ID V5I021_IXORI Unreviewed; 475 AA.
AC V5I021;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Putative peristalsis {ECO:0000313|EMBL:JAB82272.1};
DE Flags: Fragment;
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:JAB82272.1};
RN [1] {ECO:0000313|EMBL:JAB82272.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Salivary gland and midgut {ECO:0000313|EMBL:JAB82272.1};
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; GANP01002196; JAB82272.1; -; mRNA.
DR AlphaFoldDB; V5I021; -.
DR CDD; cd00071; GMPK; 1.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd11861; SH3_DLG-like; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR008144; Guanylate_kin-like_dom.
DR InterPro; IPR020590; Guanylate_kinase_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23119; DISCS LARGE; 1.
DR PANTHER; PTHR23119:SF51; DISKS LARGE 1 TUMOR SUPPRESSOR PROTEIN; 1.
DR Pfam; PF00625; Guanylate_kin; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF07653; SH3_2; 1.
DR SMART; SM00072; GuKc; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS00856; GUANYLATE_KINASE_1; 1.
DR PROSITE; PS50052; GUANYLATE_KINASE_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50002; SH3; 1.
PE 2: Evidence at transcript level;
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 9..90
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT DOMAIN 119..189
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT DOMAIN 285..460
FT /note="Guanylate kinase-like"
FT /evidence="ECO:0000259|PROSITE:PS50052"
FT REGION 229..266
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:JAB82272.1"
SQ SEQUENCE 475 AA; 53376 MW; DDA57E913CD660D8 CRC64;
EDIPRDPRKV VLSKGPTGLG FNIVGGEDGE GIFISFILAG APADASGELR RGDQILSVNG
VDLRHATHEQ AAAALKGAGH TVTMHVQYRP DEYNRFEAKI HDLREQMLNT TGSLRTSQKR
SLYVRALFEY EPSRDSGLPS RGLPFRFGDI LHVINASDDE WWQARKILPD GHEDFVGIIP
SKRRVERRER ARLKSVKFQG KSSYSDGKGT LERKKKNFSF SRKFPFMKSK DNSTEDGSDV
ERDGSPTKDT ANTSYASDSE ASSTRGIDEP VLSYEAVVQQ EISYTRPIII LGPLKDRIND
DLISEYPEKF GSCVPHTTRP KRDYEVDGRD YHFVASREQM ERDIQNHLFI EAGQYNDNLY
GTSVASVREV AEKGKHCILD VSGNAIKRLQ VAGLEPIAIF IKPKSVESIM EMNKRITEEQ
ARKTFERAAK LELEFAEYFT AIIQGEAPEE IYKKVKNVID DNGGPSAWVA AKEKL
//
