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Entry: A0A3Q3GZ25_9LABR
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ID   A0A3Q3GZ25_9LABR        Unreviewed;       713 AA.
AC   A0A3Q3GZ25;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 27.
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   Labrus bergylta (ballan wrasse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Labriformes; Labridae; Labrus.
OX   NCBI_TaxID=56723 {ECO:0000313|Ensembl:ENSLBEP00000036073.1, ECO:0000313|Proteomes:UP000261660};
RN   [1] {ECO:0000313|Ensembl:ENSLBEP00000036073.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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; A0A3Q3GZ25; -.
DR   STRING; 56723.ENSLBEP00000036073; -.
DR   Ensembl; ENSLBET00000037591.1; ENSLBEP00000036073.1; ENSLBEG00000027019.1.
DR   GeneTree; ENSGT00390000004155; -.
DR   InParanoid; A0A3Q3GZ25; -.
DR   Proteomes; UP000261660; Unplaced.
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; 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; 2.
DR   SUPFAM; SSF52200; Toll/Interleukin receptor TIR domain; 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   Reference proteome {ECO:0000313|Proteomes:UP000261660};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..713
FT                   /note="NAD(+) hydrolase SARM1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018714252"
FT   DOMAIN          410..463
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          553..696
FT                   /note="TIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50104"
SQ   SEQUENCE   713 AA;  79959 MW;  57D883F12FB879E0 CRC64;
     MLFSLALFLW RLYRHFSIMF STDRLTVPEY VSRLQRGRSG SGSDPKAVSP GINADVQAVL
     GSSLPALRCA IRRLKSANET SDSEETRGAI AEIFQLVEEA WVLPTVGRQV AEEICNRIRL
     DGGLELLLQL QQIPAVEITY ESAKLLEQIL ISENRDYIAR LGLGVILNLT RQQEDAQLAR
     SVSGILEHMF KHTEETSVHL ISNGALDALL FWCRGTDPTV LRHCAVALAN CAMYGGHRCQ
     RWMIEKQAAE WLFPLAFSKE DELIRFHACL AVTVLAANKE IEKEVVKSGT LELVEPFIAS
     LDPDDFARNL LDSTDSMQGR TASDLQHLLP LLDGTRLEGK CIAAFYLCVE SSIKSRQRNT
     KIFQEIGAVQ SLKRIVMYSS NGTACSLAKR ALSLMGEEVP KRILSSVPNW KSCEVQRWLQ
     QVGFSAYCDR FQELQVDGDL LLNVTDQDLS ADLGMTAGLT RKRQVRLASA EDYANYSTCD
     PNNMADWLAD VDPRFRQYTY GLVQSGVDLN NVQHLTDQQL QHDCHVVNGV HRAKMLSFSR
     KPSKPCHTDA QPTGPDVFIS YRRTTGSQLA SLLKVHLQVR GYSVFIDVEK LAAGKFEDKL
     IQSVQRAKNF ILVLSANALD KCMGDTAMKD WVHKEIVTAL AGKKNIVPVT DNFMWPDPMS
     LPEDMRAILN FNGIKWSHEY QEASIEKILR FLKGQQDQMD AKDASKGQKK ETK
//
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