ID A0A0K9Q134_ZOSMR Unreviewed; 811 AA.
AC A0A0K9Q134;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
GN ORFNames=ZOSMA_11G00240 {ECO:0000313|EMBL:KMZ75003.1};
OS Zostera marina (Eelgrass).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ75003.1, ECO:0000313|Proteomes:UP000036987};
RN [1] {ECO:0000313|Proteomes:UP000036987}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX PubMed=26814964; DOI=10.1038/nature16548;
RA Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA Van de Peer Y.;
RT "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT the sea.";
RL Nature 530:331-335(2016).
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 -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00358}.
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:KMZ75003.1}.
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DR EMBL; LFYR01000216; KMZ75003.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K9Q134; -.
DR STRING; 29655.A0A0K9Q134; -.
DR OMA; SICAASW; -.
DR OrthoDB; 5481936at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000036987; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd23138; RING-HC_ORTHRUS_rpt1; 1.
DR Gene3D; 2.30.280.10; SRA-YDG; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 3.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR047498; RING-HC_ORTHRUS_rpt1.
DR InterPro; IPR036987; SRA-YDG_sf.
DR InterPro; IPR003105; SRA_YDG.
DR InterPro; IPR045134; UHRF1/2-like.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR027370; Znf-RING_euk.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR14140; E3 UBIQUITIN-PROTEIN LIGASE UHRF-RELATED; 1.
DR PANTHER; PTHR14140:SF27; RING-TYPE E3 UBIQUITIN TRANSFERASE; 1.
DR Pfam; PF02182; SAD_SRA; 1.
DR Pfam; PF13920; zf-C3HC4_3; 1.
DR Pfam; PF13445; zf-RING_UBOX; 1.
DR SMART; SM00249; PHD; 1.
DR SMART; SM00184; RING; 3.
DR SMART; SM00466; SRA; 1.
DR SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF57850; RING/U-box; 2.
DR PROSITE; PS51015; YDG; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 2.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00358}; Reference proteome {ECO:0000313|Proteomes:UP000036987};
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:PRU00175}.
FT DOMAIN 12..63
FT /note="PHD-type"
FT /evidence="ECO:0000259|PROSITE:PS50016"
FT DOMAIN 149..188
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 277..425
FT /note="YDG"
FT /evidence="ECO:0000259|PROSITE:PS51015"
FT DOMAIN 520..577
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 105..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 591..623
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 112..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 702..735
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..770
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 811 AA; 90739 MW; 638DB65350FB428A CRC64;
MATAADLPCD GDGVCMLCKA KPEESESLIC NLCATPWHVP CLSKPPETMS SAVTWECPDC
SDSTFTSTVN VVALSGISAD LIVSIRAIEM DKSLSDKEKA RKRQNLLGGN MKADADEEDD
KQVKEEEISE RGKKRKTDML ELFDAKFNCS FCMQLPERPV TTPCGHNFCL KCFQKWTGQG
KNTCVKCRGP IPSKMASLPR INSALVVAIR MAKTAKLVTS GRSTQIYHFL HNDNRPDKAF
TTERAKKSGK ANACSGQIFV TIPNDYFGPI SAEYDPKRNQ GVLVGETFED RMECRQWGVH
FPHVSGIAGQ SEYGAQSVAL SGGYEDDEDH GDWFLYTGSG GRDLSGNKRT NKEHAFDQTF
EKYNQALRVS CRKGYPVRVV RSHKEKRSSY APESGVRYDG VYRIEKCWRK LGSQGFKMCR
YLFIRCDNEP APWTSDDHGD LPRPLPLIKE LKHAIDISDR KETPSWDYDE KCGWKWVKPP
PLSKKPVCTK DPKDGVRVRK IIKHVHNTSV RERLLKEFKC QICRKVMKFP LTTPCAHNFC
NSCLLDSFTD LSFVKVRSRE NGRTLRAQKI VNKCPCCPTD ISDFLQNPQV NRDMMDLIET
LQRDQEEENA EEAKEAADSF IERSSEEKSV IDVEMILENE IDNVGKFGKT NDQQKSTEEI
DVLNSNSKGC DIAKVKEITE ENSFERCQSP QTTLGDSLLS RKKKQASVDK RPSKKAKRGK
ENTTAEFDTE DSTESLTGKS KSQTSLTKLV TPSSKKALRG TKATTSGSGV RTRSMEVIAA
VTGSGAMTRG MQEKIISSPH CSPSMKKALA F
//
