ID A0A0V0V3E7_9BILA Unreviewed; 2508 AA.
AC A0A0V0V3E7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Phorbol ester/diacylglycerol-binding protein unc-13 {ECO:0000313|EMBL:KRX57937.1};
DE Flags: Fragment;
GN Name=unc-13 {ECO:0000313|EMBL:KRX57937.1};
GN ORFNames=T09_2844 {ECO:0000313|EMBL:KRX57937.1};
OS Trichinella sp. T9.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX57937.1, ECO:0000313|Proteomes:UP000054681};
RN [1] {ECO:0000313|EMBL:KRX57937.1, ECO:0000313|Proteomes:UP000054681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS409 {ECO:0000313|EMBL:KRX57937.1};
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:KRX57937.1}.
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DR EMBL; JYDN01000093; KRX57937.1; -; Genomic_DNA.
DR Proteomes; UP000054681; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0098793; C:presynapse; IEA:UniProt.
DR GO; GO:0004000; F:adenosine deaminase activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0019992; F:diacylglycerol binding; IEA:InterPro.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:InterPro.
DR GO; GO:0005543; F:phospholipid binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0007268; P:chemical synaptic transmission; IEA:InterPro.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd14978; 7tmA_FMRFamide_R-like; 1.
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 Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR InterPro; IPR002466; A_deamin.
DR InterPro; IPR046349; C1-like_sf.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
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; PF00001; 7tm_1; 1.
DR Pfam; PF02137; A_deamin; 2.
DR Pfam; PF00130; C1_1; 1.
DR Pfam; PF00168; C2; 3.
DR Pfam; PF06292; MUN; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR SMART; SM00552; ADEAMc; 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 SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1.
DR PROSITE; PS50141; A_DEAMIN_EDITASE; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054681};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 2167..2192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2204..2230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2250..2280
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2292..2310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2341..2369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2401..2423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 2443..2462
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 586..636
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 693..819
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1126..1269
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 1373..1529
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 1544..1671
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 1803..2133
FT /note="A to I editase"
FT /evidence="ECO:0000259|PROSITE:PS50141"
FT DOMAIN 2184..2459
FT /note="G-protein coupled receptors family 1 profile"
FT /evidence="ECO:0000259|PROSITE:PS50262"
