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Database: UniProt
Entry: A0A3S0ZIV1_ELYCH
LinkDB: A0A3S0ZIV1_ELYCH
Original site: A0A3S0ZIV1_ELYCH 
ID   A0A3S0ZIV1_ELYCH        Unreviewed;       810 AA.
AC   A0A3S0ZIV1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=CCHC-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EGW08_023749 {ECO:0000313|EMBL:RUS68489.1};
OS   Elysia chlorotica (Eastern emerald elysia) (Sea slug).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Sacoglossa; Placobranchoidea;
OC   Plakobranchidae; Elysia.
OX   NCBI_TaxID=188477 {ECO:0000313|EMBL:RUS68489.1, ECO:0000313|Proteomes:UP000271974};
RN   [1] {ECO:0000313|EMBL:RUS68489.1, ECO:0000313|Proteomes:UP000271974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC2010 {ECO:0000313|EMBL:RUS68489.1};
RC   TISSUE=Whole organism of an adult {ECO:0000313|EMBL:RUS68489.1};
RA   Cai H., Li Q., Fang X., Li J., Curtis N.E., Altenburger A., Shibata T.,
RA   Feng M., Maeda T., Schwartz J.A., Shigenobu S., Lundholm N., Nishiyama T.,
RA   Yang H., Hasebe M., Li S., Pierce S.K., Wang J.;
RT   "A draft genome assembly of the solar-powered sea slug Elysia chlorotica.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RUS68489.1}.
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DR   EMBL; RQTK01002578; RUS68489.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3S0ZIV1; -.
DR   STRING; 188477.A0A3S0ZIV1; -.
DR   Proteomes; UP000271974; Unassembled WGS sequence.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   Gene3D; 1.10.340.70; -; 1.
DR   Gene3D; 1.10.4020.10; DNA breaking-rejoining enzymes; 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; IPR001584; Integrase_cat-core.
DR   InterPro; IPR041588; Integrase_H2C2.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR003309; SCAN_dom.
DR   InterPro; IPR038269; SCAN_sf.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR46888:SF8; SCAN BOX DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR46888; ZINC KNUCKLE DOMAINCONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF17921; Integrase_H2C2; 1.
DR   Pfam; PF02023; SCAN; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 2.
DR   SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50804; SCAN_BOX; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271974};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          239..313
FT                   /note="SCAN box"
FT                   /evidence="ECO:0000259|PROSITE:PS50804"
FT   DOMAIN          375..390
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          730..810
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          76..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          131..155
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        131..148
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   810 AA;  91908 MW;  10FECBB8B68B81A9 CRC64;
     MHHRCDTITI REIRTGPFLQ HELYKTKVVV ADGKDERTSE ALTSLRSIKE IRLRDGDLGT
     QQKWEEREAK LLKEEREAKK EEREAKLQAE KEEREAKLQA EREEREAKLQ AEKELKMEEM
     RTQLELARIQ AQASQQSEHN LTSGSTRSVH EGEHSKFKMP KLPAFVDRKD DLDSWLLRFE
     RFATTSGWPK ESWCTPLSAL LTGRALEAFC RLSETEATDY DRVKEVLQKR YNLTEDGYRQ
     RFRTCSPEEG ENPSMFIVRL KTYLERWMKL AEAPQTYEAL RDLFVKEQFL DSSPADLSTY
     LRERRLADLE EVARSAELFL TARKRQLSDR ARQGITREQN RPSSSKEEEI ICHICRKPGH
     STRNCRNKAT HGRGCYHCGE LTHVRKDCPK LRMNNSQITS SKRAGSAAMR VMETQESASG
     EDAGKADTRY DVRTEVQDGL LQLASGKRVP AMIDCGACGG KGSARELNLP IVKGLVGDKT
     VDVLRDTGCE GVVVRRGLVG DDQLTGKCCL IVRIDNTVLL AEKARIQVKT PYLSGEVEAL
     CIPEVICDLV VGNVPGARNP DDPDMTPMVG AVTTRAQARQ EVRHRPLTVP DTPKHTGVDR
     RELIRLQQDD EAIKRMGDSV LSENRTGRTS FFEKKDGIVY RVYNDEIRGG VNVRQVVLPE
     SLRKYVMSVA HDTITGGHLG IKKTREKIMS NFFWPGMYED VARYCRSCDI CQKTVSKGTV
     QKAPMENIPV VDVPFKRVAV DLIGPIEPAS EAGHRYILTL VDYATRYPEA VPLRRIDTET
     VAEALVDIYS RLGVPEEILS DQGTQFIRIV
//
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