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Database: UniProt
Entry: A0A176WMB8_MARPO
LinkDB: A0A176WMB8_MARPO
Original site: A0A176WMB8_MARPO 
ID   A0A176WMB8_MARPO        Unreviewed;       251 AA.
AC   A0A176WMB8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   03-MAY-2023, entry version 16.
DE   RecName: Full=SP-RING-type domain-containing protein {ECO:0000259|PROSITE:PS51044};
GN   ORFNames=AXG93_4145s1130 {ECO:0000313|EMBL:OAE34278.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE34278.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE34278.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE34278.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC       {ECO:0000256|ARBA:ARBA00004718}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the NSE2 family.
CC       {ECO:0000256|ARBA:ARBA00008212}.
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:OAE34278.1}.
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DR   EMBL; LVLJ01000431; OAE34278.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176WMB8; -.
DR   OrthoDB; 935506at2759; -.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0030915; C:Smc5-Smc6 complex; IEA:InterPro.
DR   GO; GO:0019789; F:SUMO transferase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0000724; P:double-strand break repair via homologous recombination; IEA:InterPro.
DR   GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR   CDD; cd16651; SPL-RING_NSE2; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR026846; Nse2(Mms21).
DR   InterPro; IPR004181; Znf_MIZ.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR21330:SF1; E3 SUMO-PROTEIN LIGASE NSE2; 1.
DR   PANTHER; PTHR21330; UNCHARACTERIZED; 1.
DR   Pfam; PF11789; zf-Nse; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51044; ZF_SP_RING; 1.
PE   3: Inferred from homology;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00452}.
FT   DOMAIN          135..228
FT                   /note="SP-RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51044"
SQ   SEQUENCE   251 AA;  28223 MW;  9CBDCF8DB3D8EFCB CRC64;
     MAAATERIRS AARNLEGTAR SLQSDMYAQC VLFKMVAEDL EREHDSVSVE KIRGALLETV
     ECTHSLEHHC LALSSLSANF ATGNEVADFE KVLYETSAES RRVQAFDPRQ HTCYEQFNQS
     IWNIHHAGEA APGQEQDEIV MLTSQYGVKN TNCPLSGKPV TQLDDPVRSK DCEHIYEKAA
     VLEYIRKHNR EHPRKKCKCA CAGCPKELLA ANFVCDASLK MSIQELRLRE RANTQRAHVA
     DFTGENHSDD D
//
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