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Conserved domains on  [gi|1162406012|gb|OPX20715|]
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MAG: phosphohydrolase [Desulfobacca sp. 4484_104]

Protein Classification

HD domain-containing protein( domain architecture ID 10487852)

HD domain-containing protein may function as a metal dependent phosphohydrolase

CATH:  3.30.70.1370
EC:  3.1.-.-
Gene Ontology:  GO:0046872|GO:0042578
PubMed:  9868367
SCOP:  3000943

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
99-202 6.69e-20

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: 84.18  E-value: 6.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012  99 RINHARRVARYAEEIGKNEQANMAVILCAAYLHDIGIKEAERKHQNtaaryHEQEGPPVARQILEQLGARPELIDEVCDI 178
Cdd:COG1418    19 DLQHSLRVAKLAGLIAAEEGADVEVAKRAALLHDIGKAKDHEVEGS-----HAEIGAELARKYLESLGFPEEEIEAVVHA 93
                          90       100
                  ....*....|....*....|....*....
gi 1162406012 179 VRHHH-----QPRPQEAtnfKALYDADLI 202
Cdd:COG1418    94 IEAHSfsggiEPESLEA---KIVQDADRL 119
RPC10 COG1996
DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; ...
20-50 3.83e-04

DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger is part of the Pathway/BioSystem: RNA polymerase


:

Pssm-ID: 441599  Cd Length: 48  Bit Score: 37.37  E-value: 3.83e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1162406012  20 KCPECGGEIEFFKDEPSRRCKNCGHRVLNPK 50
Cdd:COG1996     7 KCPRCGAEVELDEGTPAIRCPYCGSRIFIKE 37
 
Name Accession Description Interval E-value
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
99-202 6.69e-20

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: 84.18  E-value: 6.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012  99 RINHARRVARYAEEIGKNEQANMAVILCAAYLHDIGIKEAERKHQNtaaryHEQEGPPVARQILEQLGARPELIDEVCDI 178
Cdd:COG1418    19 DLQHSLRVAKLAGLIAAEEGADVEVAKRAALLHDIGKAKDHEVEGS-----HAEIGAELARKYLESLGFPEEEIEAVVHA 93
                          90       100
                  ....*....|....*....|....*....
gi 1162406012 179 VRHHH-----QPRPQEAtnfKALYDADLI 202
Cdd:COG1418    94 IEAHSfsggiEPESLEA---KIVQDADRL 119
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
99-183 2.68e-10

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 56.09  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012  99 RINHARRVARYAEEIG-KNEQANMAVILCAAYLHDIG-IKEAERKHQNTAARYHEQEGppvaRQILEQLGaRPELIDEVC 176
Cdd:pfam01966   1 RLEHSLRVALLARELAeELGELDRELLLLAALLHDIGkGPFGDEKPEFEIFLGHAVVG----AEILRELE-KRLGLEDVL 75

                  ....*..
gi 1162406012 177 DIVRHHH 183
Cdd:pfam01966  76 KLILEHH 82
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
99-205 4.28e-10

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: 55.77  E-value: 4.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012   99 RINHARRVARYAEEIGKNE-QANMAVILCAAYLHDIGikEAERKHQNTAARYHEQEGPPVARQILEQLGARPELIDEVCD 177
Cdd:smart00471   5 VFEHSLRVAQLAAALAEELgLLDIELLLLAALLHDIG--KPGTPDSFLVKTSVLEDHHFIGAEILLEEEEPRILEEILRT 82
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1162406012  178 IVRHHH--------QPRPQEAtnfKALYDADLIVNL 205
Cdd:smart00471  83 AILSHHerpdglrgEPITLEA---RIVKVADRLDAL 115
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
99-219 3.27e-09

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 53.88  E-value: 3.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012  99 RINHARRVARYAEEIGKNE---QANMAVILCAAYLHDIGikEAERKHQNTAARY-----HEQEGPPVARQILEQLgARPE 170
Cdd:cd00077     3 RFEHSLRVAQLARRLAEELglsEEDIELLRLAALLHDIG--KPGTPDAITEEESelekdHAIVGAEILRELLLEE-VIKL 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1162406012 171 LIDEVCDIVRHHHQ--------------PRPQEAtnfKALYDADLIVNL-----EEQQEKAPLDRDRL 219
Cdd:cd00077    80 IDELILAVDASHHErldglgypdglkgeEITLEA---RIVKLADRLDALrrdsrEKRRRIAEEDLEEL 144
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
100-184 1.40e-06

HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits.


