ID V5H9N8_IXORI Unreviewed; 636 AA.
AC V5H9N8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative aprataxin and pnk-like factor {ECO:0000313|EMBL:JAB79995.1};
OS Ixodes ricinus (Common tick) (Acarus ricinus).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Ixodinae; Ixodes.
OX NCBI_TaxID=34613 {ECO:0000313|EMBL:JAB79995.1};
RN [1] {ECO:0000313|EMBL:JAB79995.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB79995.1};
RX PubMed=25765539;
RA Kotsyfakis M., Schwarz A., Erhart J., Ribeiro J.M.;
RT "Tissue- and time-dependent transcription in Ixodes ricinus salivary glands
RT and midguts when blood feeding on the vertebrate host.";
RL Sci. Rep. 5:9103-9103(2015).
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DR EMBL; GANP01004473; JAB79995.1; -; mRNA.
DR AlphaFoldDB; V5H9N8; -.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IEA:InterPro.
DR Gene3D; 2.60.200.20; -; 1.
DR InterPro; IPR039253; APLF.
DR InterPro; IPR019406; APLF_PBZ.
DR InterPro; IPR041388; FHA_2.
DR InterPro; IPR008984; SMAD_FHA_dom_sf.
DR PANTHER; PTHR21315:SF2; APRATAXIN AND PNK-LIKE FACTOR; 1.
DR PANTHER; PTHR21315; UNCHARACTERIZED; 1.
DR Pfam; PF17913; FHA_2; 1.
DR Pfam; PF10283; zf-CCHH; 2.
DR SUPFAM; SSF49879; SMAD/FHA domain; 1.
PE 2: Evidence at transcript level;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT DOMAIN 5..50
FT /note="PNK FHA"
FT /evidence="ECO:0000259|Pfam:PF17913"
FT DOMAIN 461..486
FT /note="Aprataxin and PNK-like factor PBZ"
FT /evidence="ECO:0000259|Pfam:PF10283"
FT DOMAIN 536..560
FT /note="Aprataxin and PNK-like factor PBZ"
FT /evidence="ECO:0000259|Pfam:PF10283"
FT REGION 107..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..636
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..180
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..384
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 385..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..432
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..538
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..609
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 616..630
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 636 AA; 70033 MW; AFEA553864F3FA25 CRC64;
MKKVVLKPVE GPQKPVELKI GKTIIGRGPL LECSDKKVSR NHAILEVTAD GEVILTPTHV
NPCFYQAQNK GPSRVMKKDK QHVLASGDSI ALLPTSYKYI VEVISPSTTS PSSQVADEVT
KPAGESEEKD SLADKPATAA IPAEEAKKNG SAEAHHNSSN NKDSVIKAEN GERGSSKEAS
PEVCRKPATQ PPQKKGVPSD ESKTKPQPEG KRTLPRWLVE SASKSAASKP KPAAQPRGKA
ASNRDEPASK TRRTSVPEKE PVKKRGKPPA KESESGGESK EEAKSGKSEE SGEEKSESEE
EYKPKAREEK GVTGSRESKG SRGGRSSRQN RSTMQKISLD DFVASDDDEW DNSAEEKKPR
RRRKRAAAEE EEEDDDEEDS CSDWEEENCK TKRVARRYVP SDSDSASDWE RSSSRKKKQP
ATRTRVQRKR RRRASSERES SEGESDDAPL KRPTRRTPAK RESCKYGKKC FRKSGQHLKQ
FSHPGDSDYA GESSDKEDEG GEEKDEQGQD RQNHAAEEGK KGKRDQDKEE DEEDNRPLCR
YGAGCFRKNA LHLKNFKHPT PTKKAPASQT PASKKGKRGG KAKGGSSNDE KASGDEYDWK
DEDSENGGDG NGAKEAAKTF SRRKPRASER PSAAVD
//
