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CAF1H_ARATH
ID   CAF1H_ARATH             Reviewed;         239 AA.
AC   Q9LXM4;
DT   05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Putative CCR4-associated factor 1 homolog 8;
DE            EC=3.1.13.4;
GN   Name=CAF1-8; OrderedLocusNames=At3g44240; ORFNames=T10D17_30;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA   Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA   Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA   Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA   Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA   Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA   Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA   Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA   Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA   Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA   Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA   Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA   Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA   Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA   Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA   Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA   Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA   Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA   Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
CC   -!- FUNCTION: Ubiquitous transcription factor required for a diverse set of
CC       processes. It is a component of the CCR4 complex involved in the
CC       control of gene expression (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exonucleolytic cleavage of poly(A) to 5'-AMP.; EC=3.1.13.4;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC   -!- SUBUNIT: Component of the CCR4-NOT complex, at least composed of CRR4
CC       and CAF1 proteins. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CAF1 family. {ECO:0000305}.
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DR   EMBL; AL353865; CAB88992.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77880.1; -; Genomic_DNA.
DR   PIR; T49140; T49140.
DR   RefSeq; NP_190010.1; NM_114292.1.
DR   AlphaFoldDB; Q9LXM4; -.
DR   SMR; Q9LXM4; -.
DR   STRING; 3702.AT3G44240.1; -.
DR   PaxDb; Q9LXM4; -.
DR   PRIDE; Q9LXM4; -.
DR   ProteomicsDB; 223865; -.
DR   DNASU; 823549; -.
DR   EnsemblPlants; AT3G44240.1; AT3G44240.1; AT3G44240.
DR   GeneID; 823549; -.
DR   Gramene; AT3G44240.1; AT3G44240.1; AT3G44240.
DR   KEGG; ath:AT3G44240; -.
DR   Araport; AT3G44240; -.
DR   TAIR; locus:2095705; AT3G44240.
DR   eggNOG; KOG0304; Eukaryota.
DR   HOGENOM; CLU_027974_1_3_1; -.
DR   InParanoid; Q9LXM4; -.
DR   OMA; QVFMRMT; -.
DR   OrthoDB; 931256at2759; -.
DR   PhylomeDB; Q9LXM4; -.
DR   PRO; PR:Q9LXM4; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9LXM4; baseline and differential.
DR   Genevisible; Q9LXM4; AT.
DR   GO; GO:0030015; C:CCR4-NOT core complex; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0000932; C:P-body; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004535; F:poly(A)-specific ribonuclease activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0043928; P:exonucleolytic catabolism of deadenylated mRNA; IBA:GO_Central.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR039637; CNOT7/CNOT8/Pop2.
DR   InterPro; IPR006941; RNase_CAF1.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR10797; PTHR10797; 1.
DR   Pfam; PF04857; CAF1; 2.
DR   SUPFAM; SSF53098; SSF53098; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Exonuclease; Hydrolase; Metal-binding; Nuclease; Nucleus;
KW   Reference proteome; RNA-binding; Transcription; Transcription regulation.
FT   CHAIN           1..239
FT                   /note="Putative CCR4-associated factor 1 homolog 8"
FT                   /id="PRO_0000371558"
FT   BINDING         17
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         19
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         133
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         204
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   239 AA;  27213 MW;  25EACF76A0AF6DAE CRC64;
     MSLIEDCLRS YRFIAIDTEF PSTLRETTQH ATDEERYMDM SFSVDRAKLI QLGLTLFDIN
     GRIGGTWEIN FSDFGVDDAR NEKSIEFLRR NGLDLRKIRE EGIRIEGFFS EMFWMLKKTR
     RNITWVTFHG SYDIAYLLKG FTGEALPVTS ERFSKAVARV LGSVYDLKVM AGRCEGLSSR
     LGLETLAHEF GLNRVGTAHH AGSNNELTAM VFAKVLSPFP LFLRFGSLEL RTIESEAIV
 
 
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