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Database: UniProt
Entry: A0A397JGA4_9GLOM
LinkDB: A0A397JGA4_9GLOM
Original site: A0A397JGA4_9GLOM 
ID   A0A397JGA4_9GLOM        Unreviewed;       824 AA.
AC   A0A397JGA4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=CCHC-type domain-containing protein {ECO:0000259|PROSITE:PS50158};
GN   ORFNames=Glove_84g178 {ECO:0000313|EMBL:RHZ84224.1};
OS   Diversispora epigaea.
OC   Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Glomeromycotina;
OC   Glomeromycetes; Diversisporales; Diversisporaceae; Diversispora.
OX   NCBI_TaxID=1348612 {ECO:0000313|EMBL:RHZ84224.1, ECO:0000313|Proteomes:UP000266861};
RN   [1] {ECO:0000313|EMBL:RHZ84224.1, ECO:0000313|Proteomes:UP000266861}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IT104 {ECO:0000313|EMBL:RHZ84224.1,
RC   ECO:0000313|Proteomes:UP000266861};
RA   Sun X., Fei Z., Harrison M.;
RT   "Genome and evolution of the arbuscular mycorrhizal fungus Diversispora
RT   epigaea (formerly Glomus versiforme) and its bacterial endosymbionts.";
RL   Submitted (AUG-2018) 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:RHZ84224.1}.
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DR   EMBL; PQFF01000080; RHZ84224.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A397JGA4; -.
DR   STRING; 1348612.A0A397JGA4; -.
DR   Proteomes; UP000266861; Unassembled WGS sequence.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd00303; retropepsin_like; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 1.
DR   Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR   InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR   InterPro; IPR005162; Retrotrans_gag_dom.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR33223; CCHC-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR33223:SF9; CCHC-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF03732; Retrotrans_gag; 1.
DR   Pfam; PF08284; RVP_2; 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:UP000266861};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          454..469
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   REGION          87..146
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          375..415
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          508..545
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          780..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..111
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        375..389
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        508..531
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        780..809
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   824 AA;  94999 MW;  837A6D575A72C53D CRC64;
     MVIAKRRNDC VDEAIKQKNE ALSEIVEREL SREEKDPNYE VTYTLKDLNR VKDHLDLIKH
     HVWIRDNILV DNGRTVFNIP TRENQNPVTV RLPTSDSTTT SSPSATVGTT PRHRRRSNET
     PQSFSQAVSP RRSPEQVTPR VITPPNNWDQ LQNIRTFYQP LQPLDFNLIN QQLAEAHLTA
     SDSSDSSDTD TEDEMANAIL DYLEDNLHNH TSPRVYPFYG DGTQDPLQWM LHFEKVARSN
     AWDEAKKIRK YATYLEDDVE EWHDEINAND MADWAAWRAG FVKKYCNTRW RNKWMRELEN
     NRQRQGETVD AYYARFRRLV KRVDINVNQH KRLFIKGLLP HIAPLITMQA PGTLAAALEL
     AQAYEEGLDM VNEIEPRKQK GKKKVVESSD EEEEEEAEEK RKPKKTVLKK KKKETKVTFD
     PAHNLDDLAK KFEKMQLNLI QKMEKNNNRE TRTCFKCEKE GHISWDCPDR KDNSDNSAHA
     KLVEVEEESE KEEDKLLQHL LEAYDAYLGK RERDDSSDED TPIKRPRETN TPEPKPSLNT
     FGLPKATSVP VPKVVKTEIT LKKKSKKKEV IKMVKENKEK KKENATRPPL FRKKDFDIVE
     QLQNQPAGLF WADALEVPSI RKSFFEALRK PKEKEIKLAD QEYSLKTIAL KCNVAVGVYT
     VPTIVDSGAA ISIVTRDAME QLGYEIEEAS KSIILPATGK KTQPLGVIRD LPITIQGQTI
     PIDVEVIDAA TYSLLLGNNW LMKANASYNW SDQELTLRWR GKTLTVPANC SKETKEEFSE
     LIENTDEESV NESDTETEES EEDDDEIIFK NTTIEDHDYT CSQN
//
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