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Conserved domains on  [gi|1958791414|ref|XP_038935837|]
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zinc finger CCCH domain-containing protein 10 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ZnF_C3H1 smart00356
zinc finger;
134-158 2.32e-04

zinc finger;


:

Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 37.99  E-value: 2.32e-04
                           10        20
                   ....*....|....*....|....*
gi 1958791414  134 KEEVPICRDFLKGDCQRGTKCKFRH 158
Cdd:smart00356   1 KYKTELCKFFKRGYCPRGDRCKFAH 25
ZnF_C3H1 smart00356
zinc finger;
40-62 3.57e-04

zinc finger;


:

Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 37.61  E-value: 3.57e-04
                           10        20
                   ....*....|....*....|...
gi 1958791414   40 AICRDFLRNVCKRGKRCRYRHPD 62
Cdd:smart00356   5 ELCKFFKRGYCPRGDRCKFAHPL 27
SPATA1_C super family cl23812
Spermatogenesis-associated C-terminus; This domain family is found in eukaryotes, and is ...
243-294 2.58e-03

Spermatogenesis-associated C-terminus; This domain family is found in eukaryotes, and is approximately 150 amino acids in length. There is a single completely conserved residue E that may be functionally important.


The actual alignment was detected with superfamily member pfam15743:

Pssm-ID: 464839 [Multi-domain]  Cd Length: 150  Bit Score: 38.13  E-value: 2.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791414 243 EENALLRKRVEELKKQVSNLLATNEVLLEQNAQFRNQAKVM-------TLSSTAPATEQ 294
Cdd:pfam15743   1 EEIKLVKEERKQLEKTRQELLRKAKTLLAQNRHKRNQARDIwkkkyfeTKKKTAPLEEV 59
 
Name Accession Description Interval E-value
ZnF_C3H1 smart00356
zinc finger;
134-158 2.32e-04

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 37.99  E-value: 2.32e-04
                           10        20
                   ....*....|....*....|....*
gi 1958791414  134 KEEVPICRDFLKGDCQRGTKCKFRH 158
Cdd:smart00356   1 KYKTELCKFFKRGYCPRGDRCKFAH 25
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
140-158 2.66e-04

Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.


Pssm-ID: 465719 [Multi-domain]  Cd Length: 19  Bit Score: 37.78  E-value: 2.66e-04
                          10
                  ....*....|....*....
gi 1958791414 140 CRDFLKGDCQRGTKCKFRH 158
Cdd:pfam18345   1 CKFFLKGRCRYGDKCRFAH 19
ZnF_C3H1 smart00356
zinc finger;
40-62 3.57e-04

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 37.61  E-value: 3.57e-04
                           10        20
                   ....*....|....*....|...
gi 1958791414   40 AICRDFLRNVCKRGKRCRYRHPD 62
Cdd:smart00356   5 ELCKFFKRGYCPRGDRCKFAHPL 27
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
42-60 1.34e-03

Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.


Pssm-ID: 465719 [Multi-domain]  Cd Length: 19  Bit Score: 35.86  E-value: 1.34e-03
                          10
                  ....*....|....*....
gi 1958791414  42 CRDFLRNVCKRGKRCRYRH 60
Cdd:pfam18345   1 CKFFLKGRCRYGDKCRFAH 19
SPATA1_C pfam15743
Spermatogenesis-associated C-terminus; This domain family is found in eukaryotes, and is ...
243-294 2.58e-03

Spermatogenesis-associated C-terminus; This domain family is found in eukaryotes, and is approximately 150 amino acids in length. There is a single completely conserved residue E that may be functionally important.


Pssm-ID: 464839 [Multi-domain]  Cd Length: 150  Bit Score: 38.13  E-value: 2.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791414 243 EENALLRKRVEELKKQVSNLLATNEVLLEQNAQFRNQAKVM-------TLSSTAPATEQ 294
Cdd:pfam15743   1 EEIKLVKEERKQLEKTRQELLRKAKTLLAQNRHKRNQARDIwkkkyfeTKKKTAPLEEV 59
 
Name Accession Description Interval E-value
ZnF_C3H1 smart00356
zinc finger;
134-158 2.32e-04

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 37.99  E-value: 2.32e-04
                           10        20
                   ....*....|....*....|....*
gi 1958791414  134 KEEVPICRDFLKGDCQRGTKCKFRH 158
Cdd:smart00356   1 KYKTELCKFFKRGYCPRGDRCKFAH 25
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
140-158 2.66e-04

Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.


Pssm-ID: 465719 [Multi-domain]  Cd Length: 19  Bit Score: 37.78  E-value: 2.66e-04
                          10
                  ....*....|....*....
gi 1958791414 140 CRDFLKGDCQRGTKCKFRH 158
Cdd:pfam18345   1 CKFFLKGRCRYGDKCRFAH 19
ZnF_C3H1 smart00356
zinc finger;
40-62 3.57e-04

zinc finger;


Pssm-ID: 214632 [Multi-domain]  Cd Length: 27  Bit Score: 37.61  E-value: 3.57e-04
                           10        20
                   ....*....|....*....|...
gi 1958791414   40 AICRDFLRNVCKRGKRCRYRHPD 62
Cdd:smart00356   5 ELCKFFKRGYCPRGDRCKFAHPL 27
zf_CCCH_4 pfam18345
Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch ...
42-60 1.34e-03

Zinc finger domain; This is a zinc finger domain found in Zinc finger CCCH-type with G patch domain-containing proteins such as ZIP. Functional studies indicate that ZIP specifically targets EGFR and represses its transcription, and that the zinc finger and the coiled-coil domains are central to that process.


Pssm-ID: 465719 [Multi-domain]  Cd Length: 19  Bit Score: 35.86  E-value: 1.34e-03
                          10
                  ....*....|....*....
gi 1958791414  42 CRDFLRNVCKRGKRCRYRH 60
Cdd:pfam18345   1 CKFFLKGRCRYGDKCRFAH 19
SPATA1_C pfam15743
Spermatogenesis-associated C-terminus; This domain family is found in eukaryotes, and is ...
243-294 2.58e-03

Spermatogenesis-associated C-terminus; This domain family is found in eukaryotes, and is approximately 150 amino acids in length. There is a single completely conserved residue E that may be functionally important.


Pssm-ID: 464839 [Multi-domain]  Cd Length: 150  Bit Score: 38.13  E-value: 2.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958791414 243 EENALLRKRVEELKKQVSNLLATNEVLLEQNAQFRNQAKVM-------TLSSTAPATEQ 294
Cdd:pfam15743   1 EEIKLVKEERKQLEKTRQELLRKAKTLLAQNRHKRNQARDIwkkkyfeTKKKTAPLEEV 59
zf-CCCH pfam00642
Zinc finger C-x8-C-x5-C-x3-H type (and similar);
138-160 7.93e-03

Zinc finger C-x8-C-x5-C-x3-H type (and similar);


Pssm-ID: 459885 [Multi-domain]  Cd Length: 27  Bit Score: 33.71  E-value: 7.93e-03
                          10        20
                  ....*....|....*....|....
gi 1958791414 138 PICRDFLK-GDCQRGTKCKFRHLQ 160
Cdd:pfam00642   4 ELCRFFLRtGYCKYGDRCKFAHGQ 27
 
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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