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Database: UniProt
Entry: E6ZI68_DICLA
LinkDB: E6ZI68_DICLA
Original site: E6ZI68_DICLA 
ID   E6ZI68_DICLA            Unreviewed;      1450 AA.
AC   E6ZI68;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=ribonuclease H {ECO:0000256|ARBA:ARBA00012180};
DE            EC=3.1.26.4 {ECO:0000256|ARBA:ARBA00012180};
GN   Name=POL {ECO:0000313|EMBL:CBN81752.1};
GN   ORFNames=DLA_XVIII00100 {ECO:0000313|EMBL:CBN81752.1};
OS   Dicentrarchus labrax (European seabass) (Morone labrax).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Moronidae; Dicentrarchus.
OX   NCBI_TaxID=13489 {ECO:0000313|EMBL:CBN81752.1};
RN   [1] {ECO:0000313|EMBL:CBN81752.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Kuhl H., Tine M., Hecht J., Knaust F., Reinhardt R.;
RT   "Analysis of single nucleotide polymorphisms in three chromosomes of
RT   European sea bass Dicentrarchus labrax.";
RL   Comp. Biochem. Physiol. Part D Genomics Proteomics 6:70-75(2011).
RN   [2] {ECO:0000313|EMBL:CBN81752.1}
RP   NUCLEOTIDE SEQUENCE.
RX   DOI=10.1016/j.ygeno.2011.06.004;
RA   Kuhl H., Tine M., Beck A., Timmermann B., Kodira C., Reinhardt R.;
RT   "Directed sequencing and annotation of three Dicentrarchus labrax L.
RT   chromosomes by applying Sanger- and pyrosequencing technologies on pooled
RT   DNA of comparatively mapped BAC clones.";
RL   Genomics 0:0-0(2011).
RN   [3] {ECO:0000313|EMBL:CBN81752.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Tine M., Kuhl H., Beck A., Bargelloni L., Reinhardt R.;
RT   "Comparative analysis of intronless genes in teleost fish genomes: Insights
RT   into their evolution and molecular function.";
RL   Mar. Genomics 4:109-119(2011).
CC   -!- SIMILARITY: Belongs to the beta type-B retroviral polymerase family.
CC       HERV class-II K(HML-2) pol subfamily. {ECO:0000256|ARBA:ARBA00010879}.
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DR   EMBL; FQ310508; CBN81752.1; -; Genomic_DNA.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd00303; retropepsin_like; 1.
DR   CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR   CDD; cd01647; RT_LTR; 1.
DR   Gene3D; 1.10.340.70; -; 1.
DR   Gene3D; 2.40.50.40; -; 2.
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; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR   InterPro; IPR023780; Chromo_domain.
DR   InterPro; IPR043502; DNA/RNA_pol_sf.
DR   InterPro; IPR001584; Integrase_cat-core.
DR   InterPro; IPR041588; Integrase_H2C2.
DR   InterPro; IPR005162; Retrotrans_gag_dom.
DR   InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR000477; RT_dom.
DR   InterPro; IPR041577; RT_RNaseH_2.
DR   PANTHER; PTHR24559:SF437; RIBONUCLEASE H; 1.
DR   PANTHER; PTHR24559; TRANSPOSON TY3-I GAG-POL POLYPROTEIN; 1.
DR   Pfam; PF00385; Chromo; 2.
DR   Pfam; PF17921; Integrase_H2C2; 1.
DR   Pfam; PF03732; Retrotrans_gag; 1.
DR   Pfam; PF17919; RT_RNaseH_2; 1.
DR   Pfam; PF00665; rve; 1.
DR   Pfam; PF08284; RVP_2; 1.
DR   Pfam; PF00078; RVT_1; 1.
DR   SMART; SM00298; CHROMO; 2.
DR   SUPFAM; SSF54160; Chromo domain-like; 2.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS50013; CHROMO_2; 2.
DR   PROSITE; PS50994; INTEGRASE; 1.
