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Database: UniProt
Entry: E5R137_ARTGP
LinkDB: E5R137_ARTGP
Original site: E5R137_ARTGP 
ID   E5R137_ARTGP            Unreviewed;      1114 AA.
AC   E5R137;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   SubName: Full=Meiotically up-regulated 56 protein {ECO:0000313|EMBL:EFQ97641.1};
GN   ORFNames=MGYG_00679 {ECO:0000313|EMBL:EFQ97641.1};
OS   Arthroderma gypseum (strain ATCC MYA-4604 / CBS 118893) (Microsporum
OS   gypseum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Nannizzia.
OX   NCBI_TaxID=535722 {ECO:0000313|Proteomes:UP000002669};
RN   [1] {ECO:0000313|Proteomes:UP000002669}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4604 / CBS 118893 {ECO:0000313|Proteomes:UP000002669};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
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DR   EMBL; DS989822; EFQ97641.1; -; Genomic_DNA.
DR   RefSeq; XP_003176593.1; XM_003176545.1.
DR   AlphaFoldDB; E5R137; -.
DR   STRING; 535722.E5R137; -.
DR   GeneID; 10031913; -.
DR   VEuPathDB; FungiDB:MGYG_00679; -.
DR   eggNOG; ENOG502QRAT; Eukaryota.
DR   HOGENOM; CLU_003938_0_0_1; -.
DR   InParanoid; E5R137; -.
DR   OMA; DRWVMSI; -.
DR   OrthoDB; 1360556at2759; -.
DR   Proteomes; UP000002669; Unassembled WGS sequence.
DR   GO; GO:1902657; P:protein localization to prospore membrane; IEA:InterPro.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR040345; Mug56/Spo71.
DR   InterPro; IPR039486; Mug56/Spo71_PH.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   InterPro; IPR029217; Spo7_2_N.
DR   PANTHER; PTHR28076:SF1; PROSPORE MEMBRANE ADAPTER PROTEIN SPO71; 1.
DR   PANTHER; PTHR28076; SPORULATION-SPECIFIC PROTEIN 71; 1.
DR   Pfam; PF15404; PH_4; 1.
DR   Pfam; PF15407; Spo7_2_N; 1.
DR   SMART; SM00233; PH; 2.
DR   SMART; SM01316; Spo7_2_N; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50003; PH_DOMAIN; 1.
PE   4: Predicted;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002669};
KW   Transferase {ECO:0000256|ARBA:ARBA00022676}.
FT   DOMAIN          930..1100
FT                   /note="PH"
FT                   /evidence="ECO:0000259|PROSITE:PS50003"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          104..262
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          284..338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          707..733
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          796..825
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        132..147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        180..206
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..262
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        298..327
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..378
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..729
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1114 AA;  126733 MW;  2C018859AB9F3001 CRC64;
     MDSTSPPSEQ PVPTVSHQSR SRYDHDSLEC GSFTAQKLKH ASPDHLHITN RRFFIGPLPK
     GWGQHRRRHW YKSCLGIRDY SSRNQTFSAD ISVGYQRQLT RYMGSSSTTR FKPSFPQPDD
     VEAEDEDEND QTSPAMNGQT TGESSRGNHV GPKIIKSVEA GRQAQRQDDD TGGFGLSHPS
     IKRLQTQHRP KNSPIATNSS PVVRMSSDEN VPEAYFTAPD AEPQSATPEA NPLPRNSTTS
     QELRSPENDH LQSSSSLPYR NSYATTGASA VSTTDGVGLE AEVGSQSSLI SHNKQQSSSI
     SEDRRKSKTQ QLELQRQEPR GESDQTEAEL AKSQQPHRLI NRVISDRVRF GVEERVESGQ
     RRLQNRLGLS DDSRASRKQK RQTRRHGEVL RAEKMLVRID VTAQTVPNLY NDNASVKIET
     RPIENWREYL VVCRQGYDEQ TPYLLQFYKT RVIPQVQGAK VKRKYAHEVK LSQGQANVNL
     FSTLDKTVVV WHPTKMNGTR IFIMRARAAA HSVEWYTFIR KVLGWKQPSS LFVHAPDLDV
     SLVLQNPFER YAKDNTEESE GTLSNNTSEE QAVSTAIIRT CMNTLSDCSE WPEILDIWKK
     SENMGLAWRR YDRIEWIQGG NEERMYGTMA MRTSHDLELR PKRHYPTSTA MDSSEVLMEE
     PSPVEGFLIL LTSQQGTHRR WGKNFSRRLY LYSEDQYLCF CKPTKASTPP APKLPSTLGT
     GSSTAPETIR GSPVIYPVDP YPLEDGQIPW LRDGGNKSYA NYCDQTAYAE DRRNTNNLGQ
     AEGYFNLCRV SEIRTLSETE SRGNQGNETS SGSQEPVRNH PTTGSFSLAD QDHVFELQLD
     DGLVVRLRAY NTKTRDVWIH RLRQLTMYWK ARVKADITTL KSVRQHNLEK LDIDEAQESI
     IGQFAQKWEV ARADASPELF NVCGPSGCRA IKRSGYLYRK PRRRGSFAKC DVILAEGQLL
     IFQDSVRTFS GEQVPHTHQS KQNILDLRDC YLYSGVLTNA DLLYHSQTFD NNHPGHNSTP
     RIYPSDGWTS ADEDTATTFV IWNNTRRILF HGEEEGDGKQ KKRKWRNVSR LGASGRSIVF
     KARSRAERDM WVLAIETEID RLQQEEDMRI VPEK
//
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