位置:首页 > 蛋白库 > AIG2C_ARATH
AIG2C_ARATH
ID   AIG2C_ARATH             Reviewed;         165 AA.
AC   Q9MBH1; Q8LBI2;
DT   02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Protein AIG2 C {ECO:0000305};
DE            EC=2.3.2.- {ECO:0000305};
DE   AltName: Full=Avirulence-induced gene 2 protein C {ECO:0000305};
DE   AltName: Full=Putative gamma-glutamylcyclotransferase {ECO:0000250|UniProtKB:O75223};
GN   Name=AIG2C {ECO:0000305};
GN   OrderedLocusNames=At3g28950 {ECO:0000312|Araport:AT3G28950};
GN   ORFNames=K5K13.6 {ECO:0000312|EMBL:BAA95746.1};
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 {ECO:0000312|EMBL:BAA95746.1};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10819329; DOI=10.1093/dnares/7.2.131;
RA   Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Tabata S.;
RT   "Structural analysis of Arabidopsis thaliana chromosome 3. I. Sequence
RT   features of the regions of 4,504,864 bp covered by sixty P1 and TAC
RT   clones.";
RL   DNA Res. 7:131-135(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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA   Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA   Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA   Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA   Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   STRUCTURE BY NMR OF 2-165, AND GENE FAMILY.
RX   PubMed=18214976; DOI=10.1002/prot.21936;
RA   de la Cruz N.B., Peterson F.C., Volkman B.F.;
RT   "Solution structure of At3g28950 from Arabidopsis thaliana.";
RL   Proteins 71:546-551(2008).
CC   -!- FUNCTION: Putative gamma-glutamylcyclotransferase.
CC       {ECO:0000250|UniProtKB:O75223}.
CC   -!- TISSUE SPECIFICITY: Expressed in floral organs, leaves, stems and
CC       roots. {ECO:0000305|PubMed:18214976}.
CC   -!- DEVELOPMENTAL STAGE: Expressed constitutively during the life cycle.
CC       {ECO:0000305|PubMed:18214976}.
CC   -!- INDUCTION: Expressed constitutively. {ECO:0000305|PubMed:18214976}.
CC   -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AB025615; BAA95746.1; -; Genomic_DNA.
DR   EMBL; CP002686; AEE77512.1; -; Genomic_DNA.
DR   EMBL; BT004596; AAO42842.1; -; mRNA.
DR   EMBL; AK227989; BAE99955.1; -; mRNA.
DR   EMBL; AY087193; AAM64749.1; -; mRNA.
DR   RefSeq; NP_189537.1; NM_113816.3.
DR   PDB; 2JQV; NMR; -; A=2-165.
DR   PDBsum; 2JQV; -.
DR   AlphaFoldDB; Q9MBH1; -.
DR   SMR; Q9MBH1; -.
DR   PaxDb; Q9MBH1; -.
DR   PRIDE; Q9MBH1; -.
DR   ProteomicsDB; 244934; -.
DR   DNASU; 822532; -.
DR   EnsemblPlants; AT3G28950.1; AT3G28950.1; AT3G28950.
DR   GeneID; 822532; -.
DR   Gramene; AT3G28950.1; AT3G28950.1; AT3G28950.
DR   KEGG; ath:AT3G28950; -.
DR   Araport; AT3G28950; -.
DR   TAIR; locus:2086997; AT3G28950.
DR   eggNOG; ENOG502S7T1; Eukaryota.
DR   HOGENOM; CLU_093936_0_0_1; -.
DR   InParanoid; Q9MBH1; -.
DR   OMA; DFEEWRV; -.
DR   OrthoDB; 1307538at2759; -.
DR   PhylomeDB; Q9MBH1; -.
DR   EvolutionaryTrace; Q9MBH1; -.
DR   PRO; PR:Q9MBH1; -.
DR   Proteomes; UP000006548; Chromosome 3.
DR   ExpressionAtlas; Q9MBH1; baseline and differential.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   CDD; cd06661; GGCT_like; 1.
DR   InterPro; IPR045038; AIG2-like.
DR   InterPro; IPR009288; AIG2-like_dom.
DR   InterPro; IPR013024; GGCT-like.
DR   InterPro; IPR036568; GGCT-like_sf.
DR   PANTHER; PTHR31544; PTHR31544; 1.
DR   Pfam; PF06094; GGACT; 1.
DR   SUPFAM; SSF110857; SSF110857; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..165
FT                   /note="Protein AIG2 C"
FT                   /id="PRO_0000438021"
FT   ACT_SITE        82
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O75223"
FT   BINDING         14..19
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:O75223"
FT   CONFLICT        106
FT                   /note="T -> S (in Ref. 5; AAM64749)"
FT                   /evidence="ECO:0000305"
FT   STRAND          9..15
FT                   /evidence="ECO:0007829|PDB:2JQV"
FT   HELIX           20..26
FT                   /evidence="ECO:0007829|PDB:2JQV"
FT   STRAND          32..39
FT                   /evidence="ECO:0007829|PDB:2JQV"
FT   STRAND          49..51
FT                   /evidence="ECO:0007829|PDB:2JQV"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:2JQV"
FT   STRAND          59..70
FT                   /evidence="ECO:0007829|PDB:2JQV"
FT   HELIX           72..80
FT                   /evidence="ECO:0007829|PDB:2JQV"
FT   STRAND          84..95
FT                   /evidence="ECO:0007829|PDB:2JQV"
FT   TURN            96..98
FT                   /evidence="ECO:0007829|PDB:2JQV"
FT   STRAND          101..109
FT                   /evidence="ECO:0007829|PDB:2JQV"
FT   TURN            110..113
FT                   /evidence="ECO:0007829|PDB:2JQV"
FT   HELIX           123..146
FT                   /evidence="ECO:0007829|PDB:2JQV"
FT   HELIX           153..156
FT                   /evidence="ECO:0007829|PDB:2JQV"
SQ   SEQUENCE   165 AA;  18619 MW;  883C189FD8C55DDF CRC64;
     MTSSDPQSHN VFVYGSILEP AVAAVILDRT ADTVPAVLHG YHRYKLKGLP YPCIVSSDSG
     KVNGKVITGV SDAELNNFDV IEGNDYERVT VEVVRMDNSE KVKVETYVWV NKDDPRMYGE
     WDFEEWRVVH AEKFVETFRK MLEWNKNPNG KSMEEAVGSL LSSGD
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024