ID A0AAE0RFJ3_9TELE Unreviewed; 1663 AA.
AC A0AAE0RFJ3;
DT 29-MAY-2024, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2024, sequence version 1.
DT 28-JAN-2026, entry version 9.
DE RecName: Full=ribonuclease H {ECO:0000256|ARBA:ARBA00012180};
DE EC=3.1.26.4 {ECO:0000256|ARBA:ARBA00012180};
DE Flags: Fragment;
GN ORFNames=QTP70_031538 {ECO:0000313|EMBL:KAK3551917.1};
OS Hemibagrus guttatus.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Bagridae; Hemibagrus.
OX NCBI_TaxID=175788 {ECO:0000313|EMBL:KAK3551917.1, ECO:0000313|Proteomes:UP001274896};
RN [1] {ECO:0000313|EMBL:KAK3551917.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Male_cb2023 {ECO:0000313|EMBL:KAK3551917.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:KAK3551917.1};
RA Bian C.;
RT "Male Hemibagrus guttatus genome.";
RL Submitted (JUN-2023) to the EMBL/GenBank/DDBJ databases.
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:KAK3551917.1}.
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DR EMBL; JAUCMX010000003; KAK3551917.1; -; Genomic_DNA.
DR Proteomes; UP001274896; Unassembled WGS sequence.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0031012; C:extracellular matrix; IEA:TreeGrafter.
DR GO; GO:0005615; C:extracellular space; IEA:TreeGrafter.
DR GO; GO:0030020; F:extracellular matrix structural constituent conferring tensile strength; IEA:TreeGrafter.
DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:TreeGrafter.
DR FunFam; 2.60.120.200:FF:000039; Collagen XV alpha 1 chain; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.1620.70; -; 1.
DR Gene3D; 3.60.10.10; Endonuclease/exonuclease/phosphatase; 1.
DR Gene3D; 3.10.10.10; HIV Type 1 Reverse Transcriptase, subunit A, domain 1; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 2.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR050149; Collagen_superfamily.
DR InterPro; IPR010515; Collagenase_NC10/endostatin.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR000477; RT_dom.
DR InterPro; IPR048287; TSPN-like_N.
DR InterPro; IPR045463; XV/XVIII_trimerization_dom.
DR PANTHER; PTHR24023; COLLAGEN ALPHA; 1.
DR PANTHER; PTHR24023:SF1101; COLLAGEN ALPHA-1(VII) CHAIN ISOFORM X3; 1.
DR Pfam; PF01391; Collagen; 3.
DR Pfam; PF20010; Collagen_trimer; 1.
DR Pfam; PF06482; Endostatin; 2.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SMART; SM00210; TSPN; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR SUPFAM; SSF56219; DNase I-like; 1.
DR PROSITE; PS50878; RT_POL; 1.
PE 3: Inferred from homology;
KW Collagen {ECO:0000256|ARBA:ARBA00023119};
KW Reference proteome {ECO:0000313|Proteomes:UP001274896};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 1218..1502
FT /note="Reverse transcriptase"
FT /evidence="ECO:0000259|PROSITE:PS50878"
FT REGION 190..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 499..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..842
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..212
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..239
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 249..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..290
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 312..321
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..368
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..416
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..428
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 553..563
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 589..604
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..657
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 663..674
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 781..791
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 806..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..925
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 936..945
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1663
FT /evidence="ECO:0000313|EMBL:KAK3551917.1"
SQ SEQUENCE 1663 AA; 176625 MW; 88123AC8D0F7E00C CRC64;
RGSSSQLDLT ELIGVPLPPS VSFITGFEGF PAYSFGPDAN VGRLTRSFIP DPFFHDFAII
VTAKPTTRHG GVLFAITDAL QKIVHLGVAL APVEDGSQRV ILYYTEPGAT RTQEAASFKM
GDLTGRWARF TLAVQGDEVK LYMDCEEHHR VALHRSQKSL TFEPSSGIFV GNAGGTKLER
FVGSIQQLVL TPDPRAPDEQ CEEDDPYPDE DQTLPIRAPP TEASSEAPFD DEDLEEESSG
QDVVLTENEP SRPEKAVYHK GDDYPLMMPV HKGEKGDRGP PGPPGSPGPP GTTGSYGHKG
DSSSWVGQPG AQGPPGPPGP TGAPGKDGLP GERGNPGFPG IPGDPGIKGE KGDHGVGLPG
PPGPPGPPGR SGTPRYVDAI DGSGFEDFDS DTEVIRGPPG PPGPPGKPGP PGPPVGLSPG
PVGPSGAPGK DGKDGVMGNP GIPVIEDWFS GSGFDAGSGF DAGSGFHSGS GFHSGSGFDI
ESGIDAESIF KLGSDLDLVE GVNGRDGEPG KEGQKGEKGE AGLPGNAGQK GDSGQPGLPG
AAGSEGPMGK PGPAGPPGPP GPPARFNFDV LDSEGSGVGG GSGFGPNLPR GPPGIPGLPG
PPGPKGKDGV NGLPGTSEKG EPGPEGPEGK PGLPGLPGRH GEKGEKGEIG QKGERGLDGV
SRPGPPGPPG PPGPVINIQD LLLNDTEGIY NFTGLFEPQG PLGPRGPKGD RGIPGVQGSP
GLKGDSGVPG LPGVMLDFIC LYTCYKGYSI DWKTVVPQGH DFSVFGFIKQ GPVGPRGPKG
EFGFPGRPGR PGLNGHKGEK GDSNGLPINS NSTAEGASCS TSGAKGEKGE RGLPGPPGPT
ITMLSGGTMG EKGVYGFQGE KGEKGEAGMP GVTGLPGTSG LVGPKGESVV GPPGRPGLQG
PPGSPGIGRP GATGPRGPPG PPGPPGYSSG AVIRGPPGPP GPPGPAGSAA GGSVKKYSNL
YAMKQESYLV EEGTLSMVRD TSKLYLKVQG GWREIQLGGL IEVNSPSVLS QDDLRLVALN
TPLTGDLGSI HSVNKQCRLQ AQAMGIRDEY RAFLSHHLQD LIDIVQPPYR TSLPIVNLRG
EVLFKNWESI FSSHVLPAGI PLYSFDGRDV MSDPFCTNFI PDRSRPGLTT TAIGAVDLQG
AGGNWATVGR RSRGGRRVRR QREKRKGKSV GLRIGTLNVG TMTGKGRELA DMMERRKVDI
LCVQETRWKG SKARNIGAGF KLFYYGVDSK RNGVGVVLKE EFVRNVLEVG CELEEKERFW
SELDEVMESI PKGERVVIGA DFNGHVGEGN TGDEEVMGKF GVKERNLEGQ MVVDFAKRMD
MGVVNTYFQK REEHRVTYKS GDLEKAYDRV PREELWYCMR KSGVAEKYVR VVQDMYERSR
TVVRCAVGQT EEFNVEVGLH QGSALSPFLF AIVMDQLSEE VRQESPWTMM FADDIVICSE
SREQVEENLE RWRFALERRG MKVSRSKTEY MCVNEREGSG TVRLQGEEVK KVQEFKYLGS
TVQSNGECGK EVKKRVQAVW NGWRKVSGVL CDRKISARIK GKVYRTVVRP AMLYGLETVS
LRKRQASELE VAELKMLRPQ KAIWHGSSER GRRLEDKNCE SWRAGDMAIT GQASFLYSGL
LNQQTRSCSN QFVVLCIETN PNHNTVEELQ RAQLRHRRWH YRY
//
