ID A0A195BVQ2_9HYME Unreviewed; 1407 AA.
AC A0A195BVQ2;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Protein unc-13 like protein B {ECO:0000313|EMBL:KYM92350.1};
GN ORFNames=ALC53_00805 {ECO:0000313|EMBL:KYM92350.1};
OS Atta colombica.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Atta.
OX NCBI_TaxID=520822 {ECO:0000313|EMBL:KYM92350.1, ECO:0000313|Proteomes:UP000078540};
RN [1] {ECO:0000313|EMBL:KYM92350.1, ECO:0000313|Proteomes:UP000078540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Treedump-2 {ECO:0000313|EMBL:KYM92350.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYM92350.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Atta colombica WGS genome.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KQ976401; KYM92350.1; -; Genomic_DNA.
DR STRING; 520822.A0A195BVQ2; -.
DR Proteomes; UP000078540; 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; 2.
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; 2.
DR Pfam; PF06292; MUN; 1.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00109; C1; 1.
DR SMART; SM00239; C2; 2.
DR SMART; SM01145; DUF1041; 1.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR PROSITE; PS50004; C2; 2.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000078540};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 142..192
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 279..403
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 711..854
FT /note="MHD1"
FT /evidence="ECO:0000259|PROSITE:PS51258"
FT DOMAIN 964..1144
FT /note="MHD2"
FT /evidence="ECO:0000259|PROSITE:PS51259"
FT DOMAIN 1230..1359
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 1156..1209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1166..1209
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1407 AA; 159695 MW; E6D4B536EDDC3124 CRC64;
MRISKIDHRS FHSVVLARVV FLAPFRGRAF FFSKTNGSGP GGESGGRANG HPGDNPFYST
IDSMPDIRPR RKSIPLVSEL SQDYHLLYDR ETGRYQTMAA TKRNAGLTSA VPRATLNDEE
LKMHVYKKTL QAMIYPISST TPHNFVTWTA TSPTYCYECE GLLWGIARQG VRCMECGVKC
HEKCKDLLNA DCLQRAAEKS SKHGAEDKAN TIITAMKERM KQREQEKPEI FELIRSVFGV
DEKAHMGHMM AVEQSVLDGT SKWSAKIAIT VDPDTHIDSL EQAEQIVLEG TSKWSCKIAI
TVISAQGLIA KDKSGTSDPY VTVQVGKVKK RTRTMPRELN PVWHEKFYFE CHNSSDRIKV
RVWDEDNDLK SKLRQKLTRE SDDFLGQTII EVRTLSGEMD VWYNLEKRTD KSAVSGAIRL
HISVEIKGEE KVAPYHVQYT CLHENLFHSL CEENGGMVSL PQAKGDDAWK VYFDPPGEEL
VDEFAMRYGI ESIYQAMTHF HCLSTKYLCP GVPAVMSTLL ANINAYYAHT TASPAVSASD
RFAASNFGKE KFVKLLDQLH NSLRIDLSMY RNNFPASSQE KLMDLKSTVD LLTSITFFRM
KVQELSSPPR ASTVVKDCVK ACLRSTYQFL FENCFEMYNR EFQVDPIEAA RDMDDHGPRL
DSLKFWHKLI SLIVMVNDED KNSYAPVLNQ FPQELNIGQL SCATTWSLFA VDMKYALEEH
EQHRLCKSSD YMNLHFTVKW LHSTYVKDVP PYKGAVPEYP AWFEPFVMQW LNENDDVSLE
YLHGAFSRDK KDGFQKSSEH VLFSVSVVDI FTQLTQCFDV VSRLECSDPE IWKRYMKRFA
KTIVKVLLAY ADIVKKEFPS HLKEERIACI LMNNIQQLRV QLEKMFESMG GDKLEEDAAN
ILKELQQQLN GALDDLAIQF ANSLEPRITV SVKELGDLLL AIKGGGQVTL SQPAQRNNVT
VEADDVLRPL MVLLDGSLSL YAESCEKTVL KRLLKELWKI VMRILEKTVV LPPMTDKNMM
FKNLTDNAKN LAANAKIEDM SKLFKNHMAG KPDVKNALSG VMVIEIHYSN PFLFIQDISK
EVEKNLSPKQ CAVLEVALDT IKQYFHAGGN GLKKTFLEKS PELQSLRYAL SLYTQTTDTL
IKTFVTSQVN QVPLNDASTL RQRQRSMSSE RGDEGEGAEG MESLEEPLRQ SKPSLRRESR
QGTTRADFRR SLEVSESLLS RNTAGSDEGS VGEVSIQVDL FTHPGTGEQK VTVKVVAAND
LKWQLASGMF RPYVEVNLIG PHLTGKKRKQ STKSKSNNWS PQFNESFDFM IGNEQQQLDF
YELHICVKDY CFAREDRLVG VAVMQLKDIV EEGSCACWLS LGKRIQMDET GWTILRILSQ
RNNDEIAKEF VKLKSDIRQE TLLPNPT
//
