRRCNRRK 64
 
Name Accession Description Interval E-value
McrA COG1403
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
5-61 1.13e-22

5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];


Pssm-ID: 441013 [Multi-domain]  Cd Length: 64  Bit Score: 88.12  E-value: 1.13e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 735999655   5 KRLRFEILRRDNHACRYCGRSAPEVKLTIDHVVPESLGGPDDPSNLVAACADCNGGK 61
Cdd:COG1403    8 PALRRAVLKRDNGRCQYCGRPFSGDALEVDHIIPRSRGGTDTWENLVLLCRRCNRRK 64
HNH_5 pfam14279
HNH endonuclease; This domain is related to other HNH domain families such as pfam01844. ...
 19-72 7.89e-16

HNH endonuclease; This domain is related to other HNH domain families such as pfam01844. Suggesting that these proteins have a nucleic acid cleaving function.


Pssm-ID: 464124 [Multi-domain]  Cd Length: 56  Bit Score: 69.67  E-value: 7.89e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 735999655   19 CRYCGRSAPEVKLTIDHVVPESLGGPDDPSNLVAACADCNGGKSSvPVDAPLVN 72
Cdd:pfam14279   1 CIYCGKEFPEKNLTIEHIIPESLGGKNKISNLQTLCKKCNSKKGH-DVDAALSR 53
guided_IscB NF040563
RNA-guided endonuclease IscB;
11-66 3.26e-14

RNA-guided endonuclease IscB;


Pssm-ID: 468538 [Multi-domain]  Cd Length: 315  Bit Score: 71.04  E-value: 3.26e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 735999655  11 ILRRDNHACRYCGrsAPEVKLTIDHVVPESLGGPDDPSNLVAACADCNGGKSSVPV 66
Cdd:NF040563 188 LLERDGRTCQYCG--AKDVPLEVHHIVPRSKGGSDRVSNLILACEPCNQKKGNQPV 241
HNHc cd00085
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
 10-62 1.94e-11

HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins.


Pssm-ID: 238038 [Multi-domain]  Cd Length: 57  Bit Score: 57.87  E-value: 1.94e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 735999655  10 EILRRDNHACRYCGRSAPEVKLTIDHVVPESLGGPDDPSNLVAACADCNGGKS 62
Cdd:cd00085    5 LVLLARDGLCPYCGKPGGTEGLEVDHIIPLSDGGNNDLDNLVLLCRKCHRKKH 57
HNHc smart00507
HNH nucleases;
6-58 2.46e-11

HNH nucleases;


Pssm-ID: 214702 [Multi-domain]  Cd Length: 52  Bit Score: 57.47  E-value: 2.46e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 735999655     6 RLRFEILRRDnHACRYCGRSaPEVKLTIDHVVPESLGGPDDPSNLVAACADCN 58
Cdd:smart00507   1 KLRRLLLHRD-GVCAYCGKP-ASEGLEVDHIIPLSDGGNDDLDNLVLLCPKCH 51
 
Name Accession Description Interval E-value
McrA COG1403
5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];
5-61 1.13e-22

5-methylcytosine-specific restriction endonuclease McrA [Defense mechanisms];


Pssm-ID: 441013 [Multi-domain]  Cd Length: 64  Bit Score: 88.12  E-value: 1.13e-22
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 735999655   5 KRLRFEILRRDNHACRYCGRSAPEVKLTIDHVVPESLGGPDDPSNLVAACADCNGGK 61
Cdd:COG1403    8 PALRRAVLKRDNGRCQYCGRPFSGDALEVDHIIPRSRGGTDTWENLVLLCRRCNRRK 64
HNH_5 pfam14279
HNH endonuclease; This domain is related to other HNH domain families such as pfam01844. ...
 19-72 7.89e-16

HNH endonuclease; This domain is related to other HNH domain families such as pfam01844. Suggesting that these proteins have a nucleic acid cleaving function.


Pssm-ID: 464124 [Multi-domain]  Cd Length: 56  Bit Score: 69.67  E-value: 7.89e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 735999655   19 CRYCGRSAPEVKLTIDHVVPESLGGPDDPSNLVAACADCNGGKSSvPVDAPLVN 72
Cdd:pfam14279   1 CIYCGKEFPEKNLTIEHIIPESLGGKNKISNLQTLCKKCNSKKGH-DVDAALSR 53
guided_IscB NF040563
RNA-guided endonuclease IscB;
11-66 3.26e-14

RNA-guided endonuclease IscB;


Pssm-ID: 468538 [Multi-domain]  Cd Length: 315  Bit Score: 71.04  E-value: 3.26e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 735999655  11 ILRRDNHACRYCGrsAPEVKLTIDHVVPESLGGPDDPSNLVAACADCNGGKSSVPV 66
Cdd:NF040563 188 LLERDGRTCQYCG--AKDVPLEVHHIVPRSKGGSDRVSNLILACEPCNQKKGNQPV 241
HNHc cd00085
HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic ...
 10-62 1.94e-11

HNH nucleases; HNH endonuclease signature which is found in viral, prokaryotic, and eukaryotic proteins. The alignment includes members of the large group of homing endonucleases, yeast intron 1 protein, MutS, as well as bacterial colicins, pyocins, and anaredoxins.


