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Conserved domains on  [gi|71998960|ref|NP_001022536|]
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C4H2-type domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-C4H2 super family cl24228
Zinc finger-containing protein; This is a family of proteins which appears to have a highly ...
 4-194 3.74e-35

Zinc finger-containing protein; This is a family of proteins which appears to have a highly conserved zinc finger domain at the C terminal end, described as -C-X2-CH-X3-H-X5-C-X2-C-. The structure is predicted to contain a coiled coil. Members are annotated as being tumour-associated antigen HCA127 in humans but this could not confirmed.


The actual alignment was detected with superfamily member pfam10146:

Pssm-ID: 462963 [Multi-domain]  Cd Length: 213  Bit Score: 122.87  E-value: 3.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998960     4 RTKVDDYFAKRNELLEELSELENTEKFIKETAKTIDELNKEKEEHSEIIQLINQDKSDLEREIAAAETEKKDRESKIVKR 83
Cdd:pfam10146   6 RHKTAQLEKLKERLLKELEAHENEEKCLKEYKKEMELLLQEKMAHVEELRLIHADINKMEKVIKEAEEERNRVLEGAVRL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998960    84 YEALLKLIESTNEKLKE-TGCD----IALSQDDLPQTHL--------KIEPPAAPVTPVLSGGLPSPFPNfnfrnlfqpm 150
Cdd:pfam10146  86 HEEYIPLKLEIDRMRRElLGLEelplLHEEEEDLIQTTIfekqytswPPTPSVPPVPPDPPGGLPSPGPP---------- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 71998960   151 lleqlgsfstnsptpqfrPPPHMAAAMQHHQlKVTDHQSPPMKV 194
Cdd:pfam10146 156 ------------------APLQTLAAFRAMQ-PSGSQQPPPMKA 180
 
Name Accession Description Interval E-value
zf-C4H2 pfam10146
Zinc finger-containing protein; This is a family of proteins which appears to have a highly ...
 4-194 3.74e-35

Zinc finger-containing protein; This is a family of proteins which appears to have a highly conserved zinc finger domain at the C terminal end, described as -C-X2-CH-X3-H-X5-C-X2-C-. The structure is predicted to contain a coiled coil. Members are annotated as being tumour-associated antigen HCA127 in humans but this could not confirmed.


Pssm-ID: 462963 [Multi-domain]  Cd Length: 213  Bit Score: 122.87  E-value: 3.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998960     4 RTKVDDYFAKRNELLEELSELENTEKFIKETAKTIDELNKEKEEHSEIIQLINQDKSDLEREIAAAETEKKDRESKIVKR 83
Cdd:pfam10146   6 RHKTAQLEKLKERLLKELEAHENEEKCLKEYKKEMELLLQEKMAHVEELRLIHADINKMEKVIKEAEEERNRVLEGAVRL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998960    84 YEALLKLIESTNEKLKE-TGCD----IALSQDDLPQTHL--------KIEPPAAPVTPVLSGGLPSPFPNfnfrnlfqpm 150
Cdd:pfam10146  86 HEEYIPLKLEIDRMRRElLGLEelplLHEEEEDLIQTTIfekqytswPPTPSVPPVPPDPPGGLPSPGPP---------- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 71998960   151 lleqlgsfstnsptpqfrPPPHMAAAMQHHQlKVTDHQSPPMKV 194
Cdd:pfam10146 156 ------------------APLQTLAAFRAMQ-PSGSQQPPPMKA 180
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 26-87 3.49e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 3.49e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71998960  26 NTEKFIKETAKTIDELNKEKEEHSEIIQLINQDKSDLEREIAAAETEKKDRESKIVKRYEAL 87
Cdd:COG3883  27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
32-112 5.20e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 5.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998960   32 KETAKTIDELNKEKEEHSEIIQLINQDKSDLEREIAAAETEKKDRESKIVKRYEALLKLIESTNEKLKETGCD------I 105
Cdd:PRK02224 233 RETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeaV 312


                 ....*..
gi 71998960  106 ALSQDDL 112
Cdd:PRK02224 313 EARREEL 319
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 31-120 3.62e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 37.74  E-value: 3.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998960     31 IKETAKTIDELNKEKE--EHSEIIQLINQD----------------KSDLEREIAAAETEKKDRESKI---VKRYEALLK 89
Cdd:TIGR02169  193 IDEKRQQLERLRREREkaERYQALLKEKREyegyellkekealerqKEAIERQLASLEEELEKLTEEIselEKRLEEIEQ 272

