ID A0A1V9XLI7_9ACAR Unreviewed; 700 AA.
AC A0A1V9XLI7;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Tyrosine-protein kinase transmembrane receptor ROR1-like {ECO:0000313|EMBL:OQR74400.1};
DE Flags: Fragment;
GN ORFNames=BIW11_09101 {ECO:0000313|EMBL:OQR74400.1};
OS Tropilaelaps mercedesae.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Parasitiformes; Mesostigmata; Gamasina; Dermanyssoidea; Laelapidae;
OC Tropilaelaps.
OX NCBI_TaxID=418985 {ECO:0000313|EMBL:OQR74400.1, ECO:0000313|Proteomes:UP000192247};
RN [1] {ECO:0000313|EMBL:OQR74400.1, ECO:0000313|Proteomes:UP000192247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wuxi-XJTLU {ECO:0000313|EMBL:OQR74400.1};
RX PubMed=28327890; DOI=10.1093/gigascience/gix008;
RA Dong X., Armstrong S.D., Xia D., Makepeace B.L., Darby A.C., Kadowaki T.;
RT "Draft genome of the honey bee ectoparasitic mite, Tropilaelaps mercedesae,
RT is shaped by the parasitic life history.";
RL Gigascience 6:1-17(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171};
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00121}.
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:OQR74400.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MNPL01008046; OQR74400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V9XLI7; -.
DR STRING; 418985.A0A1V9XLI7; -.
DR InParanoid; A0A1V9XLI7; -.
DR OrthoDB; 1614410at2759; -.
DR Proteomes; UP000192247; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd07459; CRD_TK_ROR_like; 1.
DR CDD; cd00108; KR; 1.
DR CDD; cd05048; PTKc_Ror; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 1.
DR Gene3D; 2.40.20.10; Plasminogen Kringle 4; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR018056; Kringle_CS.
DR InterPro; IPR038178; Kringle_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR041775; Ror-like_CRD.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR PANTHER; PTHR24416:SF611; TYROSINE-PROTEIN KINASE TRANSMEMBRANE RECEPTOR ROR; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF00051; Kringle; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00018; KRINGLE.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00130; KR; 1.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50038; FZ; 1.
DR PROSITE; PS00021; KRINGLE_1; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Kinase {ECO:0000313|EMBL:OQR74400.1};
KW Kringle {ECO:0000256|ARBA:ARBA00022572, ECO:0000256|PROSITE-
KW ProRule:PRU00121}; Membrane {ECO:0000256|SAM:Phobius};
KW Receptor {ECO:0000313|EMBL:OQR74400.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192247};
KW Transferase {ECO:0000313|EMBL:OQR74400.1};
KW Transmembrane {ECO:0000256|SAM:Phobius, ECO:0000313|EMBL:OQR74400.1};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 273..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..180
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 195..269
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 355..642
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 654..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OQR74400.1"
SQ SEQUENCE 700 AA; 78583 MW; 44C3A94696D105DC CRC64;
FLLKVTTVSQ PTQVSLSASS TNVSGFSVFL FYYNSEFHPD DPNIYLSGGK CEIYRGTACE
DHLINQTVYV RPGLSIAMLE EKLAGVLTVV RTSHDVSPDC LKFAIPSLCM FAFPPCDKTV
HTHKPRLVCR DECELLEENI CRMEYTIAKR HPVIGRANIL PDCKKLPDRD TREGANCLAL
GIPLPKIIQL DEDQHCYEGS GESYRGAVSV GISGAACQPW HHQILYSRVA AHEGILGGHT
YCRNPDGSEL GPWCFTEGNR QEICNIPKCA DYMWLYVIVP SVAAIALISL LVSVFCIKRR
TSSKPPPTSL VNNSLQALKV AKNGSAAQSR INTMELNKLL PRTQVRAPEF PLSSIKFIEE
LGEGAFGKVY RGSIIGYDWL ATQQPTVFNN RYLNGTPNGT PNGELPVAVK TLKENATAKI
QQDFQREAEL MADLQHPNIV CLVGVVTRQE PMCLLFEYME HGDLHEYLIA HSPARADSIN
QTLEFADFLH ICRQIAAGME FLAAHHYVHR DLAARNVLVG ENTTVKISDF GLSRDIYSSD
YYRVQAKSLL PVRWMPPEAI LYGKFTAESD VWSFGVVMWE VFSYGCQPYY GYSNQEVTEM
IRARQLLPCP EECPSHVYSM MVECWHEVSA RRPSFSELHN RLCTWQTMHC RSVSQGSRSQ
SSTTNSTMLS QQRRAMDTSM DRCSTPNSHV YQHLIHDPKA
//