Pssm-ID: 238038 [Multi-domain]  Cd Length: 57  Bit Score: 57.87  E-value: 1.94e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 735999655  10 EILRRDNHACRYCGRSAPEVKLTIDHVVPESLGGPDDPSNLVAACADCNGGKS 62
Cdd:cd00085    5 LVLLARDGLCPYCGKPGGTEGLEVDHIIPLSDGGNNDLDNLVLLCRKCHRKKH 57
HNHc smart00507
HNH nucleases;
6-58 2.46e-11

HNH nucleases;


Pssm-ID: 214702 [Multi-domain]  Cd Length: 52  Bit Score: 57.47  E-value: 2.46e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 735999655     6 RLRFEILRRDnHACRYCGRSaPEVKLTIDHVVPESLGGPDDPSNLVAACADCN 58
Cdd:smart00507   1 KLRRLLLHRD-GVCAYCGKP-ASEGLEVDHIIPLSDGGNDDLDNLVLLCPKCH 51
HNH pfam01844
HNH endonuclease; His-Asn-His (HNH) proteins are a very common family of small nucleic ...
 19-63 6.30e-11

HNH endonuclease; His-Asn-His (HNH) proteins are a very common family of small nucleic acid-binding proteins that are generally associated with endonuclease activity.


Pssm-ID: 396422 [Multi-domain]  Cd Length: 47  Bit Score: 56.21  E-value: 6.30e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 735999655   19 CRYCGRS-APEVKLTIDHVVPESLGGPDDPSNLVAACADCNGGKSS 63
Cdd:pfam01844   1 CQYCGRPfHISDALTVDHIIPLSDGGADDIENLILLCPSCHNKKHN 46
HNH_4 pfam13395
HNH endonuclease; This HNH nuclease domain is found in CRISPR-related proteins.
 19-63 1.24e-05

HNH endonuclease; This HNH nuclease domain is found in CRISPR-related proteins.


Pssm-ID: 433172 [Multi-domain]  Cd Length: 55  Bit Score: 41.84  E-value: 1.24e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 735999655   19 CRYCGR--SAPEVKLT----IDHVVPESLGGPDDPSNLVAACADCNGGKSS 63
Cdd:pfam13395   1 CPYTGEqiSIDDLFSEknydIDHILPYSRSFDDSFSNKVLVLRSANQEKGN 51
Cas9 COG3513
CRISPR-Cas system type-II protein Cas9 [Defense mechanisms]; CRISPR-Cas system type-II protein ...
 6-62 2.70e-05

CRISPR-Cas system type-II protein Cas9 [Defense mechanisms]; CRISPR-Cas system type-II protein Cas9 is part of the Pathway/BioSystem: CRISPR-Cas system


Pssm-ID: 442735 [Multi-domain]  Cd Length: 812  Bit Score: 45.34  E-value: 2.70e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 735999655   6 RLRFEILRRDNHACRYCGRSAP-----EVKLTIDHVVPESLGGPDDPSNLVAACADCNGGKS 62
Cdd:COG3513  530 ILKYRLWEEQNGRCPYTGKPISisdllDGSVEIDHILPRSRTLDDSFNNKVLCLADANREKG 591
Csn1 cd09643
CRISPR/Cas system-associated protein Cas9; CRISPR (Clustered Regularly Interspaced Short ...
 16-62 4.94e-03

CRISPR/Cas system-associated protein Cas9; CRISPR (Clustered Regularly Interspaced Short Palindromic Repeats) and associated Cas proteins comprise a system for heritable host defense by prokaryotic cells against phage and other foreign DNA; Very large protein containing McrA/HNH-nuclease related domain and a RuvC-like nuclease domain; signature gene for type II


Pssm-ID: 187774 [Multi-domain]  Cd Length: 799  Bit Score: 38.17  E-value: 4.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 735999655  16 NHACRYCGRSAP------EVKLTIDHVVPESLGGPDDPSNLVAACADCNGGKS 62
Cdd:cd09643  577 NGKCMYTGKEIDiddlfdLSYYEIDHILPQSRSFDDSISNKVLVLASENQEKG 629
 
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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