Pssm-ID: 272994 [Multi-domain]  Cd Length: 80  Bit Score: 45.02  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012 100 INHARRVARYAEEIGKNEQANMAVILCAAYLHDIGiKEAERKHQNTaaRYHEQEGPpvarQILEQLGARPELIDEvcdIV 179
Cdd:TIGR00277   6 LQHSLEVAKLAEALARELGLDVELARRGALLHDIG-KPITREGVIF--ESHVVVGA----EIARKYGEPLEVIDI---IA 75

                  ....*
gi 1162406012 180 RHHHQ 184
Cdd:TIGR00277  76 EHHGK 80
PRK10119 PRK10119
putative hydrolase; Provisional
100-200 7.42e-05

putative hydrolase; Provisional


Pssm-ID: 182251  Cd Length: 231  Bit Score: 42.80  E-value: 7.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012 100 INHARRVARYAEEIGKNEQANMAVILCAAYLHDIG--IKEAERKHQNTAARYHEqegppvARQILEQLGAR--PELIDEV 175
Cdd:PRK10119   27 ICHFRRVWATAQKLAADDDVDMLVVLTACYFHDIVslAKNHPQRHRSSILAAEE------TRRILREDFPDfpAEKIEAV 100
                          90       100       110
                  ....*....|....*....|....*....|
gi 1162406012 176 CDIVRHHH-----QPRPQEAtnfKALYDAD 200
Cdd:PRK10119  101 CHAIEAHSfsaqiAPLTLEA---KIVQDAD 127
RPC10 COG1996
DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; ...
20-50 3.83e-04

DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger is part of the Pathway/BioSystem: RNA polymerase


Pssm-ID: 441599  Cd Length: 48  Bit Score: 37.37  E-value: 3.83e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1162406012  20 KCPECGGEIEFFKDEPSRRCKNCGHRVLNPK 50
Cdd:COG1996     7 KCPRCGAEVELDEGTPAIRCPYCGSRIFIKE 37
 
Name Accession Description Interval E-value
RnaY COG1418
HD superfamily phosphodieaserase, includes HD domain of RNase Y [Translation, ribosomal ...
99-202 6.69e-20

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: 84.18  E-value: 6.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012  99 RINHARRVARYAEEIGKNEQANMAVILCAAYLHDIGIKEAERKHQNtaaryHEQEGPPVARQILEQLGARPELIDEVCDI 178
Cdd:COG1418    19 DLQHSLRVAKLAGLIAAEEGADVEVAKRAALLHDIGKAKDHEVEGS-----HAEIGAELARKYLESLGFPEEEIEAVVHA 93
                          90       100
                  ....*....|....*....|....*....
gi 1162406012 179 VRHHH-----QPRPQEAtnfKALYDADLI 202
Cdd:COG1418    94 IEAHSfsggiEPESLEA---KIVQDADRL 119
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
99-183 2.68e-10

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 56.09  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012  99 RINHARRVARYAEEIG-KNEQANMAVILCAAYLHDIG-IKEAERKHQNTAARYHEQEGppvaRQILEQLGaRPELIDEVC 176
Cdd:pfam01966   1 RLEHSLRVALLARELAeELGELDRELLLLAALLHDIGkGPFGDEKPEFEIFLGHAVVG----AEILRELE-KRLGLEDVL 75

                  ....*..
gi 1162406012 177 DIVRHHH 183
Cdd:pfam01966  76 KLILEHH 82
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
99-205 4.28e-10

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: 55.77  E-value: 4.28e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012   99 RINHARRVARYAEEIGKNE-QANMAVILCAAYLHDIGikEAERKHQNTAARYHEQEGPPVARQILEQLGARPELIDEVCD 177
Cdd:smart00471   5 VFEHSLRVAQLAAALAEELgLLDIELLLLAALLHDIG--KPGTPDSFLVKTSVLEDHHFIGAEILLEEEEPRILEEILRT 82
                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1162406012  178 IVRHHH--------QPRPQEAtnfKALYDADLIVNL 205
Cdd:smart00471  83 AILSHHerpdglrgEPITLEA---RIVKVADRLDAL 115
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
99-219 3.27e-09

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 53.88  E-value: 3.27e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012  99 RINHARRVARYAEEIGKNE---QANMAVILCAAYLHDIGikEAERKHQNTAARY-----HEQEGPPVARQILEQLgARPE 170
Cdd:cd00077     3 RFEHSLRVAQLARRLAEELglsEEDIELLRLAALLHDIG--KPGTPDAITEEESelekdHAIVGAEILRELLLEE-VIKL 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1162406012 171 LIDEVCDIVRHHHQ--------------PRPQEAtnfKALYDADLIVNL-----EEQQEKAPLDRDRL 219
Cdd:cd00077    80 IDELILAVDASHHErldglgypdglkgeEITLEA---RIVKLADRLDALrrdsrEKRRRIAEEDLEEL 144
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
72-183 9.07e-08

HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];


