ID A8N9I1_COPC7 Unreviewed; 1424 AA.
AC A8N9I1;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=CC1G_09016 {ECO:0000313|EMBL:EAU90334.2};
OS Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)
OS (Inky cap fungus) (Hormographiella aspergillata).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Psathyrellaceae; Coprinopsis.
OX NCBI_TaxID=240176 {ECO:0000313|EMBL:EAU90334.2, ECO:0000313|Proteomes:UP000001861};
RN [1] {ECO:0000313|EMBL:EAU90334.2, ECO:0000313|Proteomes:UP000001861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003
RC {ECO:0000313|Proteomes:UP000001861};
RX PubMed=20547848; DOI=10.1073/pnas.1003391107;
RA Stajich J.E., Wilke S.K., Ahren D., Au C.H., Birren B.W., Borodovsky M.,
RA Burns C., Canback B., Casselton L.A., Cheng C.K., Deng J., Dietrich F.S.,
RA Fargo D.C., Farman M.L., Gathman A.C., Goldberg J., Guigo R., Hoegger P.J.,
RA Hooker J.B., Huggins A., James T.Y., Kamada T., Kilaru S., Kodira C.,
RA Kues U., Kupfer D., Kwan H.S., Lomsadze A., Li W., Lilly W.W., Ma L.J.,
RA Mackey A.J., Manning G., Martin F., Muraguchi H., Natvig D.O.,
RA Palmerini H., Ramesh M.A., Rehmeyer C.J., Roe B.A., Shenoy N., Stanke M.,
RA Ter-Hovhannisyan V., Tunlid A., Velagapudi R., Vision T.J., Zeng Q.,
RA Zolan M.E., Pukkila P.J.;
RT "Insights into evolution of multicellular fungi from the assembled
RT chromosomes of the mushroom Coprinopsis cinerea (Coprinus cinereus).";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11889-11894(2010).
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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBUNIT: Associated with the spliceosome.
CC {ECO:0000256|ARBA:ARBA00011524}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAU90334.2}.
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DR EMBL; AACS02000007; EAU90334.2; -; Genomic_DNA.
DR RefSeq; XP_001831487.2; XM_001831435.2.
DR STRING; 240176.A8N9I1; -.
DR GeneID; 6007958; -.
DR KEGG; cci:CC1G_09016; -.
DR VEuPathDB; FungiDB:CC1G_09016; -.
DR eggNOG; KOG1812; Eukaryota.
DR HOGENOM; CLU_004949_0_0_1; -.
DR InParanoid; A8N9I1; -.
DR OMA; DQQPNLW; -.
DR OrthoDB; 1789161at2759; -.
DR Proteomes; UP000001861; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0031124; P:mRNA 3'-end processing; IEA:UniProtKB-UniRule.
DR GO; GO:0000209; P:protein polyubiquitination; IEA:InterPro.
DR CDD; cd20335; BRcat_RBR; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR002867; IBR_dom.
DR InterPro; IPR045072; MKRN-like.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR11224; MAKORIN-RELATED; 1.
DR PANTHER; PTHR11224:SF10; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF01485; IBR; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR Pfam; PF14608; zf-CCCH_2; 4.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00356; ZnF_C3H1; 8.
DR SUPFAM; SSF90229; CCCH zinc finger; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50103; ZF_C3H1; 8.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; Reference proteome {ECO:0000313|Proteomes:UP000001861};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00176};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 10..37
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 101..127
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 292..319
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 381..408
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 427..454
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 534..561
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 580..607
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 709..735
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 815..890
FT /note="RRM"
FT /evidence="ECO:0000259|PROSITE:PS50102"
FT ZN_FING 10..37
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 101..127
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 292..319
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 381..408
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 427..454
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 534..561
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 580..607
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT ZN_FING 709..735
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 35..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 130..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..519
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 572..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 649..689
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..766
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1424 AA; 155750 MW; EACBE2B524B056A4 CRC64;
MSERPKPKHS KSRICTAFAQ KGKCAFGAMC KSSHDVGANG SARGSQQSPK PSSSAKSVKS
SSKPQKKRPP PTPVVKPAES IPSRSPTPDD PLEKQEMIDE DDEKEPCVFW PGNCGSGDQC
AFLHVDPAPA PAEAKTVAES STSKQKENLV WTSSSTESRS SKGKGKEPAP TYRPASPFGY
GHVENDTSDD ETEQGNDSDT DTESRYADSS AGGWVKARTS ARKTHARDPP IVEDKESVFE
FSNNPKHRGP TQVAQPPAVA PPPPQIQTPT IAVPHITQAM FHWSQFADPN ADPNVAFCKQ
LTQNNCALQA QCRFRHSLTP EEYTTLFKDQ QPMLMTLNQS LGTAQGAVPQ AQPVYYQVAQ
PPPIAPTIPV IQSPPPPAKP PISKVLCAFW IRNKCQNGDK CPFRHEGTPI TETASGYDSM
DNLRGTSPVQ DICRHFQKGH CIFGDKCQNS HIMHSDIQNY RTKARADANG WGAPAEEDNG
WGVSSGNPDA WGESDDHTGS KADDGWWGSD DRSNNRTERR DNWSSNSNTR TSDRSSGRIC
YDYQVGRCTR GDRCRFSHDL GSGRGGPNDE YRGTQSRGSG SSSSRCKFYD QGDCRRGNAC
SRRHEDGGSW KRADSYQAEG WGSAQDEGQD HEANGWGAEE GTTGDVWGQD AADDHRDEDE
GEPRDGDVTH EDERESAKGS EDEGDGSDGW NTSRKWFEPS DNTDRSTSAK KRPLCLKFGQ
GACRRDDCAF QHSLPSDQAA IHSRAESAVE DDEIEETQEA EPEVDVTPVE DVPPARSPSP
EIEEHPLVQR FVNNCTVRFD AQCQPEEIMT AADSKKLVLS HLPIGITDEE IQRLVKHIGA
VKEIVELGTG EATATFSVEF EDAAAALIAV RLLNGKDYSG QTVVAKLDSR ATVSGRSPLG
SQVLLVSWPC PTLTAWIFYE TVTIAKQAAQ KINGVKFQDR TIKALYEAGK GNKRGPWPVR
VTNLPPAASK DDLKGLCDVP FVVTDLGQPT YTESPRDAIQ EALEEYGGVL SFEDSLEENT
VSKNFVYATM EGHAAAQAAA KALNKTKPSY IGEQYLTVQH IYLAGFQMPA KAFECVADQV
KVIREVQKGT CTVVDWPLVD THVVKIYAPV DQAVAFCTAH AELEKVADGL VVTSEDGANV
WDDYLETTSA EKAIEKFNER PTDVPCFVYI DKRYQVVRVY GAPDGQKRGQ AALMKILKTV
NEQRHELAVP REKMAAIIDN GLSELHNSLG GSKVTLDIVS PKLVIRGTPD DLGKAKLVLS
VAPASSIPST VARSKLCPVC EREPVDRVRL SCRHVYCKAC LKFALTKTAK GEMAGQPFFS
CIYSDEGGDD DGSTPAQTCG APISYAVVRD TLQMAGEVEF LKAAFAFFIR AHRDQYFFCP
TPDCVAVYRS AEEEIVIRCT MCSGDICPLC RSRSHDGRLC AERM
//
