ID   F8P697_SERL9            Unreviewed;       703 AA.
AC   F8P697;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit {ECO:0000256|PIRNR:PIRNR028043};
GN   ORFNames=SERLADRAFT_452105 {ECO:0000313|EMBL:EGO20964.1};
OS   Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=578457;
RN   [1] {ECO:0000313|EMBL:EGO20964.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S7.9 {ECO:0000313|EMBL:EGO20964.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA   Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA   Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA   Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA   Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA   Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "Evolution of plant cell wall degrading machinery underlies the functional
RT   diversity of forest fungi.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The B regulatory subunit might modulate substrate selectivity
CC       and catalytic activity, and also might direct the localization of the
CC       catalytic enzyme to a particular subcellular compartment.
CC       {ECO:0000256|PIRNR:PIRNR028043}.
CC   -!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit.
CC       {ECO:0000256|PIRNR:PIRNR028043}.
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DR   EMBL; GL945439; EGO20964.1; -; Genomic_DNA.
DR   RefSeq; XP_007321921.1; XM_007321859.1.
DR   AlphaFoldDB; F8P697; -.
DR   GeneID; 18816804; -.
DR   KEGG; sla:SERLADRAFT_452105; -.
DR   HOGENOM; CLU_012437_1_1_1; -.
DR   OrthoDB; 5473951at2759; -.
DR   Proteomes; UP000008064; Unassembled WGS sequence.
DR   GO; GO:0000159; C:protein phosphatase type 2A complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0019888; F:protein phosphatase regulator activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR002554; PP2A_B56.
DR   PANTHER; PTHR10257; SERINE/THREONINE PROTEIN PHOSPHATASE 2A PP2A REGULATORY SUBUNIT B; 1.
DR   PANTHER; PTHR10257:SF3; WELL-ROUNDED, ISOFORM B; 1.
DR   Pfam; PF01603; B56; 1.
DR   PIRSF; PIRSF028043; PP2A_B56; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   3: Inferred from homology;
FT   REGION          1..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          637..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..30
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..47
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..94
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..140
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   703 AA;  78807 MW;  EAA2406C27D3DB77 CRC64;
     MKGLKKSFLN RKSSQDSSSS KNKDSKSNNT PAAAPPPPPP NTAKPLPQPV PAVGGQSSSI
     PPSSSVPSPA ASPATPDRRF ASSGNSSPIP PIVVVSSDTP SDLGGGRSGQ YGSPERTSLN
     LDHGGNATPP RANTLNRLRS GPRDTIPIVG KPPRKQRSSR FVVTEKVDIE RLPPFAETPP
     SERSQLFIKK LHQCRVLFDF NDASAELKGK QIKAQTLHEM LDYITTQRGV ITENIYPEVV
     NMFATNLFRS IPPPVNPTGD AFDPEEDEPV LELAWPHLQI VYEFFLRFVE SPDFNTNLAK
     RYIDQPFVLN LLELFDSEDP RERDFLKTTL HRIYGKFLNL RAFIRRSINN VFYHFVYETE
     RHNGIAELLE ILGSIINGFA LPLKDEHKTF LTRVLIPLHK VKSLSLYHPQ LAYCVVQFLE
     KDPSLAEEVM LGLLKYWPKV NSPKEVMFLN EVEEVLDVTD PVEFQKIQTS LFQQLARCIN
     SQHFQVAERA LLYWNNEYVV NLMSDNLAII LPIVFPALYT NSKSHWNRTI HGMVYNALKL
     FMEINPDLFD ETTQHYKQRK IEEQQHAVDR YDQWQKMREK AIENAGGKLP QGFVEIEHAP
     PPPPSAADDS DILELSMELN AVSIDGEVPG DLDESGIERV PMADPGLDRP FPEVSGEHSP
     VSQSPHVRRK SVLPVDPSVI RDLQAHRSLD DAVVSGGVRT NGA
//