ID D8TQP1_VOLCA Unreviewed; 2442 AA.
AC D8TQP1;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=protein-serine/threonine phosphatase {ECO:0000256|ARBA:ARBA00013081};
DE EC=3.1.3.16 {ECO:0000256|ARBA:ARBA00013081};
GN ORFNames=VOLCADRAFT_89056 {ECO:0000313|EMBL:EFJ50184.1};
OS Volvox carteri f. nagariensis.
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Chlorophyceae;
OC CS clade; Chlamydomonadales; Volvocaceae; Volvox.
OX NCBI_TaxID=3068 {ECO:0000313|Proteomes:UP000001058};
RN [1] {ECO:0000313|EMBL:EFJ50184.1, ECO:0000313|Proteomes:UP000001058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=f. Nagariensis / Eve {ECO:0000313|Proteomes:UP000001058};
RX PubMed=20616280; DOI=10.1126/science.1188800;
RA Prochnik S.E., Umen J., Nedelcu A.M., Hallmann A., Miller S.M., Nishii I.,
RA Ferris P., Kuo A., Mitros T., Fritz-Laylin L.K., Hellsten U., Chapman J.,
RA Simakov O., Rensing S.A., Terry A., Pangilinan J., Kapitonov V., Jurka J.,
RA Salamov A., Shapiro H., Schmutz J., Grimwood J., Lindquist E., Lucas S.,
RA Grigoriev I.V., Schmitt R., Kirk D., Rokhsar D.S.;
RT "Genomic analysis of organismal complexity in the multicellular green alga
RT Volvox carteri.";
RL Science 329:223-226(2010).
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}.
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DR EMBL; GL378332; EFJ50184.1; -; Genomic_DNA.
DR RefSeq; XP_002948804.1; XM_002948758.1.
DR STRING; 3068.D8TQP1; -.
DR GeneID; 9627378; -.
DR KEGG; vcn:VOLCADRAFT_89056; -.
DR eggNOG; KOG0323; Eukaryota.
DR eggNOG; KOG2217; Eukaryota.
DR InParanoid; D8TQP1; -.
DR OrthoDB; 11699at2759; -.
DR Proteomes; UP000001058; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd17729; BRCT_CTDP1; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR039189; Fcp1.
DR InterPro; IPR004274; FCP1_dom.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; PF03031; NIF; 1.
DR SMART; SM00577; CPDc; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF52113; BRCT domain; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS50172; BRCT; 1.
DR PROSITE; PS50969; FCP1; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001058};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..2442
FT /note="protein-serine/threonine phosphatase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003123781"
FT TRANSMEM 852..875
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 882..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 908..927
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 939..960
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 747..814
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT DOMAIN 2045..2239
FT /note="FCP1 homology"
FT /evidence="ECO:0000259|PROSITE:PS50969"
FT DOMAIN 2340..2442
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT REGION 293..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 489..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..683
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1011..1244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1404..1580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1618..1964
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2306..2327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1289..1316
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 296..311
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..425
