ID A0A2T7EE98_9POAL Unreviewed; 551 AA.
AC A0A2T7EE98;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=GQ55_3G284300 {ECO:0000313|EMBL:PUZ66159.1};
OS Panicum hallii var. hallii.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Panicinae; Panicum;
OC Panicum sect. Panicum.
OX NCBI_TaxID=1504633 {ECO:0000313|EMBL:PUZ66159.1, ECO:0000313|Proteomes:UP000244336};
RN [1] {ECO:0000313|EMBL:PUZ66159.1, ECO:0000313|Proteomes:UP000244336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HAL2 {ECO:0000313|Proteomes:UP000244336};
RA Lovell J., Jenkins J., Lowry D., Mamidi S., Sreedasyam A., Weng X.,
RA Barry K., Bonette J., Campitelli B., Daum C., Gordon S., Gould B.,
RA Lipzen A., MacQueen A., Palacio-Mejia J., Plott C., Shakirov E., Shu S.,
RA Yoshinaga Y., Zane M., Rokhsar D., Grimwood J., Schmutz J., Juenger T.;
RT "WGS assembly of Panicum hallii var. hallii HAL2.";
RL Submitted (APR-2018) 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}.
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DR EMBL; CM009751; PUZ66159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7EE98; -.
DR EnsemblPlants; PUZ66159; PUZ66159; GQ55_3G284300.
DR Gramene; PUZ66159; PUZ66159; GQ55_3G284300.
DR Proteomes; UP000244336; Chromosome 3.
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; RNA POLYMERASE II CTD PHOSPHATASE; 1.
DR PANTHER; PTHR23081:SF36; RNA POLYMERASE II SUBUNIT A C-TERMINAL DOMAIN 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:UP000244336}.
FT DOMAIN 159..331
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 376..468
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..65
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..82
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..539
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 551 AA; 61353 MW; 206021DFDFDD473F CRC64;
MSLAEAPSSS PSSSSGSEDF AALLDAELEL ASGADSAFPG DPSSASPATD DEGEEEDSEE
EVEVEVLEQN GAKRRRVEEQ RQDQGMSISP DKFATGPSKN VQVELCPHPG YFGGLCFRCG
KPRDEEDVSG VAFGYIHKGL RLGTSEIDRL RGADLKNLLR ERKLVLILDL DHTLINSTKL
QDISSAENEL GIRTAALKDD PDRSIFTLDS MQMLTKLRPF VHKFLKEASN MFEMYIYTMG
DKAYAIEIAK LLDPTNVYFP SKVISNSDCT QRHQKGLDVI LGAESVAVIL DDTEYVWQKH
KENLILMERY HYFASSCRQF GFGVRSLSES MQDERESDGA LATVLDVLKR IHAIFFDTAA
ETDLSSQDVR QVIKAVRKEV LKGCKLVFSR VFPNNARPQE QMMWKMAEHL GAVCSTDVDS
TVTHVVAVDL GTEKARWAVG NKKFLVHPRW IEAANFRWHR QPEEDFHVIP PKEKSRDKVN
AVCGQKETSK DKEENTVAGE KETSNDRKEE NDVADQKETS NDYDGNDVDG QKKDDAKENA
VVTAATGPAD S
//
