ID A0A0V1MIH0_9BILA Unreviewed; 1746 AA.
AC A0A0V1MIH0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 08-NOV-2023, entry version 31.
DE SubName: Full=Phorbol ester/diacylglycerol-binding protein unc-13 {ECO:0000313|EMBL:KRZ71656.1};
GN Name=adat {ECO:0000313|EMBL:KRZ71656.1};
GN ORFNames=T10_3007 {ECO:0000313|EMBL:KRZ71656.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ71656.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ71656.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ71656.1};
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:KRZ71656.1}.
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DR EMBL; JYDO01000092; KRZ71656.1; -; Genomic_DNA.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0098793; C:presynapse; IEA:UniProt.
DR GO; GO:0019992; F:diacylglycerol binding; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
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 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 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:UP000054843};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 47..155
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 641..691
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 748..861
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1138..1281
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 1392..1548
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 1563..1690
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 264..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 360..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 189..226
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 360..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1746 AA; 198816 MW; 3439443F87894C8A CRC64;
MKSISDENFA TLILCYIRDL KLDKVKKARL HGVNVELGNE NLFIISPCQG NLFRLFYVQQ
KMELNAEMFR VEVRKHEVHS YVTLKLQNVK STTVAVKGSE PCWEQEFIFE TERLDLGLIF
ELWSQGVLWD KLMGVYFMPL TSVHYSNVAG SGKWLQLFSE VETKNGEVVG HRGQTSHLLL
ADVRFELPLE FNDEEAQILQ QKLEALNRMD EEISTAQLQM KRAQFNRSGI SEDSDYTSDI
SFPVHLNNSS AHQFGSHLRT CCKSTDNAEQ PSSIRMSLED ERDYATSSNK NAEEQSSFEY
QYYDEQHLGE PQSPSSVSRV NYNSTDVHDN SYHANDKPNM PFDSKNCHTE VNTAAKRRAN
LRASKERTYS SEHEVSDHMS PCSDSEPLFY NSRPNDSHGI YSDSFGDSIC RNSISRKGSN
SSSMSSQQNF STLLKSKCSD SHPMVSPQTS LESASTHTVK TGFGSKDEFS VLKQQPCDGL
ENTASSLINS CAEQSTSVRP FDSVTNDTSA INERPSEENC LQAVNGSEMN ITSVNQEMSN
AKKRWVTAFR RICEQLGPKE SFLESSPKTY DFYTSIDAMP NIALLKKKSV PLVSELTMAT
KRAQAGLASA ACTTFGNEEL KMRVYRKTLQ ALIYPISVST PHNFQVWTAT SPTYCYECEG
LLWGLARQGL RCSECGVKCH EKCKDLLSAD CLQRAAEKSS KHSGSGDRAQ SIISAMKDRM
KIQERNKAEV FEYIRRVFDV DKKMHHEAMK QVKQCILEGT AKWSAKIAIT VICAQGLSAK
DKTGKSDPYV TVQVGKVKKR TRTIHQELNP FWMNVIILLI EDEDNDLKSK LRQKLTRESD
DFLGQTIIEV RTLSGEMDVW YNLEKRTDKS AVSGAIRLQI NVEIKGEEKV APYHDQYTCL
HEHIFNYYCS KEMGQLKLPD ARGDESWKVY FDEIGQEIVD EFAMRYGIES IYQAMIHFAC
LCTKYMCQGV PAVISTLLAN INAYYAHTTA TSAVSASDRF AASNFGKDRF VKLLDQLHNS
LRIDISMYRV LELTSPPRAS TVVRECATAC IKSTYQFLFE NCYELFQREF EGNQALTTNP
ELVGPSTDSV EFWHKMIALM ISVIEEDRNI YTPVLNQFPQ ELNIGQLSAA TMWSQYTIDL
KLALEEHSEQ RKCKSSDYMN LYFKVKWFYN NYVSDIPPYK GTIPEFPVWF IPFVMQWLNE
NDEISMDFLR GAFERDKKDN YPQSSEHTLF SNSVVDVFTQ LNQGLDVLRK MDCPDPDVYG
DMMKRFSKTV NKVLLAYADM VQKDFSRYVG NEKLVKFDLK QACILMNNVQ QLRVQLEKMY
ESMGGAMLDQ DAQQVLKGLQ SKLNNVLEGL THVFAASLES NIYDSTVKLG NLLMRVKGGG
QVQKSQVTAE ADLILEPLMD LLDVSLTQYA QQCEKTVLKK LLKELWRITI SCMEKLVVLP
VFPDRNLLKQ LPNAKIGDMS KLLSNHLKEV KNISSVKEVM DLARESDRSL TPKQCTVLDA
SLDTVKSYFH AGGSGLKKSF LEKSAEYQSL KYALSLYTQT TDQLIKTFIA LQKEQDSPSQ
EEPVGEVSVQ VDLFTHPGTG EHKVTVKILA ANDLRWQTTG VFRPFIEVHI VGPNQADKKR
KFATKTKTNN WAPKFNEVFY FILGNEDELE NYELIFQAKD YCFAREDRLI GVGVLQLRSF
AEHGSCACWV QLGRRQYIDD TGLILLRILS QRHYDEIAKQ FVKLKTESRY EKKSLIACDY
NLKQNW
//
