ID A0A067CT47_SAPPC Unreviewed; 1015 AA.
AC A0A067CT47;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=protein-tyrosine-phosphatase {ECO:0000256|ARBA:ARBA00013064};
DE EC=3.1.3.48 {ECO:0000256|ARBA:ARBA00013064};
GN ORFNames=SPRG_05166 {ECO:0000313|EMBL:KDO29977.1};
OS Saprolegnia parasitica (strain CBS 223.65).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Saprolegnia.
OX NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO29977.1, ECO:0000313|Proteomes:UP000030745};
RN [1] {ECO:0000313|EMBL:KDO29977.1, ECO:0000313|Proteomes:UP000030745}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO29977.1,
RC ECO:0000313|Proteomes:UP000030745};
RX PubMed=23785293;
RA Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA Russ C., Tyler B.M., van West P.;
RT "Distinctive expansion of potential virulence genes in the genome of the
RT oomycete fish pathogen Saprolegnia parasitica.";
RL PLoS Genet. 9:E1003272-E1003272(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004170}.
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DR EMBL; KK583203; KDO29977.1; -; Genomic_DNA.
DR RefSeq; XP_012199160.1; XM_012343770.1.
DR AlphaFoldDB; A0A067CT47; -.
DR STRING; 695850.A0A067CT47; -.
DR EnsemblProtists; KDO29977; KDO29977; SPRG_05166.
DR GeneID; 24127571; -.
DR KEGG; spar:SPRG_05166; -.
DR VEuPathDB; FungiDB:SPRG_05166; -.
DR OMA; WWSALEG; -.
DR OrthoDB; 74847at2759; -.
DR Proteomes; UP000030745; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IEA:UniProtKB-EC.
DR CDD; cd00065; FYVE_like_SF; 1.
DR CDD; cd14507; PTP-MTM-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR010569; Myotubularin-like_Pase_dom.
DR InterPro; IPR030564; Myotubularin_fam.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000306; Znf_FYVE.
DR InterPro; IPR017455; Znf_FYVE-rel.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR10807; MYOTUBULARIN-RELATED; 1.
DR PANTHER; PTHR10807:SF8; PHOSPHATIDYLINOSITOL-3-PHOSPHATE PHOSPHATASE; 1.
DR Pfam; PF01363; FYVE; 1.
DR Pfam; PF06602; Myotub-related; 1.
DR SMART; SM00064; FYVE; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS51339; PPASE_MYOTUBULARIN; 1.
DR PROSITE; PS50178; ZF_FYVE; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 94..154
FT /note="FYVE-type"
FT /evidence="ECO:0000259|PROSITE:PS50178"
FT DOMAIN 100..150
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 616..995
FT /note="Myotubularin phosphatase"
FT /evidence="ECO:0000259|PROSITE:PS51339"
FT REGION 244..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..260
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 832
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-1"
FT BINDING 832..838
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR630564-2"
SQ SEQUENCE 1015 AA; 113901 MW; 411E463ADBD8FEC4 CRC64;
MRMPSSSKIN THSRMHVQTH TKEFVSISSL SDAAVALRVL CEAHSLGLEK DESDIVRRTL
KTVAYVSGKL QHRMGTLKKG AGDVGVPRVG ATPDTTSAKC AKCARSWNAF QRGHNCQACG
HLFCSRCLTP TQLPRSFGFE SPAKTCDLCR TWLAEFMSAK FEEAHLGSRK EGPAVPNAPE
ALEPLDHSPQ AFVELLKGAL EKGLSPSLSA RLQEVFEVYG GTPHAKTKAM SELKTAMTCL
LADVPEDEDD EDEDDDETAV SDTTTTTKMA FPKDALQTVL SLMLALEAVD WTLDSKDDEN
KGNDEDDEAR SSVDHRLSRD PSVALLRRET PMLEYQESTV GSNDDDDASL KSPATPPLPP
AMVEYFIVNR TETSPLFASS AKKDDRCRIE VFTYQGMIRV KSIFNMNRRF TFRISDMQLV
QLEKEYLRWT FPYRSELVLQ FQNEATKNHF CKLIQAYLTT LDPSTKLKRT LPLVPFLRGE
VKMHTQHFPA ACLTSLGEFA WRGLVLVTNY RVLVVPFESA PLVEIPLFSI LSVSRESSFG
YRSPFLLLTS KDVRTLRLDV TPDDRLLTLL HLVTKLSEST QKFQTGQPTK DSVLSLQVPH
FSFAYTMTSV TPETNGWKFA DILVEYGRQG LDTNPLLQVV ENGDGAVCDS YPPKLLFPAS
LSMGDVLAAV NFRAKNRVPL ITWQHPRNHS VLTRSSQPLL GRLLTSQSCG IDEGLIAFYK
KLSTKSSSSL YIFDARKVKA AKGNRLMGKG GVEASGQYTG AIINHLNIAN MYKMQTSYLA
LMKLCLSPEH DKSWWSALEG TRWFEHLHLV LDGAVKIARV LEFEGASVLV HCSDGWDRTC
QLVSLAQIML DPYFRTLDGF ATLVEKDWLA FGHKFMERLG GNRSKDPTRA KVSPIFLQFL
DAVYQLTTQF PTAFEFDERY LVHVANALTS GLYGTFLYDN VLQRTAARAC DKTISVWTPQ
LVSPQLFRNA SYEARPDPLW PWPGHQALKL WTGYYFQHHE VHAHNHIDEE ERQKA
//
