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Database: UniProt
Entry: A0A077ZE30_TRITR
LinkDB: A0A077ZE30_TRITR
Original site: A0A077ZE30_TRITR 
ID   A0A077ZE30_TRITR        Unreviewed;       739 AA.
AC   A0A077ZE30;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=TTRE_0000694001 {ECO:0000313|EMBL:CDW58616.1};
OS   Trichuris trichiura (Whipworm) (Trichocephalus trichiurus).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichuridae; Trichuris.
OX   NCBI_TaxID=36087 {ECO:0000313|EMBL:CDW58616.1};
RN   [1] {ECO:0000313|EMBL:CDW58616.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Aslett M.;
RL   Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CDW58616.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Foth B.J., Tsai I.J., Reid A.J., Bancroft A.J., Nichol S., Tracey A.,
RA   Holroyd N., Cotton J.A., Stanley E.J., Zarowiecki M., Liu J.Z.,
RA   Huckvale T., Cooper P.J., Grencis R.K., Berriman M.;
RT   "The whipworm genome and dual-species transcriptomics of an intimate host-
RT   pathogen interaction.";
RL   Submitted (MAR-2014) 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; HG806380; CDW58616.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A077ZE30; -.
DR   STRING; 36087.A0A077ZE30; -.
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; 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   Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT   DOMAIN          396..460
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   DOMAIN          542..686
FT                   /note="TIR"
FT                   /evidence="ECO:0000259|PROSITE:PS50104"
SQ   SEQUENCE   739 AA;  83358 MW;  FF69F32C8BF83330 CRC64;
     MPKGHREIVP YGILEDNGSP IFGRKHSFEY GAAKHLHTEL LVSKHTLKGK MNKFQRLIDR
     AVSLLSIGNV NSICEGCALL ARVLKSSWTT PKIGSDLAHG LCDYIRDSGF LDTLLQLFLH
     PRSTDQVKVA SGLVLVECLS SSNREYLVQN NHLEEVVNVC KAMKEGDKLR TSVSLFESLF
     KYSVESNARL IELGALDHIL AACKATTCRK TFRYASLALA NLSMYSDSEC QQKMIAKNVP
     DWLFLLASSQ DDVTRYYACL AICALVSNKE VESAVTKSGT LALVEPFLLS HKPEDFSQFD
     YRHQQGRSKE WLELLMPMLS AKRREPRSMA AFHFAIEASV KKEQEALSLL LEIGAVDALK
     QVASMPDEVA PKFASQALHI IGEEVPYKLS QQVPFWSVED VQYWVSQIGF EKYSPLFSEQ
     KVDGDLLLLL TDAELERDIG MRSGLLRKRF MRELESLKMA ADYTSVDETH LDRFLVSVSP
     QFSVYTYQLL ELGVDRSTLS SMSNEILKSE CGISNPVHRL KLLQSIEDCK HVEDLDIAIL
     SKHIDIFISY RRSTGNQLAS LIKVLLQLRG HKVFIDVDRL YAGNFDSSLL KNIQAAKHFV
     LVLTPRSLDR CLGDEECQDW VHREVKCALE HNKNLIPVFD PMFEWPDENQ IPADIRAITR
     VNGVRWVHEY QEACVDKLEK FINGELNVNR GFFPLPQFGS LSRSMFVNSS PTTMNVSGSS
     STDMVIESLA KSRPRGNSQ
//
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