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Database: UniProt
Entry: A0A3M0J9V1_HIRRU
LinkDB: A0A3M0J9V1_HIRRU
Original site: A0A3M0J9V1_HIRRU 
ID   A0A3M0J9V1_HIRRU        Unreviewed;      1265 AA.
AC   A0A3M0J9V1;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:RMB97030.1};
GN   ORFNames=DUI87_26477 {ECO:0000313|EMBL:RMB97030.1};
OS   Hirundo rustica rustica.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Sylvioidea; Hirundinidae;
OC   Hirundo.
OX   NCBI_TaxID=333673 {ECO:0000313|EMBL:RMB97030.1, ECO:0000313|Proteomes:UP000269221};
RN   [1] {ECO:0000313|EMBL:RMB97030.1, ECO:0000313|Proteomes:UP000269221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Chelidonia {ECO:0000313|EMBL:RMB97030.1};
RC   TISSUE=Blood {ECO:0000313|EMBL:RMB97030.1};
RA   Formenti G., Chiara M., Poveda L., Francoijs K.-J., Bonisoli-Alquati A.,
RA   Canova L., Gianfranceschi L., Horner D.S., Saino N.;
RT   "A high quality draft genome assembly of the barn swallow (H. rustica
RT   rustica).";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes viral DNA integration into the host chromosome, by
CC       performing a series of DNA cutting and joining reactions.
CC       {ECO:0000256|ARBA:ARBA00003235}.
CC   -!- SIMILARITY: Belongs to the beta type-B retroviral polymerase family.
CC       HERV class-II K(HML-2) pol subfamily. {ECO:0000256|ARBA:ARBA00010879}.
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:RMB97030.1}.
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DR   EMBL; QRBI01000170; RMB97030.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0J9V1; -.
DR   STRING; 333673.A0A3M0J9V1; -.
DR   Proteomes; UP000269221; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
DR   CDD; cd07557; trimeric_dUTPase; 1.
DR   Gene3D; 1.10.10.200; -; 1.
DR   Gene3D; 1.10.1200.30; -; 1.
DR   Gene3D; 2.70.40.10; -; 1.
DR   Gene3D; 3.30.70.270; -; 2.
DR   Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR   Gene3D; 1.10.375.10; Human Immunodeficiency Virus Type 1 Capsid Protein; 1.
DR   Gene3D; 2.30.30.10; Integrase, C-terminal domain superfamily, retroviral; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 2.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR029054; dUTPase-like.
DR   InterPro; IPR036157; dUTPase-like_sf.
DR   InterPro; IPR033704; dUTPase_trimeric.
DR   InterPro; IPR045345; Gag_p24_C.
DR   InterPro; IPR017856; Integrase-like_N.
DR   InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
DR   InterPro; IPR001037; Integrase_C_retrovir.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR003308; Integrase_Zn-bd_dom_N.
DR   InterPro; IPR008916; Retrov_capsid_C.
DR   InterPro; IPR008919; Retrov_capsid_N.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR002156; RNaseH_domain.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR010661; RVT_thumb.
DR   PANTHER; PTHR41694; ENDOGENOUS RETROVIRUS GROUP K MEMBER POL PROTEIN; 1.
DR   PANTHER; PTHR41694:SF3; RNA-DIRECTED DNA POLYMERASE-RELATED; 1.
DR   Pfam; PF00692; dUTPase; 1.
DR   Pfam; PF00607; Gag_p24; 1.
DR   Pfam; PF19317; Gag_p24_C; 1.
DR   Pfam; PF00552; IN_DBD_C; 1.
DR   Pfam; PF02022; Integrase_Zn; 1.
DR   Pfam; PF00075; RNase_H; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   Pfam; PF06817; RVT_thumb; 1.
DR   SUPFAM; SSF50122; DNA-binding domain of retroviral integrase; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF51283; dUTPase-like; 1.
DR   SUPFAM; SSF46919; N-terminal Zn binding domain of HIV integrase; 1.
DR   SUPFAM; SSF47353; Retrovirus capsid dimerization domain-like; 1.
DR   SUPFAM; SSF47943; Retrovirus capsid protein, N-terminal core domain; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 2.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS51027; INTEGRASE_DBD; 1.
DR   PROSITE; PS50879; RNASE_H_1; 1.
