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Database: UniProt
Entry: B3RRR7_TRIAD
LinkDB: B3RRR7_TRIAD
Original site: B3RRR7_TRIAD 
ID   B3RRR7_TRIAD            Unreviewed;       580 AA.
AC   B3RRR7;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=SP-RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=TRIADDRAFT_54339 {ECO:0000313|EMBL:EDV26398.1};
OS   Trichoplax adhaerens (Trichoplax reptans).
OC   Eukaryota; Metazoa; Placozoa; Uniplacotomia; Trichoplacea; Trichoplacidae;
OC   Trichoplax.
OX   NCBI_TaxID=10228 {ECO:0000313|EMBL:EDV26398.1, ECO:0000313|Proteomes:UP000009022};
RN   [1] {ECO:0000313|EMBL:EDV26398.1, ECO:0000313|Proteomes:UP000009022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Grell-BS-1999 {ECO:0000313|EMBL:EDV26398.1,
RC   ECO:0000313|Proteomes:UP000009022};
RX   PubMed=18719581; DOI=10.1038/nature07191;
RA   Srivastava M., Begovic E., Chapman J., Putnam N.H., Hellsten U.,
RA   Kawashima T., Kuo A., Mitros T., Salamov A., Carpenter M.L.,
RA   Signorovitch A.Y., Moreno M.A., Kamm K., Grimwood J., Schmutz J.,
RA   Shapiro H., Grigoriev I.V., Buss L.W., Schierwater B., Dellaporta S.L.,
RA   Rokhsar D.S.;
RT   "The Trichoplax genome and the nature of placozoans.";
RL   Nature 454:955-960(2008).
CC   -!- PATHWAY: Protein modification; protein sumoylation.
CC       {ECO:0000256|ARBA:ARBA00004718}.
CC   -!- SIMILARITY: Belongs to the PIAS family.
CC       {ECO:0000256|ARBA:ARBA00005383}.
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DR   EMBL; DS985243; EDV26398.1; -; Genomic_DNA.
DR   RefSeq; XP_002110394.1; XM_002110358.1.
DR   AlphaFoldDB; B3RRR7; -.
DR   STRING; 10228.B3RRR7; -.
DR   EnsemblMetazoa; TriadT54339; TriadP54339; TriadG54339.
DR   GeneID; 6751609; -.
DR   KEGG; tad:TRIADDRAFT_54339; -.
DR   CTD; 6751609; -.
DR   eggNOG; KOG2169; Eukaryota.
DR   HOGENOM; CLU_470389_0_0_1; -.
DR   InParanoid; B3RRR7; -.
DR   OMA; ANQIHVT; -.
DR   OrthoDB; 20246at2759; -.
DR   PhylomeDB; B3RRR7; -.
DR   UniPathway; UPA00886; -.
DR   Proteomes; UP000009022; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0061665; F:SUMO ligase activity; IBA:GO_Central.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016925; P:protein sumoylation; IBA:GO_Central.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR   CDD; cd16650; SP-RING_PIAS-like; 1.
DR   Gene3D; 2.60.120.780; PINIT domain; 1.
DR   Gene3D; 1.10.720.30; SAP domain; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR   InterPro; IPR023321; PINIT.
DR   InterPro; IPR038654; PINIT_sf.
DR   InterPro; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   InterPro; IPR004181; Znf_MIZ.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   PANTHER; PTHR10782:SF94; SUPPRESSOR OF VARIEGATION 2-10, ISOFORM I; 1.
DR   PANTHER; PTHR10782; ZINC FINGER MIZ DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF14324; PINIT; 1.
DR   Pfam; PF02891; zf-MIZ; 1.
DR   SMART; SM00513; SAP; 1.
DR   SUPFAM; SSF68906; SAP domain; 1.
DR   PROSITE; PS51466; PINIT; 1.
DR   PROSITE; PS50800; SAP; 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:UP000009022};
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:PRU00452}.
FT   DOMAIN          2..36
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   DOMAIN          120..287
FT                   /note="PINIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51466"
FT   DOMAIN          317..408
FT                   /note="SP-RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51044"
FT   REGION          444..475
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        451..475
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   580 AA;  65829 MW;  E8F6C9E38BEBBD9F CRC64;
     MLNNFRVPEL QQLLTSFNSR KTGRKPMLIS RALELLETCD SRNVKIKIRE IYNLRNHYHH
     QASNHVVIHN HNHVVPSYSN QSNNNNTNFH VVNNNSRNQI GWYIGDLNNS TSKGHREFHF
     ALNTASKLDF KSLKITPFHE PLESISNTFL LDIKYKGRYY EKEITFTLSS SQIEMLNKTR
     HHINKPENES LHHLFLRLGT VDSNGLFADY YPHALCVKAN GSSCPIPNIA PSASNNSKSG
     TAKKSKKPID ITQYINITPN YTNRVKVSCT PLTVEKYYGS IILVRQSTPG LLLQKILDKD
     DASQEQTISL VKEKLKQNSD VIVTTKLNMS LQCPLMKNLM TYPCRSSSCK HLQCFDAMSF
     LRMNESYCRK IIESIPANVL EISFNEDGSW TAENEDEKSS NVIKDTVEIA HVVKDKPKEH
     NKSVEVIDLT AGSDSEDDNY VPFDDLFTDF QGDTPEPKRL KSDSQPEKRE RQEIPNHSAA
     ITTVFPDYHL YAVPGHSQRS NNYLPNAMPN NLLPHLPITS SLAPEMNNYV CGTYDTVDSE
     FANTMYPDEQ EFIRNCLGNL ASIITPSSNP PSSNRPSKDV
//
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