ID A0A067GU16_CITSI Unreviewed; 960 AA.
AC A0A067GU16;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=RNA polymerase II C-terminal domain phosphatase-like {ECO:0000256|RuleBase:RU366066};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU366066};
GN ORFNames=CISIN_1g000897mg {ECO:0000313|EMBL:KDO83173.1};
OS Citrus sinensis (Sweet orange) (Citrus aurantium var. sinensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=2711 {ECO:0000313|EMBL:KDO83173.1, ECO:0000313|Proteomes:UP000027120};
RN [1] {ECO:0000313|EMBL:KDO83173.1, ECO:0000313|Proteomes:UP000027120}
RP NUCLEOTIDE SEQUENCE.
RG International Citrus Genome Consortium;
RA Gmitter F., Chen C., Farmerie W., Harkins T., Desany B., Mohiuddin M.,
RA Kodira C., Borodovsky M., Lomsadze A., Burns P., Jenkins J., Prochnik S.,
RA Shu S., Chapman J., Pitluck S., Schmutz J., Rokhsar D.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: This promotes the activity of RNA polymerase II.
CC {ECO:0000256|RuleBase:RU366066}.
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 Evidence={ECO:0000256|ARBA:ARBA00001512,
CC ECO:0000256|RuleBase:RU366066};
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 Evidence={ECO:0000256|ARBA:ARBA00001482,
CC ECO:0000256|RuleBase:RU366066};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU366066}.
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; KK784875; KDO83172.1; -; Genomic_DNA.
DR EMBL; KK784875; KDO83173.1; -; Genomic_DNA.
DR Proteomes; UP000027120; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:UniProtKB-UniRule.
DR CDD; cd17729; BRCT_CTDP1; 1.
DR CDD; cd07521; HAD_FCP1-like; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR011947; FCP1_euk.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR NCBIfam; TIGR02250; FCP1_euk; 1.
DR PANTHER; PTHR23081:SF2; RNA POLYMERASE II C-TERMINAL DOMAIN PHOSPHATASE-LIKE 3; 1.
DR PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR Pfam; PF00533; BRCT; 1.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00292; BRCT; 1.
DR SMART; SM00577; CPDc; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366066};
KW Nucleus {ECO:0000256|RuleBase:RU366066};
KW Reference proteome {ECO:0000313|Proteomes:UP000027120}.
FT DOMAIN 642..822
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 865..958
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 157..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 960 AA; 105318 MW; 1F9DF685BEB83A26 CRC64;
MEAMLSSLVT RANDKEKDML AMHGVNGKDS NIVTENAVND LNFKEKVPLP VDSLMQNKPL
EASKPGPPGY RSRGVLLPLL DPHKVHDVDS LPSPTRETTP SVPVQRALVV GDGMVKSWAA
AAKLSHNAEV HKTPHYETDA LRAFSSYQQK FGRNSFFMNS ELPSPTPSEE SGDGDGDTGG
EISSATAVDQ PKPVNMPTLG QQPVSSQPMD ISQPMDISSV QALTTANNSA PASSGYNPVV
KPNPVVKAPI KSRDPRLRFA SSNALNLNHQ PAPILHNAPK VEPVGRVMSS RKQKTVEEPV
LDGPALKRQR NGFENSGVVR DEKNIYGSGG WLEDTDMFEP QIMNRNLLVD SAESNSRKLD
NGATSPITSG TPNVVVSGNE PAPATTPSTT VSLPALLKDI AVNPTMLLNI LKMGQQQKLA
ADAQQKSNDS SMNTMHPPIP SSIPPVSVTC SIPSGILSKP MDELGKVRMK PRDPRRVLHG
NALQRSGSLG PEFKTDGPSA PCTQGSKENL NFQKQLGAPE AKPVLSQSVL QPDITQQFTK
NLKHIADFMS VSQPLTSEPM VSQNSPIQPG QIKSGADMKA VVTNHDDKQT GTGSGPEAGP
VGAHPQSAWG DVEHLFEGYD DQQKAAIQKE RTRRLEEQKK MFSARKLCLV LDLDHTLLNS
AKFHEVDPVH DEILRKKEEQ DREKPHRHLF RFPHMGMWTK LRPGIWTFLE RASKLFEMHL
YTMGNKLYAT EMAKVLDPKG VLFAGRVISR GDDGDPFDGD ERVPKSKDLE GVLGMESAVV
IIDDSVRVWP HNKLNLIVVE RYTYFPCSRR QFGLLGPSLL EIDHDERSED GTLASSLGVI
ERLHKIFFSH QSLDDVDVRN ILAAEQRKIL AGCRIVFSRV FPVGEANPHL HPLWQTAEQF
GAVCTKHIDD QVTHVVANSL GTDKVNWALS TGRFVVHPGW VEASALLYRR ANEQDFAIKP
//