DR   PROSITE; PS50878; RT_POL; 1.
DR   PROSITE; PS50876; ZF_INTEGRASE; 1.
PE   3: Inferred from homology;
KW   DNA integration {ECO:0000256|ARBA:ARBA00023195};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Endonuclease {ECO:0000256|ARBA:ARBA00022759};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000269221};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884};
KW   RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transposable element {ECO:0000256|ARBA:ARBA00022464};
KW   Viral genome integration {ECO:0000256|ARBA:ARBA00023195};
KW   Virus entry into host cell {ECO:0000256|ARBA:ARBA00023296};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00450};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00450}.
FT   DOMAIN          402..596
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          816..952
FT                   /note="RNase H type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50879"
FT   DOMAIN          957..998
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50876"
FT   DOMAIN          1006..1168
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   DOMAIN          1180..1227
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51027"
FT   DNA_BIND        1180..1227
FT                   /note="Integrase-type"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00506"
FT   REGION          390..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1219..1265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1240..1265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1265 AA;  138867 MW;  EEB8648FB9E3D93D CRC64;
     MQVLRSFNVS LLTPFDIRSL ARALFPPVEY DFFENKWTQL AVRAVEWNTT LGPGDPRRMV
     NIDMLMGTGN YTRAEGQAGY EPLVQEQCQQ TGMAALVQTL QLATPQQPFA TIVQGVDEPF
     LCFAGRLTAA VEKQVSDPAA RKLMIQSVAQ GNCNAACKRI IEALPGEPSM SDMVGACAKI
     SPSSQQVVAV HTAVQPAVAT IVQPTVATAV QPAVPAAVQP AVAAAVQPAW VVPQGVQQQQ
     WGARARKKQR KAQKPTAVLF YCARCGRPNH AANACKATVH VNAPTNGDLL SRLAASTRGS
     AGVDVCTAES VVIDSDKIRK VPLDAFGPLG DGMSAFLMGR SSATIQGIIV HLGLIDADFS
     GQIHAMVSTP TPPLTIPKGT RTAQLVPFKS SVSRTEDRSR GDGGFGSTGP PQVRWTAVLT
     KDRPETLCTV SMVAATPSEI HLRGLLDGMV ASLQAGMPSP TMLPADWLVL IVDLKDCFFT
     IPLHPDDRPK FAFTVPTINN AEPAQRYQWR VLPQGMRNSP MLCQWYVARA LSGVRKRFPG
     AHVYHYMDDI LVATPTQEEL LRLQPQLLNA LHSHGLQVAP EKVQQQPPWK YLGVKILERT
     IRHQEVQFVQ SVKTLNDAQK LVGVITWLRP YLGLTTAQLS PLFELLKGDT DLKSPRELTP
     EARKVLEEVQ QAVSACQVYR IEPSIDVTVF ITTPDLHPTG IIGQWNDDWT DPLHVLEWVF
     LPHQPHKTAT ALFELIARLI IKCRQRCLQL MGADPSKIIL PVQREEFDWS YANNVSLQSA
     LEGFSGQITY HLPSHKLLQV AKNTQFSLRP KSSQEPVQGP TVFTDGSGKT GKAIVTWQDG
     SEWQVLEGHE DGSAQLVELK AAVMAFEKFS QEPFNLITDS AYVADIAQRL SCSVLKEVSN
     PALFDLLKAL WCAIQARVHP YYVLHVRSHT NLPGFVAEGN ARADKLANPA WVAPQPDVLA
     QAKASHGFFH QNAHTLQKQF QLTATEAREI VESCDDCHAL GVPLPAGVNP RGLKALELWQ
     TDVTQVAEFG RLKYVHVTVD TFSSAMWASA HTEEKARDVI AHWRQAFAVL GIPSAVKTDN
     GPAYASQQVR QFLQSWGVSH NFGIPHSPTG QAIVERNHGT LKCVLQKQKQ GMQGETPKSR
     LAKALYTINH LTVPQNSNNP VILNHHLSLQ ASDGEQQPRA KARVRNLVTK QWEGPYDLIA
     MGRGYACVST DTGTRWLPSK CVRPDLRPQR QNSADRQGGS RDQLESHQVD ESSSDHSDDS
     STDSD
//
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