ID   A0A183P438_9TREM        Unreviewed;       545 AA.
AC   A0A183P438;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=RING-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012483};
DE            EC=2.3.2.27 {ECO:0000256|ARBA:ARBA00012483};
OS   Schistosoma mattheei.
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=31246 {ECO:0000313|WBParaSite:SMTD_0000912301-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SMTD_0000912301-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
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};
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DR   AlphaFoldDB; A0A183P438; -.
DR   STRING; 31246.A0A183P438; -.
DR   WBParaSite; SMTD_0000912301-mRNA-1; SMTD_0000912301-mRNA-1; SMTD_0000912301.
DR   GO; GO:0005856; C:cytoskeleton; IEA:InterPro.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   CDD; cd12873; SPRY_DDX1; 1.
DR   Gene3D; 2.60.120.920; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   InterPro; IPR001870; B30.2/SPRY.
DR   InterPro; IPR043136; B30.2/SPRY_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000299; FERM_domain.
DR   InterPro; IPR018980; FERM_PH-like_C.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR045129; RNF123/RSPRY1-like.
DR   InterPro; IPR003877; SPRY_dom.
DR   PANTHER; PTHR13363:SF5; E3 UBIQUITIN-PROTEIN LIGASE RNF123; 1.
DR   PANTHER; PTHR13363; RING FINGER AND SRY DOMAIN-CONTAINING; 1.
DR   Pfam; PF09380; FERM_C; 1.
DR   Pfam; PF00622; SPRY; 1.
DR   SMART; SM01196; FERM_C; 1.
DR   SMART; SM00449; SPRY; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   PROSITE; PS50188; B302_SPRY; 1.
DR   PROSITE; PS50057; FERM_3; 1.
PE   4: Predicted;
FT   DOMAIN          1..70
FT                   /note="FERM"
FT                   /evidence="ECO:0000259|PROSITE:PS50057"
FT   DOMAIN          267..466
FT                   /note="B30.2/SPRY"
FT                   /evidence="ECO:0000259|PROSITE:PS50188"
SQ   SEQUENCE   545 AA;  60649 MW;  552C0D9098F4F372 CRC64;
     LLYRNRIRLM RVSWPRIISL SHRGRNFIIA RRPGDDSLDR NMTFKCISAT LAKRLYNVCV
     DHHNFFRLRG SSRPKKPSLF PSFATRKYHY PGTTVNSSSI DATVGVGGHN QTSRPLSKFR
     PMPAHPSETG WFTFANRGEM DHMNGAVASQ YQYQPAMVSG DPACMDPTYF CNQNVINGLP
     IPNAQGVQRY YQPSSNDVTG LMNGHHPNSN NNHINNMPTM ITRISFEPEH WRITGADCTA
     GLGIDARGLD VASTRGAGWQ KARLAFANLR DIHLSTKGRV YCAAVRSILL YGSETWPVRV
     EDIRRLLVFD HRCLRNIARI SWDYRVSNGC RANKGVKAPG AYYYEAACLE EGLIRVGWST
     NDANLELGAD NYGFGYGSDA VGSAGMNGTG RVMHRNTGHD YGIMVHQGDV IGCLLDLDKG
     SISWSCNGKI FQRAFTIPDQ LRGEAFLPAA SLKDSRILFN FGEEQPLEFP PDGSFIPVAQ
     SADDSQVSNR NPGWRMNQYD ATNALDVAPD GSQVQSHFNQ GWQGCRSNHV STFRLLAYIA
     LALIE
//