ID A9NRP2_PICSI Unreviewed; 355 AA.
AC A9NRP2;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS Picea sitchensis (Sitka spruce) (Pinus sitchensis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Pinopsida; Pinidae; Conifers I; Pinales; Pinaceae; Picea.
OX NCBI_TaxID=3332 {ECO:0000313|EMBL:ABK23303.1};
RN [1] {ECO:0000313|EMBL:ABK23303.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Green portion of the leader tissue
RC {ECO:0000313|EMBL:ABK23303.1};
RX PubMed=18854048; DOI=10.1186/1471-2164-9-484;
RA Ralph S.G., Chun H.J., Kolosova N., Cooper D., Oddy C., Ritland C.E.,
RA Kirkpatrick R., Moore R., Barber S., Holt R.A., Jones S.J., Marra M.A.,
RA Douglas C.J., Ritland K., Bohlmann J.;
RT "A conifer genomics resource of 200,000 spruce (Picea spp.) ESTs and 6,464
RT high-quality, sequence-finished full-length cDNAs for Sitka spruce (Picea
RT sitchensis).";
RL BMC Genomics 9:484-484(2008).
RN [2] {ECO:0000313|EMBL:ACN40836.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Bark {ECO:0000313|EMBL:ACN40836.1};
RA Reid K.E., Liao N., Ralph S., Kolosova N., Oddy C., Moore R., Mayo M.,
RA Wagner S., King J., Yanchuk A., Holt R., Jones S., Marra M., Ritland C.E.,
RA Ritland K., Bohlmann J.;
RT "Full length sequence-verified cDNA sequences from Sitka spruce (Picea
RT sitchensis).";
RL Submitted (FEB-2009) 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 -!- SIMILARITY: Belongs to the RING-type zinc finger family.
CC {ECO:0000256|ARBA:ARBA00038033}.
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DR EMBL; EF083971; ABK23303.1; -; mRNA.
DR EMBL; BT071373; ACN40836.1; -; mRNA.
DR AlphaFoldDB; A9NRP2; -.
DR OMA; KCSHLEY; -.
DR UniPathway; UPA00143; -.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProt.
DR GO; GO:0140096; F:catalytic activity, acting on a protein; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd23127; RING-HC_BAH1-like; 1.
DR CDD; cd14482; SPX_BAH1-like; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR033326; BAH1.
DR InterPro; IPR004331; SPX_dom.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR46764; E3 UBIQUITIN-PROTEIN LIGASE BAH1; 1.
DR PANTHER; PTHR46764:SF2; E3 UBIQUITIN-PROTEIN LIGASE BAH1-LIKE-RELATED; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00184; RING; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51382; SPX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 1..184
FT /note="SPX"
FT /evidence="ECO:0000259|PROSITE:PS51382"
FT DOMAIN 251..300
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
SQ SEQUENCE 355 AA; 40346 MW; C7D859C6F549EC8D CRC64;
MKFGERFSEY LHGEDEHFLD KCSHLEYKRL KKVLKKCRVG YLRDGTASDF EGGFYCSETT
ENEDVICGKT AGGISKSSDS FSTCSSETCA VCDRIFFYEL TKEVSSIVGC FSSRARRLLD
LHLASGFQRY LWRVKHFFAD DHEAMIREGR HLVNYVAMNA IAIRKILKKY DKVHSSVNGR
NFKTKLQAKH IELLKSPWLI ELIAFQINTT DSENGHISEI FPECSCDFTA NDPFITCTLP
DSVKLEFSLT CPICLDTVFD PVALGCGHVF CNSCACTGAS IPTIEGLKAA NQHARCPICR
QMGVYADSIH LPELGLLVKK RCRGYWKERL HTERAERVKQ AKEHWDLQSR FVLGF
//
