GenomeNet

Database: UniProt
Entry: A0A452CI44_BALAS
LinkDB: A0A452CI44_BALAS
Original site: A0A452CI44_BALAS 
ID   A0A452CI44_BALAS        Unreviewed;       574 AA.
AC   A0A452CI44;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
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};
GN   Name=SARM1 {ECO:0000313|RefSeq:XP_028022678.1};
OS   Balaenoptera acutorostrata scammoni (North Pacific minke whale)
OS   (Balaenoptera davidsoni).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Mysticeti;
OC   Balaenopteridae; Balaenoptera.
OX   NCBI_TaxID=310752 {ECO:0000313|Proteomes:UP000261681, ECO:0000313|RefSeq:XP_028022678.1};
RN   [1] {ECO:0000313|RefSeq:XP_028022678.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_028022678.1};
RG   RefSeq;
RL   Submitted (JAN-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   RefSeq; XP_028022678.1; XM_028166877.1.
DR   AlphaFoldDB; A0A452CI44; -.
DR   Proteomes; UP000261681; 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: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; 2.
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:UP000261681};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          304..368
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          378..440
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          452..574
FT                   /note="TIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50104"
SQ   SEQUENCE   574 AA;  63733 MW;  74EBC6C7102AB51F CRC64;
     MGREVAQGLC DAIRLDGGLD LLLRLLQAPE LETRVQAARL LEQILVAENR DRVARIGLGV
     ILNLAKEREP VELARSVAGI LEHMFKHSEE TCQRLVAAGG LDAVLYWCRR TDPPLLRHCA
     LALANCALHG GQAAQRRMVE KRAAEWLFPL AFSEDELLRL HACLAVAVLA TNKEVEREVE
     RSGTLALVEP LVASLDPGRF ARCLVDASDT SQGRGPDDLQ RLVPLLDSSR LEAQCIGAFY
     LCAEAAIKSL QGKTKVFSDI GAIQSLKRLV SYSTNGTTSA LAKRALRLLG EEVPRPILPS
     VASWKEAEVQ TWLQQIGFSQ YCESFREQQV DGDLLLRLTD EELQTDLGMK SGITRKRFFR
     ELTELKTFAS YATCDRSNLA DWLGSLDPRF RQYTYGLVSC GLDRSLLHRV SEQQLLEDCG
     IRLGVHRARI LTAAREMLHS PLPCTGCKPS GDTPDVFISY RRNSGSQLAS LLKVHLQLHG
     FSVFIDVEKL EAGKFEDKLI QSIMGARNFV LVLSAGALDK CMQDHDCKDW VHKEIVTALN
     CGKNIVPVID GFQWPEPQAL PEDMRAVLTF NGIK
//
DBGET integrated database retrieval system