ID A0A0V0RRR7_9BILA Unreviewed; 1725 AA.
AC A0A0V0RRR7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Phorbol ester/diacylglycerol-binding protein unc-13 {ECO:0000313|EMBL:KRX17080.1};
GN Name=unc-13 {ECO:0000313|EMBL:KRX17080.1};
GN ORFNames=T07_4375 {ECO:0000313|EMBL:KRX17080.1};
OS Trichinella nelsoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6336 {ECO:0000313|EMBL:KRX17080.1, ECO:0000313|Proteomes:UP000054630};
RN [1] {ECO:0000313|EMBL:KRX17080.1, ECO:0000313|Proteomes:UP000054630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS37 {ECO:0000313|EMBL:KRX17080.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRX17080.1}.
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DR EMBL; JYDL01000094; KRX17080.1; -; Genomic_DNA.
DR STRING; 6336.A0A0V0RRR7; -.
DR Proteomes; UP000054630; Unassembled WGS sequence.
DR GO; GO:0098793; C:presynapse; IEA:UniProt.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019992; F:diacylglycerol binding; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR CDD; cd04027; C2B_Munc13; 1.
DR CDD; cd08395; C2C_Munc13; 1.
DR Gene3D; 1.10.357.50; -; 1.
DR Gene3D; 1.20.58.1100; -; 1.
DR Gene3D; 3.30.60.20; -; 1.
DR Gene3D; 2.60.40.150; C2 domain; 3.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR010439; MUN_dom.
DR InterPro; IPR014770; Munc13_1.
DR InterPro; IPR014772; Munc13_dom-2.
DR InterPro; IPR002219; PE/DAG-bd.
DR InterPro; IPR027080; Unc-13.
DR InterPro; IPR037302; Unc-13_C2B.
DR PANTHER; PTHR10480; PROTEIN UNC-13 HOMOLOG; 1.
DR PANTHER; PTHR10480:SF12; UNC-13, ISOFORM E; 1.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00168; C2; 3.
DR Pfam; PF06292; MUN; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00239; C2; 3.
DR SMART; SM01145; DUF1041; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 3.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR PROSITE; PS50004; C2; 3.
DR PROSITE; PS51258; MHD1; 1.
DR PROSITE; PS51259; MHD2; 1.
DR PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054630};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 1..98
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 579..629
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 686..810
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1117..1260
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 1364..1520
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 1535..1662
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 208..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 132..169
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 301..322
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1725 AA; 195876 MW; E1B794B2AE5DAF4D CRC64;
MNTISDENFA TLILCYIRDE VHSYVTLKLQ NVKSTTVAVK GSEPCWEQEF IFETERLDLG
LIFELWSQGV LWDKLMGVYF MPLTSVHYSN VAGSGKWLQL FSEVETKNGE VVGHRGQTSH
LLLADVRFEL PLEFNDEEAQ ILQQKLEALN RMDEEISTAQ LQMKRAQFNR SGISEDSDYT
SDISFPVHLN NSSAHQFGNH LRTCCKSTDN AEQPSSVRMS LEDERDYATS SKQNAEEQTS
FEYQYYDEQH LGEPQSPGSV SRVNYNSTSV HENSYHANDK PSNFDSKNCH PEVNTAAKRR
ANLRASKERT YSSEHEVSDH MSPCSDSEPL FYNSRPNDSH GIYSDSFGDS ICRNSISRKG
SNSSSMSSQQ NFGTLLKSKC SDSHPMVSPQ TSLESASTHT VKTEFGSKDE SSVLIKEQPC
DGLVNTASSQ IGFSTEQPVS VRPTNDISAI IKPSEENCLQ PVNGSEMNLT SVNLEMSNAK
KRWVTAFRRI CEQLGPKESF LESSPKTYDF YTSIDAMPNI ALLKKKSVPL VSELTMATKR
AQAGLASAAC TTFGNEELKM RVYRKTLQAL IYPISVSTPH NFQVWTATSP TYCYECEGLL
WGLARQGLRC SECGVKCHEK CKDLLSADCL QRAAEKSSKH SGSGDRAQSI ISAMKDRMKI
QERNKAEVFE YIRRVFDVDK KMHHEAMKQV KQCILEGTAK WSAKIAITVI CAQGLSAKDK
TGKSDPYVTV QVGKVKKRTR TIHQELNPFW SEKFYFECHN STDRVKVRVW DEDNDLKSKL
RQKLTRESDD FLGQTIIEVR TLSGEMDVWY NLEKRTDKSA VSGAIRLQIN VEIKGEEKVA
PYHDQYTCLH EHIFNYYCSK EMGQLKLPDA RGDESWKVYF DETGQEIVDE FAMRYGIESI
YQAMIHFACL CTKYMCQGVP AVISTLLANI NAYYAHTTAT SAVSASDRFA ASNFGKDRFV
KLLDQLHNSL RIDISMYRNN FPASNAGKLQ DLKSTVDLLT SITFFRMKVL ELTSPPRAST
VVRECATACI KSTYQFLFEN CYELFQREFE GNQALTTNPE LVGPSTDSVE FWHKMIALMI
SVIEEDRNIY TPVLNQFPQE LNIGQLSAAT MWSQYTIDLK LALEEHSEQR KCKSSDYMNL
YFKVKWFYNN YVADIPPYKG TIPEFPVWFI PFVMQWLNEN DEISMDFLRG AFERDKKDNY
PQSSEHTLFS NSVVDVFTQL NQGLDVLRKM DCPDPDVYGD MMKRFSKTVN KVLLAYADMV
QKDFSRYVGN EKLACILMNN VQQLRVQLEK MYESMGGAML DQDAQQVLKG LQSKLNNVLE
SLTHVFAASL ENNIYDSTVK LGNLLMRVKG GGQVQKSQVT AEADLILEPL MDLLDVSLTQ
YAQQCEKTVL KKLLKELWRI TISCMEKLVV LPVFPDRNLL KQLPNAKIGD MSKLLSNHLK
EVKNISSVKE VMDLARESDR SLTPKQCTVL DASLDTVKSY FHAGGSGLKK SFLEKSAEYQ
SLKYALSLYT QTTDQLIKTF IALQKEQDSP SQEEPVGEVS VQVDLFTHPG TGEHKVTVKI
LAANDLRWQT TGVFRPFIEV HIVGPNQADK KRKFATKTKT NNWAPKFNEV FYFILGNEDE
LENYELIFQA KDYCFAREDR LIGVGVLQLR SFAEHGSCAC WVQLGRRQYI DDTGLILLRI
LSQRHYDEIA KQFVKLKTES RYESELHTTG SSFQLDKLSA NSTAG
//
