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Database: UniProt
Entry: W8AYV9_CERCA
LinkDB: W8AYV9_CERCA
Original site: W8AYV9_CERCA 
ID   W8AYV9_CERCA            Unreviewed;       623 AA.
AC   W8AYV9;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=E3 SUMO-protein ligase PIAS3 {ECO:0000313|EMBL:JAB86101.1};
GN   Name=PIAS3 {ECO:0000313|EMBL:JAB86101.1};
OS   Ceratitis capitata (Mediterranean fruit fly) (Tephritis capitata).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Tephritoidea;
OC   Tephritidae; Ceratitis; Ceratitis.
OX   NCBI_TaxID=7213 {ECO:0000313|EMBL:JAB86101.1};
RN   [1] {ECO:0000313|EMBL:JAB86101.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Geib S.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAB86101.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=24495485; DOI=10.1186/1471-2164-15-98;
RA   Calla B., Hall B., Hou S., Geib S.M.;
RT   "A genomic perspective to assessing quality of mass-reared SIT flies used
RT   in Mediterranean fruit fly (Ceratitis capitata) eradication in
RT   California.";
RL   BMC Genomics 15:98-98(2014).
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; GAMC01020454; JAB86101.1; -; mRNA.
DR   RefSeq; XP_004520545.1; XM_004520488.2.
DR   AlphaFoldDB; W8AYV9; -.
DR   EnsemblMetazoa; XM_004520488.3; XP_004520545.1; LOC101456739.
DR   GeneID; 101456739; -.
DR   OrthoDB; 20246at2759; -.
DR   UniPathway; UPA00886; -.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
DR   GO; GO:0060255; P:regulation of macromolecule metabolic process; IEA:UniProt.
DR   CDD; cd16790; SP-RING_PIAS; 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:SF97; 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   2: Evidence at transcript level;
KW   Ligase {ECO:0000313|EMBL:JAB86101.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
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          76..110
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   DOMAIN          195..360
FT                   /note="PINIT"
FT                   /evidence="ECO:0000259|PROSITE:PS51466"
FT   DOMAIN          392..473
FT                   /note="SP-RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51044"
FT   REGION          1..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          530..561
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..623
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..551
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        586..614
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   623 AA;  68189 MW;  173872DBEF7CD20E CRC64;
     MRKTRSQTQA EAAMANAGRT VSSTSNTPSV VSSSDNSNQP TMVGRGSANI QVAAVSAQKR
     IPQPDHFKIK ECEEMVNLLR VVELQQILSF LNISFAGRKV DLQRRIINLL HSNYDLLAPK
     IREVYTQSIA EQQAQQYGPT DPKRMYSHMQ MPPVPPNSAP GIPNAGQPTA VGGPPIAGVP
     PTGPGVANNM VPFMNPIPTH IPIHPDVRLK KLAFYDVLGV LIKPSSLVPR NTQRIQEVPF
     YFTLTPQQAT EIASNRDIRN SNKIEHAIQV QLRFCLLETS CEQEDCFPPS VSVKVNNKLC
     QLPNVIPTNR PNVEPKRPPR PVNVTANVKL SPTVTNTITV QWCPDYTRGY CIAVYLVKKL
     TSAQLLHRMK TKGVKPADYT RGLIKEKLTE DADCEIATTM LKVSLNCPLG KMKMSIPCRA
     STCSHLQCFD ASLYLQMNER KPTWNCPVCD KAAIYDNLVI DGYFQEVLAS SLLKPDDTEI
     QLHKDGSWST HSLRNEAQVI DTPTKPIEKV EVISDDIVIT TEDVKMVKAG APPATSNDQP
     TSTTNSETVD LTLSDSDDDM PLAKRRPAIK QSAAANTASA VSTSNINING NGGNGNSAGN
     GGSNANQRNA FAQQRTGVRV VLR
//
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