ID A0A3R7MB83_PENVA Unreviewed; 970 AA.
AC A0A3R7MB83;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=C7M84_009671 {ECO:0000313|EMBL:ROT71961.1};
OS Penaeus vannamei (Whiteleg shrimp) (Litopenaeus vannamei).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
OC Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
OC Penaeoidea; Penaeidae; Penaeus.
OX NCBI_TaxID=6689 {ECO:0000313|EMBL:ROT71961.1, ECO:0000313|Proteomes:UP000283509};
RN [1] {ECO:0000313|EMBL:ROT71961.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT71961.1};
RA Zhang X., Yuan J., Li F., Xiang J.;
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ROT71961.1, ECO:0000313|Proteomes:UP000283509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Muscle {ECO:0000313|EMBL:ROT71961.1};
RA Sun Y., Gao Y., Yu Y.;
RT "The decoding of complex shrimp genome reveals the adaptation for benthos
RT swimmer, frequently molting mechanism and breeding impact on genome.";
RL Submitted (JAN-2019) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ROT71961.1}.
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DR EMBL; QCYY01002222; ROT71961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R7MB83; -.
DR STRING; 6689.A0A3R7MB83; -.
DR EnsemblMetazoa; XM_027363252.1; XP_027219053.1; LOC113811490.
DR Proteomes; UP000283509; 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 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; 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; 1.
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:UP000283509};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 622..686
FT /note="SAM"
FT /evidence="ECO:0000259|PROSITE:PS50105"
FT DOMAIN 769..912
FT /note="TIR"
FT /evidence="ECO:0000259|PROSITE:PS50104"
FT REGION 62..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 932..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..127
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..225
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 946..961
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 970 AA; 106578 MW; 89D359F17145CEDF CRC64;
MSLASNASLQ QSSSAAALQA GSGFNKLKAS GFNMGSMDAL DALQMGSTEQ LALPDVENDF
DLQNALSAQQ DQLSSSPLTS GSASSNGNPK ELKFEQKKVT SSSKRKVVTD KNSFESASGQ
TSESCKLQAG DVSYEESSKK AATKAKLEVD GVTAEKAAAI QQEARQLRAG DVTHREGSQV
KGATMRVAGE GFSAHKSAVS EQQQRQTKTP AGTINQESSR QAASSGITIK TKGVCTKQTS
SMTASQSNVS ITGFEDLDLL NDASQPVDIQ NAIMRYSGVM SNFVEQLKTM TFSEGFKDAP
SLLDNIDEMI RKAWSVPTHG HELGFSLCNV LRNNGGIDVL LKNCTSDDSD LKFSSAKVLE
QCLTTENRGY VVENGLEDVV NVACDCTKNG TSVDKSRVGT GILEHLFKHS EGTCSEIINL
GGLDAVLSEC RKSDVETLRH CAGALANLSL YGGSDNQQQM IRRNVPMWLF PLAFHTDDNI
KYYACLAIAT LVANKELEAA VLQSGTLDLV EPFVMNQMPD QFANSTVAHR HGQSSNWLKR
LVPVLSSKRE EARNLAAFHF CMEAGIKKRQ GNLELFREIG AIEPLKEVAS SPNAIASKYA
VKALKLIGEE VPHILSQQVP LWTPEDVQNW VKRIGFSEFA DDFVASRVDG DLLLQMTEQN
LCEDIGMKNG ILRQRFLREL KKLKLMADFS SCDSTKLNEF MLQVDPDFAV YTYSMLNAGV
TRDCLRYLTE EQLISECRIY NSIHRQKVRE KIREYYAVGQ ISNGDPVDKN LDVFISYRRS
NGSQLASLLK VHMQLKEFSV FIDVERLEAG KFDNNLLNSI RQAKNFLLVL TPNALDRCIG
DTECKDWVHR EIVAALQSGC NIIPILDNFQ WPDPEELPED MRAVCYFNGV RWIHDYQDAC
VDKIERFIRG ECNMPGDGPL ARYVSGSALG GMATPGTPST LPRAPPPYQR TTSTESGKGS
SCSDKDFAKD
//
