ID   Q6M9G8_NEUCS            Unreviewed;       326 AA.
AC   Q6M9G8;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 92.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN   ORFNames=G21B4.040 {ECO:0000313|EMBL:CAF05989.1};
OS   Neurospora crassa.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=5141 {ECO:0000313|EMBL:CAF05989.1};
RN   [1] {ECO:0000313|EMBL:CAF05989.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Schulte U., Aign V., Hoheisel J., Brandt P., Fartmann B., Holland R.,
RA   Nyakatura G., Mewes H.W., Mannhaupt G.;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAF05989.1}
RP   NUCLEOTIDE SEQUENCE.
RA   German Neurospora genome project;
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC         [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC         cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC         EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
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DR   EMBL; BX908808; CAF05989.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6M9G8; -.
DR   VEuPathDB; FungiDB:NCU10270; -.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd16654; RING-Ubox_CHIP; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR045202; CHIP_RING-Ubox.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR003613; Ubox_domain.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46803; E3 UBIQUITIN-PROTEIN LIGASE CHIP; 1.
DR   PANTHER; PTHR46803:SF2; E3 UBIQUITIN-PROTEIN LIGASE CHIP; 1.
DR   Pfam; PF04564; U-box; 1.
DR   SMART; SM00028; TPR; 2.
DR   SMART; SM00504; Ubox; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS51698; U_BOX; 1.
PE   4: Predicted;
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786}.
FT   DOMAIN          250..323
FT                   /note="U-box"
FT                   /evidence="ECO:0000259|PROSITE:PS51698"
FT   REGION          39..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          198..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..59
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   326 AA;  37373 MW;  8A837C06C2C93E5D CRC64;
     MSTQSSLALK EEGNRHFQKG DYVAAEALYT KAQVLPSAPP APSLSLHPIH SPSSSTPPPH
     ISLGPTQKNQ IKTNSPPFFE THRILADPTN PLLYTNRAMA RLKMSRWDSV IEDCEECLRL
     SSSSTHLPLR NYDQAVAYAL EAHKICAETH DKSLAAVTSQ VLKCKKERWE HREKLRKREE
     QELEGEVVEM LRREMDGLLK TTSSSGGEDG DKDEEEEERK ETEKMYEEKI ERIRAVFERA
     RDKENQRRPN PPDWAIDDIS FQVMVDPVMT KTGKSYERAS IEEHLRRSET DPLTRTPLTI
     KDLLPNIDLK HACEEFLNEN GWAVDW
//