ID A1CRE1_ASPCL Unreviewed; 1727 AA.
AC A1CRE1;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 100.
DE SubName: Full=PHD finger and BAH domain protein (Snt2), putative {ECO:0000313|EMBL:EAW08212.1};
GN ORFNames=ACLA_029400 {ECO:0000313|EMBL:EAW08212.1};
OS Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 /
OS NRRL 1 / QM 1276 / 107).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=344612 {ECO:0000313|EMBL:EAW08212.1, ECO:0000313|Proteomes:UP000006701};
RN [1] {ECO:0000313|EMBL:EAW08212.1, ECO:0000313|Proteomes:UP000006701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1
RC {ECO:0000313|Proteomes:UP000006701};
RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT fumigatus.";
RL PLoS Genet. 4:E1000046-E1000046(2008).
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DR EMBL; DS027059; EAW08212.1; -; Genomic_DNA.
DR RefSeq; XP_001269638.1; XM_001269637.1.
DR STRING; 344612.A1CRE1; -.
DR EnsemblFungi; EAW08212; EAW08212; ACLA_029400.
DR GeneID; 4701237; -.
DR KEGG; act:ACLA_029400; -.
DR VEuPathDB; FungiDB:ACLA_029400; -.
DR eggNOG; KOG0955; Eukaryota.
DR HOGENOM; CLU_001514_0_0_1; -.
DR OMA; WVMDEPP; -.
DR OrthoDB; 1409291at2759; -.
DR Proteomes; UP000006701; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd04710; BAH_fungalPHD; 1.
DR CDD; cd15571; ePHD; 1.
DR CDD; cd15497; PHD1_Snt2p_like; 1.
DR Gene3D; 2.30.30.490; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR001025; BAH_dom.
DR InterPro; IPR043151; BAH_sf.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR029617; Snt2.
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; PTHR47672; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR PANTHER; PTHR47672:SF1; E3 UBIQUITIN-PROTEIN LIGASE SNT2; 1.
DR Pfam; PF01426; BAH; 1.
DR Pfam; PF00628; PHD; 1.
DR Pfam; PF13831; PHD_2; 1.
DR Pfam; PF13832; zf-HC5HC2H_2; 1.
DR SMART; SM00439; BAH; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 2.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS51038; BAH; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51805; EPHD; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000006701};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00146}.
FT DOMAIN 252..370
FT /note="BAH"
FT /evidence="ECO:0000259|PROSITE:PS51038"
FT DOMAIN 550..724
FT /note="ELM2"
FT /evidence="ECO:0000259|PROSITE:PS51156"
FT DOMAIN 737..780
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT DOMAIN 1004..1054
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 1007..1043
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 1112..1230
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS51805"
FT REGION 1..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 464..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 842..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 943..997
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1293..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1399..1418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1483..1631
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1676..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1086..1115
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..209
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..492
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..507
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 853..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1293..1315
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1561..1585
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1595..1625
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1701..1727
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1727 AA; 188356 MW; 4F773E21E3B1A3A4 CRC64;
MASSDRSPSQ KLSHHQQHQS PHVKPHSSPS GAARRMPTPG QSSRRGSTDS STNVGTATTN
ESLSQSMTAS ATPEVAGAEP PSTSATPAPY GTRSRGRNAA PRPNYAEERD IDMDLEILTP
ANRVKKSSGA ATHNSTNGAK AEGEKTVSSS NSRKSLTTVN GSNPASAKDA IPGTSSFSAK
PEDGSASSGS SKKRKQPASA PNSNSANGSA AKKLFTTAPG LDSNLAPVTN MVSFEKRGAR
LKDGALVADD GTTFAVNDHV YLICEPPGEP YYLARIMELL PSKDKPNGPI EALRVNWYYR
PRDIQRTVAD TRVVFASMHS DTCPLTSLRG KCQIKHLSEI ENFEAYRKTR DCFWFDKMFD
RYIHRYYEVV PTKKVINVPA NVKKVLDERW KFVLVEIGKR KELFSAVKTC TRCSLYAANN
DSVDCAVCRN TYHMHCVRPV LTKKPARGFA WACAACSRAQ ERKLEARNTP TVGEAPAEPE
EEIVEEEEED LNGTANGTNG STPAPTEEVT IRPATAEQIA QARMWPYRYL GIHCRVEDAL
DYDDRIYPRA SSRLGPRHQA VVNPWPGRPV EYAKPIDIKK KYLTKSGRKE SKLSKEAQAA
IEAARQEKAN RPKWVQDEPV GYIRRGEDEP VSVNGKPTRT AELLFKMPTA SQISSRGEDD
APAAELSAAD REKFMDEYME RAKELAPQLG VEKYSTNFLD KALELLYANS FDVEAALAKL
KQQNKYKDLK EPHLRPEEVK VFEQGVAKYG SELRFVTKHV GTVPHYQIVR FYYMWKKTPR
GRQIWGNYEG RKGKREARRQ STTAKLVDDV ADDQDDSAFD NGKAVEKKRG FQCKFCSTRS
SRQWRRAPGV PPGTTTPSES SSKKADKGPQ LTVALCLRCA QLWRKYGIQW ESVDEVAKKM
AQSGNKSWRR RVDEELLTQL LASEDPANIN STTAAAAASI GIPVNATPPA QPQEPVKKKA
KSGEKDSAAT SAATSVEPAP KKKVPVEKPP EPAPIVPDPP KAKVLPCAIC NKLEPVGDQH
LSCRDCRLTV HRNCYGVSSS RNCAKWLCDM CSNDRNPMIS TCYECVLCPV TWTEHELMEA
PKVSHKKKTE RDREKERLEK EMVQEAIKLY RQRQEAVGKP IGPREPLKRT AGNNWVHVTC
AVWTPEIRFG NAKELEPAEG FGLISADRYR DVCKLCRTSK GACVTCNHTG CNARFHVGCA
FQAQYVFGFN ITPVKSSRRD TVNSIRLGEE VGAATAGIWC PHHAPSSGVH QVGEMTGETG
LNALQQYVQS YKQADLTLPG TVRRAAYVQQ ALNASQPATT ASTRRSSTIN GLVTATSHPP
PPPKDSQKVI VTAAPEQNPD GMVIDSGNPF PRQVASPEME RKCCRCSTSF SPRWWPIDNA
RRAAVLNSRT SSVNGVGMSE PAGRFPHPSS ASPPFLSRNL SQHSLSKLNG EYNIGIEGPL
YECHKCYLKT AVAQPSPEPR PSPYPAQRPV LPAPRISEYQ VHPYGTHAHP TPPPTGPTGV
LPRPLGAAPS HNGPEWYSGY DQRSTEYGDG KLRNGLPIPG YHGAPPAAPT LPMNGFPHPS
TAHHAPPPPP PHYPGGAPPP PHQSYSAHQS PYAPVSMPSP HPSHAPVSMP SPHPSHAPGP
RPFASSASPP VAQATIIRHS PQHSLSALNG GPPRMYSVDR VLGAPTQSPI VAHARIDPRG
LTPPGKLEET SVGPAGGAMS TGRSATVNGT NGGSGASASP SLKNLLS
//
