ID A0A0D2CU28_9EURO Unreviewed; 1762 AA.
AC A0A0D2CU28;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KIW68706.1};
GN ORFNames=PV04_04630 {ECO:0000313|EMBL:KIW68706.1};
OS Phialophora macrospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1851006 {ECO:0000313|EMBL:KIW68706.1, ECO:0000313|Proteomes:UP000054266};
RN [1] {ECO:0000313|EMBL:KIW68706.1, ECO:0000313|Proteomes:UP000054266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 27337 {ECO:0000313|EMBL:KIW68706.1,
RC ECO:0000313|Proteomes:UP000054266};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Capronia semiimmersa CBS27337.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KN846958; KIW68706.1; -; Genomic_DNA.
DR STRING; 5601.A0A0D2CU28; -.
DR HOGENOM; CLU_000991_0_0_1; -.
DR OrthoDB; 48111at2759; -.
DR Proteomes; UP000054266; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15518; PHD_Ecm5p_Lid2p_like; 1.
DR Gene3D; 1.10.150.60; ARID DNA-binding domain; 1.
DR Gene3D; 2.60.120.650; Cupin; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR001606; ARID_dom.
DR InterPro; IPR036431; ARID_dom_sf.
DR InterPro; IPR003347; JmjC_dom.
DR InterPro; IPR003349; JmjN.
DR InterPro; IPR013637; Lys_sp_deMease-like_dom.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR004198; Znf_C5HC2.
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; PTHR10694; LYSINE-SPECIFIC DEMETHYLASE; 1.
DR PANTHER; PTHR10694:SF33; LYSINE-SPECIFIC DEMETHYLASE LID; 1.
DR Pfam; PF01388; ARID; 1.
DR Pfam; PF02373; JmjC; 1.
DR Pfam; PF02375; JmjN; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF08429; PLU-1; 1.
DR Pfam; PF02928; zf-C5HC2; 1.
DR SMART; SM01014; ARID; 1.
DR SMART; SM00501; BRIGHT; 1.
DR SMART; SM00558; JmjC; 1.
DR SMART; SM00545; JmjN; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF46774; ARID-like; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS51011; ARID; 1.
DR PROSITE; PS51184; JMJC; 1.
DR PROSITE; PS51183; JMJN; 1.
DR PROSITE; PS01359; ZF_PHD_1; 2.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054266};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 82..123
FT /note="JmjN"
FT /evidence="ECO:0000259|PROSITE:PS51183"
FT DOMAIN 147..240
FT /note="ARID"
FT /evidence="ECO:0000259|PROSITE:PS51011"
FT DOMAIN 469..519
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 611..777
FT /note="JmjC"
FT /evidence="ECO:0000259|PROSITE:PS51184"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 249..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1010..1030
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1485..1762
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..80
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..325
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..418
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 425..441
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1507..1535
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1544..1588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1606..1620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1673..1688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1736..1762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1762 AA; 198554 MW; 9509FD94BC5A1B94 CRC64;
MVAPPSTGGV APQAATAKQS SSAIPGPASR MAGGPAASMA TPLFPYSARR AQPLDMRSVE
RKGHPSSRDP PTRKRPHDLL EAPTFRPTEA EFRDPMEYIR SISEKASKFG ICKIIPPESW
NPDFAIDTER FHFRTRRQEI NLVEGGNRTN LNYLDQLAKF HKQYGAHLNR FPSVDKRPLD
LYKLKKAVEV RGGFERVCKD KKWAEIGRDL GYSGKIMSSL STSLKNSYQR WLYPYEEWLR
HAKPGVQEQL QNEQGGSYSP SVMPPQPMLN HMSHPQSAPP VMGINSPNLQ PAMSLPPQMQ
HTPGPSQQPP PPPSIPPPTP PTQPRPVSSS GFTAVNSGFT AVNGPSGFTA VNTLPPPVVK
KEVNGAPPPN QSPAPSFPPI NGPTITTIRN TASPMPNGTS NPLKRTLSHD SLNGESGSEG
MNGEADGPDG RRSKRPKKDV MPTIPGNHIP AMRPTTPQVR AKPVQRRHGE KCEKCGKSDN
KENILVCDSC ELGYHRNCVD PPVISLPEYD WHCPKCLVGT NDYGFEEGSI YSLKQFQEKA
NNFKEHYFSA RMQFDPVTNT QRKPTEDDVE REFWRLVEDI TESVEVEYGA DIHSTTHGSG
FPTVEKNPLN PYSKDLWNLN VMPFLEESLF RHIKGDISGM TVPWLYVGMC FSTFCWHNED
HYAYSANYQH FGATKTWYGI PGKDAYRFED AMRKAVPELF ETQPDLLFQL VTILPPNQLR
KAGVEVYALD QRAGQFVITF PQAYHAGFNH GFNFNEAVNF APADWEPFGE AGVQRLQEFR
RQPCFSHDEL LFTAAASDTT IKTSKWLGPA LERTRNRELA ERENFVAMHK RHFPHDDCTF
DSLAEQPPEA CGLTIKIENT ELEEEEYQCC YCKAFSYLSQ FRCHRSGKVT CLLHPEVADC
CADTPEERLR GSNHSLLLRY TNHELSGIVQ KVVDKANVPE AWEAKFDALL ADDARPALKA
MHTLLSEGEK IPYPLKGLDD LADFVKKCDQ WVDEANLYLL RKQQNRRKNE KAWRRSSLRT
GKADEKDTEP QLTLDRMKAL IEDGEQLGFS ALQLENLKDK VKMIDEWRAN VKRILSGLNN
PTADELETIL DEGRGFMAAM PELTSLEQVH AQTHWLEEVR QVQKEVQSKT LDECKELLKR
ASELETAPQM PEVLFLTEVV RQGEFWEIKA REVMGAEDVH YPQLESLHAQ TQTQAFPVNK
DTLEQMDAIL AKNREAKRQI ITLVERSHDP DFRKRPMYAH VRDVVKSLED LNGKPHGAAD
LEKELRRHED WMRKGKKLFG KANAPLHILE QHMKFVEEKN SFCFDLNDTF RPPVEPASRE
ATPTDGHEKG ALGDEEKPVF CICRQPEAGL MIECEICHDW YHAKCLKLAR GKVKECETFT
CPICDWRVKI PRDAARPKLE DLQSWQDEIQ DLPFQPEEEE LLKRIIDKAQ AFRDFLMQYT
SGNQLCRTIE EMPEMLFYLR KIEGAEVLLA FETNVFRQEL HKWQPIAPEP PPILDQSLST
RKPRPTKQQK LMKELGVEKP EDLPPHLRTK TYVRRKTQES FVTGPLLPKP STQSPSAPGS
AASPGQNGNA DGSSAMQRQE SNDNAGPSRT YEAGFLSETP YADHRPSPFS PNSPSLFSPT
RDPPQDGLRD PMMPTFGGDN AGGRNHDPSF PLFRPNAGLG LDAEDDLRNG LANASESVPN
STRDASPPVF ESDNMFMDMT NPDGDASNDA VPSLEQEASH ASEALDMIRS ASHDSANDNV
ELEDGDNVSK HFDDFINGDE QT
//