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Database: UniProt
Entry: Q0CJI2_ASPTN
LinkDB: Q0CJI2_ASPTN
Original site: Q0CJI2_ASPTN 
ID   Q0CJI2_ASPTN            Unreviewed;       646 AA.
AC   Q0CJI2;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   27-MAR-2024, entry version 82.
DE   RecName: Full=FHA domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=ATEG_06152 {ECO:0000313|EMBL:EAU33913.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU33913.1, ECO:0000313|Proteomes:UP000007963};
RN   [1] {ECO:0000313|Proteomes:UP000007963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CH476601; EAU33913.1; -; Genomic_DNA.
DR   RefSeq; XP_001215330.1; XM_001215330.1.
DR   AlphaFoldDB; Q0CJI2; -.
DR   STRING; 341663.Q0CJI2; -.
DR   EnsemblFungi; EAU33913; EAU33913; ATEG_06152.
DR   GeneID; 4321845; -.
DR   VEuPathDB; FungiDB:ATEG_06152; -.
DR   eggNOG; KOG3872; Eukaryota.
DR   HOGENOM; CLU_017542_1_1_1; -.
DR   OMA; VMTENSS; -.
DR   OrthoDB; 463769at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:UniProt.
DR   GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR   Gene3D; 2.60.200.20; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR000253; FHA_dom.
DR   InterPro; IPR008984; SMAD_FHA_dom_sf.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR15067; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR   PANTHER; PTHR15067:SF8; E3 UBIQUITIN-PROTEIN LIGASE RNF8; 1.
DR   Pfam; PF00498; FHA; 1.
DR   Pfam; PF17123; zf-RING_11; 1.
DR   SMART; SM00240; FHA; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF49879; SMAD/FHA domain; 1.
DR   PROSITE; PS50006; FHA_DOMAIN; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          278..341
FT                   /note="FHA"
FT                   /evidence="ECO:0000259|PROSITE:PS50006"
FT   DOMAIN          418..464
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          1..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          179..242
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          474..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..220
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..500
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        503..529
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..570
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..596
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        607..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   646 AA;  69471 MW;  7955CDDA12EDA244 CRC64;
     MAASVSASAS NHLSSDQPRS GASSSASAPA PAGPLRRLSQ LRAYTQSHFL SSSSSSFFPS
     STTSHRLSRR NTHSTRGVRS ASSTTVTPPA PTPAPATGSE PLPPSSATVG TPPSTTTTTT
     TTTTTAANTT ESASCPESEQ QPTLTLDSSV LFSSGLDIDL GFHADPHQSS FSSALLATAT
     EPDDRPSTQG RTMARQRGSS QPPETILEGA TPSAPSTLQP GLLDSADPVM TENSSASPRP
     KQKATIRFYP HQDSHQSSRP SLPFIPISRT LPSDSCVIRV GRYSERDGLP AANPSEPSDA
     PVGFKSKVVS RKHCEFLYMN GQWHIKDVGS SSGTFLNHMR LSQPNMASRL YTIKDGDIVQ
     LGIDFRGGEE MIFRCVRIRI ECNRSWQQQP NEFNKNTESL IRNLGKGETA DYSGCRECSI
     CLGSVLRPYQ CLFMAACAHV WHYKCVSRLI HTPDYPMFQC PNCRAYTDLS AEVDDSNDYE
     EVEQKPTTTP EEKKDSGELG GEQPPAETNS SSSNIPSSNT SSSGSNRSSD VPRHSEDRFS
     TSLPMEAGLA ANIENMRFDL RDEPTEAAEE SPRSTDPSLT ISTTDRSANS DVPGWQAIAR
     TPSAVHCQQA HLRSDTPVRS DSSDENPLTP LNDSGPLAFD GRAGMS
//
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