ID D8UHM6_VOLCA Unreviewed; 896 AA.
AC D8UHM6;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
GN ORFNames=VOLCADRAFT_84366 {ECO:0000313|EMBL:EFJ40773.1};
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:EFJ40773.1, 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 ECO:0000256|RuleBase:RU004273};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family. BSU subfamily.
CC {ECO:0000256|ARBA:ARBA00005671}.
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DR EMBL; GL378407; EFJ40773.1; -; Genomic_DNA.
DR RefSeq; XP_002958148.1; XM_002958102.1.
DR AlphaFoldDB; D8UHM6; -.
DR STRING; 3068.D8UHM6; -.
DR GeneID; 9623245; -.
DR KEGG; vcn:VOLCADRAFT_84366; -.
DR eggNOG; KOG0374; Eukaryota.
DR eggNOG; KOG0379; Eukaryota.
DR InParanoid; D8UHM6; -.
DR OrthoDB; 311640at2759; -.
DR Proteomes; UP000001058; 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:0009742; P:brassinosteroid mediated signaling pathway; IEA:InterPro.
DR CDD; cd07419; MPP_Bsu1_C; 1.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 2.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR041758; MPP_BSL_C.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR012391; Ser/Thr_prot_Pase_BSU1.
DR PANTHER; PTHR46422; SERINE/THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR PANTHER; PTHR46422:SF4; SERINE_THREONINE-PROTEIN PHOSPHATASE BSL3; 1.
DR Pfam; PF13415; Kelch_3; 1.
DR Pfam; PF13418; Kelch_4; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PIRSF; PIRSF036363; PPP_BSU1; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004273};
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000001058}.
FT DOMAIN 656..661
FT /note="Serine/threonine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS00125"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 429..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 843..896
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 896 AA; 96538 MW; 794AEF95530CFEEA CRC64;
MDSDLRPSPV PRPRVFPVVG TAPGPRCGHT LTAISGPEGD LSKAKLVLFG GATALEGSSG
KSEGAQSTPG SAASGRALFA GIRLAGATND VHIFDVRTGK WEKTTPAGEP PSPRAAHAAA
AVGNMVVIQG GIGPAGLASE DLHVLDFTDP DRPRWHRVLV SGPGPSARYA HTLSLVANRF
LVAMGGNDGK STLGDAWALD TSEKPYAWRK ITDAGEMPSP RMYATAAARS DGLLLLCGGR
DVGGTPLGDA YGFARHRDGR WEWHSAPGAM PTGRYQHGAV FVGNRLHISG GAVGGGRMVD
EGTSTVVLDT THGCWVTPTS VASGEDFTRR CRHAVASVGP FVFIYGGLKA RWYGSQLLDD
LLVADDSNGT ELSIFDPRSS AWQQYMESMH GNAAASRMLE KAAAEEAAAA AALNVRRVSA
MEDLRCVDEQ LDGSGNGAGG SRTSDSPSTN RSSSPDVSLG KDHVPGTTPY TPDVKLWHRA
VVVHQENSLR GLVRQLSIDQ LDNEGRRVSI YENGGPGGAK EKSPLFTRSM SVTGVHKRVI
NELLRPRTWK APEDRRFLLN ASEIEELCNN AESIFREEPT VLNVGAPIKI FGDLHGQFGD
LMRLFEEYGT PSTAGDITYI DYLFLGDYVD RGSHSLETIC LLLALKIEHP RSVHLIRGNH
EAHDINALFG FRLECLERLG DEPGVFVWRR INELFNYLPL AAIIENKILC MHGGIGRCIH
KVDQIAELKR PITMEDGGPV LMDLLWSDPT TNDGVQGVQP SPRGPGLVTF GPDRVKEFCK
NNNLQMIVRA HECVMDGFER FAQGHLITLF SATNYCGTAG NAGAILVLGR DLVMVPKLIH
PLPPNTPHTP DSTGGLDEDP PTPHPANDTW MQSINDERPP TPPRGRPHMG SSLEYF
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