ID   SSU72_ASPOR             Reviewed;         262 AA.
AC   Q2UPU5;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=AO090005001504;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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; AP007151; BAE56420.1; -; Genomic_DNA.
DR   RefSeq; XP_001818422.2; XM_001818370.2.
DR   AlphaFoldDB; Q2UPU5; -.
DR   SMR; Q2UPU5; -.
DR   STRING; 510516.Q2UPU5; -.
DR   EnsemblFungi; BAE56420; BAE56420; AO090005001504.
DR   GeneID; 5990367; -.
DR   KEGG; aor:AO090005001504; -.
DR   HOGENOM; CLU_062463_0_0_1; -.
DR   Proteomes; UP000006564; 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..262
FT                   /note="RNA polymerase II subunit A C-terminal domain
FT                   phosphatase ssu72"
FT                   /id="PRO_0000255604"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   262 AA;  29311 MW;  ED1369D24ADB98DC CRC64;
     MAAPTETESS DGTAAAPTQE QQSDSYKLRF CTVCASNQNR SMEAHLRLST APSPFPVISF
     GTGSLVRLPG PSITQPNVYN FNTTSYSQMY EELYSKDERL YRNNGLLNML ERNRNLKWGP
     ERFQDWVPGM PRVDHVAKGD KGALGTEGGV VDVIITCEER CWDAVVDDLM NKGSLLNRPV
     HVFNVDIKDN HEEALVGGKA ILELANRLNE AAVQERKANN SEGWENGTGE ARRSFDEKVP
     EILAAWQEKW PNLPALWTLA WL