SSU72_GIBZE
ID SSU72_GIBZE Reviewed; 255 AA.
AC Q4IPC8; A0A0E0RNZ9; V6QVB7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=RNA polymerase II subunit A C-terminal domain phosphatase SSU72;
DE Short=CTD phosphatase SSU72;
DE EC=3.1.3.16;
DE AltName: Full=Suppressor of SUA7 protein 2 homolog;
GN Name=SSU72; ORFNames=FGRRES_00930, FGSG_00930;
OS Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX NCBI_TaxID=229533;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=17823352; DOI=10.1126/science.1143708;
RA Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT "The Fusarium graminearum genome reveals a link between localized
RT polymorphism and pathogen specialization.";
RL Science 317:1400-1402(2007).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA Hammond-Kosack K.E.;
RT "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT graminearum.";
RL BMC Genomics 16:544-544(2015).
CC -!- FUNCTION: Processively dephosphorylates Ser-5 of the heptad repeats
CC YSPTSPS in the C-terminal domain of the largest RNA polymerase II
CC subunit (RPB1). {ECO:0000250}.
CC -!- FUNCTION: Component of the cleavage and polyadenylation factor (CPF)
CC complex, which plays a key role in polyadenylation-dependent pre-mRNA
CC 3'-end formation and cooperates with cleavage factors including the
CC CFIA complex and NAB4/CFIB. SSU72 is required for 3'-end formation of
CC snoRNAs (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] +
CC phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:83421; EC=3.1.3.16;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-threonyl-[protein] = L-threonyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:47004, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC COMP:11605, ChEBI:CHEBI:15377, ChEBI:CHEBI:30013, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61977; EC=3.1.3.16;
CC -!- SUBUNIT: Component of the cleavage and polyadenylation factor (CPF)
CC complex. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SSU72 phosphatase family. {ECO:0000305}.
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DR EMBL; DS231663; ESU06186.1; -; Genomic_DNA.
DR EMBL; HG970332; CEF72974.1; -; Genomic_DNA.
DR RefSeq; XP_011316671.1; XM_011318369.1.
DR AlphaFoldDB; Q4IPC8; -.
DR SMR; Q4IPC8; -.
DR STRING; 5518.FGSG_00930P0; -.
DR EnsemblFungi; ESU06186; ESU06186; FGSG_00930.
DR GeneID; 23548396; -.
DR KEGG; fgr:FGSG_00930; -.
DR VEuPathDB; FungiDB:FGRAMPH1_01G02345; -.
DR eggNOG; KOG2424; Eukaryota.
DR HOGENOM; CLU_062463_0_0_1; -.
DR InParanoid; Q4IPC8; -.
DR PHI-base; PHI:1531; -.
DR PHI-base; PHI:5700; -.
DR Proteomes; UP000070720; Chromosome 1.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR InterPro; IPR006811; RNA_pol_II_suA.
DR PANTHER; PTHR20383; PTHR20383; 1.
DR Pfam; PF04722; Ssu72; 1.
PE 3: Inferred from homology;
KW Hydrolase; mRNA processing; Nucleus; Protein phosphatase;
KW Reference proteome.
FT CHAIN 1..255
FT /note="RNA polymerase II subunit A C-terminal domain
FT phosphatase SSU72"
FT /id="PRO_0000255609"
SQ SEQUENCE 255 AA; 28124 MW; 991E8D237B5B6057 CRC64;
MEVANGSSAA QGQNGSSEGS NGYKLKFCTV CASNNNRSME AHLRLSQADY PVISFGTGSL
VRLPGPTITQ PNVYHFNKTS YDSMFKELES KDARLYKNNG ILNMLNRNRG VKWGPERWQD
WQVGVPRLQH AKDRGSEGTE GGLVDIVITC EERCWDAVVD DLMNRGSPLN RPVHVINVEI
KDNHEEAAVG GQGILDLANS LNAAAREERD AVGASAFDNG SASSRATFDE RVPDILASWQ
ERWPNLPATW TVAWF
