ID A0A2P6U3L0_CHLSO Unreviewed; 1171 AA.
AC A0A2P6U3L0;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 03-MAY-2023, entry version 26.
DE RecName: Full=RNA polymerase II subunit B1 CTD phosphatase RPAP2 homolog {ECO:0000256|RuleBase:RU367080};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU367080};
GN ORFNames=C2E21_0180 {ECO:0000313|EMBL:PRW60901.1};
OS Chlorella sorokiniana (Freshwater green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW60901.1, ECO:0000313|Proteomes:UP000239899};
RN [1] {ECO:0000313|EMBL:PRW60901.1, ECO:0000313|Proteomes:UP000239899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
CC -!- FUNCTION: Putative RNA polymerase II subunit B1 C-terminal domain (CTD)
CC phosphatase involved in RNA polymerase II transcription regulation.
CC {ECO:0000256|RuleBase:RU367080}.
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:RU367080};
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:RU367080};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC ECO:0000256|RuleBase:RU367080}.
CC -!- SIMILARITY: Belongs to the RPAP2 family.
CC {ECO:0000256|ARBA:ARBA00005676, ECO:0000256|PROSITE-ProRule:PRU00812,
CC ECO:0000256|RuleBase:RU367080}.
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:PRW60901.1}.
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DR EMBL; LHPG02000001; PRW60901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6U3L0; -.
DR STRING; 3076.A0A2P6U3L0; -.
DR OrthoDB; 325287at2759; -.
DR Proteomes; UP000239899; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0043175; F:RNA polymerase core enzyme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008420; F:RNA polymerase II CTD heptapeptide repeat phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR GO; GO:0016540; P:protein autoprocessing; IEA:InterPro.
DR CDD; cd00081; Hint; 1.
DR Gene3D; 1.25.40.820; -; 1.
DR Gene3D; 2.170.16.10; Hedgehog/Intein (Hint) domain; 1.
DR InterPro; IPR001767; Hedgehog_Hint.
DR InterPro; IPR003587; Hint_dom_N.
DR InterPro; IPR036844; Hint_dom_sf.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR039693; Rtr1/RPAP2.
DR InterPro; IPR007308; Rtr1/RPAP2_dom.
DR InterPro; IPR038534; Rtr1/RPAP2_sf.
DR PANTHER; PTHR14732:SF0; RNA POLYMERASE II SUBUNIT B1 CTD PHOSPHATASE RPAP2-RELATED; 1.
DR PANTHER; PTHR14732; UNCHARACTERIZED; 1.
DR Pfam; PF01079; Hint; 1.
DR Pfam; PF04181; RPAP2_Rtr1; 1.
DR SMART; SM00306; HintN; 1.
DR SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR PROSITE; PS50817; INTEIN_N_TER; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51479; ZF_RTR1; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU367080};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367080};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU367080};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW ECO:0000256|RuleBase:RU367080};
KW Reference proteome {ECO:0000313|Proteomes:UP000239899};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367080};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|RuleBase:RU367080}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1171
FT /note="RNA polymerase II subunit B1 CTD phosphatase RPAP2
FT homolog"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015173604"
FT DOMAIN 357..450
FT /note="RTR1-type"
FT /evidence="ECO:0000259|PROSITE:PS51479"
FT REGION 469..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 651..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1012
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..673
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..805
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 827..855
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1003
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1171 AA; 121511 MW; 3DD9DED4B0CC8B26 CRC64;
MRCSTIVGIF LAAMAAACVS ATAASTPRRL LSDPICAGLD LACSASCSAA GYSHYRYKCG
ARSCGCTNKA NCFPGSATVH LRGGGCKPMS QLALGDEVLT VGHDGALRYD KVFLFSSRRP
HERASFVRII TASTNVTATP SHYFYTRRAG AALHSSPASL AGWELLPAGE LRLGDAVLVA
HDGQAAAAPA VVTGVEQVAS VGVYNPHTRA GTIVVDGIVA SELTTFVPRW AAHPFLLRAT
AAALHTAFAI LPRSADAPIA ATLSGLAHGG PGDAIVDRTA FLHTPHQRST MTSDAGSVAA
AGLAPQEAAA PAAAAKGKQP ARRRQPLTLP EMRSKAAFRA CDRLMERGAD SQEQLWSVAR
VMSGEEYEQA AEERALAGKC GNPLCTHPPA SSSSSSSSSL PRARYHISTS QQAVYEAAAQ
ERPVYCSPDC QVAVKKLAAR LGSGALALDR FTAVYEELKR REAEVTSAAK LAQQAEQPQQ
AEQQQDGQPP PAQQEGAAAS AAASSGEAAA ASSSSSSACA SGADSGPGGI CSDTPLVPRL
AVEQVEVKHI DSSAGQFGDF SRKLKQRPAG EAAGAAPRPK GVLKKQSQFA AGTAKVPIML
AEVKERDLSI VEAETARNLP AEGEAPAAPS AARRSAKAAV AVEGYVPRAI NSQRQRRVRW
SDEVEESSEE PSPERSSPEP QAAAAQPAEL PPAVQPQEGT SQAAAGAVAA APAATAQQQQ
GAAGTTSSVL VFEVEDPKGP LEAGGLSAQM GRLRVADPSE LPSSAAASTA ASTAAEIRSS
ARSPSPGGSS HSSPSPSLSP VSSSIDIQRR EFVVPPEWRD APQFYAHSPV GSSSSLAGSL
SSPYGSNSNL AAIASVSSPP KRPPVASPPG LPRPPSRGNS AGASRLGAAQ PSQQAASSSS
SSQTGGQGQP ATEAAPQQQM QPQSQQQPQP QQQPQQQPAE APALTRRQAE QLQRAFPGLS
ATLPPELQAM LASDSEGESG AEDEEEGSDW MNSDDEQDAS SGEDEDGFVG PAGRSGFRLQ
MSFFGTLFTH LEAWVTPNTV ELLAAGPAVE LVLPPPTSPE VLATLSRFLA QALPPVLSSL
QAAAPRNEVE RALEELLRTL RLVGPLPAFK VSQWQVVVVL LLKALSLERC PALRPCFETR
DGIARLNRLL GTLTFTSEEF YAALELLCAT E
//
