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Database: UniProt
Entry: G4UGZ6_NEUT9
LinkDB: G4UGZ6_NEUT9
Original site: G4UGZ6_NEUT9 
ID   G4UGZ6_NEUT9            Unreviewed;      1548 AA.
AC   G4UGZ6;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=PP2C-domain-containing protein {ECO:0000313|EMBL:EGZ74588.1};
GN   ORFNames=NEUTE2DRAFT_163591 {ECO:0000313|EMBL:EGZ74588.1};
OS   Neurospora tetrasperma (strain FGSC 2509 / P0656).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=510952 {ECO:0000313|EMBL:EGZ74588.1, ECO:0000313|Proteomes:UP000008513};
RN   [1] {ECO:0000313|EMBL:EGZ74588.1, ECO:0000313|Proteomes:UP000008513}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=strain FGSC 2509 / P0656 {ECO:0000313|Proteomes:UP000008513};
RX   PubMed=21750257; DOI=10.1534/genetics.111.130690;
RA   Ellison C.E., Stajich J.E., Jacobson D.J., Natvig D.O., Lapidus A.,
RA   Foster B., Aerts A., Riley R., Lindquist E.A., Grigoriev I.V., Taylor J.W.;
RT   "Massive changes in genome architecture accompany the transition to self-
RT   fertility in the filamentous fungus Neurospora tetrasperma.";
RL   Genetics 189:55-69(2011).
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- SIMILARITY: Belongs to the PP2C family.
CC       {ECO:0000256|RuleBase:RU003465}.
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DR   EMBL; GL891107; EGZ74588.1; -; Genomic_DNA.
DR   STRING; 510952.G4UGZ6; -.
DR   eggNOG; ENOG502QURR; Eukaryota.
DR   HOGENOM; CLU_246490_0_0_1; -.
DR   Proteomes; UP000008513; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004722; F:protein serine/threonine phosphatase activity; IEA:InterPro.
DR   CDD; cd00143; PP2Cc; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR006644; Cadg.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR015655; PP2C.
DR   InterPro; IPR000222; PP2C_BS.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   PANTHER; PTHR13832:SF565; AT28366P-RELATED; 1.
DR   PANTHER; PTHR13832; PROTEIN PHOSPHATASE 2C; 1.
DR   Pfam; PF05345; He_PIG; 3.
DR   Pfam; PF00481; PP2C; 1.
DR   SMART; SM00736; CADG; 2.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00332; PP2Cc; 1.
DR   SUPFAM; SSF49313; Cadherin-like; 3.
DR   SUPFAM; SSF81606; PP2C-like; 1.
DR   PROSITE; PS01032; PPM_1; 1.
DR   PROSITE; PS51746; PPM_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003465};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912,
KW   ECO:0000256|RuleBase:RU003465};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008513};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..1548
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003469668"
FT   TRANSMEM        465..491
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1132..1404
FT                   /note="PPM-type phosphatase"
FT                   /evidence="ECO:0000259|PROSITE:PS51746"
FT   REGION          432..459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          544..566
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          775..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          835..866
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          902..1005
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1440..1459
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1499..1548
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        434..454
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        846..866
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        902..948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        957..995
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1440..1456
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1504..1521
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1548 AA;  166211 MW;  7AF90F526E1FF920 CRC64;
     MASLLRLLAS LLFVAVSNAA PGVYFPISSQ IPPIARIGEP FSFIFSKSTF TSTTSITYSL
     ANSPHWLSID SDARKLYGTP KEADVGLGDR VNVPFGLVAT DETGSTTLDI TLVVSRKAGP
     KLDIPFNQQI PGFGFFSNPY TILSPPMNQF SFVLDPKTFS VPSDKPLTYY AVMSDNTPLP
     AWISFDAGKL AFSGQTPAFE ALVDPPQTFE FQLLATDTPG FADASLRFNI VVGNHRVTAD
     QTTVVINATA GKSFSYDGLR GNIDVDGQPM PSGDGIIVVS TFNTPSWLTL DMDSLHITGT
     PPLTAKSTNF TLTLEDSFAD RFNLTVMVQV SGTQAQIFGM LKEELPVIQA HAGEHISFEL
     DPFLKDPDGT EIVVDDDTSP SWIRVREGTI FGDVPKSSKD SIVSATIRLT SKASGASESV
     LLSVHMLADT GDAVDTTDTD STPGSTSTGD LGGTKPTQKH APTPIGLILL VTILPGLLLL
     GALMGMLVCC LRRRREAKRP KLSTRDIPGP LPGTFTINVT GPDGQSSMEH ITGPYNTQST
     ISQMSLAEQD RKSDPESGIS RHQSFDADVP RPLSTVRMLP TNEELLPASS SLLDITGSPL
     MSGAITGTPR NRRHERTQTL LSHISETSYY EEHSSGITIE NTLEFLGNSN TRGSFRDGVE
     VDIPCLGDLS SIQPTPNSAY TGESYWSKLG SGPSVHNRSP AIGSVHNDPT GAARTQPAML
     VRKLVWPWFK GRVISIKGVA EKFGEAAKTT LAGLPSLSSV QASLHDKTPD ISLLSNKQSE
     SSDIPDFPSP PQGTKRPIMT KYARPVTRRA VGTGRIVIPR QRLVSTKVEV VGGPTEDLYK
     PAEDKKQASP TSSFDRPSRN SLGISYADMA SNSPFHQSST WSTIPSSHEW HDETLQSLEN
     ADSVLPSSSL RRSRSASQPN WAPYKDSLSN INDGASSKYP QSQWSFAPIP RPQPLGDASS
     IASQGLSNSV SGHARAPTLS SVGFSKAPSS FRLDGNENTH TDDAEKENKW AGGTSGFLNA
     HLHLSTRTGT LPLPGCTSIL PPAKEPNLAN NLLQSTPEQQ TTTCTSTVPF LDSKARSKFP
     LSVTSLVADY SSTTPTPTPP PTTTHTDIIM GQTLSEPVVE KASATGGDER LIYGVSAMQG
     WRISMEDAHT TVLDLLANNP KEAKDHSQKL SFFGVFDGHG GDKVALFAGA NIHDIIAKQD
     TFKTGNYEQA LKDGFLATDR AILNDPKYEE EVSGCTACVG LITDDKIFVA NAGDSRSVLG
     VKGRAKPLSF DHKPQNEGEK ARITAAGGFV DFGRVNGNLA LSRAIGDFEF KKSAELAPEQ
     QIVTAYPDVM VHDLADDDEF LVLACDGIWD CQSSQAVVEF VRRGIAAKQD LDKICENMMD
     NCLASNSETG GVGCDNMTMI IVGFLRGRTK EEWYEEIAKR VANGDGPCAP PEYAEFRGPG
     VHHNFDDSDS GYDLEDNGNK GKPFGMGGYK GRIIFLGDGT EVLTDADDTE MFDNVEEDKD
     LASQVSKSPS SITTNDQDQK EQAAVAAAAA DNSTQNAKKE ETSSPAKA
//
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