FT REGION 210..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 134..171
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 303..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX57937.1"
SQ SEQUENCE 2508 AA; 285304 MW; 25C1C6408EE1529D CRC64;
LLLTQEMSLL CICVKKARLH GASDEVHSYV TLKLQNVKST TVAVKGSEPC WEQDETERLD
LGLIFELWSQ GVLWDKLMGV YFMPLTSVHY SNVAGSGKWL QLFSEVETKN GEVVGHRGQT
SHLLLADVRF ELPLEFNDEE AQILQQKLEA LNRMDEEIST AQLQMKRAQF NRSGISEDSD
YTSDISYPVH LNNSSAHQFG NHLRTCCKST DNAEQPSSVR MSLEDERDYA TNSKQNAEEQ
TSFEYQYYDE QHLGEPQSPG SVSRVDYNST SVHENSYHAN DKPSNFDSKN CHPEVNTAAK
RRANLRASKE RTYSSEHEVS DHMSPCSDSE PLFYNTMAFI RTLLAIQYAE IPSHAKAPIR
RSSYLYVTGV LFTVVSGLDW PAEFTKCSDS HPMVSPQTSL ESASTHTVKT EFGSKDESSV
LIKEQPCDGL VNTASSQIGF TTEQPVSVRP TNDISAIIKP SEENCLQPVN GSEMNLTSVN
LEMSNAKKRW VTAFRRICEQ LGPKESFLES SPKTYDFYTS IDAMPNIALL KKKSVPLVSE
LTMATKRAQA GLASAACTTF GNEELKMRVY RKTLQALIYP ISVSTPHNFQ VWTATSPTYC
YECEGLLWGL ARQGLRCSEC GVKCHEKCKD LLSADCLQRA AEKSSKHSGS GDRAQSIISA
MKDRMKIQER NKAEVFEYIR RVFDVDKKMH HEAMKQVKQC ILEGTAKWSA KIAITVICAQ
GLSAKDKTGK SDPYVTVQVG KVKKRTRTIH QELNPFWSEK FYFECHNSTD RVKLSLCCRD
EDNDLKSKLR QKLTRESDDF LGQTIIEVRT LSGEMDVWYN LEKRTDKSAV SGAIRLQINV
EIKGEEKVAP YHDQYTCLHE HIFNYYCSKE MGQLKLPDAR GDESWKVYFD ETGQEIVDEF
AMRYGIESIY QAMIHFACLC TKYMCQGVPA VISTLLANIN AYYAHTTATS AVSASDRFAA
SNFGKDRFVK LLDQLHNSLR IDISMYRNNF PASNAGKLQD LKSTVDLLTS ITFFRMKVLE
LTSPPRASTV VRECATACIK STYQFLFENC YELFQREFEG NQALTTNPEL VGPSTDSVEF
WHKMIALMIS VIEEDRNIYT PVLNQFPQEL NIGQLSAATM WSQYTIDLKL ALEEHSEQRK
CKSSDYMNLY FKVKWFYNNY VADIPPYKGT IPEFPVWFIP FVMQWLNEND EISMDFLRGA
FERDKKDNYP QSSEHTLFSN SVVDVFTQLN QGLDVLRKMD CPDPDVYGDM MKRFSKTVNK
VLLAYADMVQ KDFSRYVGNE KLACILMNNV QQLRVQLEKM YESMGGAMLD QDAQQVLKGL
QSKLNNVLES LTHVFAASLE SNIYDSTVKL GNLLMRVKGG GQVQKSQVTA EADLILEPLM
DLLDVSLTQY AQQCEKTVLK KLLKELWRIT ISCMEKLVVL PVFPDRNLLK QLPNAKIGDM
SKLLSNHLKE VKNISSVKEV MDLARESDRS LTPKQCTVLD ASLDTVKSYF HAGGSGLKKS
FLEKSAEYQS LKYALSLYTQ TTDQLIKTFI ALQKEQDSPS QEEPVGEVSV QVDLFTHPGT
GEHKVTVKIL AANDLRWQTT GVFRPFIEVH IVGPNQADKK RKFATKTKTN NWAPKFNEVF
YFILGNEDEL ENYELIFQAK DYCFAREDRL IGVGVLQLRS FAEHGSCACW VQLGRRQYID
DTGLILLRIL SQRHYDEIAK QFVKLKTESR YEKKSLIAFD YNVWQTFYYA MMQVIVFHFQ
NCEMVLICPN PQWKHLNNDS LNLTVAPSDT QLWLIGLPKY EDEWTHFASI CASFPDESVE
VLSFGMGTKC LGASQLDKNG YSINDSHAEV LARRGFVGFL FEEFQNVYFG LVSKYFYLVD
SKIGLIDGGD ASIFSVNEAE NSVMNNSRPM HADDIFRTGA KCVLSGPQDP HGKLNKFHIV
SQFRTKPGRG EPTLSMSCSD KIAKWSVMGI QGCLASAFLL QPIYLSSVIL GKCPYSEAAL
RRAIVERNFG FQSDHQEYTF HEPKFHFSDM QDYSLSSGSS CRQKPLSRRQ RKPCSTSSVW
FCGLSRAEIL VDGYLQGSTK LSRSRFGSGG RCSAVCRRRL AVRSLSIGRL IASVEHSHSS
GQSPLGGVIY ENFKSAHSAY MNVWKQLKEH YRHWIHNNMQ SERGVNVSLE ILNMDSCNHY
PYDRFSFVIR VSCMIPIVLF GLITNSINIA VFRHRSMRSS VVNWYLIALS VSDLIVLLGA
FCMLSLPAIS EESGILKLMN LACLTQRWTY AIALIGQTWS VGMTLMVSTH RFLGVCYPFV
AQRWCTSEKV KVVLYSTIGF AFLFNMPRWA EIETAPCWSN VFNTTAVHVI TSKIRQNPTY
YIAYMMISYT TVMFGLPFIL LSIVSVCIVR SLRHSCTLRR QLTRLNNVDD RREMRENRTT
LMLVAIVIMF LICNSLAFIN NIIEAFLDNN DTLEVFYLKS VEISNLLVGI NSSANIFIYS
FFSVKYRLVC KRYFLLLFGG KNGRQQARDL KPKESRYEQR RRSFRLKQ
//
