ID A0A178DRS1_9PLEO Unreviewed; 1988 AA.
AC A0A178DRS1;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=PHD-type domain-containing protein {ECO:0000259|PROSITE:PS50016};
GN ORFNames=IQ07DRAFT_634751 {ECO:0000313|EMBL:OAL46507.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL46507.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL46507.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL46507.1,
RC ECO:0000313|Proteomes:UP000077535};
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.
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DR EMBL; KV441654; OAL46507.1; -; Genomic_DNA.
DR STRING; 765867.A0A178DRS1; -.
DR InParanoid; A0A178DRS1; -.
DR OrthoDB; 2719054at2759; -.
DR Proteomes; UP000077535; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd15505; PHD_ING; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR018849; Urb2/Npa2_C.
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; PTHR15682; UNHEALTHY RIBOSOME BIOGENESIS PROTEIN 2 HOMOLOG; 1.
DR PANTHER; PTHR15682:SF2; UNHEALTHY RIBOSOME BIOGENESIS PROTEIN 2 HOMOLOG; 1.
DR Pfam; PF00628; PHD; 2.
DR Pfam; PF10441; Urb2; 1.
DR SMART; SM00249; PHD; 2.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 2.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 67..121
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 272..322
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT REGION 1..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 345..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 621..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..66
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 356..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 627..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1988 AA; 218718 MW; E86250FF9AB6BC15 CRC64;
MSHKHRTKRH STPPSDDSAS EEEQDIRIPH TSHQKRHYAQ SQQQPNVHGD SEDESSEEED
DDPNEPPGYC LPDCGGDDTA AMIACDANCK RQWFHYRCMG ISADSVPGED RAWYCPRCRY
YHPDHMKPLS GTPSTLSAAT ALLSGGSTGL SSPVKSKLGL GHGHGSASAS GSGRSSPVKK
AGHARSTSSS TATSRVRGSS ICKPNSKAKA KSAGLHHQTH SPSQAKRASQ ADRALQEWRE
RYAAAAAALP TPPVTATTTA ASTAADEDEE EEEYCFCGEP GNDDMIACDA NCERQWFHYE
CVGLTPASVP STAWFCPDCS MGFGSTCALA VILDPAHVVT LFPCSSSTET NADPSRPRAS
LEEQDREDDS ERQAEAGADE HRRETAIPLS GRSEKESQGW LEPRVERHVT AIELQESLGL
HSVAALILQS HRQCFKQRPS WGTPLHHGPA ELAPTLLGRF EMAAVKPGKS GKPVKAKSEK
NPATKSTEQQ AAKSESSATR PRLQAINQDF SDLDEQIRQA AHIIGLPGDW ASIQEESARS
HIIQRLVRAR AEWVLRWALD KLKDETDTGK AARRNVTAWC LLDWMIHVLP VSRSAPHLRD
AGLPSILERT LLENFDAQLG AQSDSSSDDI HMRDASEDES QPVVQHSRKR KRGTTDTTAS
KRIALAGNRS DLFLAVQSCI SSIATVAIAK DKSEDATEVE LMKMVLRTES AQAARILRFW
FTAVQHILSS ISDTSDPKTT LDQYLDLSLV LEVWDVRTVD SKDEAGASAE DFSTECLIPT
LILLDTLTQT RSADALLSSS LAPDRAIQAL EKLLARHLLA PSRAAFLGGV GTDSTNPKPR
EATALAGSLE PLRAKLLQAA QIEDAGESLP TDFVSLFNAI PHLLDLAVRA SPTRTPKGRL
VEKPWIEATF RSLVECVGCS LDAPPKHVTR HTAVGALEGT LRVLKSSNVS VDTETLKKLF
WYHSGVKYPE QEDREIHWSL IASLISLDAS VFVSEPKTEQ AEDLAEFIFD QISIVDIKNN
GFGNDELHAV AASKDTRKEA QHQTQSRTQR RLVLEQIIVP IMSAFVQNRN LLGFLRRWDH
QLVKSYKHEN RKALQGREDL IWEDRLINKG LVEHFERSLT QDQIATLIQE HTTRMTDLCD
AIGAQTDGKA SMKKLSGYKK ASSSVLIIPA LLQAIHGDRT LESLKPQLHA LLVIYSTWIQ
DDLYSVHFKL ENLWFTLCQL LEKLWPIELQ QSRELQEQFL HPLLERASQD ASISRKHLGN
RQVDSPSRAA ATLFLLNVCE RIRILPGSED RIQTSLVKFV KTLSSKRLEP KEHLKIIEIF
CADFSTLLQY LSTEASQKAI STLLSRMPDF QEDERDLIGK ALCESIIEGG SVALKNAFFD
ALLVAPLEES QNSLNPVVMK AFLSISPSAL PREKREKILN SLADLITFQP REAGTILGVM
VHLMSVPNAT ANLSTKSGTL FDITTELQKI QAASSTLQLF GQLIELALGH ILPNQSQAQN
AAFLKGFGKK VTSIVKAPAS CSAPQLAILR ATVTAQKEAE LLDIKRYVRM LQKCLGDDDT
DAAPLDQVLN AFNELPISAL KEAGCLEETT AWLNTWVKKN SDLDAYISSV GSSPIEVSEH
VARLQAMVVK FKLFPSTKWL VDLTLRLLQE PISDRVKRGA LDALEQVFTS LTLHERLDLV
PSLTETSNLV TQARSYVILS HLITTLEDRV EDNAELKQKQ FALLPTLCTL LTDSSDYASF
NALLNSITTL LNDKPSLASQ HGIESIFAAL VKLTSPHSPS LPVSHGPAIY TRICETARLI
LLVHRGRLGG RFHLLLPLLQ NLLACLFTPN SRRSGALPLW LRTPTSSAPP PRLTPANAAQ
FTHLLTTLCN PPHSSLTKAH HYTSRTSSSL NDPVKAARDR AAHFLYPLLA AYCKFTLNGR
LERGVREKLM PGLWEVMGTA NLRREGLGAM FKGLGRGERD VWRGVWGEWE GVVGRRVGGG
AGGGGEEG
//