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Database: UniProt
Entry: A0A427YEH5_9TREE
LinkDB: A0A427YEH5_9TREE
Original site: A0A427YEH5_9TREE 
ID   A0A427YEH5_9TREE        Unreviewed;       729 AA.
AC   A0A427YEH5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Integrase catalytic domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EHS25_002476 {ECO:0000313|EMBL:RSH89364.1};
OS   Saitozyma podzolica.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Trimorphomycetaceae; Saitozyma.
OX   NCBI_TaxID=1890683 {ECO:0000313|EMBL:RSH89364.1, ECO:0000313|Proteomes:UP000279259};
RN   [1] {ECO:0000313|EMBL:RSH89364.1, ECO:0000313|Proteomes:UP000279259}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27192 {ECO:0000313|EMBL:RSH89364.1,
RC   ECO:0000313|Proteomes:UP000279259};
RA   Aliyu H., Gorte O., Ochsenreither K.;
RT   "Genome sequence of Saitozyma podzolica DSM 27192.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.49;
CC         Evidence={ECO:0000256|ARBA:ARBA00024557};
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:RSH89364.1}.
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DR   EMBL; RSCD01000014; RSH89364.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A427YEH5; -.
DR   STRING; 1890683.A0A427YEH5; -.
DR   Proteomes; UP000279259; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
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; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR001878; Znf_CCHC.
DR   InterPro; IPR036875; Znf_CCHC_sf.
DR   PANTHER; PTHR42648; TRANSPOSASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR42648:SF11; TRANSPOSON TY4-P GAG-POL POLYPROTEIN; 1.
DR   Pfam; PF14223; Retrotran_gag_2; 1.
DR   Pfam; PF00098; zf-CCHC; 1.
DR   SMART; SM00343; ZnF_C2HC; 1.
DR   SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50158; ZF_CCHC; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Reference proteome {ECO:0000313|Proteomes:UP000279259};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   Transposable element {ECO:0000256|ARBA:ARBA00022464};
KW   Transposition {ECO:0000256|ARBA:ARBA00022578};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT   DOMAIN          273..289
FT                   /note="CCHC-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50158"
FT   DOMAIN          508..686
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   REGION          50..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          228..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   729 AA;  79482 MW;  77EA8A3B57CFC84B CRC64;
     MSTDSATPTT LSAVPKLRGN ANYIEWREAI EEQLLAHDLL DIVEGTEEEP FGQKGVRKRR
     AGSVMPTGGT GDPGDAPKAL SAVEVKQWKD WSKRESKAQA WLRMTCTEGP KRSIMGMLSA
     HEMWSHLENT HMVRTIERQG QLLQTLASFR LLSANSKAMT THMESFLVTL SRYETAGGIL
     PESQQIVLFL NSLPAAMEQW KDTYAALDEY RQTWVELERL WNRKVEDKER YETSKGSHSN
     GDALATHGGN HGQKGKKTGE KKEKKQRDMS KVKCWTCEKT GHFKRDCPDA EDSSKKDKTD
     GQANAAVEAE FEAFVGQAVQ DATGLDSEWV IDSGATHHLS GDPKVFASRS DLPEPFSFSL
     AGQGSLTAEQ MGEVPLRLPS GHGLSLQDVY FTPSARLNLL SASRLLSRGW TISLAPSGGR
     ISNGKVDVPL EKRKGLWVLT AKSANQPTHG RVLVTTGAES LHAALGHIRG KKLEDAAAQA
     GLKVADVMRS AEGCSTCAEA KATKQPKAGT SPRGAYAGEL VHVDIAGPFQ PAKAGEDHFL
     ALVDDWSKIS LVVPMGGKTE AYRHLRAFVS IMARLAAPRA VRFVRSDGGG EFGSLEAQAW
     YRETGIQHQV SPPYTPELNG VVERFMRTAK EMITAMLKGS ALPHEYWTHA ARHAACIIMK
     TTKVQGKTAW ERLTGREPTL PTSRVFGQSI TVAIPRAVRT KGSLTNARGV RGTLAQGIGL
     GSLLQSSDQ
//
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