ID A0A1I8CQH9_9BILA Unreviewed; 972 AA.
AC A0A1I8CQH9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=receptor protein-tyrosine kinase {ECO:0000256|ARBA:ARBA00011902};
DE EC=2.7.10.1 {ECO:0000256|ARBA:ARBA00011902};
OS Rhabditophanes sp. KR3021.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Tylenchina; Panagrolaimomorpha; Strongyloidoidea; Alloionematidae;
OC Rhabditophanes.
OX NCBI_TaxID=114890 {ECO:0000313|Proteomes:UP000095286, ECO:0000313|WBParaSite:RSKR_0000735400.1};
RN [1] {ECO:0000313|WBParaSite:RSKR_0000735400.1}
RP IDENTIFICATION.
RC STRAIN=KR3021 {ECO:0000313|WBParaSite:RSKR_0000735400.1};
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
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DR AlphaFoldDB; A0A1I8CQH9; -.
DR WBParaSite; RSKR_0000735400.1; RSKR_0000735400.1; RSKR_0000735400.
DR Proteomes; UP000095286; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005003; F:ephrin receptor activity; IEA:InterPro.
DR GO; GO:0000003; P:reproduction; IEA:UniProt.
DR CDD; cd00063; FN3; 2.
DR CDD; cd00192; PTKc; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR Gene3D; 2.10.50.10; Tumor Necrosis Factor Receptor, subunit A, domain 2; 1.
DR InterPro; IPR027936; Eph_TM.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR011641; Tyr-kin_ephrin_A/B_rcpt-like.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR016257; Tyr_kinase_ephrin_rcpt.
DR PANTHER; PTHR46877; EPH RECEPTOR A5; 1.
DR PANTHER; PTHR46877:SF14; RECEPTOR PROTEIN-TYROSINE KINASE; 1.
DR Pfam; PF14575; EphA2_TM; 1.
DR Pfam; PF07699; Ephrin_rec_like; 1.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000666; TyrPK_ephrin_receptor; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM01411; Ephrin_rec_like; 1.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF57184; Growth factor receptor domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRSR:PIRSR000666-
KW 2}; Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRSR:PIRSR000666-2}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 449..470
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 207..315
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 553..827
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 855..891
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 855..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 688
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-1"
FT BINDING 559..567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
FT BINDING 594
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PIRSR:PIRSR000666-2"
SQ SEQUENCE 972 AA; 109879 MW; 5AB2CCCA32468E07 CRC64;
MVRDEDTHPK NIPADRWVLL TTISLYTQKQ TVGRDKRSVV VVDYVPVSDA VMFAIKEKDA
CMVVYRLQVY FNVCPGTTIN QIQLPETIVS ADEYVPTYFH AHCVKNAVDV SNANTDRNVF
CQGNGQWKIG EKSRCQCNAG YTASDEGACS ACPKGSYKSD TGNEVCKPCP RNSKSHENGS
KICECENDFY RADNEDHTNI CSQPPSAPLN LKVISLHQSE AVLTWAKPTY LGHRSDIYYS
VTCELCNDNG KDCTKCPSTV IFNFNSERIV THEISMSKLE PGKQYVATVF ANNAVSKKEM
NPKNSMRIAF VTKKANGYKI SAPTLLTHEN NGTLVIAWLA ADNISKYHNV YYQVELKNSK
EVILHDSSQN AMKIDNVDVY ESHAIRVRVN DARDGWSEWS DALVVKNKYS KAESAVKNVQ
DVVVSEDGQE KVEKDSYLYR YVYLENPKLV YIFGCVMLLI FVVCVMCYFC PRRSKKGDYF
AELVKSQNQE LPYNFGIPSS GFRESNNCLE SFKGSSTFID GNTNKNYIDP STYGDLTVAM
REFTRQIPKA NIFMTNEMLG EGEFGNVEKG IILLNGNLKT ASVAEGTEVT VACKTLKKVA
TEMEKKLFTM EATTMGQFQH DNVLRLLGVV GTDYVEIIIT EFMVNGSLIN YLKLNSINTC
SKVQLTQICL DISEGMQYLH KTGYIHRDLA SRNILLDQFY RCKISDFGLS RNGFAEGSDE
MEYTNAMAKK IPIRWTAPEA LEKGTYTAAS DIWSYGVVMW EIFSFGERPY YDWPHRKIYE
EVLQGYRLPK SMDCPEAIYQ IMTQCWNKEK GERPTFFTIT PKLRAYIRIY EESLDYAVNS
PLYQTPTEAT YEVARDDNCN NGNSRNGFYQ PPPNHSEAPT GTTRNTKSSK WEIAESPKDQ
LERLSEMDLT LTEQKQLAVA IDSIVTSRRP QTGNKARKNP YHADQSFRGS SMNIKAFSSS
LKKEPTDGGF LV
//
