ID A0A178A7V5_9PLEO Unreviewed; 1163 AA.
AC A0A178A7V5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=MAGE-domain-containing protein {ECO:0000313|EMBL:OAK93785.1};
GN ORFNames=IQ06DRAFT_340989 {ECO:0000313|EMBL:OAK93785.1};
OS Stagonospora sp. SRC1lsM3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Massarinaceae; Stagonospora.
OX NCBI_TaxID=765868 {ECO:0000313|EMBL:OAK93785.1, ECO:0000313|Proteomes:UP000077206};
RN [1] {ECO:0000313|EMBL:OAK93785.1, ECO:0000313|Proteomes:UP000077206}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lsM3a {ECO:0000313|EMBL:OAK93785.1,
RC ECO:0000313|Proteomes:UP000077206};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; KV441729; OAK93785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178A7V5; -.
DR STRING; 765868.A0A178A7V5; -.
DR InParanoid; A0A178A7V5; -.
DR OrthoDB; 124870at2759; -.
DR Proteomes; UP000077206; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd16039; PHD_SPP1; 1.
DR Gene3D; 1.10.10.1200; MAGE homology domain, winged helix WH1 motif; 1.
DR Gene3D; 1.10.10.1210; MAGE homology domain, winged helix WH2 motif; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR041898; MAGE_WH1.
DR InterPro; IPR041899; MAGE_WH2.
DR InterPro; IPR002190; MHD_dom.
DR InterPro; IPR037869; Spp1/CFP1.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46174; CXXC-TYPE ZINC FINGER PROTEIN 1; 1.
DR PANTHER; PTHR46174:SF1; CXXC-TYPE ZINC FINGER PROTEIN 1; 1.
DR Pfam; PF01454; MAGE; 1.
DR Pfam; PF00628; PHD; 1.
DR SMART; SM01373; MAGE; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR PROSITE; PS50838; MAGE; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000077206};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT TRANSMEM 172..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 51..111
FT /note="MAGE"
FT /evidence="ECO:0000259|PROSITE:PS50838"
FT DOMAIN 790..841
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..339
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 458..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 672..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 887..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..335
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..526
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 576..590
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..617
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 638..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1121..1138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1145..1163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1163 AA; 127594 MW; EA4DAAC0B07B8F5F CRC64;
MPPRTGRRRA PVEEETPPPT QTQRRRRDAT PDEDEDVDMD DQEQGGGSGS LEQLSKGLVR
YALSCEYSRK PIKRQDINEK VLGSHARLFK DVFSRANTEL MEVFGMQLVE LPKAERVTMR
QKRAAAASES QSKSSSLWIL QTILPEQYRI PEIIGPSRPI ESDEINREDS YVGLYTMVIA
LITIAGGMIA EGKLDRAFRR MNADNSTPLG TKDKTLALMA KDGYIVRVKD NSSGEETVDY
IVGPRGKVEV GRDGFAKFVR TIYGEEADQE ELERSIERTL NVADAFNSSG VPAEPAAGAS
QTAGRKRGRP RRDEDDDGST TELRAKLRHD SRLHHQPSTT WAGCRGRIGP CSMQYCPRDA
REGTRCSARV VPRPSSAAAL AHCPHHLSPP EPIVPRPSRN VQQPLSAVSM SSINALLNHE
AASERRPSMT MSSPQHFTQT TTYEAADALT TLATLGSGQQ YAPAPARELP SPTASASAPR
RTSSFGSHHA PVEPSPPLDQ PPVHSPTLDH YHHGSRSPEE LKRRQSLLSR SSPAPVLAPI
QNLSSALQEQ MADPPASTPI GEDMSQIVPP SSRSSEGGEA ERDSTQDREP AFARNEPTTS
QIRKPDSPSQ APQSLANDAP LPSPRPFIKD EPAGTPREST PAASTSQLDQ QTSNAAEMLD
SDTLKALEIA KQADLGLRTK RNASITDRMP SPVDSKPAVA PSKKRPAPSS ASTVKKKGTA
KAMKPSKKRK IESEEPGRSV TPTSRNPKSS KGGKKGSQAG TPGLESSPAP DNSSQAHASD
DDGESSEDHN LYCICKKPDN HKWMIGCDGG CDDWFHGDCV NMKQADEELV DRFICPQCEE
NGRGHTTWKP MCRRDGCRKP ARVNKDRESK YCTDACGTLF MTEQLQRTAG AKGANGTRDR
SKKSKKKGGK NEDDAEEEEP TPLGGVLRSK DLKALVDASP NIQAFKNLGT GVLTPPQTAS
PNRTSFSGID GYAFTASETE RLNALHNEKT QLNERLEALK DREKFVSMAK EQAVRVAERE
KIKLKEFCGY DSRLSWSDAE FLAWRHKKHG QAAFKFNTLS PTAEQVASIS GADSDADEVK
ESVCLKKRCP KHPQWQKLNL QDARFEELEV VEAIRECEKE EKSVKERARR RGAKDAISRE
ITAGEGGSGE ERNRNREGWV EVV
//
