ID   B8LPQ1_PICSI            Unreviewed;       186 AA.
AC   B8LPQ1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=RING-type domain-containing protein {ECO:0000259|PROSITE:PS50089};
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:ABR17631.1};
RN   [1] {ECO:0000313|EMBL:ABR17631.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Green portion of the leader tissue
RC   {ECO:0000313|EMBL:ABR17631.1};
RA   Ralph S.G., Chun H.E., Liao N., Ali J., Reid K., Kolosova N., Cooper N.,
RA   Cullis C., Jancsik S., Moore R., Mayo M., Wagner S., Holt R.A.,
RA   Jones S.J.M., Marra M.A., Ritland C.E., Ritland K., Bohlmann J.;
RT   "Full length cDNA sequences from Sitka Spruce (Picea sitchensis).";
RL   Submitted (JUN-2007) 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. {ECO:0000256|ARBA:ARBA00043952}.
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DR   EMBL; EF677831; ABR17631.1; -; mRNA.
DR   AlphaFoldDB; B8LPQ1; -.
DR   OMA; LEANTHM; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:InterPro.
DR   CDD; cd16461; RING-H2_EL5-like; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR044602; ATL10/ATL75-79-like.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR46905; RING-H2 FINGER PROTEIN ATL78; 1.
DR   PANTHER; PTHR46905:SF7; RING-H2 FINGER PROTEIN ATL78; 1.
DR   Pfam; PF13639; zf-RING_2; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   2: Evidence at transcript level;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT   TRANSMEM        33..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          99..141
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
SQ   SEQUENCE   186 AA;  20498 MW;  ADDEAC1AF0D6D440 CRC64;
     MVLEATTDTF PPMDLSYESP QAVISPHMSE GTILILLALL CALICLAGLA SIVPWHYIWR
     SRHDHMATRV ANTGMKEKSI EALPSVIYGK SIPQLATQCA ICLAEFAEGE GVRVLPSCNH
     GFHMECVDRW LLSHSSCPTC RHYLLDPGCK RVANHIQPRK SNAREVQIHQ PGPAQESGEI
     IDLECG
//