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Conserved domains on  [gi|74197215|dbj|BAE35151|]
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unnamed protein product [Mus musculus]

Protein Classification

C2H2-type zinc finger protein( domain architecture ID 10533256)

Cys2His2 (C2H2)-type zinc finger protein may be involved in transcriptional regulation, similar to U1 small nuclear ribonucleoprotein C that is a component of the spliceosomal U1 snRNP

CATH:  3.30.160.60
Gene Ontology:  GO:0008270|GO:0003676
PubMed:  11179890|12665246|11361095|10940247|22803940
SCOP:  4003583

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
zf-U1 pfam06220
U1 zinc finger; This family consists of several U1 small nuclear ribonucleoprotein C (U1-C) ...
 8-44 2.86e-12

U1 zinc finger; This family consists of several U1 small nuclear ribonucleoprotein C (U1-C) proteins. The U1 small nuclear ribonucleoprotein (U1 snRNP) binds to the pre-mRNA 5' splice site (ss) at early stages of spliceosome assembly. Recruitment of U1 to a class of weak 5' ss is promoted by binding of the protein TIA-1 to uridine-rich sequences immediately downstream from the 5' ss. Binding of TIA-1 in the vicinity of a 5' ss helps to stabilize U1 snRNP recruitment, at least in part, via a direct interaction with U1-C, thus providing one molecular mechanism for the function of this splicing regulator. This domain is probably a zinc-binding. It is found in multiple copies in some members of the family.


:

Pssm-ID: 368798  Cd Length: 38  Bit Score: 60.53  E-value: 2.86e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 74197215     8 QPKKFGDYCKCWIADNRPSV-EFHERGKNHKENVARRI 44
Cdd:pfam06220   1 MPKYYCDYCDCYLTHDSPSVrKSHNGGRKHKDNVKDYY 38
PRP40 super family cl34905
Splicing factor [RNA processing and modification];
129-195 4.75e-10

Splicing factor [RNA processing and modification];


The actual alignment was detected with superfamily member COG5104:

Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 60.86  E-value: 4.75e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74197215 129 WVEGVTADGHCYYYDLITGASQWEKPEGFQGNLKKTAAKAVWVEGLSEDGYTYYYNTETGESKWEKP 195
Cdd:COG5104  17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIP 83
 
Name Accession Description Interval E-value
zf-U1 pfam06220
U1 zinc finger; This family consists of several U1 small nuclear ribonucleoprotein C (U1-C) ...
 8-44 2.86e-12

U1 zinc finger; This family consists of several U1 small nuclear ribonucleoprotein C (U1-C) proteins. The U1 small nuclear ribonucleoprotein (U1 snRNP) binds to the pre-mRNA 5' splice site (ss) at early stages of spliceosome assembly. Recruitment of U1 to a class of weak 5' ss is promoted by binding of the protein TIA-1 to uridine-rich sequences immediately downstream from the 5' ss. Binding of TIA-1 in the vicinity of a 5' ss helps to stabilize U1 snRNP recruitment, at least in part, via a direct interaction with U1-C, thus providing one molecular mechanism for the function of this splicing regulator. This domain is probably a zinc-binding. It is found in multiple copies in some members of the family.


Pssm-ID: 368798  Cd Length: 38  Bit Score: 60.53  E-value: 2.86e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 74197215     8 QPKKFGDYCKCWIADNRPSV-EFHERGKNHKENVARRI 44
Cdd:pfam06220   1 MPKYYCDYCDCYLTHDSPSVrKSHNGGRKHKDNVKDYY 38
PRP40 COG5104
Splicing factor [RNA processing and modification];
129-195 4.75e-10

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 60.86  E-value: 4.75e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74197215 129 WVEGVTADGHCYYYDLITGASQWEKPEGFQGNLKKTAAKAVWVEGLSEDGYTYYYNTETGESKWEKP 195
Cdd:COG5104  17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIP 83
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 170-195 2.29e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 49.43  E-value: 2.29e-08
                          10        20
                  ....*....|....*....|....*.
gi 74197215   170 WVEGLSEDGYTYYYNTETGESKWEKP 195
Cdd:pfam00397   5 WEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 170-197 8.66e-08

