ID A0A151GJG7_9HYPO Unreviewed; 717 AA.
AC A0A151GJG7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit {ECO:0000256|PIRNR:PIRNR028043};
GN ORFNames=DCS_04280 {ECO:0000313|EMBL:KYK57273.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK57273.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK57273.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK57273.1,
RC ECO:0000313|Proteomes:UP000076580};
RX PubMed=26975455; DOI=10.1038/srep23122;
RA Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA Molnar I., Lin M.;
RT "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL Sci. Rep. 6:23122-23122(2016).
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}.
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:KYK57273.1}.
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DR EMBL; LAYC01000002; KYK57273.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151GJG7; -.
DR STRING; 98403.A0A151GJG7; -.
DR InParanoid; A0A151GJG7; -.
DR OrthoDB; 5473951at2759; -.
DR Proteomes; UP000076580; Chromosome 02.
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; 2.
DR PIRSF; PIRSF028043; PP2A_B56; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000076580}.
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..717
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..30
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..691
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 692..717
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 717 AA; 81247 MW; 932149EF7FDDD443 CRC64;
MKRFSQRVLS RGKDAGKSSK KNKDSKDGTS SPSPRDSSNQ SPVLTPSSST STLNDIRNKP
LPPNASHGAD HGVLGQPSSL SNITQQGGMP DRFGSMGGAS SPNGGNRMTP TVVISPTPGV
SRPRRDADTA TPARCPVDFE QACSLKHWLT PTKIVQHIPP PGAAETMPHD LAPPKAGQKS
SLLIHRGIDN RDAIPEGLRT PRRQHSSRFD ISVHRELEKL PGFHEVPPNR RQELFMQKID
QCNVIFDFND ASADMKAKEI KRLALHELLD YVANNRQVIT EPMYPRVVDM FAKNLFRPIP
PPVNPQGEAF DPEEDEPVLE VAWPHIQVVY EFFLRFIESQ DFNTNIAKAY IDHSFVLQLL
DLFDSEDPRE RDFLKTTLHR IYGKFLNLRS FIRRSINNVF FQFTYETERF NGIAELLEIL
GSIINGFALP LKEEHKIFLT RVLLPLHKPK SLSMYHPQLA YCIVQFLEKD ASLTEDVVLG
LLRYWPKVNS TKEVMFLNEV EDIFEVMDPA EFAKVQEPLF HQLAKSVASP HFQVAERALY
FWNNEYFCNL VSDNVEIILP IMFAPLFENS KGHWNRYERA DPLSLSLGWH AADECRTIHG
MVYNAMKLFM EINPQLFDDC SHDYTEQQNS AAEREALRER KWAALGEQAT QRRESLGGGV
VDADPRPQAA VLPRLDEVDP ITDDNQKRLD SLKLQDASGQ RPSVHERQSS VGSTRSR
//
