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Database: UniProt
Entry: A0A0N5CMU0_THECL
LinkDB: A0A0N5CMU0_THECL
Original site: A0A0N5CMU0_THECL 
ID   A0A0N5CMU0_THECL        Unreviewed;      1205 AA.
AC   A0A0N5CMU0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Doublecortin domain-containing protein {ECO:0000313|WBParaSite:TCLT_0000147901-mRNA-1};
GN   ORFNames=TCLT_LOCUS1480 {ECO:0000313|EMBL:VDM96949.1};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000147901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TCLT_0000147901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM96949.1, ECO:0000313|Proteomes:UP000276776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00152}.
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DR   EMBL; UYYF01000194; VDM96949.1; -; Genomic_DNA.
DR   STRING; 103827.A0A0N5CMU0; -.
DR   WBParaSite; TCLT_0000147901-mRNA-1; TCLT_0000147901-mRNA-1; TCLT_0000147901.
DR   OMA; WILSMTI; -.
DR   Proteomes; UP000046394; Unplaced.
DR   Proteomes; UP000276776; Unassembled WGS sequence.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   Gene3D; 1.20.5.190; -; 1.
DR   Gene3D; 3.10.20.230; Doublecortin domain; 2.
DR   Gene3D; 2.60.60.20; PLAT/LH2 domain; 2.
DR   InterPro; IPR003533; Doublecortin_dom.
DR   InterPro; IPR036572; Doublecortin_dom_sf.
DR   InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001024; PLAT/LH2_dom.
DR   InterPro; IPR036392; PLAT/LH2_dom_sf.
DR   PANTHER; PTHR45901:SF6; LIPOXYGENASE HOMOLOGY DOMAIN-CONTAINING PROTEIN 1; 1.
DR   PANTHER; PTHR45901; PROTEIN CBG12474; 1.
DR   Pfam; PF03607; DCX; 1.
DR   Pfam; PF00612; IQ; 2.
DR   Pfam; PF01477; PLAT; 1.
DR   SMART; SM00537; DCX; 2.
DR   SMART; SM00015; IQ; 2.
DR   SUPFAM; SSF89837; Doublecortin (DC); 2.
DR   SUPFAM; SSF49723; Lipase/lipooxygenase domain (PLAT/LH2 domain); 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50309; DC; 1.
DR   PROSITE; PS50096; IQ; 2.
DR   PROSITE; PS50095; PLAT; 3.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000276776}.
FT   DOMAIN          65..147
FT                   /note="Doublecortin"
FT                   /evidence="ECO:0000259|PROSITE:PS50309"
FT   DOMAIN          608..726
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DOMAIN          746..861
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   DOMAIN          1158..1205
FT                   /note="PLAT"
FT                   /evidence="ECO:0000259|PROSITE:PS50095"
FT   REGION          1..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          308..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          377..420
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          580..602
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        377..395
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..420
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1205 AA;  136339 MW;  2F9DD9A3AAB402F2 CRC64;
     MSEAEYTATT LPWSSSRSTS DPQSTSQMLN HQPFKLSSNA PNLTNGGVRN FPASNRSFNH
     PYSAKIVFFY KEGDIYFTGI RVPVSKARYR TIESLLDDLN SNISMPFGVR RLTTPRGKTV
     IKNIDQLQHY GRYVASSFKT SRPLNLSMVE KFKKIRQINR TNGLQLNRRA WFNQKQKKNG
     GSKLSPKLSD VPITAKQILF VLNGQPSRIY WVALDSLRSR TIESVLEEVS EGLQTTIFKL
     HTFSGKRIIS INDIFSLNEA RLLAVPRNER PKICGSNISM HLPPLLPPTK ILPPSFNAQT
     CIAKQTIHSS TRENSIEQSQ RSNSNSKTMP LTVMNRMNSI NKLQTLSPKS YREIRIESPQ
     YCPGSLLCEK SVEKQGEMNI TNDEEKSKTV NERNESERMS GNQNLSAEGN DQSNQSSKNT
     DLEMLMTEKV LLEKNSGTEL EANRRQLMNC TETDEQKIQH ICPSFSNRFE HNKNFDAEEV
     SEVQKAATKI QAVYRGYSVR KKFKDEHKSH TELPKYSQQD DQFKLQTEAA IIIQASWRGH
     HSRKLLKQQK LAQAMERQVT TTESDFGAVK LLESQTSNCG SNGCPVASDP SSNFDENDMS
     STDDSENITY TVSVITGNRW AADTDLDLFI ILYGELNKSD KQFLRQDTNE PKFRQNRMDS
     FHIKSAKLGL LQKIIIGHDH IGYGAGVYIE RILVTENIAD GRQYLFQCTK WLDSGQVDGK
     IERILKTTAF CYLTPILYDD IKATSGRWEL ILHSGKPDGS GATTSNLNIV GYSNDSCSVT
     SKIYDNRMAK VPSASLVQVD FGDIGNLLKI RIEIDGYGDM PDYYLDYVEL RDLDTEEHMV
     SYVRKWMKIG SDDKNAQPFR EFPVFRAAFE PLNIFSYEGK IKLTSRKIPF LDGSIAYTKI
     FGELGETGLI PINFQNASDS TLEVPFKAEA VSVGRIRNIR IYIKMSNIGD EIYEGMQVLQ
     SIYHKRLGKR SIPVAGDWIT DKVTIRESHH APYRFVLSFN QQTEMEGLPT KMRKKKVSPK
     KQQHWILSMT IGKESTLVPK VMICSQIDCV EMAIISTTPT DMIINFEKTT NIPIITKVRV
     SVSGDRKLNH TSSNYKPASS HNMIEILKMK LHDSLNGDEV RFPAVNTILT SESVYEFPAV
     WPDIPPSSSK FYFSIADVVY IITIKSGESN GHFDVHLTLI GSKGETGFRK LTNGDTDPFQ
     AQKVC
//
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