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 47.52  E-value: 8.66e-08
                        10        20
                ....*....|....*....|....*...
gi 74197215 170 WVEGLSEDGYTYYYNTETGESKWEKPED 197
Cdd:cd00201   4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 170-197 2.31e-07

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 46.44  E-value: 2.31e-07
                           10        20
                   ....*....|....*....|....*...
gi 74197215    170 WVEGLSEDGYTYYYNTETGESKWEKPED 197
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 8-43 6.40e-06

U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.


Pssm-ID: 197732 [Multi-domain]  Cd Length: 35  Bit Score: 42.62  E-value: 6.40e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 74197215      8 QPKKFGDYCKCWIADNrPSVEFHERGKNHKENVARR 43
Cdd:smart00451   1 TGGFYCKLCNVTFTDE-ISVEAHLKGKKHKKNVKKR 35
 
Name Accession Description Interval E-value
zf-U1 pfam06220
U1 zinc finger; This family consists of several U1 small nuclear ribonucleoprotein C (U1-C) ...
 8-44 2.86e-12

U1 zinc finger; This family consists of several U1 small nuclear ribonucleoprotein C (U1-C) proteins. The U1 small nuclear ribonucleoprotein (U1 snRNP) binds to the pre-mRNA 5' splice site (ss) at early stages of spliceosome assembly. Recruitment of U1 to a class of weak 5' ss is promoted by binding of the protein TIA-1 to uridine-rich sequences immediately downstream from the 5' ss. Binding of TIA-1 in the vicinity of a 5' ss helps to stabilize U1 snRNP recruitment, at least in part, via a direct interaction with U1-C, thus providing one molecular mechanism for the function of this splicing regulator. This domain is probably a zinc-binding. It is found in multiple copies in some members of the family.


Pssm-ID: 368798  Cd Length: 38  Bit Score: 60.53  E-value: 2.86e-12
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 74197215     8 QPKKFGDYCKCWIADNRPSV-EFHERGKNHKENVARRI 44
Cdd:pfam06220   1 MPKYYCDYCDCYLTHDSPSVrKSHNGGRKHKDNVKDYY 38
PRP40 COG5104
Splicing factor [RNA processing and modification];
129-195 4.75e-10

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 60.86  E-value: 4.75e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74197215 129 WVEGVTADGHCYYYDLITGASQWEKPEGFQGNLKKTAAKAVWVEGLSEDGYTYYYNTETGESKWEKP 195
Cdd:COG5104  17 WEELKAPDGRIYYYNKRTGKSSWEKPKELLKGSEEDLDVDPWKECRTADGKVYYYNSITRESRWKIP 83
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 170-195 2.29e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 49.43  E-value: 2.29e-08
                          10        20
                  ....*....|....*....|....*.
gi 74197215   170 WVEGLSEDGYTYYYNTETGESKWEKP 195
Cdd:pfam00397   5 WEERWDPDGRVYYYNHETGETQWEKP 30
WW pfam00397
WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds ...
 128-154 6.92e-08

WW domain; The WW domain is a protein module with two highly conserved tryptophans that binds proline-rich peptide motifs in vitro.


Pssm-ID: 459800 [Multi-domain]  Cd Length: 30  Bit Score: 47.88  E-value: 6.92e-08
                          10        20
                  ....*....|....*....|....*..
gi 74197215   128 GWVEGVTADGHCYYYDLITGASQWEKP 154
Cdd:pfam00397   4 GWEERWDPDGRVYYYNHETGETQWEKP 30
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 170-197 8.66e-08

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 47.52  E-value: 8.66e-08
                        10        20
                ....*....|....*....|....*...
gi 74197215 170 WVEGLSEDGYTYYYNTETGESKWEKPED 197
Cdd:cd00201   4 WEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW cd00201
Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; ...
 126-156 1.44e-07

Two conserved tryptophans domain; also known as the WWP or rsp5 domain; around 40 amino acids; functions as an interaction module in a diverse set of signalling proteins; binds specific proline-rich sequences but at low affinities compared to other peptide recognition proteins such as antibodies and receptors; WW domains have a single groove formed by a conserved Trp and Tyr which recognizes a pair of residues of the sequence X-Pro; variable loops and neighboring domains confer specificity in this domain; there are five distinct groups based on binding: 1) PPXY motifs 2) the PPLP motif; 3) PGM motifs; 4) PSP or PTP motifs; 5) PR motifs.