Pssm-ID: 441808 [Multi-domain]  Cd Length: 316  Bit Score: 51.90  E-value: 9.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012  72 ELLAKRDDLLKDRVAIAMKRYFGQDFRRINHARRVARYAEEIGKN---EQANMAVILCAAYLHDIG---IKEA--ERKHQ 143
Cdd:COG2206   117 KLVEELDELLPDALLALLAALDAKDPYTYGHSVRVAVLALALARElglSEEELEDLGLAALLHDIGkigIPDEilNKPGK 196
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1162406012 144 NTAARYHE-QEGPPVARQILEQLGArpelIDEVCDIVRHHH 183
Cdd:COG2206   197 LTDEEFEIiKKHPEYGYEILKKLPG----LSEVAEIVLQHH 233
HDIG TIGR00277
HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number ...
100-184 1.40e-06

HDIG domain; This domain is found in a few known nucleotidyltransferes and in a large number of uncharacterized proteins. It contains four widely separated His residues, the second of which is part of an invariant dipeptide His-Asp in a region matched approximately by the motif HDIG. This model may annotate homologous domains in which one or more of the His residues is conserved but misaligned, and some probable false-positive hits.


Pssm-ID: 272994 [Multi-domain]  Cd Length: 80  Bit Score: 45.02  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012 100 INHARRVARYAEEIGKNEQANMAVILCAAYLHDIGiKEAERKHQNTaaRYHEQEGPpvarQILEQLGARPELIDEvcdIV 179
Cdd:TIGR00277   6 LQHSLEVAKLAEALARELGLDVELARRGALLHDIG-KPITREGVIF--ESHVVVGA----EIARKYGEPLEVIDI---IA 75

                  ....*
gi 1162406012 180 RHHHQ 184
Cdd:TIGR00277  76 EHHGK 80
HDOD pfam08668
HDOD domain;
96-185 9.56e-06

HDOD domain;


Pssm-ID: 430141 [Multi-domain]  Cd Length: 196  Bit Score: 44.91  E-value: 9.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012  96 DFRRI-NHARRVARYAEEIGKneQANMAV---ILCAAYLHDIGI----KEAERKHQNTAARYHEQEGPPVA--RQILE-- 163
Cdd:pfam08668  91 DLKGFwEHSLACALAARLLAR--RLGLDDpeeAFLAGLLHDIGKlillSLLPDKYEELLEKAAEEGISLLEaeRELLGtd 168
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1162406012 164 --QLGAR-------PElidEVCDIVRHHHQP 185
Cdd:pfam08668 169 haEVGAAllerwnlPE---ELVEAIAYHHNP 196
HDOD COG1639
HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];
85-207 3.24e-05

HD-like signal output (HDOD) domain, no enzymatic activity [Signal transduction mechanisms];


Pssm-ID: 441246 [Multi-domain]  Cd Length: 244  Bit Score: 43.80  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012  85 VAIAMKRYF-------GQDFRRI-NHARRVARYAEEIGKN-EQANMAVILCAAYLHDIGI----KEAERKHQNTAARYHE 151
Cdd:COG1639    83 LALALRQLFsaklpayGLDLRRFwRHSLAVAAAARALARRlGLLDPEEAFLAGLLHDIGKlvllSLFPEEYAELLALAEA 162
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1162406012 152 QEGPPVA--RQIL----EQLGAR-------PElidEVCDIVRHHHQPRPQEATNF--KALYDADLIVNLEE 207
Cdd:COG1639   163 DGLSLAEaeREVLgtdhAELGAAlarkwglPE---ELVEAIRYHHDPEAAGEHRRlaALVHLANRLARALG 230
PRK10119 PRK10119
putative hydrolase; Provisional
100-200 7.42e-05

putative hydrolase; Provisional


Pssm-ID: 182251  Cd Length: 231  Bit Score: 42.80  E-value: 7.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012 100 INHARRVARYAEEIGKNEQANMAVILCAAYLHDIG--IKEAERKHQNTAARYHEqegppvARQILEQLGAR--PELIDEV 175
Cdd:PRK10119   27 ICHFRRVWATAQKLAADDDVDMLVVLTACYFHDIVslAKNHPQRHRSSILAAEE------TRRILREDFPDfpAEKIEAV 100
                          90       100       110
                  ....*....|....*....|....*....|
gi 1162406012 176 CDIVRHHH-----QPRPQEAtnfKALYDAD 200
Cdd:PRK10119  101 CHAIEAHSfsaqiAPLTLEA---KIVQDAD 127
RPC10 COG1996
DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; ...
20-50 3.83e-04

DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger [Transcription]; DNA-directed RNA polymerase, subunit RPC12/RpoP, contains C4-type Zn-finger is part of the Pathway/BioSystem: RNA polymerase


