ID A0A8T0IKA4_CERPU Unreviewed; 805 AA.
AC A0A8T0IKA4;
DT 12-OCT-2022, integrated into UniProtKB/TrEMBL.
DT 12-OCT-2022, sequence version 1.
DT 28-JAN-2026, entry version 12.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=KC19_3G132500 {ECO:0000313|EMBL:KAG0583389.1};
OS Ceratodon purpureus (Fire moss) (Dicranum purpureum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC Bryophytina; Bryopsida; Dicranidae; Pseudoditrichales; Ditrichaceae;
OC Ceratodon.
OX NCBI_TaxID=3225 {ECO:0000313|EMBL:KAG0583389.1, ECO:0000313|Proteomes:UP000822688};
RN [1] {ECO:0000313|EMBL:KAG0583389.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R40 {ECO:0000313|EMBL:KAG0583389.1};
RA Carey S.B., Jenkins J., Shu S., Lovell J.T., Sreedasyam A., Maumus F.,
RA Tiley G.P., Fernandez-Pozo N., Barry K., Chen C., Wang M., Lipzen A.,
RA Daum C., Saski C.A., Payton A.C., Mcbreen J.C., Conrad R.E., Kollar L.M.,
RA Olsson S., Huttunen S., Landis J.B., Wickett N.J., Johnson M.G.,
RA Rensing S.A., Grimwood J., Schmutz J., Mcdaniel S.F.;
RT "WGS assembly of Ceratodon purpureus strain R40.";
RL Submitted (JUN-2020) 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 SINA (Seven in absentia) family.
CC {ECO:0000256|ARBA:ARBA00009119}.
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:KAG0583389.1}.
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DR EMBL; CM026423; KAG0583389.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A8T0IKA4; -.
DR Proteomes; UP000822688; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR CDD; cd16571; RING-HC_SIAHs; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 2.
DR InterPro; IPR052088; E3_ubiquitin-ligase_SINA.
DR InterPro; IPR049548; Sina-like_RING.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR013010; Znf_SIAH.
DR PANTHER; PTHR10315; E3 UBIQUITIN PROTEIN LIGASE SIAH; 1.
DR PANTHER; PTHR10315:SF83; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF21362; Sina_RING; 1.
DR Pfam; PF21361; Sina_ZnF; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF49599; TRAF domain-like; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
DR PROSITE; PS51081; ZF_SIAH; 1.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000822688};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00455}.
FT DOMAIN 578..614
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 631..691
FT /note="SIAH-type"
FT /evidence="ECO:0000259|PROSITE:PS51081"
FT REGION 190..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..208
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..316
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..350
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 805 AA; 89438 MW; C6BE4B62E5208EBB CRC64;
MMAPNLQALI SSTTYPNLSG LTNEDAVAVL KGRATVLNVG TLDPKWQKLI STIQPGIVPG
LIVQGKFGAE LVIVCQSTWT SKTPNRDAFT WSEYEWLMVE VNTLWRRAKA EVIGSGIRKK
IPFVCRYCNQ DMVDKSYLGW HRQTDQCNGY DMAKQGILKI FPSMGQDGNK AARAVFTKYG
MNIPNQMFHV SSKKSPKHGQ EFTRESTKNA KNATGAKGTK GKRVECDDYH ITNATDFSSD
DDLPLAFLTS KTKNQNVHMK SSITDKLKKR PATHAGIGEQ GGKKTWQGQN KMQDKGTSRP
GHSSHTTRAG QETPTIGVSA PLKAPGRPWT RSTQIKEMSP STTPSMDTTT IGLRPTSFGL
KEYTVEARKE VEVAALDQSL QRFPNIDPTL RPTKLGTSPG LYTLVEQSGH IISLDLMTDL
VAPGMEIKML YEAGRLARKI FEAWGIFQWR HEATGEFNAC VIKAVDKCTD AFKQKSTALM
DAEIEAFDRH HNDVHSYSKR LEDFSNAVKH TERKRAEYVE EQMGKFDRGV QMVLEEMLIA
AQKQVQSGKR KVVENAVAPI GKKHVGPKYD LDPDMLECPI CLEALSPPVY QCDNGHTACS
GCCQMITKGC PSCSKPIGRI RNIAIEKVIE SLQVECKHAC HGCNTMLKYT ERAKHEEKLC
DYRPIPCPVT RHCAYAGPKA SIPVHLADEH NMRIVESSGS VMSASFKRKS SHGGVLFKAN
EIWLMVCWLE HFQGDAFRCD TVGASEGVGY KLTVKPVNKS SRVYSMENVA HDKTGEASCL
DTNLLLVPGG FEEHEITVSL IRQRR
//
