(data stored in ACNUC13479 zone)

SWISSPROT: ATL49_ARATH

ID   ATL49_ARATH             Reviewed;         423 AA.
AC   Q9ZV53;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   30-AUG-2017, entry version 120.
DE   RecName: Full=Putative RING-H2 finger protein ATL49;
DE            EC=2.3.2.27 {ECO:0000305};
DE   AltName: Full=Protein MATERNAL EFFECT EMBRYO ARREST 16;
DE   AltName: Full=RING-type E3 ubiquitin transferase ATL49 {ECO:0000305};
GN   Name=ATL49; Synonyms=MEE16; OrderedLocusNames=At2g18650;
GN   ORFNames=MSF3.3;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   GENE FAMILY ORGANIZATION.
RX   PubMed=11983057; DOI=10.1186/gb-2002-3-4-research0016;
RA   Kosarev P., Mayer K.F.X., Hardtke C.S.;
RT   "Evaluation and classification of RING-finger domains encoded by the
RT   Arabidopsis genome.";
RL   Genome Biol. 3:RESEARCH0016.1-RESEARCH0016.12(2002).
RN   [4]
RP   FUNCTION.
RX   PubMed=15634699; DOI=10.1242/dev.01595;
RA   Pagnussat G.C., Yu H.-J., Ngo Q.A., Rajani S., Mayalagu S.,
RA   Johnson C.S., Capron A., Xie L.-F., Ye D., Sundaresan V.;
RT   "Genetic and molecular identification of genes required for female
RT   gametophyte development and function in Arabidopsis.";
RL   Development 132:603-614(2005).
RN   [5]
RP   NOMENCLATURE, AND GENE FAMILY ORGANIZATION.
RX   PubMed=16557337; DOI=10.1007/s00239-005-0038-y;
RA   Serrano M., Parra S., Alcaraz L.D., Guzman P.;
RT   "The ATL gene family from Arabidopsis thaliana and Oryza sativa
RT   comprises a large number of putative ubiquitin ligases of the RING-H2
RT   type.";
RL   J. Mol. Evol. 62:434-445(2006).
CC   -!- FUNCTION: May be involved in female gametophyte development.
CC       {ECO:0000269|PubMed:15634699}.
CC   -!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
CC       enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
CC       conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
CC       protein]-L-lysine. {ECO:0000305}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
CC       ubiquitin-conjugating enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RING-type zinc finger family. ATL
CC       subfamily. {ECO:0000305}.
DR   EMBL; AC005724; AAD08934.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC06789.1; -; Genomic_DNA.
DR   PIR; H84566; H84566.
DR   RefSeq; NP_179455.1; NM_127421.2.
DR   UniGene; At.66220; -.
DR   ProteinModelPortal; Q9ZV53; -.
DR   SMR; Q9ZV53; -.
DR   STRING; 3702.AT2G18650.1; -.
DR   iPTMnet; Q9ZV53; -.
DR   PaxDb; Q9ZV53; -.
DR   EnsemblPlants; AT2G18650.1; AT2G18650.1; AT2G18650.
DR   GeneID; 816380; -.
DR   Gramene; AT2G18650.1; AT2G18650.1; AT2G18650.
DR   KEGG; ath:AT2G18650; -.
DR   Araport; AT2G18650; -.
DR   TAIR; locus:2054049; AT2G18650.
DR   eggNOG; KOG0800; Eukaryota.
DR   eggNOG; ENOG41121N2; LUCA.
DR   HOGENOM; HOG000239562; -.
DR   InParanoid; Q9ZV53; -.
DR   OMA; CHSKREG; -.
DR   OrthoDB; EOG09360CG2; -.
DR   PhylomeDB; Q9ZV53; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q9ZV53; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   Genevisible; Q9ZV53; AT.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0009793; P:embryo development ending in seed dormancy; IMP:TAIR.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.40.10; -; 1.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q9ZV53.
DR   SWISS-2DPAGE; Q9ZV53.
KW   Complete proteome; Membrane; Metal-binding; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix;
KW   Ubl conjugation pathway; Zinc; Zinc-finger.
FT   CHAIN         1    423       Putative RING-H2 finger protein ATL49.
FT                                /FTId=PRO_0000055777.
FT   TRANSMEM     43     63       Helical. {ECO:0000255}.
FT   ZN_FING     126    168       RING-type; atypical.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00175}.
FT   COMPBIAS     19     22       Poly-Pro.
SQ   SEQUENCE   423 AA;  47287 MW;  D305615B04028965 CRC64;
     MNKILPEMKS TQNLISSSPP PPLIPLKSNT SLSNLNSKIT PNILLIIIIL SIIFFISGLL
     HILVKFLLTP SRESREDYFD NVTALQGQLQ QLFNLHDSGV DQSLIDTLPV FHYKSIVGLK
     ISPFDCPVCL CEFETEDKLR LLPKCSHAFH VECIDTWLLS HSTCPLCRSN LLSGFSSHHN
     LSSSYLLVLE SEQSSRDMVP VLESNSQLGY DVNNDSESTR IRSGRKSCDP DGDMDGLDEK
     VVPLEVKLGK FRNIDHVGEG SDQKKNSISG NSKNVDGRRC LSMGSYEYIM DQEATLKVHV
     STKKLSGKDR VPSHRTVMSE CGFDPTVKGI EKSVVERESF SLSKIWLRGK KEKQKGTSAR
     DSDCSFVSSS SLRFPNHRIP PEESLKSENS ESLETKTPSF ARRTMHWLAG RQNKIVQPST
     SNV
//

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