ID A0A1W0A4D9_9STRA Unreviewed; 2624 AA.
AC A0A1W0A4D9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Serine/threonine-protein phosphatase {ECO:0000256|RuleBase:RU004273};
DE EC=3.1.3.16 {ECO:0000256|RuleBase:RU004273};
DE Flags: Fragment;
GN ORFNames=THRCLA_02685 {ECO:0000313|EMBL:OQS05137.1};
OS Thraustotheca clavata.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Thraustotheca.
OX NCBI_TaxID=74557 {ECO:0000313|EMBL:OQS05137.1, ECO:0000313|Proteomes:UP000243217};
RN [1] {ECO:0000313|EMBL:OQS05137.1, ECO:0000313|Proteomes:UP000243217}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 34112 {ECO:0000313|EMBL:OQS05137.1,
RC ECO:0000313|Proteomes:UP000243217};
RX PubMed=25527045; DOI=10.1093/gbe/evu276;
RA Misner I., Blouin N., Leonard G., Richards T.A., Lane C.E.;
RT "The secreted proteins of Achlya hypogyna and Thraustotheca clavata
RT identify the ancestral oomycete secretome and reveal gene acquisitions by
RT horizontal gene transfer.";
RL Genome Biol. Evol. 7:120-135(2014).
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|RuleBase:RU004273};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the PPP phosphatase family.
CC {ECO:0000256|ARBA:ARBA00008294, ECO:0000256|RuleBase:RU004273}.
CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha subunit
CC family. {ECO:0000256|RuleBase:RU000677}.
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:OQS05137.1}.
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DR EMBL; JNBS01000499; OQS05137.1; -; Genomic_DNA.
DR STRING; 74557.A0A1W0A4D9; -.
DR OrthoDB; 46665at2759; -.
DR Proteomes; UP000243217; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0017018; F:myosin phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 2.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 2.30.30.190; CAP Gly-rich-like domain; 1.
DR Gene3D; 1.10.238.10; EF-hand; 3.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 1.
DR HAMAP; MF_01988; Succ_CoA_alpha; 1.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR036859; CAP-Gly_dom_sf.
DR InterPro; IPR000938; CAP-Gly_domain.
DR InterPro; IPR010402; CCT_domain.
DR InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS.
DR InterPro; IPR033847; Citrt_syn/SCS-alpha_CS.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR005810; CoA_lig_alpha.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR NCBIfam; TIGR01019; sucCoAalpha; 1.
DR PANTHER; PTHR11117:SF2; SUCCINATE--COA LIGASE [ADP_GDP-FORMING] SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR11117; SUCCINYL-COA LIGASE SUBUNIT ALPHA; 1.
DR Pfam; PF01302; CAP_GLY; 1.
DR Pfam; PF06203; CCT; 1.
DR Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF13499; EF-hand_7; 3.
DR Pfam; PF00549; Ligase_CoA; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01798; SCOASYNTHASE.
DR SMART; SM01052; CAP_GLY; 1.
DR SMART; SM00881; CoA_binding; 1.
DR SMART; SM00054; EFh; 6.
DR SMART; SM00156; PP2Ac; 1.
DR SUPFAM; SSF74924; Cap-Gly domain; 1.
DR SUPFAM; SSF47473; EF-hand; 2.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 1.
DR PROSITE; PS50245; CAP_GLY_2; 1.
DR PROSITE; PS51017; CCT; 1.
DR PROSITE; PS00018; EF_HAND_1; 6.
DR PROSITE; PS50222; EF_HAND_2; 6.
DR PROSITE; PS00125; SER_THR_PHOSPHATASE; 1.
DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1.
DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Hydrolase {ECO:0000256|RuleBase:RU004273};
KW Ligase {ECO:0000256|RuleBase:RU000677};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000243217};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 310..353
FT /note="CCT"
FT /evidence="ECO:0000259|PROSITE:PS51017"
FT DOMAIN 1765..1797
FT /note="CAP-Gly"
FT /evidence="ECO:0000259|PROSITE:PS50245"
FT DOMAIN 2340..2375
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 2376..2411
