ID A0A2H5N2K5_CITUN Unreviewed; 957 AA.
AC A0A2H5N2K5;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=CUMW_011540 {ECO:0000313|EMBL:GAY34448.1};
OS Citrus unshiu (Satsuma mandarin) (Citrus nobilis var. unshiu).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Sapindales; Rutaceae; Aurantioideae; Citrus.
OX NCBI_TaxID=55188 {ECO:0000313|EMBL:GAY34448.1};
RN [1] {ECO:0000313|EMBL:GAY34448.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=29259619; DOI=10.3389/fgene.2017.00180;
RA Shimizu T., Tanizawa Y., Mochizuki T., Nagasaki H., Yoshioka T., Toyoda A.,
RA Fujiyama A., Kaminuma E., Nakamura Y.;
RT "Draft sequencing of the heterozygous diploid genome of Satsuma (Citrus
RT unshiu Marc.) using a hybrid assembly approach.";
RL Front. Genet. 8:180-180(2017).
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 -!- 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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAY34448.1}.
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DR EMBL; BDQV01000002; GAY34448.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2H5N2K5; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:InterPro.
DR Gene3D; 3.30.160.20; -; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR014720; dsRBD_dom.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR PANTHER; PTHR23081; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR PANTHER; PTHR23081:SF0; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN PHOSPHATASE; 1.
DR Pfam; PF00035; dsrm; 2.
DR Pfam; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SMART; SM00358; DSRM; 2.
DR SUPFAM; SSF54768; dsRNA-binding domain-like; 2.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50137; DS_RBD; 2.
DR PROSITE; PS50969; FCP1; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00266}.
FT DOMAIN 138..386
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 706..772
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT DOMAIN 838..908
FT /note="DRBM"
FT /evidence="ECO:0000259|PROSITE:PS50137"
FT REGION 519..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 935..957
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..664
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..691
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 957 AA; 106731 MW; 7F13849539B15035 CRC64;
MYKTVAYLGK EILGEVEIYP QQQGEGGEGE EKNKKVFDEI RISYFSEASE RCPPLAVLHT
ITASGICFKM ESKSSDNVQL HLLHSSCIRE NKTAVMLLGL TEELHLVAMY SRNNEKQYPC
FWAFSVGSGL YNSCLTMLNL RCLGIVFDLD ETLIVANTMR SFEDRIEALL RKISTEVDPQ
RIAGMQAEVK RYQDDKNILK QYAENDQVNE NGKVIKVQSE VVPALSDSHQ ALVRPLIRLQ
EKNIILTRIN PQIRDTSVLV RLRPAWEDLR SYLTARGRKR FEVYVCTMAE RDYALEMWRL
LDPESNLINT KELLDRIVCV KSGSRKSLFN VFQDGTCHPK MALVIDDRLK VWDEKDQSRV
HVVPAFAPYY APQAEANNAI PVLCVARNIA CNVRGGFFKE FDEGLLQRIP EISYEDDVKE
IPSPPDVSNY LVSEDDAATA NGIKDPLSFD GMADAEVERR LKEAIAASAT ISSAVANLDP
RLAPFQYTMP SSSSTTTLPT SQAAVMPLAN MQFPPATSLV KPLGHVGPPE QSLQSSPARE
EGEVPESELD PDTRRRLLIL QHGMDTRENA PSEAPFPART QMQVSVPRVP SRGSWFPVEE
EMSPRQLNRA VPKEFPLNSE AMQIEKHRPP HPSFFPKIEN SITSDRPHEN QRMPKEALRR
DDRLRLNHTL SDYQSFSGEE IPLSRSSSSS RDVDFESGRD VSSTETPSGV LQDIAMKCGT
KVEFRPALVA STELQFSIEA WFAGEKIGEG IGRTRREAQR QAAEGSIKHL ANVYVLRVKS
DSGSGHGDGS RFSNANENCF MGEINSFGGQ PLAKDESLSS EPSKLVDPRL EGSKKLMGSV
SALKELCMTE GLGVVFQQQP PSSANSVQKD EVYAQVEIDG QVLGKGIGST WDEAKMQAAE
KALGSLRSMF GQFPQKHQGS PRSLQGMPNK RLKPEFPRVL QRMPPSGRYP KNAPPVP
//