DR   PROSITE; PS50878; RT_POL; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022918};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          455..634
FT                   /note="Reverse transcriptase"
FT                   /evidence="ECO:0000259|PROSITE:PS50878"
FT   DOMAIN          973..1132
FT                   /note="Integrase catalytic"
FT                   /evidence="ECO:0000259|PROSITE:PS50994"
FT   DOMAIN          1274..1324
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   DOMAIN          1388..1446
FT                   /note="Chromo"
FT                   /evidence="ECO:0000259|PROSITE:PS50013"
FT   REGION          48..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          278..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..861
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..67
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..89
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1450 AA;  162149 MW;  2121B25AE4999AFF CRC64;
     MDPADPDSVR SALAYQGQRV GQHEKVLDEI VAAIQDLRCS VAALGSKLDQ VSTPPTAPTT
     ATEAATPSAS PAMPHAASPP PPPREPHVPT PERYAGDLGA CGRFLLQCSL VFQQQPLTYS
     SDSAQVAFVI SLLSGKAAQW ATALWEKHSP ICDSFQRFSE ELRKVFDHPV QGKEAAKRLL
     NLRQGSGSVA EFSVEFRILA AESGWDEEAL QTVFVHGLSE VMKDELAARD SAASLDELIS
     LAIRLDNRLR ERQRERRGRP QASPFPALPR ATISVGPQLA APSKHPSSQI PPEPVEEPMQ
     LGRTRLTQAE RQRRISPPYS HAIKCVPSLA VNSIPLTALV DSGAEESFID SAFVLQARIP
     TVKLPDNQPV NALDGKHLAN ITRQTVPLTL ILSGNHQYHD LGEVFSKHRA VTLPPHRPYD
     CAIELLPGST LPTSRLYNLS RPEREAMEKY IGDSLAAGLI RPSSSPVGAG FFFVTKKDQT
     LRPCIDYRGL NDITIKNKYP LPLIDPAFEP LHKAQVFSKL DLRNAYHLVR IREGDEWKTA
     FNTPLGHFEY LVMPFGLTNA PAVFQALVND VLRDMLNRFL FVYLDDILIF SQSQEEHVQH
     VRQVLQRLLE NKLFVKAEKC EFHVTSVSFL GFIIERGQVK ADPAKIQAVA DWPSPTTRKQ
     LQRFLGFANF YRRFIRNYSK VAAPLTKLTS VKVPFAWSPE AENAFLALKE LFTSAPVLHH
     PDPSLQFVVE VDASDTGVGA VLSQRSPKDQ KLHPCAFLSR RLSPAERNYD VGNRELLAVV
     VALQEWRHWL EGAALPFIVW TDHKNLAYLR SAKRLNSRQA RWALFLDRFV FTLTYRPGSR
     NAKPDALSRQ ADPETQETEP ETILPASCVV PAVNWRIEAL VKQAQRSQPD PGNGPPNRLF
     VPDSARSQVL QWAHASKISC HPGYQRTLDF LRRKFWWPSM ARDTRAFVAA CSVCARGKSS
     HQPPAGLLHP LPVPRRPWSH IAVDFVTGLP TSEGNDTILT IVDRFSKSVH FVPLPKLPSS
     LETAKLLVTH VFRLHGIPQD IVSDRGPQFA SQVWRAFCQA LGASVSLSSG YHPQSNGQTE
     RANQQLEAAL RCVAARHPVS WCSFLPWIEY AHNSLTCAAT GMSPFMAAYG FQPPLFPSQE
     GEVAVPSVQD HLRRCRRIWT EARAALLRTA ARNQRLADRH RLPAPDYTPG QKVWLSSRDL
     PLQVESRKLA PRFIGPFEVD RIINPVAVRL KLPPSLHVHP VFHVSLLKPV SSSPLCPPAD
     PPPPPRLIDD HPAYTVRQIL DVRRRGRGFQ YLVDWEGYGP EERSWVPRHF ILDSSLLSDF
     YRSHPDKPGS LCAVWLPVSA HLCLCVSGLF RHLTHPFLLW PPLIPPAPLC PPADPPPPPR
     LIDDHPAYTV RQILDVRRRG RGFQYLVDWE GYGPEERSWV PRHFILDSSL LSDFYRSHPD
     KPGRPPGGVL
//
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