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Database: UniProt
Entry: A0A2G8SNN8_9APHY
LinkDB: A0A2G8SNN8_9APHY
Original site: A0A2G8SNN8_9APHY 
ID   A0A2G8SNN8_9APHY        Unreviewed;      1403 AA.
AC   A0A2G8SNN8;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Paladin {ECO:0000256|ARBA:ARBA00040012};
GN   ORFNames=GSI_02098 {ECO:0000313|EMBL:PIL35372.1};
OS   Ganoderma sinense ZZ0214-1.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Ganoderma.
OX   NCBI_TaxID=1077348 {ECO:0000313|EMBL:PIL35372.1, ECO:0000313|Proteomes:UP000230002};
RN   [1] {ECO:0000313|EMBL:PIL35372.1, ECO:0000313|Proteomes:UP000230002}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ZZ0214-1 {ECO:0000313|EMBL:PIL35372.1,
RC   ECO:0000313|Proteomes:UP000230002};
RX   PubMed=26046933; DOI=10.1038/srep11087;
RA   Zhu Y., Xu J., Sun C., Zhou S., Xu H., Nelson D.R., Qian J., Song J.,
RA   Luo H., Xiang L., Li Y., Xu Z., Ji A., Wang L., Lu S., Hayward A., Sun W.,
RA   Li X., Schwartz D.C., Wang Y., Chen S.;
RT   "Chromosome-level genome map provides insights into diverse defense
RT   mechanisms in the medicinal fungus Ganoderma sinense.";
RL   Sci. Rep. 5:11087-11087(2015).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000256|ARBA:ARBA00004514}.
CC   -!- SIMILARITY: Belongs to the paladin family.
CC       {ECO:0000256|ARBA:ARBA00037958}.
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:PIL35372.1}.
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DR   EMBL; AYKW01000003; PIL35372.1; -; Genomic_DNA.
DR   STRING; 1077348.A0A2G8SNN8; -.
DR   OrthoDB; 49159at2759; -.
DR   Proteomes; UP000230002; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd14496; PTP_paladin; 2.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 3.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR23339:SF96; PALADIN; 1.
DR   PANTHER; PTHR23339; TYROSINE SPECIFIC PROTEIN PHOSPHATASE AND DUAL SPECIFICITY PROTEIN PHOSPHATASE; 1.
DR   Pfam; PF14566; PTPlike_phytase; 3.
DR   SMART; SM01301; PTPlike_phytase; 3.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 3.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000230002}.
FT   DOMAIN          762..834
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          53..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          324..343
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1403 AA;  157623 MW;  20203B9E84F57D11 CRC64;
     MATNFRPPDG GVMRPLSAPP QSTSEAIATR RPPEDDLRRR LLSSSLLDGS IDLPETPPLD
     LMPQLQRSGP SIVKTRSGSV LSRGFILKTD HYPSGRALDL DINVHGAPNF RAPRQGNLNV
     YGVAQPRTQG LRAILSLLRC RPNIPNATHV VWFCTREEPI VYISGRPFVL RDASEPRRTL
     KLSDRAENLE AIELRLKNDI LSEAAKFGGL VLTHNEVASD SGEGAVLPTW TAVDTNNVRT
     QRELMENMRK DGWNVEYHRI PISPERPIED NYLDAYLRVI KETDALSTAL VFNCGMGAVR
     TTFAMVAACI IRRKQLIDRG LDDPYSARSA GSRSGISTPS GMSPPTNAKI LQSLEQASAQ
     QDLNRSLLRI TYILQQQLDT KNTQSAIELL LSQPSLLEAL QKAHMGNYGI VLSLLGCLEH
     GIKSKKLVDK VIDVCDHVVN LREEIFLNRI RYSLTTAVDD KERDDFLSRA VKALEKYFFA
     IAFANYVEMQ DEFQQSFADW LKARTEISNQ ITFLRKSHGS RLNVFAPIND LSTLSRSGVD
     RRLLLPGQQN HVAIAGGQIL GDEYSDHVVK TRSGIILREG TLLKSDQWLS RSSVVSHGVR
     GAINFRNIPG TNIYALGQPT LEAIDEVVCR IHDAHPEATR IVWITLREEP LVYVNGAPYC
     LRRERFSLRN MKDYGGISSS RLEVLEERFR DDVVNEVHSF GGRLLLHTET PDGSVIPIWE
     EVNSDNVLVL KDVMAERKHI AEYLELSYAR IPITAERPPD FTDLSELIEV MIRSNATNAP
     IVINCQLGRG RSTLTAVILV LIKQWLAMAT RLRDPSTPSR LQRSITMTSM TDMVPHHTPR
     QSYQIINNLL RVIRKGPMVK LAVDDAIDQC AEVFNLRDSI EEARSQAELA TDEQQRRSHA
     HRGLNNLRRY FELIIFQAYL QSAEPDTIAT HESFESFVKS RPVIKTFEKE LLSEDLNTLK
     PLERVDVSGG DVAHPDEVQQ VVANRSGSIL SASTILKSDF FSNLQKMSLP ERIDGAPNFR
     RAPLSLRLVA TPVSSPGANG ADRFDFVAGD NDKWVCGSGM PTVDGLRRAL ERVNAHPEGN
     HWVYWTSLRE EPVIYVAGRP HVLRLVDKPL ENVEATGVTT AVVEAMEENL KRDVIREVRA
     GEGRILLHDE VEERPGVFSI IPIWEHVEEK DIMTPSDVYN LMVREGYKVD YGRVAVTDEQ
     APLPGALSQL LMRVRTGLQS GRPADFVFNC QMGRGRTTSG MVTACLIATT MTWEHEKEES
     LQEDEDQSAN ALEQYDSIDG PSEEEAYLQG EYKVILQLVS VLSHGKLAKR LTDRAIDQMQ
     DVQNLRKAIY DYKLKVSACE KGSAKERKLM SIGVNYLYRY GTLIVFANYL IEVREGMSAE
     VNFPEWLQER REITMLLGRR SLD
//
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