Pssm-ID: 238122 [Multi-domain]  Cd Length: 31  Bit Score: 47.14  E-value: 1.44e-07
                        10        20        30
                ....*....|....*....|....*....|.
gi 74197215 126 KGGWVEGVTADGHCYYYDLITGASQWEKPEG 156
Cdd:cd00201   1 PPGWEERWDPDGRVYYYNHNTKETQWEDPRE 31
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 170-197 2.31e-07

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 46.44  E-value: 2.31e-07
                           10        20
                   ....*....|....*....|....*...
gi 74197215    170 WVEGLSEDGYTYYYNTETGESKWEKPED 197
Cdd:smart00456   6 WEERKDPDGRPYYYNHETKETQWEKPRE 33
WW smart00456
Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds ...
 125-156 3.48e-07

Domain with 2 conserved Trp (W) residues; Also known as the WWP or rsp5 domain. Binds proline-rich polypeptides.


Pssm-ID: 197736 [Multi-domain]  Cd Length: 33  Bit Score: 46.05  E-value: 3.48e-07
                           10        20        30
                   ....*....|....*....|....*....|..
gi 74197215    125 SKGGWVEGVTADGHCYYYDLITGASQWEKPEG 156
Cdd:smart00456   2 LPPGWEERKDPDGRPYYYNHETKETQWEKPRE 33
ZnF_U1 smart00451
U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ...
 8-43 6.40e-06

U1-like zinc finger; Family of C2H2-type zinc fingers, present in matrin, U1 small nuclear ribonucleoprotein C and other RNA-binding proteins.


Pssm-ID: 197732 [Multi-domain]  Cd Length: 35  Bit Score: 42.62  E-value: 6.40e-06
                           10        20        30
                   ....*....|....*....|....*....|....*.
gi 74197215      8 QPKKFGDYCKCWIADNrPSVEFHERGKNHKENVARR 43
Cdd:smart00451   1 TGGFYCKLCNVTFTDE-ISVEAHLKGKKHKKNVKKR 35
PRP40 COG5104
Splicing factor [RNA processing and modification];
155-199 9.28e-05

Splicing factor [RNA processing and modification];


Pssm-ID: 227435 [Multi-domain]  Cd Length: 590  Bit Score: 44.30  E-value: 9.28e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 74197215 155 EGFQGNLKKTAAkAVWVEGLSEDGYTYYYNTETGESKWEKPEDFI 199
Cdd:COG5104   3 AALLGMASGEAR-SEWEELKAPDGRIYYYNKRTGKSSWEKPKELL 46
PQQ_DH_like cd00216
PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases ...
 133-203 3.28e-03

PQQ-dependent dehydrogenases and related proteins; This family is composed of dehydrogenases with pyrroloquinoline quinone (PQQ) as a cofactor, such as ethanol, methanol, and membrane-bound glucose dehydrogenases. The alignment model contains an 8-bladed beta-propeller, and the family also includes distantly related proteins which are not enzymatically active and do not bind PQQ.


Pssm-ID: 199833 [Multi-domain]  Cd Length: 434  Bit Score: 39.13  E-value: 3.28e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74197215 133 VTADGHCYYYDLITGASQWEKPEGFQ--GNLKKTAAKAVwVEGlSEDGYTYYYNTETGESKWEKPedfIPHGG 203
Cdd:cd00216 319 VPANGRIMALDPVTGVVVWEKSELHPllGGPLSTAGNLV-FVG-TSDGYLKAYNADTGEKLWQQK---VPSGF 386
 
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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