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XB33_ARATH
ID   XB33_ARATH              Reviewed;         513 AA.
AC   Q4FE45; Q9LYN9;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   30-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=E3 ubiquitin-protein ligase XBAT33;
DE            EC=2.3.2.27;
DE   AltName: Full=Ankyrin repeat domain and RING finger-containing protein XBAT33;
DE   AltName: Full=Protein XB3 homolog 3;
DE   AltName: Full=RING-type E3 ubiquitin transferase XBAT33;
GN   Name=XBAT33; OrderedLocusNames=At5g07270; ORFNames=T28J14.210;
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 [MRNA], AND FUNCTION.
RC   STRAIN=cv. Columbia; TISSUE=Seedling;
RX   PubMed=15644464; DOI=10.1104/pp.104.052423;
RA   Stone S.L., Hauksdottir H., Troy A., Herschleb J., Kraft E., Callis J.;
RT   "Functional analysis of the RING-type ubiquitin ligase family of
RT   Arabidopsis.";
RL   Plant Physiol. 137:13-30(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=11130714; DOI=10.1038/35048507;
RA   Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA   Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA   Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA   Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA   Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA   O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA   Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA   Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA   Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA   Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA   Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA   Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA   Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA   Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA   Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA   Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA   McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA   Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA   Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA   Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA   Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA   Bevan M., Fransz P.F.;
RT   "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL   Nature 408:823-826(2000).
RN   [3]
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).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Bautista V.R., Kim C.J., Chen H., Quinitio C., Ecker J.R.;
RT   "Arabidopsis ORF Clones.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Possesses E3 ubiquitin-protein ligase activity when
CC       associated with the E2 enzyme UBC8 in vitro.
CC       {ECO:0000269|PubMed:15644464}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27;
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB87283.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; DQ086846; AAZ14070.1; -; mRNA.
DR   EMBL; AL163652; CAB87283.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002688; AED91131.1; -; Genomic_DNA.
DR   EMBL; BT029297; ABK32111.1; -; mRNA.
DR   PIR; T48498; T48498.
DR   RefSeq; NP_196344.2; NM_120809.5.
DR   AlphaFoldDB; Q4FE45; -.
DR   SMR; Q4FE45; -.
DR   STRING; 3702.AT5G07270.1; -.
DR   iPTMnet; Q4FE45; -.
DR   PaxDb; Q4FE45; -.
DR   PRIDE; Q4FE45; -.
DR   ProteomicsDB; 242454; -.
DR   EnsemblPlants; AT5G07270.1; AT5G07270.1; AT5G07270.
DR   GeneID; 830618; -.
DR   Gramene; AT5G07270.1; AT5G07270.1; AT5G07270.
DR   KEGG; ath:AT5G07270; -.
DR   Araport; AT5G07270; -.
DR   TAIR; locus:2182860; AT5G07270.
DR   eggNOG; ENOG502QR1Y; Eukaryota.
DR   HOGENOM; CLU_035461_0_0_1; -.
DR   InParanoid; Q4FE45; -.
DR   OMA; EFNPCLA; -.
DR   OrthoDB; 432910at2759; -.
DR   PhylomeDB; Q4FE45; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q4FE45; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q4FE45; baseline and differential.
DR   Genevisible; Q4FE45; AT.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB.
DR   Gene3D; 1.25.40.20; -; 2.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   Pfam; PF00023; Ank; 2.
DR   Pfam; PF12796; Ank_2; 1.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   ANK repeat; Metal-binding; Reference proteome; Repeat; Transferase;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN           1..513
FT                   /note="E3 ubiquitin-protein ligase XBAT33"
FT                   /id="PRO_0000395741"
FT   REPEAT          44..73
FT                   /note="ANK 1"
FT   REPEAT          77..106
FT                   /note="ANK 2"
FT   REPEAT          111..140
FT                   /note="ANK 3"
FT   REPEAT          171..200
FT                   /note="ANK 4"
FT   REPEAT          214..244
FT                   /note="ANK 5"
FT   ZN_FING         312..362
FT                   /note="RING-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT   REGION          397..417
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          455..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   513 AA;  55347 MW;  19785AABFC6C853D CRC64;
     MGNSFGCSAS GERLVSAARD GDFVEAKMLL DCNPCLAKYS TFGGLNSPLH FAAAKGHNEI
     VGLLLENGAD VNSRNYCGQT ALMQACRYGH WEVVQTLLLF RCNVTRADYL AGRTALHFAA
     VNGHARCIRL VLADFLPSDK LNSLPETGVV TAKNKSEQSA LSKFVNKAAD GGITALHMAA
     LNGLFDCVQL LLDLEANVSA VTFHYGTSMD MIGAGSTPLH YAACGGNLKC CQILLARGAR
     KMTLNCNGWL PIDIARMWSR HWLEPLLSPN SDVVIPAFPH SNYLSLPLLS ILNIAREFGL
     QSATIGDEVD ICAVCLERTC TVAAEGCEHQ LCVRCALYLC SSSNVPSVTV GPPGSIPCPL
     CRHGITAFKR LPSSLTREMK LPMSLGFCAP CMLHTGDTTD QSSPTCPPTE QRSSKTRAAS
     VSSDIFCPVT CSPFPSVNIP MCTCNEGTCP NFETHGTERH SEEHVESSPS RTTTEQEKIE
     EGQRLGKTTT CSSMFWGRRS CSRENQCNSE INA
 
 
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