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GPA4_USTMA
ID   GPA4_USTMA              Reviewed;         580 AA.
AC   P87035; A0A0D1BWN0; Q4P3C8;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Guanine nucleotide-binding protein alpha-4 subunit;
GN   Name=GPA4; ORFNames=UMAG_05385;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=FB1;
RX   PubMed=9155019; DOI=10.1093/emboj/16.8.1934;
RA   Regenfelder E., Spellig T., Hartmann A., Lauenstein S., Boelker M.,
RA   Kahmann R.;
RT   "G proteins in Ustilago maydis: transmission of multiple signals?";
RL   EMBO J. 16:1934-1942(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved
CC       as modulators or transducers in various transmembrane signaling
CC       systems.
CC   -!- SUBUNIT: G proteins are composed of 3 units; alpha, beta and gamma. The
CC       alpha chain contains the guanine nucleotide binding site.
CC   -!- SIMILARITY: Belongs to the G-alpha family. {ECO:0000305}.
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DR   EMBL; U85778; AAC49727.1; -; Genomic_DNA.
DR   EMBL; CM003158; KIS66392.1; -; Genomic_DNA.
DR   RefSeq; XP_011392079.1; XM_011393777.1.
DR   AlphaFoldDB; P87035; -.
DR   STRING; 5270.UM05385P0; -.
DR   EnsemblFungi; KIS66392; KIS66392; UMAG_05385.
DR   GeneID; 23565294; -.
DR   KEGG; uma:UMAG_05385; -.
DR   VEuPathDB; FungiDB:UMAG_05385; -.
DR   eggNOG; KOG0082; Eukaryota.
DR   HOGENOM; CLU_014184_1_1_1; -.
DR   InParanoid; P87035; -.
DR   OMA; WRTVIYF; -.
DR   OrthoDB; 754573at2759; -.
DR   PHI-base; PHI:79; -.
DR   Proteomes; UP000000561; Chromosome 19.
DR   GO; GO:0005834; C:heterotrimeric G-protein complex; IBA:GO_Central.
DR   GO; GO:0001664; F:G protein-coupled receptor binding; IBA:GO_Central.
DR   GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IBA:GO_Central.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IEA:InterPro.
DR   GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IBA:GO_Central.
DR   CDD; cd00066; G-alpha; 1.
DR   Gene3D; 1.10.400.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR001019; Gprotein_alpha_su.
DR   InterPro; IPR011025; GproteinA_insert.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR10218; PTHR10218; 2.
DR   Pfam; PF00503; G-alpha; 1.
DR   PRINTS; PR00318; GPROTEINA.
DR   SMART; SM00275; G_alpha; 1.
DR   SUPFAM; SSF47895; SSF47895; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51882; G_ALPHA; 1.
PE   3: Inferred from homology;
KW   GTP-binding; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Transducer.
FT   CHAIN           1..580
FT                   /note="Guanine nucleotide-binding protein alpha-4 subunit"
FT                   /id="PRO_0000203615"
FT   DOMAIN          93..579
FT                   /note="G-alpha"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          96..109
FT                   /note="G1 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          160..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..325
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          387..395
FT                   /note="G2 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          411..420
FT                   /note="G3 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          480..487
FT                   /note="G4 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   REGION          549..554
FT                   /note="G5 motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01230"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..325
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         101..108
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         389..395
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         395
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         415..419
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         484..487
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
FT   BINDING         551
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   580 AA;  65199 MW;  7EA38F8BC0F4CFCC CRC64;
     MSPSVSSPQL RHTKSNRAIS RIDRTDPLAL ALQPPANEAP ADKYARLHQE KLAKQRSDEI
     DKFLKQHQED RATHGLASSP STSVDGANFK KGRVYKMVLL GQAGAGKTTV LKQMRLLYDP
     PAHERERRGW TKIVLLNLTS SVRVLLETLS LYHDQRLERK SSELSRLESS TSASTSTSAS
     ASSPKHVDTE SQPNDATRLE LAKQLGTTKK INTSSLPWLT HIPSVVQLER ALRTELGAFG
     EEAVLSASSD EAAITNQKVR TRLDAQGSSS IRGEKSPLVL RPGWQERLFT YARRSLSLTQ
     NGRAAAARRE TDGGDSQSES EKDNSETLKL LRAIRPEVLA LWNDDAGCRA LRKRGLFLDG
     QSDAATSYFL DNYSRITDAA YRPTDEDILH SRVRTLGVTE DVFRVDRSLI YRIYDVGGSR
     SQRAAWAPFL DDIESIIFLA PLSAFDQPLV EDCSTNRLAD TFTLFNQIVT NPLLEHATMI
     LFLNKIDLLE KKLRQGVQLH KYWPEYVGDN DFEAVWRWFR AKFRDALRRA EDEVNLDQTS
     RRRLYVHTTV ATSTVQIRAI LMSVKDSILR ENLKLTGLVG
 
 
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