SSU72_ASPFU
ID SSU72_ASPFU Reviewed; 287 AA.
AC Q4WHY5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=AFUA_2G03760;
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(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; AAHF01000008; EAL87470.1; -; Genomic_DNA.
DR RefSeq; XP_749508.1; XM_744415.1.
DR AlphaFoldDB; Q4WHY5; -.
DR SMR; Q4WHY5; -.
DR STRING; 746128.CADAFUBP00002032; -.
DR EnsemblFungi; EAL87470; EAL87470; AFUA_2G03760.
DR GeneID; 3506785; -.
DR KEGG; afm:AFUA_2G03760; -.
DR VEuPathDB; FungiDB:Afu2g03760; -.
DR eggNOG; KOG2424; Eukaryota.
DR HOGENOM; CLU_062463_0_0_1; -.
DR InParanoid; Q4WHY5; -.
DR OMA; NMLGRNR; -.
DR OrthoDB; 1304061at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
DR GO; GO:0005847; C:mRNA cleavage and polyadenylation specificity factor complex; IBA:GO_Central.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IBA:GO_Central.
DR GO; GO:0070940; P:dephosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0006378; P:mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0006369; P:termination of RNA polymerase II transcription; IBA:GO_Central.
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..287
FT /note="RNA polymerase II subunit A C-terminal domain
FT phosphatase ssu72"
FT /id="PRO_0000255603"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..30
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 287 AA; 31559 MW; 5366D17B18D8BC1D CRC64;
MAHDPRLSSA GTATPNPPPP PPPPPPEPST TGTGETQAAE PSAPAQSSDS FKLKFCTVCA
SNQNRSMEAH LRLSTAPSPF PVISFGTGSL VRLPGPSITQ PNVYNFNTTS YSQMYDELLA
KDERLYRNNG LLNMLDRNRN LKWGPERFQD WVPGMPRVDH VSKGDKGALG TEGGTVDVII
TCEERCWDAV VDDLMNKGAA LNRPVHVFNV DIRDNHEEAL VGGKAILELA TRLNDAATQE
RKIHGAEGWE NGNGEARRSF DERVPEILAS WQEKWPNLPA LWTLAWL
