ID W4VR57_9DIPT Unreviewed; 1353 AA.
AC W4VR57;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=RNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012493};
DE EC=2.7.7.49 {ECO:0000256|ARBA:ARBA00012493};
DE Flags: Fragment;
OS Corethrella appendiculata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Chaoboridae;
OC Corethrella.
OX NCBI_TaxID=1370023 {ECO:0000313|EMBL:JAB55725.1};
RN [1] {ECO:0000313|EMBL:JAB55725.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary glands {ECO:0000313|EMBL:JAB55725.1};
RA Ribeiro J.M.C., Chagas A.C., Pham V.M., Lounibos L.P., Calvo E.;
RT "An insight into the sialome of the frog biting fly, Corethrella
RT appendiculata.";
RL Insect Biochem. Mol. Biol. 44:23-32(2014).
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DR EMBL; GANO01004146; JAB55725.1; -; mRNA.
DR GO; GO:0042575; C:DNA polymerase complex; IEA:UniProt.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0071897; P:DNA biosynthetic process; IEA:UniProt.
DR GO; GO:0015074; P:DNA integration; IEA:InterPro.
DR CDD; cd09274; RNase_HI_RT_Ty3; 1.
DR CDD; cd01647; RT_LTR; 1.
DR Gene3D; 1.10.340.70; -; 1.
DR Gene3D; 3.10.20.370; -; 1.
DR Gene3D; 3.30.70.270; -; 2.
DR Gene3D; 2.40.70.10; Acid Proteases; 1.
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 Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 1.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR001584; Integrase_cat-core.
DR InterPro; IPR041588; Integrase_H2C2.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
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; IPR041373; RT_RNaseH.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR PANTHER; PTHR37984:SF7; INTEGRASE CATALYTIC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR37984; PROTEIN CBG26694; 1.
DR Pfam; PF17921; Integrase_H2C2; 1.
DR Pfam; PF17917; RT_RNaseH; 1.
DR Pfam; PF00665; rve; 1.
DR Pfam; PF00078; RVT_1; 1.
DR SMART; SM00343; ZnF_C2HC; 2.
DR SUPFAM; SSF50630; Acid proteases; 1.
DR SUPFAM; SSF56672; DNA/RNA polymerases; 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 2: Evidence at transcript level;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Transposable element {ECO:0000256|ARBA:ARBA00022464};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 197..211
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 1042..1197
FT /note="Integrase catalytic"
FT /evidence="ECO:0000259|PROSITE:PS50994"
FT REGION 239..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1213..1242
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1295..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..256
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 257..271
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1306..1329
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB55725.1"
SQ SEQUENCE 1353 AA; 155048 MW; 1D008F8658F71CC6 CRC64;
LGNLEAYTQD TCINFWLLRL DQFIICNNVH DNKKVAMLLT MIGGDAFAYL VKHFLPTSPD
TKTYPELVEA CKKLFSKKVN KRVARYRFHK CIQQDAQPIK EYVMVLKEVS QDCDYGDALM
EQLLDQFIVG VSDGSLREKL WDEEGDLDFE KACKLAESHE MNLKSNREIE TKAEIHAFNR
SKVPEKRNYG AKTFGTCFRC GKRTHDETEC PARNYKCYFC FEKGHSKFQC PKRRNLNHGG
ADASGTSGAN GKKWGNTKNY RKSHRNKGKG AGNYHRVQEL SDAVEDLNIW PFNMISDDGV
AGDEIIAVGG AVKKLSEPVM LSINVQGHQI QFEVDSGACT SVICEDKYSK YFPNIKLLKA
NRCFTSVTGQ RIPALGKINV RVKLGSGPVH ELELVVIKTK TEVNPLLGRV WLDKLFPEWR
ETWKSSQVRI NAIETFSGVE KLHVQFPDVF EDKPGQTIEG FEADIILQKD AIPIFHVPYT
IPYKLRPKVD QELDRMIKEG VLVPKRYSKW ASPIVVAAKK NGSIRICLDG KATINRYIST
EHYPLPKIED FFPKVANCKY FCVLDLSGAY LQLKVSESSQ EFLTINTFRG LFSYTVMVFG
IKCAPSIFQS VMDQILIGIE NCFCFLDDIC VAGRTFKECW YNLIKVLERL QTHKVRVNMD
KCKFFQSEVN YLGHTISEGS IKPNKDKIRA ITEVKPPNNI TELQSYLGIL NYYGRFIPNL
SSKLLILYNL LHKKEEFVWT SECQRVFEES KHYLTEHNVL EPYDPEKPVI LTVDASPFGV
GAVLSHLVNG QEKPIMFASS TLSISEKRYS QIHREALAVM FGIRKFKNYL YGTKFKLITD
NQALKEIYNP NKGTSSLSMS RLQRWAITLS MFDYEIEHRS AKFLHHADGL SRLPMDNKTG
IEFQAVNCFN ENNSNPIDLK IVEKATRKDP ILSEVFKFLS EGWPINIPKN LVSYFRVTNY
LSTENNCIYF TDRVVIPKEL QNKVLELMHG NHDGIVRTKM LARSHFWWLG MDKSIESYIK
SCEVCEKTQR VKKEVVTSKW PACHKPFQRI HIDFFHFQSE LFLLIVDAYS KYLETIFLTK
SDAKTVIKKL ENFFTIFGLP DEICSDQGPP FESAEFLTFC RSNGIEKSKS PSYHPQSNGL
AERGVSTVKT VLRKFLIDEK SRNFSTTEKL NRFLINYRNT PSTTTGQTPS ELIFKYKPKT
LVSLVKNFPG QHENPNVGKK IVDSEKNSKK RSNESFEMPK PEAHFKRGEK VMYRNHFKEI
VRWIPARVCE QISPLTYNIL VNGRKKMVHQ NQIRKSNLSD KLHPEVISAE NSSSANIPEE
TSVPANSGAS EPINAPRYPK RNLKAPDRYR ASS
//
