ID A0A0M8ZPL3_9HYME Unreviewed; 966 AA.
AC A0A0M8ZPL3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase {ECO:0000256|ARBA:ARBA00011982};
DE EC=3.2.2.6 {ECO:0000256|ARBA:ARBA00011982};
DE Flags: Fragment;
GN ORFNames=WN51_03981 {ECO:0000313|EMBL:KOX68495.1};
OS Melipona quadrifasciata.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Melipona.
OX NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX68495.1, ECO:0000313|Proteomes:UP000053105};
RN [1] {ECO:0000313|EMBL:KOX68495.1, ECO:0000313|Proteomes:UP000053105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0111107301 {ECO:0000313|EMBL:KOX68495.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KOX68495.1};
RA Pan H., Kapheim K.;
RT "The genome of Melipona quadrifasciata.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:16301, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17154, ChEBI:CHEBI:57540, ChEBI:CHEBI:57967; EC=3.2.2.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000404};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16302;
CC Evidence={ECO:0000256|ARBA:ARBA00000404};
CC -!- SIMILARITY: Belongs to the SARM1 family.
CC {ECO:0000256|ARBA:ARBA00008291}.
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DR EMBL; KQ435922; KOX68495.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8ZPL3; -.
DR STRING; 166423.A0A0M8ZPL3; -.
DR OrthoDB; 5475697at2759; -.
DR Proteomes; UP000053105; Unassembled WGS sequence.
DR GO; GO:0050135; F:NAD(P)+ nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0061809; F:NAD+ nucleotidase, cyclic ADP-ribose generating; IEA:UniProtKB-EC.
DR GO; GO:0035591; F:signaling adaptor activity; IEA:InterPro.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0019677; P:NAD catabolic process; IEA:UniProt.
DR GO; GO:0034128; P:negative regulation of MyD88-independent toll-like receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048678; P:response to axon injury; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd09501; SAM_SARM1-like_repeat1; 1.
DR CDD; cd09502; SAM_SARM1-like_repeat2; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR Gene3D; 3.40.50.10140; Toll/interleukin-1 receptor homology (TIR) domain; 1.
DR Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR039184; SARM1.
DR InterPro; IPR000157; TIR_dom.
DR InterPro; IPR035897; Toll_tir_struct_dom_sf.
DR PANTHER; PTHR22998:SF1; NAD(+) HYDROLASE SARM1; 1.
DR PANTHER; PTHR22998; SARM1; 1.
DR Pfam; PF07647; SAM_2; 2.
DR Pfam; PF13676; TIR_2; 1.
DR SMART; SM00454; SAM; 2.
DR SMART; SM00255; TIR; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 2.
DR PROSITE; PS50104; TIR; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Immunity {ECO:0000256|ARBA:ARBA00022588};
KW Innate immunity {ECO:0000256|ARBA:ARBA00022588};
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 437..501
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 507..573
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 585..728
FT /note="TIR"
FT /evidence="ECO:0000259|PROSITE:PS50104"
FT REGION 734..863
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 741..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 809..863
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 933..966
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KOX68495.1"
FT NON_TER 966
FT /evidence="ECO:0000313|EMBL:KOX68495.1"
SQ SEQUENCE 966 AA; 108286 MW; 4095935485855834 CRC64;
QKAMAAQQQR QTVTSTGIFN HEKHISTASS QSSITIAKGI SKSSMISAAS AVNQLMNGMR
PAEDELLSLP LDDLDLLCAK SNPQDVDRAI AKYSNFLDSF VERLKANDYK NGKAPLLLNR
VNEIIRKAWA VPTHGHELGY SLCNTLRTRG GLDLLMSNCV ASDKELQFSS ARLLEQCLTT
ENRAHVVEHG LEKVVNVACV CTKNANSVDH SRVGTGILEH LFKHSEGTCS DVIRLGGLDA
VLFECRKNDI ETLRHCAGAL ANLSLYGGAE NQEAMIKRKV PMWLFPLAFH NDDNIKYYAC
LAIAVLVANK EIEAAVLKSG TLDLVEPFVT SHNPYEFAKS NLAHAHGQSK NWLERLVPVL
SSKREEARNL AAFHFCMEAG IKKQQGNTEI FRAIGAIEPL KKVASCPNAI ASKYAAQALR
LIGEEIPHKL SQQVPLWSTE DVREWVKQIG FAECAQNFVE SRVDGDLLLQ LTEENLKEDI
GLTNGIRRRR FTRELQNLKK MADYSSRDTG NLNSFLQSIG QEFSIYTYSM LNAGVDKDSI
RNLSEDQLLT ECGITNSIHR LRILDAIKNM QHNQLGSSEN ESPDKSLDVF VSYRRSNGSQ
LASLLKVHLQ LRGFSVFIDV ERLEAGKFDN NLLQSIRQAK HFLLVLTPKA LERCIQDSEC
KDWVHREIVA ALQSQCNIIP IIDNFQWPEP EELPEDMRAV CHFNGVRWIH DYQDACVDKL
ERFMRGEIPV RSDIPRSIAP KDVTQPNTPS NTNIRQPPSY QRMHSNESRG SLPPTSPRLK
FTHAQSGGSP MPRRPPRHPP SPSSRSRSLE LLDQDEEKSI SPVKEPEVQA RPRSRSLDGL
LDEDDTVPEM KTEELMKPDN ESKIDSRMFL EALDKLSDTK VKDSLSQVVP EKAERNVEEG
TIVKLHSDKS DNQKAKSNEN QSPIPVPRQR LKTAAETKSE PVDIVEREDV QKEPCASSHE
VNSDKE
//