Pssm-ID: 441599  Cd Length: 48  Bit Score: 37.37  E-value: 3.83e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1162406012  20 KCPECGGEIEFFKDEPSRRCKNCGHRVLNPK 50
Cdd:COG1996     7 KCPRCGAEVELDEGTPAIRCPYCGSRIFIKE 37
COG3294 COG3294
Metal-dependent phosphatase/phosphodiesterase, HD supefamily [General function prediction only] ...
102-187 1.12e-03

Metal-dependent phosphatase/phosphodiesterase, HD supefamily [General function prediction only];


Pssm-ID: 442523  Cd Length: 259  Bit Score: 39.12  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012 102 HARRVARYAEEI-----------------GKNEQANMAVILCAAYLHDIGikeaerkhqNTAARY-HEQEGPPVARQILE 163
Cdd:COG3294    57 HARIVANRALEIlellkeagvepsgakdgGGYPEDEAELAALAAYLHDIG---------NVVHRDdHEQSGAILAAPILD 127
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1162406012 164 QLGarPELIDEVCD----------IVRHHHQPRP 187
Cdd:COG3294   128 RIL--MDIYDTEKRvrlkaeilhaIGNHDEETEP 159
Cas3''_I cd09641
CRISPR/Cas system-associated protein Cas3''; CRISPR (Clustered Regularly Interspaced Short ...
101-217 1.55e-03

CRISPR/Cas system-associated protein Cas3''; 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; HD-like nuclease, specifically digesting double-stranded oligonucleotides and preferably cleaving at G:C pairs; signature gene for Type I


Pssm-ID: 193608 [Multi-domain]  Cd Length: 200  Bit Score: 38.41  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012 101 NHARRVARYAEEIGKNEQANMAVILCAAYLHDIG---------IKEAERKHQNTAARY--HEQEGPPVARQILEQLGARP 169
Cdd:cd09641    19 WDAELAEEFARKLGLELGLSRELLALAGLLHDLGkatpafqkyLRGGKEALREGKRKEvrHSLLGALLLYELLKELGLDE 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1162406012 170 ELIDEVCDIVRHHHQPRPQEATNFKALYDADLIVNLEEQQEKAPLDRD 217
Cdd:cd09641    99 ELALLLAYAIAGHHGGLPDVLLLLDEDDESALKERLEELDEEKLLLEL 146
nadD PRK07152
nicotinate-nucleotide adenylyltransferase;
96-149 2.51e-03

nicotinate-nucleotide adenylyltransferase;


Pssm-ID: 235947 [Multi-domain]  Cd Length: 342  Bit Score: 38.39  E-value: 2.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1162406012  96 DFRRINHARRVARYAEEIGKNEQANMAVILCAAYLHDIGIKEAERKHQNTAARY 149
Cdd:PRK07152  194 DEYRYKHCLRVAQLAAELAKKNNLDPKKAYYAGLYHDITKEWDEEKHRKFLKKY 247
PRK03381 PRK03381
PII uridylyl-transferase; Provisional
102-182 3.51e-03

PII uridylyl-transferase; Provisional


Pssm-ID: 235123 [Multi-domain]  Cd Length: 774  Bit Score: 38.43  E-value: 3.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012 102 HARRVARyaeeigkneqanMAVILCAAYLHDIGikeaerKHQNTAaryHEQEGPPVARQILEQLGARPELIDEVCDIVRH 181
Cdd:PRK03381  435 LTRRVAR------------PDLLLLGALLHDIG------KGRGGD---HSVVGAELARQIGARLGLSPADVALLSALVRH 493

                  .
gi 1162406012 182 H 182
Cdd:PRK03381  494 H 494
cas3_HD TIGR01596
CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for ...
97-244 7.88e-03

CRISPR-associated endonuclease Cas3-HD; CRISPR/Cas systems are widespread, mobile systems for host defense against invasive elements such as phage. In these systems, Cas3 designates one of the core proteins shared widely by multiple types of CRISPR/Cas system. This model represents an HD-like endonuclease that occurs either separately or as the N-terminal region of Cas3, the helicase-containing CRISPR-associated protein.


Pssm-ID: 273711 [Multi-domain]  Cd Length: 176  Bit Score: 36.03  E-value: 7.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1162406012  97 FRRINHARRvaRYAEEIGKnEQANMAVILCaaYLHDIG---------IKEAERKHQNTAARyHEQEGPPVARQILEQLGA 167
Cdd:TIGR01596  12 AEALPALRP--RLAEKLGL-ELRELLKLAG--LLHDLGkaspafqkkLRKAEERGDRGEVR-HSTLSAALLYDLLEELGL 85
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1162406012 168 RPELIDEVCDIVRHHH--QPRPQEATNFKALYDADLIVNLEEQQEKAPLDRDRLAAKIDKAFLTDSGQALARRVLLKLL 244
Cdd:TIGR01596  86 EEELALLLALAIAGHHggLIDDDDLEELLELLERELEEALGELLEELEELLDEVLKALPLRLLLDKEEPIELYLLARLL 164
 
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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