ID A0A3B3DP62_ORYME Unreviewed; 714 AA.
AC A0A3B3DP62;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=NAD(+) hydrolase SARM1 {ECO:0000256|ARBA:ARBA00024128};
DE EC=3.2.2.6 {ECO:0000256|ARBA:ARBA00011982};
DE AltName: Full=NADP(+) hydrolase SARM1 {ECO:0000256|ARBA:ARBA00032222};
DE AltName: Full=Sterile alpha and TIR motif-containing protein 1 {ECO:0000256|ARBA:ARBA00031160};
OS Oryzias melastigma (Marine medaka).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Atherinomorphae; Beloniformes; Adrianichthyidae; Oryziinae;
OC Oryzias.
OX NCBI_TaxID=30732 {ECO:0000313|Ensembl:ENSOMEP00000031907.1, ECO:0000313|Proteomes:UP000261560};
RN [1] {ECO:0000313|Ensembl:ENSOMEP00000031907.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + NADP(+) = ADP-D-ribose 2'-phosphate + H(+) +
CC nicotinamide; Xref=Rhea:RHEA:19849, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58673; Evidence={ECO:0000256|ARBA:ARBA00023911};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19850;
CC Evidence={ECO:0000256|ARBA:ARBA00023911};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NAD(+) = cyclic ADP-beta-D-ribose + H(+) + nicotinamide;
CC Xref=Rhea:RHEA:38611, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154,
CC ChEBI:CHEBI:57540, ChEBI:CHEBI:73672;
CC Evidence={ECO:0000256|ARBA:ARBA00034259};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38612;
CC Evidence={ECO:0000256|ARBA:ARBA00034259};
CC -!- SIMILARITY: Belongs to the SARM1 family.
CC {ECO:0000256|ARBA:ARBA00008291}.
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DR AlphaFoldDB; A0A3B3DP62; -.
DR STRING; 30732.ENSOMEP00000031907; -.
DR PaxDb; 30732-ENSOMEP00000031907; -.
DR Ensembl; ENSOMET00000023615.1; ENSOMEP00000031907.1; ENSOMEG00000017036.1.
DR GeneTree; ENSGT00390000004155; -.
DR OMA; KSCEVQT; -.
DR OrthoDB; 5475697at2759; -.
DR Proteomes; UP000261560; Unplaced.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
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:Ensembl.
DR GO; GO:0034128; P:negative regulation of MyD88-independent toll-like receptor signaling pathway; IEA:InterPro.
DR GO; GO:0048679; P:regulation of axon regeneration; IEA:Ensembl.
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; IPR001763; Rhodanese-like_dom.
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 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; 2.
DR SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
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 Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..714
FT /note="NAD(+) hydrolase SARM1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5017440802"
FT DOMAIN 356..438
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 412..476
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 556..699
FT /note="TIR"
FT /evidence="ECO:0000259|PROSITE:PS50104"
SQ SEQUENCE 714 AA; 80658 MW; E1C533727905D4B5 CRC64;
MLFTPTFLLW RLFRHLCIMF SSDRLTVPEY VSRLQRGRSS SGGSDSKTAV SPGLSTDIQA
VLNTSLPALR SAIRRLKSAQ ENSDSNETRR AVAEIYQLVE EAWVLPALGR QVAEEICNRI
RLDGGLELLL QLQQTPEVEI IYESAKLLEQ ILISENRDYV ARLGLGVILN LARQQEDAQL
ARSVSGILEH MFKHTEETSV HLISNGALDA LLFWCRGTDP TVLRHCAVAL ANCAMYGGHR
CQRWMIEKQA AEWLFPLAFS KEDELIRFHA CLAVTVLAAN REIEKEVVKS GTLELVEPFI
ASLDPDDFAR SLLDSADCMQ GKTASDLQHL LPLLDGTRVE GKCIAAFYLC VEASIKSRQR
NTKIFQEIGA VQSLKRIVMY CSNGTACLLA KRALSMMGEE VPKRILSCVS NWKTCEVRVW
LQQVGFSAYC DRFQELQVDG DLLLNITDQD LSSDLGMAAG LTRKRFLREL RVLKTYADYS
TCDPNNMADW LAEVDPHFRQ YTYGMVQSGV DRNNVLNLND HQLQYDCHIE NGVHRAKILS
ANRKPAKPCY TDAQPAGPDV FISYRRTTGS QLASLLKVHL QVRGYSVFID VEKLEAGKFE
DKLIQSVQRA RNFILVLSAS ALDKCMGDTG MKDWVHKEIV TALTCKKNIV PVTDNFMWPE
PASLPEDMRA ILNFNGIKWS HEYQEATIEK IIRFLKEPQD QTDRPKKSKE QEKK
//