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..524
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1041
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1080
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1110..1124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1466..1485
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1546..1570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1641..1661
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1699..1719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1792..1949
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2310..2327
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2442 AA; 250812 MW; 08A3A0446D8C2FEC CRC64;
MRQRYSPWFC WTLFLLALNV ATPPSGAGAS GINGNSKDLA KQAASAVLSS DVAKRLVALL
AEVRALGEDL RAAGDEWLTR RADGMEAAAG RLRQTLRPAS ERLQQAFGRQ CSQPVFTPPS
DVNATVVGPG LSYTRTGGSC QLRRNAQATQ RDLNLTCNNA GVTITRTAAR YTSAYQAPAT
FVGTECKRSY QFGLSATVTV DLWRPGARPS DAVATWQQRL GRRRQRRAEM QQSFAGRVGN
GGGAGFGGFG GGGGGNGGGG GGGNGGGDMA QLSQMHAVPA EALLEALTRR ASGGLLLQPP
PPPPPHPPPW SFNTFTATAS SPGGGDGEEQ QQQQHGADSV FLSAPGGVGG PGDGGHQQQG
GTGSPAGGSV WAAADGVAAA GGSVSDVFHM VGQAGLAALR GEMSSEAAAT AAAASPTTRG
SSTPPWAIRR NHPRDDEDSK GMANEGSGSC CAAERHSDVP QGKQSARRIH PPEGMRKAEV
GMKALERFVQ RQPRHYITTD PDLKDSRAHE VKKKQKKKDG KKEGKGKGKG KEEAEVLEEV
DGGGSEEGNS GDVDSAAVRD AAIAKAAAAA TAMAAAARDA SLFLDDRHLA AVVAVIAFAT
DFAPAARPTP SLSAGAAAAA AAVPPSLLSA QLLQCFTHTG SQELQLAQWT PPPAPPASPQ
QQLYSSTSLS LPSPPMPPPP LLQQRQTAAV TGGISVSVSC STTSAASLSS CSARCGSVRQ
AAAAVDRALT AAAALAAGSS DTGSGGSDGS EEQCCRVCLD PVSETELQLG TALRLGCRCG
AGLDLLHRAC ADRWFRGVRC CTTCEVCGAE ATNLPAQMRA AIRWQQLLNP RGRGPVGRSG
GPLSLSSLPS FLGLYTLVCL IPATLSSLLL VIFYLRHLGV GAGPTMALSI LTASGTILHW
VYVPYRPLFH VLFCTTALTC VFAQTLLLKA LCPSWRPSVV AAVGAAVGFM AGASLFYGLL
NPLVALLRLF LPQLWAAWRR RRQQQQAVSG AAWVIEHIVL QLFYTPSTGV TKTMPGPPLE
EGELEDGEVH EDKHADLEES GEASGCDGED DAGTLAADHN QHDQTQQQPL RATSGQLGLN
TSPLPPPPLL LQSPSGASLP APTRSGRAPD TGVIPSSSAI SDGGVHQAQA GPPKGRPRPH
GHDPSASGNA PAVRSRFRAP DGAQPGPSDS LPSSQQQQPP PHPFSPSGAS SQPSSHSQHP
HPHPHSLPLQ RQSHSYAGGP GTAGGPAGGH PSPGRPLLAG QGPGAATAGA AAAAAAAGGP
VAVREDREVE ELTGLLRELT RGCSFQEVMR SLEAVCRDLK QAIKKLDKLF RRVKRRKGDS
IEDYPDCFQF SRRILEGLTS INKFSATSAF HAAPPSGAEA ARALFKAAMN YRHDIFNASL
KAELEDLVRN SKAFKCVLEN RHRSGATAPA ATAPAPAAAA AARPRSGSGG GGGGGGTEGA
DRTDMRAGEV AAGAEGQLAP QPPPQRQSRS RSPPPLPPPP PVVAQTATSE PELMDTGGED
GPGAAAATAS APPPPRGSSC SPVRSDEDGG GAGGTVPPPP KDDSPQLQLQ RLNSATGGTG
VRSTTGRSGA GGGSGGGAAG GFKLKIVVAS TPGDLDAAAA AGAAATSDVA ANGAWPLASA
AAGDGSGGGG GGGRTRSLTP QDADTDLERP RAAKRSRVSK ELVETGVPGA LPPPPSSPLA
SVGTVLRWDH PDQHPVADVL REQQQQPQPH YSLQEQEQSA LGMMAPGVLL PPPESPVSEA
GADSEGGALH GGVLEPPPAP LTAGAAGPVA TAGGGGVSEG QVQGAAHGSV SSSHSDRDRD
RDRDRDRGGG GSGGAREKDG KEGRDGRERD RERERDRDRE REREKEREKE PKEKDKDKEK
DKEKEKERDR GRDRERERDS RHRSRQDKDS KERDGGKDGG KDRDGGKDNR DRDREKDKEK
EKESKVDKDR EHGGAGRSSS YRHRDRDTGL PLPPPPPPPT DASSLLGTAA AAAAAAAAAA
AATKQELFDG PPAGLGSGGR SAAVTASSED TAAAVAAAAA AAGGGGGGGG GGGSATAAEA
TVGLLSRGKL VLVVDLDGVL ADSCWDDQLD PAAAAALSRH AAAEAGLPED RRELFRLPLD
AGATAGAASG GSGLWLKLRP GARAFLARAH ERFELWAHSR QGRPYADAVV ELLDPSLALF
GSRVVAQGEL ARRLLTALDA RAPITAILDT PSAAWMGEQL APGLLPLPPY SYFSYRPACT
ADAAAGVGGG GAAPGARTLA PSASGMAGRS LLEVNRDECP ERGVLAAALP LLYVLYTRVM
STYGAAATTT ASSSAGSTAA AAAAAAIAKP PTDGPPPPPP PAPPLAGLEP WDVRRVLREQ
RQRVLAGFHI TFSRVFTSGG GGGDGGGGGA AGPQHPLWRL AEAFGATVGA SCSDATTHVV
ALSAGTEKAI WAAQHGRFVV YPSWLEASCF LWRKVDESLF LL
//
