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Database: UniProt
Entry: Q7SHW3_NEUCR
LinkDB: Q7SHW3_NEUCR
Original site: Q7SHW3_NEUCR 
ID   Q7SHW3_NEUCR            Unreviewed;       794 AA.
AC   Q7SHW3;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=IBR domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=NCU00691 {ECO:0000313|EMBL:EAA36595.1};
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110 {ECO:0000313|EMBL:EAA36595.1, ECO:0000313|Proteomes:UP000001805};
RN   [1] {ECO:0000313|EMBL:EAA36595.1, ECO:0000313|Proteomes:UP000001805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987
RC   {ECO:0000313|Proteomes:UP000001805};
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D., Jaffe D.,
RA   FitzHugh W., Ma L.J., Smirnov S., Purcell S., Rehman B., Elkins T.,
RA   Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M., Qui D.,
RA   Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P., Glass L., Orbach M.J., Berglund J.A., Voelker R., Yarden O.,
RA   Plamann M., Seiler S., Dunlap J., Radford A., Aramayo R., Natvig D.O.,
RA   Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I., Sachs M.S.,
RA   Lander E.S., Nusbaum C., Birren B.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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DR   EMBL; CM002236; EAA36595.1; -; Genomic_DNA.
DR   RefSeq; XP_965831.1; XM_960738.2.
DR   AlphaFoldDB; Q7SHW3; -.
DR   PaxDb; 5141-EFNCRP00000000726; -.
DR   EnsemblFungi; EAA36595; EAA36595; NCU00691.
DR   GeneID; 3881893; -.
DR   KEGG; ncr:NCU00691; -.
DR   VEuPathDB; FungiDB:NCU00691; -.
DR   HOGENOM; CLU_025203_1_0_1; -.
DR   InParanoid; Q7SHW3; -.
DR   OrthoDB; 2725066at2759; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000151; C:ubiquitin ligase complex; IBA:GO_Central.
DR   GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR   GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR   CDD; cd20335; BRcat_RBR; 1.
DR   CDD; cd22584; Rcat_RBR_unk; 1.
DR   Gene3D; 1.20.120.1750; -; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR031127; E3_UB_ligase_RBR.
DR   InterPro; IPR002867; IBR_dom.
DR   InterPro; IPR044066; TRIAD_supradom.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR11685; RBR FAMILY RING FINGER AND IBR DOMAIN-CONTAINING; 1.
DR   PANTHER; PTHR11685:SF457; TRANSLATION TERMINATION INHIBITOR PROTEIN ITT1; 1.
DR   Pfam; PF01485; IBR; 2.
DR   SUPFAM; SSF57850; RING/U-box; 2.
DR   PROSITE; PS51873; TRIAD; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001805};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          203..406
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51873"
FT   DOMAIN          207..253
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   REGION          95..135
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..449
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          686..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          726..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          479..506
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          604..635
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        735..760
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   794 AA;  90254 MW;  2B1D2C30C13E0518 CRC64;
     MAESTSVSLS SAHLVGTVAN PPKLDESEYL REVFGITTED ATATEAEIEE SLTAKASSLG
     IDVSNLTDSL GNPTALNATS ARSSTLVAHQ RSNTICSNDS TTGTETATGT DNDMASNSSA
     AMPATLTQST SRKRSNTVNF SQYEKYLTQL KPALHQPKFS NPAAPTRRPS HNIFGFGHFK
     GVRELRRGLT GRLKRRKTYP ALPIVICICC REEFAQENHL LQTLPCGHTY CQNCLAVMIN
     QSTTDESKMP PRCCTQPIPS SIIKTILTRE EQQAFLKAVL QYSTPWESRI FCPNPACGEF
     IPPRAKLDPK HPFETMCKTC KMRVCLICKR SAHRLGQDCP EDIELETVLK MGEKSGWRRC
     YKCRNLVELT QGCTHMTCRC KAQFCYICGA VWDPVVGCPN FCNGEEELER RRREEETRLA
     ELEVKKREQE EAAAAEGRAQ QAAERRTRDS VEFQALRERQ NHEMSRVLAY EARMRKDMRT
     KQSEKKKALL EKYAELTEKM KERHAKTEQH LEDRQIEAEM ELRSSLDASE RSIKIQLKHM
     EAYCKTLSQV EEVSEKDQAL QDSKMPSREV TQKHLDQLSE QYRIRDGMER RHQAQINVLR
     EKQGKKMEQL LDRHEDEMEA LLHKKSEELE DLAVEFANEA DAVSRTFAQR KVKLQKRWLV
     SVEILRVEQE KKTGMRYASM AVPQWPAATT TESDTETESE EEETTAAAHL QEQEVIELAR
     PKAEAEMKED GWPLSNNDNI KTTEIELPST PKTVTPAVTP TQARFEAELR RYRSRTRLVA
     PGEQSPPVSP RTMR
//
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