ID   A0A0K0EA42_STRER        Unreviewed;       527 AA.
AC   A0A0K0EA42;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=CCHC-type domain-containing protein {ECO:0000313|WBParaSite:SSTP_0000636900.1};
OS   Strongyloides stercoralis (Threadworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Strongyloididae;
OC   Strongyloides.
OX   NCBI_TaxID=6248 {ECO:0000313|WBParaSite:SSTP_0000636900.1};
RN   [1] {ECO:0000313|WBParaSite:SSTP_0000636900.1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (AUG-2015) to UniProtKB.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; A0A0K0EA42; -.
DR   STRING; 6248.A0A0K0EA42; -.
DR   WBParaSite; SSTP_0000636900.1; SSTP_0000636900.1; SSTP_0000636900.
DR   Proteomes; UP000035681; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0019899; F:enzyme binding; IEA:UniProt.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR019103; Peptidase_aspartic_DDI1-type.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   Pfam; PF09668; Asp_protease; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000035681};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          205..220
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
SQ   SEQUENCE   527 AA;  61354 MW;  464B3EA290C8F132 CRC64;
     MTTWTTVGEF KVDKGEAIGH WLGMLTNRLA VDNITSNERC KAALLSLLCE DAIEYVDTLG
     IEKKDTYEHL CNALKEKYDG SVSRLTAESM LRSYVIDMRE NEFLESCIKF VDLIKCVSKS
     TGTTLTQLQI ERLTSKLENK HELWSISVGT KNQTDIKELL AELNTVHLLT CQRNRRISRI
     QNEHRHENES VKDGKKRLDN NNKQCFNCKE EGHFKRNCPK LKVEKNETFD GNKLYRVLKN
     PMVKTIILPM KVNGIETEGL VDLGAEQSVA TVEAAKKFNM KKIKPSNAQL ILGNGSRWSV
     LGTAEKEITL GKTKVPLEIM LMNKQEFELA CPTEFLIGTD LTMKLKRYTI DHEKHNFLFK
     ILRAIEIILK RLNYLEVKQD RQENMNKCEK CLRTNNPHKK KYAKSKDNEE YMANMDKKLK
     KVTLYHHQEN SITERQIRSV NNRMRKISNK KGCDKRTFKE NYFNREMAFK VTELITKENE
     NKSNNTIHTT SGQTPHKFFY GWESNTTYNR KTFKDPGYVV DFKKFRN
//