ID A0A0R3PB96_ANGCS Unreviewed; 695 AA.
AC A0A0R3PB96;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 2.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=ShKT domain-containing protein {ECO:0000313|WBParaSite:ACOC_0000093801-mRNA-1};
GN ORFNames=ACOC_LOCUS939 {ECO:0000313|EMBL:VDM52524.1};
OS Angiostrongylus costaricensis (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Metastrongylidae;
OC Angiostrongylus.
OX NCBI_TaxID=334426 {ECO:0000313|Proteomes:UP000050601, ECO:0000313|WBParaSite:ACOC_0000093801-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ACOC_0000093801-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDM52524.1, ECO:0000313|Proteomes:UP000267027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Costa Rica {ECO:0000313|EMBL:VDM52524.1,
RC ECO:0000313|Proteomes:UP000267027};
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU01005}.
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DR EMBL; UYYA01000119; VDM52524.1; -; Genomic_DNA.
DR STRING; 334426.A0A0R3PB96; -.
DR WBParaSite; ACOC_0000093801-mRNA-1; ACOC_0000093801-mRNA-1; ACOC_0000093801.
DR OMA; WATIGEC; -.
DR Proteomes; UP000050601; Unplaced.
DR Proteomes; UP000267027; Unassembled WGS sequence.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004601; F:peroxidase activity; IEA:InterPro.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd09823; peroxinectin_like; 1.
DR Gene3D; 1.10.640.10; Haem peroxidase domain superfamily, animal type; 1.
DR InterPro; IPR019791; Haem_peroxidase_animal.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR037120; Haem_peroxidase_sf_animal.
DR InterPro; IPR003582; ShKT_dom.
DR PANTHER; PTHR11475; OXIDASE/PEROXIDASE; 1.
DR PANTHER; PTHR11475:SF51; SHK DOMAIN AND PEROXIDASE DOMAIN CONTAINING PROTEIN; 1.
DR Pfam; PF03098; An_peroxidase; 1.
DR Pfam; PF01549; ShK; 2.
DR PRINTS; PR00457; ANPEROXIDASE.
DR SMART; SM00254; ShKT; 2.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS50292; PEROXIDASE_3; 1.
DR PROSITE; PS51670; SHKT; 2.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU01005};
KW Heme {ECO:0000256|PIRSR:PIRSR619791-2};
KW Iron {ECO:0000256|PIRSR:PIRSR619791-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR619791-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000267027}.
FT DOMAIN 27..61
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT DOMAIN 67..101
FT /note="ShKT"
FT /evidence="ECO:0000259|PROSITE:PS51670"
FT BINDING 465
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR619791-2"
FT DISULFID 27..61
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
FT DISULFID 67..101
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01005"
SQ SEQUENCE 695 AA; 78636 MW; 8E8D2A0B19EB71AA CRC64;
MAFPTLPTLT SKNDSPPLLE RNRVSRCVDQ HDLCKFWGSI GECQANKEWM EDHCPVSCDV
CNGTMACVDR HRLCSFWSAI RECETNAVWM LANCARACKA CKGRTVGITG GSGKDGVFRE
EDCTFVTTHE GKAYTSHRKT LSINDVRNSN ANFNCAPTQQ SPNCNRNLCY HLRFRTFDGT
CNNLNRPLAG SAFSALVRLK TPMYDNGLNA PTSSFTRTRP SSRDASRLLL SSPAQIPHHS
NALLMQWGQF IAHDMSKTTM LNNQECAACT SNQGRCFSVF LSRADPTFGR FMCLPVARST
PVCGTGQSNI REQFNENTAF VDGSMIYGSS DRDQFLFRRG AFLKTKLVKN RVFPPIDTNM
NVVAGDDRAN IFVGLAALHT LFVREHNKIA STLQQVNPHW DQERIFHETR KIIGAIIQKI
TYYEYLPRVL GEEFERRIGD YTGYDKNTDP SVANEFTSCA FRFGHGMIQE FYPFLDEKFQ
NVGGIPFNDG MFKSIHILNN GIDPLLRGFI TLPAKMPQRL TPAVTERIFG NSDLGSINIQ
RGRDHGVPAF TRWRTFCGLP EIKEFDDLNK TITNKVVIEN LRVMYKHVDA IDMYVGSLLE
DPVKDSLVGP TLACVIGEQF KRSRNGDRFY FENEKVFTLD QLHQIRKITI ARVLCDSGEN
FAFVPRRAFN VFKPSRDSLM RSVQFQLHDI KLITS
//
