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Database: UniProt
Entry: A0A498M992_LABRO
LinkDB: A0A498M992_LABRO
Original site: A0A498M992_LABRO 
ID   A0A498M992_LABRO        Unreviewed;       932 AA.
AC   A0A498M992;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Gypsy retrotransposon integrase-like protein 1 {ECO:0000256|ARBA:ARBA00039658};
GN   ORFNames=ROHU_009261 {ECO:0000313|EMBL:RXN14095.1};
OS   Labeo rohita (Indian major carp) (Cyprinus rohita).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Labeoninae; Labeonini; Labeo.
OX   NCBI_TaxID=84645 {ECO:0000313|EMBL:RXN14095.1, ECO:0000313|Proteomes:UP000290572};
RN   [1] {ECO:0000313|EMBL:RXN14095.1, ECO:0000313|Proteomes:UP000290572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DASCIFA01 {ECO:0000313|EMBL:RXN14095.1};
RC   TISSUE=Testis {ECO:0000313|EMBL:RXN14095.1};
RA   Das P., Kushwaha B., Joshi C.G., Kumar D., Nagpure N.S., Sahoo L.,
RA   Das S.P., Bit A., Patnaik S., Meher P.K., Jayasankar P., Koringa P.G.,
RA   Patel N.V., Hinsu A.T., Kumar R., Pandey M., Agarwal S., Srivastava S.,
RA   Singh M., Iquebal M.A., Jaiswal S., Angadi U.B., Kumar N., Raza M.,
RA   Shah T.M., Rai A., Jena J.K.;
RT   "Draft genome sequence of Rohu Carp (Labeo rohita).";
RL   Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like
CC       GTPase superfamily. AIG1/Toc34/Toc159-like paraseptin GTPase family.
CC       IAN subfamily. {ECO:0000256|ARBA:ARBA00008535}.
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:RXN14095.1}.
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DR   EMBL; QBIY01012924; RXN14095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A498M992; -.
DR   STRING; 84645.A0A498M992; -.
DR   Proteomes; UP000290572; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   Gene3D; 1.10.340.70; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR006703; G_AIG1.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR041588; Integrase_H2C2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR47266; ENDONUCLEASE-RELATED; 1.
DR   PANTHER; PTHR47266:SF37; INTEGRASE CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF04548; AIG1; 1.
DR   Pfam; PF17921; Integrase_H2C2; 1.
DR   Pfam; PF00665; rve; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS51720; G_AIG1; 1.
DR   PROSITE; PS50994; INTEGRASE; 1.
PE   3: Inferred from homology;
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000290572}.
FT   DOMAIN          131..289
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   DOMAIN          637..820
FT                   /note="AIG1-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51720"
FT   REGION          421..489
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          903..932
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        443..463
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        464..489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        903..918
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   932 AA;  106924 MW;  D305FBFBC4069E5D CRC64;
     MDPKLFEQIF NYKTRGIYPF GIKKEQKYVI RRRSSNFQVD DDKLYHVSKK KNVELRRKVV
     VGRKEANQIF VEFHASPYGA HCGTEKTKLA ISSRFYWPGM GVDIDKWVLQ CADCQFSRLS
     IKQEPKYIPI CVTKPLELLG MDLVGKVTRT RKGNEYICVL VDYYTKWAEA YAIPNKSAAV
     VSRCIINFFY RFGAPKRILT DQGSEFVNQI NRELCGFLSV ERSLCAPYHP QTNGLVEKLN
     GTIQRALCKL VGSQSEKWDE YLDAVMFGLR TKTQLTTRYS PFFLMFGMEA RYPCEVPETF
     EINSTVESVI AENTVSEAIS LKEKMDHIVK ENVGKKQERR HRVATQAPFS VGQKVLRKNI
     RTQQRKGEKL ERSWLGPYEI VFLKEKSADL RDEKGHTYPK INTDHLKLFK EETPRVPHRL
     LLDEPQLKRP HQETSPSPVD IITKEEQPPP SPPSSPTAPK PSPCDSPKSS TSLSPLDLSA
     PLSSPVSHPT TLPTVIPADA KDAVHSYIKS AWAGNDSVVL LSKVGPHKLF YQDILQVINA
     YLMLKVRHHN LTSPEKAFHM DTFAITAMWN GKYQGLKVNP ANYDVIVGIV NECHHWFLVF
     AEHILQNTNI DFSNAPQDVA QFRMEIASTL LEQSDDSQEL RIVLLGVCGA GKSSTANAIL
     GRDVFEESGT RARNISIIDM PGFFNTQLTD EELQEQMMKS LSLTHPGPHV FLLIINLETF
     EEDERNVVQQ IQQNFGEEAL KYTLVLFTGR EHMSNRKWVV FKSNRKFHHL VSHFRGQYHE
     INSKNEIKHS HNAKLLKKID EFIEQNGGQH YNNKSYAVSL MESRTDDEKQ EEKKYTEKQQ
     DIERHQQIIW ETLETNTAME EITAQALSQP QNECFIAYVR HTKKTIYVHE EVIQQRKKSL
     DRMTSFSAEE KHPTRSEKAQ TTSEGVLGSN FF
//
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