ID   A0A183IHK0_9BILA        Unreviewed;       793 AA.
AC   A0A183IHK0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase {ECO:0000256|ARBA:ARBA00011982};
DE            EC=3.2.2.6 {ECO:0000256|ARBA:ARBA00011982};
GN   ORFNames=SBAD_LOCUS3095 {ECO:0000313|EMBL:VDO99984.1};
OS   Soboliphyme baturini.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Dioctophymatida; Dioctophymatoidea; Soboliphymatidae; Soboliphyme.
OX   NCBI_TaxID=241478 {ECO:0000313|Proteomes:UP000050793, ECO:0000313|WBParaSite:SBAD_0000324101-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:SBAD_0000324101-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO99984.1, ECO:0000313|Proteomes:UP000270296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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; UZAM01007566; VDO99984.1; -; Genomic_DNA.
DR   WBParaSite; SBAD_0000324101-mRNA-1; SBAD_0000324101-mRNA-1; SBAD_0000324101.
DR   Proteomes; UP000050793; Unplaced.
DR   Proteomes; UP000270296; 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   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; PF00536; SAM_1; 1.
DR   Pfam; PF07647; SAM_2; 1.
DR   SMART; SM00454; SAM; 2.
DR   SMART; SM00255; TIR; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 2.
DR   SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 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:UP000270296};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          464..528
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   REGION          54..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   793 AA;  89330 MW;  93D2763D8E0B1806 CRC64;
     MNDVLELASL RALSLVVDDE KIAAEGKVER RAPIFKPVRN VNFESPESLR LHDEGSSTVV
     SRSGDSGFGE SSVRSSSRRH VNPFRMFESN QNGCSFFNRK GSIEYGAAKH LHTELLISRH
     SLKSKMNKYQ RLLDKAFALI NLRNDESICE GCTVFAKVMM NGWATPKIGS DLAHGLCDYV
     REIGYLATLI HLFECLSAAN REFVVSRNYV EDLVYVAKTM KDGEKLKVSV SLLESLFKHN
     VETNARLIEM GALDHVLNAC KATTCTKTYR FAALALANLA MYSDSDCQQK IIAKNVPDWL
     FLLASAQDDV TRYYACLAIC ALVCNKEIEA AVIKSGTLTL VEPFLLVHKP EDFAHFDYKH
     QQGRSKEWLE RMLPMLTSKK REPRIMAAFH FTLEAGVKNE XXXXXXXXXX XXXXXSMLFE
     IGAVDALKQV ASLPDEVSSK FAVQALQIIG EEVPYKLSQQ VPFWSVEDVQ YWVSQIGFDK
     YSTQFLEQKV DGDLLLLLTD VELEKDIGMT SGLLRKRFMR ELESLKMAAD YSCVDETHLD
     RFLVSVSPQF SVYTYQLLEL GIDRSVLPSL SDDILKTDCS ILNPVHRMKL LQAIEECKHM
     DDLDIAILSK HIDIFISYRR TTGSQLASLI KVLLQLKGHK NIQAAKHFLL VLTPNSLERC
     IGDTACQDWV HREVKCALEH NKNVIPVFDP NFEWCDESEL PADIRAITKL NGVRWVHEYQ
     EACVDKLEKF IKGEINVNRG FFPLPPRGSV CRGLFMDSCS NNSLNLCGGN STDFGKSAAT
     ELIDCLDVPA GYF
//