ID   A0A158QCC4_HYMDI        Unreviewed;       814 AA.
AC   A0A158QCC4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Lactamase_B domain-containing protein {ECO:0000313|WBParaSite:HDID_0000126901-mRNA-1};
OS   Hymenolepis diminuta (Rat tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Hymenolepididae; Hymenolepis.
OX   NCBI_TaxID=6216 {ECO:0000313|Proteomes:UP000046397, ECO:0000313|WBParaSite:HDID_0000126901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:HDID_0000126901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
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DR   AlphaFoldDB; A0A158QCC4; -.
DR   STRING; 6216.A0A158QCC4; -.
DR   WBParaSite; HDID_0000126901-mRNA-1; HDID_0000126901-mRNA-1; HDID_0000126901.
DR   Proteomes; UP000046397; Unplaced.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050313; F:sulfur dioxygenase activity; IEA:InterPro.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   CDD; cd07724; POD-like_MBL-fold; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
DR   Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR044528; POD-like_MBL-fold.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR43084; PERSULFIDE DIOXYGENASE ETHE1; 1.
DR   PANTHER; PTHR43084:SF1; PERSULFIDE DIOXYGENASE ETHE1, MITOCHONDRIAL; 1.
DR   Pfam; PF00753; Lactamase_B; 1.
DR   Pfam; PF00096; zf-C2H2; 4.
DR   SMART; SM00849; Lactamase_B; 1.
DR   SMART; SM00355; ZnF_C2H2; 4.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 2.
DR   SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          512..539
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          540..567
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          568..595
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          596..623
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          280..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..381
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          398..441
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          469..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..814
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..322
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        398..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..504
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        679..814
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   814 AA;  87743 MW;  EC7BC053744CF4D0 CRC64;
     LIKMTSKISI LAAGGPLIFR QLFEKTSSTF TYLLGDGTSK QALIIDPVLE TAERDARLIN
     ELGLDLRYVM DTHVHADHVT GVGMLKRIFG PTCKSVIPEV SGGRADILVR DAEVLKCGNI
     ELDCHTNGCF TYVLHSARSA FTGDALLIRG CGRTDFQEGS PERLYESVHS KILSLPEDYL
     LFPAHEYAGR MMTTVAEEKK FNPSKFPCSM DSPPQLECLK ADQFHTVNDQ RIALEVAQSE
     VSASIDRLQN TLNQQLFISD YLRNCITKLS AVSRVFSEIE NGDENSGGEE PPSLKSDDRQ
     TPPQCDSNST TTSALNLSVP SPTHTQSLSL IPSFFNSTSP LLSSTSRNLL LHSSLNSQSA
     KSDSMQVKSE GSPGSQRITP TTMENAVRCM VDDISAATSK VNSSHGHHFH SSNHQQGQQQ
     LPSHLTPPGP PPLSLPSDDF PANTFNAARS VAAAVSAALG FHFPPPDMFN LNPPQSSSQT
     PSSLSSKHNG IPGSPESHNS KSTAEDYASR PYRCTTCGRG FAVKAGLMQH LRTHTDERPY
     PCPECGRAFK QKIQLTTHMR VHSGERPYGC RICGKLFRQQ SHVVQHLRTH TGEKPHKCTR
     CNKAFRQKYS LISHQRRMCQ SRSSSSSALM AGMTMWIGPG GRAAEKAAAK AAAAALQNGL
     RTAHSTNLLP PPPLGNCTSP ISLPFSAPQP ASNERNSSPV VSTKMEDRVS SSPASSHGGD
     VGGNSNSFRQ PSPHLKHSPT GGLNSASSSA GRSFHENDYS IATTSSTSSY PSPYHSGATD
     LRMNTGNGGA TSESAFPTRL DNTPSATPME TAGV
//