ID A0A1R3GGU2_COCAP Unreviewed; 1024 AA.
AC A0A1R3GGU2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=CCACVL1_25865 {ECO:0000313|EMBL:OMO57277.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO57277.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO57277.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO57277.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) 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};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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:OMO57277.1}.
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DR EMBL; AWWV01014394; OMO57277.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3GGU2; -.
DR STRING; 210143.A0A1R3GGU2; -.
DR EnsemblPlants; OMO57277; OMO57277; CCACVL1_25865.
DR Gramene; OMO57277; OMO57277; CCACVL1_25865.
DR OMA; YCISEGH; -.
DR OrthoDB; 1219767at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000188268; Unassembled WGS sequence.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd21037; MLKL_NTD; 1.
DR Gene3D; 1.20.930.20; Adaptor protein Cbl, N-terminal domain; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 3.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR036537; Adaptor_Cbl_N_dom_sf.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR003613; Ubox_domain.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR45958; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR PANTHER; PTHR45958:SF11; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF04564; U-box; 1.
DR SMART; SM00185; ARM; 4.
DR SMART; SM00504; Ubox; 1.
DR SUPFAM; SSF48371; ARM repeat; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50176; ARM_REPEAT; 1.
DR PROSITE; PS51698; U_BOX; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Reference proteome {ECO:0000313|Proteomes:UP000188268};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 255..329
FT /note="U-box"
FT /evidence="ECO:0000259|PROSITE:PS51698"
FT DOMAIN 262..300
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REPEAT 451..481
FT /note="ARM"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00259"
FT COILED 74..101
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 195..232
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1024 AA; 113921 MW; EFD64FD5AC8EF4B7 CRC64;
MSSMDFSFGI EDVGVAILQE LWNRVALQTA ELAKETRDGV LEKDSFQEFS RTISELDILL
RALNVRKIEA AMGSDFTKAA LENLNSEIRE ARKIIKDYKS GSRLRLLLHS NSVLSQMQAL
AKRMAATISS FQLINLDMAV NLKNMNHQII NNLNSMEFRM AAATETIASE IENSISQSSK
NRENAVKLLE KIAEAVGANA NASLVQNELE LLKQEKEEME IQKKQAEALQ LSQLIQLLYS
TEIVSRPQSE DISSYPIGSF ICPLCDEMMV DPVAVYCGHS FERKAIQDYF KSGKKNCPSC
GEELQSLDLT PNVNLRSSIE EWKKRDRDWK FQAAIRGINS SDNVRINKAL EDMQVLLEIP
QYAVKAAEEG LILKFVESMK ETNLNTMAAV KCLYCLARYC DDHKQEIVQA GAVRRIVKRI
YNGRTEPTTV GILLELSKTE TLIDKIGNTK DCIPLLVSLL SNPNSDISDK AQNVLQNLSS
NTHFAVKMAE AGYFQSFVAR FNEGHQETRA LMAAALVNMQ LKENSISDLK DKQFVQNLVH
LLSSNSPACK SACIKCIKKL IQYPKMVKRF LSDPATIPLL LNLISFRSDP LLKQEAAEIL
ALLIETCQHA QFEMNQGLQE LQSEHNVSLF LQHVANSDPK FKIQFLHLLI ELSNKSNIAQ
NLIRSNTGDI NHLFSCLDSD RPEVRRWAMK LIHCLSEGHP DGVPLPPSPT KEIAINTLSS
ILTCSLDCEE RSIAAGIISQ LPKDDTDIDE TLRKSETLKA IHEVICSSDD RFSGGIGATI
NQDKSLLENA LAALLRFTEP SKPELQRQVG ELELYPSLVR VLSTGSSLAK QRTALALAQL
SRSSSLSVSD IRAKQENSLP LLHMMKLFPN MSWCCTASTT NEMSCSVHGF ACSNRHAFCL
VKADAVKPLL QTLSDTDSGV AEAALMALET LLEDHNTLSH ATAAIVESQG VVAILQVLEK
GSLSAKSKAL DLFLKILNHS KISDTLFQRA EGILIQLLHE DEIRKKVALV LKQMKVLPEQ
SSYF
//