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 2453..2488
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 2489..2524
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 2547..2582
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 2587..2622
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 17..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 855..930
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1278..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..79
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 111..139
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 859..874
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 883..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1287..1315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OQS05137.1"
SQ SEQUENCE 2624 AA; 297140 MW; A078298E6B4869C6 CRC64;
TQFKYRKMES QLLDLQAQLA MNSAPTTAPS KARPPPPFQR APLSYMHPEA PSTFNSARVY
APPPPPQELA RPMYPPPEET SAPAQQAQAP PSRPAKSSSG RYFPKGYGQP YEHTKSSQPL
PQTTTYAQHS SSNRHQQIGH HVATLPPPSS HRGTGPVNYR PSGPFEFPKH NMPFPPRTQV
EPRPLMTPPP TLAPLTTRAP MQEETLPHTH ALKGPMPVQT PPRSYRPYGD TSNEEVKIKP
DVDMNENNEQ ERKTWTESSV YQRTQEADSD AADVLTSIRQ SDRPVPRLSL TPRSDLSDIK
KIGVYTPRSR RLLLERYHLK RAKRLTRQKW FKYPVRKTLA DSRPRVKGRF VKNDELDESP
SQSPPTEDPY ETKPPIVVPT DFDYIQAFAN CVKDTQSSVE DVVADIVSQK QRQGELIAWD
TWTMDLEHSL IALLPKEYVS SPFPAIFAEL LYILGDAEEE SSQPNYCKAL QAAAIYVAIC
LSLYTSLDPP NVYANEDDLS PIVRYYLASI EEMYRVAPKV ERCHTFAFMK SIVDGIAAVI
CTGFENGRVI VYLIIQMITS CILVPMDLPR QNGPWLTSQV QLAHFLIELF QLGVLQNVRN
GTKLSTWLPA ILHCFRRRVQ RKYIMSSIQL ELSTYQYNQV LVDSMPLQYL NLKLNNLVHR
LNQTPSPPTR IEDDDVAMHI AAIDAPDYDF ANDLVIAWTN EVIEWINQAQ WHLLASFPHK
TKETMPPKAK KSTNEMPLRM GPWTPEEVAY THRLSQDFQL GLLEDVRQGM SLRQWLSQML
NCSPMRISKK FEVEPSLRAR CNYVVNWQRI KNLTPHEAFV RKKELETLER NFKRSTESQD
YMRLMQSMRN CYDKYRKGPK KAKATKRQKA LQAKERKKSS RVRIPSSPNY NESTSSSSPA
TSSPSSPPPN YEQSSSSESE VPSSPIVKRS MDSIDHTTIL QEYLKLMQTI NSNDAIAVVQ
AKECLHRLHR QMEEQSQQVG MTPLTLGVLN AIQAGICIAD ALSLSDSSAI ETLLRLSQED
CLGWHLTISY KMPTSSESEF EFRAGPFTTE EVEYIEQVAE DFRKGLLDDL TNGTHLRQYL
STLLHCRPMR LSKRFGQPTK VLGLCIYDSK RYDGVTDKHA KRLKREKLRQ AFLKSIECQT
KYFVPIRQKR KKSMVKKIRK KRKKIVKCDM SDSEPEFQPR ISSRTLTSTS AKKQLVIKTT
PKQDQIKPKE DDTIKKETNI KTNERSIRRK SIIKDNSSDE EYVEPDHSYV EYRWEFSLRE
RKPVTRYTPD WSTTYRKKKS SLRKSSDEPP KQTSSSTISY DDVKKTIPPS TTPKPSSMDY
IFAEFPHQPS EEFVSLETID MDTFDTIKID PIGCDFFNKA DFNKLNINID NGLDMDLLHD
FITDGNVYKL QVDLKVRFGT LHFVTMLRQP KQTMRFMSAS AKVWINKETK VICQGFTGKQ
GTFHSEQAIA YGTNMVGGVT PKKGGTTHLG LPVFNTVAEA KKETGADASV IYVPPPFCAA
AIIDAIEAEI PLIVAITEGI PQQDMVKVKY ALRQQNVSRL IGPNCPGIIK PGECKMGIMP
GYIHKAGKIG IVSRSGTLTY EAVHQTTSTG LGQSTVIGIG GDPFNGTNFI DCLERFTNDP
ETEGIIMIGE IGGTAEEEAA EWLKEYGNPN KPVVSFIAGI TAPPGRRMGH AGAIVSGGKG
TAEGKFAALE AAGVTSLSID SIDCIDHLIS SRHMSKRKRI ADDELETLKR QQHEPVDGYS
VGSRVMVFGK HAAYIRYIAK ESGLVGVEMD RSVGNCDGIH NEQRYFQCKP HRGLFVRIEN
IQNFSKKDAA ACTIQVVWRR RKCLQAFRTL VLTSSWNILD NHQEQLNLKR GEQTKRASDT
LLSLAGKKQP VLVRSISTLP PNYVGPTLSW PLTLPVVLNL LEAFKNNQVL HAFFVLQALD
NAIAIFTKEA TVQRINLPSP EHKLTIVGDL HGQIQDLYCI FLANGIPSPT NFYLFNGDFV
DRGVYGAEVY LLIICFKLLY PTSVFLNRGN HECRNQNGWM GFEEEILFKY KSDDVKSQPS
TVLERFQTCF DSLPLCAMVL NKIFVVHGGL FSKPRVTINE LQSINRVREP PLHSTEPLDK
LFEEMLWSDP RQIHGRQQST RGAGVEFGDD VTVDFCSTNR VALIIRSHEC VPDGYAIQHG
GRLITLFSAS RYCGTQLNQG AYLTLGIDCK PEIQQFMAPP WSSYTQKNGC LFTTQHNDNP
NGNAQSDESS KESLEEDLLR MIAERICDHK TELFLYFSSH DTKPHGLVSR IVWAEALKSV
LKLDVPFLHY LSKLVDVDSN NMINYSKFLS RYRIENPTVD ASGWQESIIS TICKKLYRAM
GAGSIEQAFQ IFDTDSNGTI EYDEFVATLK QMDTGLSEQQ MFDLMRTADT NDDGRLDFKE
FVQRFEVIFT HVRTKIKDDS QKTILDSPQD IPVNNVDAET MVALVKIGKA FFRLEGSLLD
AFERFDTNHD GVLQADEFKA ALVQLELKFS PELFNKIWQT IDLDGGNTVD YKEFLQAFTV
QDKHIENNDS LTWQQTILQQ VSNVFYQHRI HIRSAFRLFD QDNSGSISRD EFRAGISTFN
AILDRPLSED QVEALLSHLD INGDNCISYA EFLKGFQVVG SETK
//