                           90       100       110
                   ....*....|....*....|....*....|..
gi 71998960     90 LIESTNEKLKETGCDIALS-QDDLPQTHLKIE 120
Cdd:TIGR02169  273 LLEELNKKIKDLGEEEQLRvKEKIGELEAEIA 304
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 27-93 3.64e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 37.30  E-value: 3.64e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998960     27 TEKFIKETAKTIDELNKEKEEHSEIIQLINQDKSDLEREIAAAETEKKDR---ESKIVKRYEALLKLIES 93
Cdd:smart00787 216 LLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgfTFKEIEKLKEQLKLLQS 285
 
Name Accession Description Interval E-value
zf-C4H2 pfam10146
Zinc finger-containing protein; This is a family of proteins which appears to have a highly ...
 4-194 3.74e-35

Zinc finger-containing protein; This is a family of proteins which appears to have a highly conserved zinc finger domain at the C terminal end, described as -C-X2-CH-X3-H-X5-C-X2-C-. The structure is predicted to contain a coiled coil. Members are annotated as being tumour-associated antigen HCA127 in humans but this could not confirmed.


Pssm-ID: 462963 [Multi-domain]  Cd Length: 213  Bit Score: 122.87  E-value: 3.74e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998960     4 RTKVDDYFAKRNELLEELSELENTEKFIKETAKTIDELNKEKEEHSEIIQLINQDKSDLEREIAAAETEKKDRESKIVKR 83
Cdd:pfam10146   6 RHKTAQLEKLKERLLKELEAHENEEKCLKEYKKEMELLLQEKMAHVEELRLIHADINKMEKVIKEAEEERNRVLEGAVRL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998960    84 YEALLKLIESTNEKLKE-TGCD----IALSQDDLPQTHL--------KIEPPAAPVTPVLSGGLPSPFPNfnfrnlfqpm 150
Cdd:pfam10146  86 HEEYIPLKLEIDRMRRElLGLEelplLHEEEEDLIQTTIfekqytswPPTPSVPPVPPDPPGGLPSPGPP---------- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 71998960   151 lleqlgsfstnsptpqfrPPPHMAAAMQHHQlKVTDHQSPPMKV 194
Cdd:pfam10146 156 ------------------APLQTLAAFRAMQ-PSGSQQPPPMKA 180
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 26-87 3.49e-04

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 40.58  E-value: 3.49e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71998960  26 NTEKFIKETAKTIDELNKEKEEHSEIIQLINQDKSDLEREIAAAETEKKDRESKIVKRYEAL 87
Cdd:COG3883  27 ELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL 88
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 28-96 4.05e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 39.91  E-value: 4.05e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71998960  28 EKFIKETAKTIDELNKEKEEHSEIIQLINQDKSDLEREIAAAETEKKDRESKIvKRYEALLKLIESTNE 96
Cdd:COG1579  23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI-KKYEEQLGNVRNNKE 90
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
32-112 5.20e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 5.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998960   32 KETAKTIDELNKEKEEHSEIIQLINQDKSDLEREIAAAETEKKDRESKIVKRYEALLKLIESTNEKLKETGCD------I 105
Cdd:PRK02224 233 RETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDdadaeaV 312


                 ....*..
gi 71998960  106 ALSQDDL 112
Cdd:PRK02224 313 EARREEL 319
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
31-100 2.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 37.74  E-value: 2.96e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998960   31 IKETAKTIDELNKEKEEHSEIIQLINQDKSDLEREIAAAETEKKDRESKiVKRYEALLKLIESTNEKLKE 100
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEK-EERLEELKKKLKELEKRLEE 356
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 31-120 3.62e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 37.74  E-value: 3.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998960     31 IKETAKTIDELNKEKE--EHSEIIQLINQD----------------KSDLEREIAAAETEKKDRESKI---VKRYEALLK 89
Cdd:TIGR02169  193 IDEKRQQLERLRREREkaERYQALLKEKREyegyellkekealerqKEAIERQLASLEEELEKLTEEIselEKRLEEIEQ 272

                           90       100       110
                   ....*....|....*....|....*....|..
gi 71998960     90 LIESTNEKLKETGCDIALS-QDDLPQTHLKIE 120
Cdd:TIGR02169  273 LLEELNKKIKDLGEEEQLRvKEKIGELEAEIA 304
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 27-93 3.64e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 37.30  E-value: 3.64e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71998960     27 TEKFIKETAKTIDELNKEKEEHSEIIQLINQDKSDLEREIAAAETEKKDR---ESKIVKRYEALLKLIES 93
Cdd:smart00787 216 LLQEIMIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCrgfTFKEIEKLKEQLKLLQS 285
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
31-92 6.98e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 36.82  E-value: 6.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71998960   31 IKETAKTIDELNKEKEEHSEIIQLI-NQDKSDLEREIAAAETEKKDRESKiVKRYEALLKLIE 92
Cdd:COG4913  311 LERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERR-RARLEALLAALG 372
 
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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