ID A0A1S3REI2_SALSA Unreviewed; 1421 AA.
AC A0A1S3REI2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=NACHT, LRR and PYD domains-containing protein 3-like isoform X1 {ECO:0000313|RefSeq:XP_014050731.1, ECO:0000313|RefSeq:XP_014050732.1};
GN Name=LOC106602558 {ECO:0000313|RefSeq:XP_014050731.1,
GN ECO:0000313|RefSeq:XP_014050732.1, ECO:0000313|RefSeq:XP_014050733.1};
OS Salmo salar (Atlantic salmon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC Salmonidae; Salmoninae; Salmo.
OX NCBI_TaxID=8030 {ECO:0000313|Proteomes:UP000087266, ECO:0000313|RefSeq:XP_014050733.1};
RN [1] {ECO:0000313|RefSeq:XP_014050731.1, ECO:0000313|RefSeq:XP_014050732.1}
RP IDENTIFICATION.
RC TISSUE=Muscle {ECO:0000313|RefSeq:XP_014050731.1,
RC ECO:0000313|RefSeq:XP_014050732.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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_014050731.1; XM_014195256.1.
DR RefSeq; XP_014050732.1; XM_014195257.1.
DR RefSeq; XP_014050733.1; XM_014195258.1.
DR PaxDb; 8030-ENSSSAP00000034713; -.
DR KEGG; sasa:106602558; -.
DR OrthoDB; 3951219at2759; -.
DR Proteomes; UP000087266; Chromosome ssa04.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR CDD; cd19802; Bbox1_TRIM8-like; 1.
DR CDD; cd19769; Bbox2_TRIM16-like; 1.
DR CDD; cd00116; LRR_RI; 1.
DR CDD; cd16040; SPRY_PRY_SNTX; 1.
DR Gene3D; 2.60.120.920; -; 1.
DR Gene3D; 4.10.830.40; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 1.10.533.10; Death Domain, Fas; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 3.
DR InterPro; IPR001870; B30.2/SPRY.
DR InterPro; IPR043136; B30.2/SPRY_sf.
DR InterPro; IPR003879; Butyrophylin_SPRY.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR011029; DEATH-like_dom_sf.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR029495; NACHT-assoc.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR041267; NLRP_HD2.
DR InterPro; IPR041075; NOD2_WH.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR006574; PRY.
DR InterPro; IPR003877; SPRY_dom.
DR InterPro; IPR000315; Znf_B-box.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR24106; NACHT, LRR AND CARD DOMAINS-CONTAINING; 1.
DR PANTHER; PTHR24106:SF151; NACHT, LRR AND PYD DOMAINS-CONTAINING PROTEIN 12-RELATED; 1.
DR Pfam; PF14484; FISNA; 1.
DR Pfam; PF13516; LRR_6; 5.
DR Pfam; PF05729; NACHT; 1.
DR Pfam; PF17776; NLRC4_HD2; 1.
DR Pfam; PF17779; NOD2_WH; 1.
DR Pfam; PF13765; PRY; 1.
DR Pfam; PF00622; SPRY; 1.
DR Pfam; PF00643; zf-B_box; 1.
DR Pfam; PF00097; zf-C3HC4; 1.
DR PRINTS; PR01407; BUTYPHLNCDUF.
DR SMART; SM00336; BBOX; 1.
DR SMART; SM01288; FISNA; 1.
DR SMART; SM00368; LRR_RI; 9.
DR SMART; SM00589; PRY; 1.
DR SMART; SM00449; SPRY; 1.
DR SUPFAM; SSF57845; B-box zinc-binding domain; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF52047; RNI-like; 1.
DR PROSITE; PS50188; B302_SPRY; 1.
DR PROSITE; PS50837; NACHT; 1.
DR PROSITE; PS50119; ZF_BBOX; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000087266};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00024}.
FT DOMAIN 233..273
FT /note="B box-type"
FT /evidence="ECO:0000259|PROSITE:PS50119"
FT DOMAIN 437..570
FT /note="NACHT"
FT /evidence="ECO:0000259|PROSITE:PS50837"
FT DOMAIN 1223..1421
FT /note="B30.2/SPRY"
FT /evidence="ECO:0000259|PROSITE:PS50188"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1421 AA; 158678 MW; BF528D0CD41E23D4 CRC64;
MSRPGEKKEG TTASKMSHPG KKKEGTTASK MSHPGKKKEG TTASKMSLPQ DIRSESVQQH
RAESPTPSLL SMKSDNSMFL PPTFNQETQT VDKGVRKRAE SPTSSLLSMK SDNSMFLPPT
FNQHPLNDKS GITIDLCERG PKDQVSIPCG HSYCKQCISV LVSPKPLQHQ HAESSHYYAG
PGDVACDLCT EKKLKAVKSC LICTASYCES HVRQHYTVAA LQKHTLVEVT GNLEQKLCQL
HHKALEVFCK TDQILICNMC AVEDHRGHRK RYIEIPMLLD TSSLLGQSLK NMSDLNLFKN
HLIHCYPECF ETQLDNEDVQ DLVEKMLESF GTEGALKITL NFLDIRNKTL WKAREIKTKL
GQKFQQIFEG IGHNGKQTLL NDIYTELYIT EGGSGEVNNE HEVRHIETVS KEQTTQKTAI
KCNNIFKRLP GQRKPIRTVL TKGIAGIGKT VSVQKFILDW AEGKANQDIH FIFPLPFRDL
NLKKGQYSLM QLLQYYCPDL KDIDSIQCGE IKTLFIFDGL DECRHPLNFQ NNEDLYDITE
PTSVDVLLTN LIKGNLLPSS HLWITTRPAA ANQIPFECVD QVTEVKGFSD PQKEEYFRKI
IGDEDLASRI ITQMKTSKSL YIMCHMPVFC WISATVLETM LKETKNVKVP KSLTQMNTHF
LLIQTSVKNK KYNKATEKNP KKLSQLDKVM ILKLGKLAFQ QLQKGNLIFY EEDLTECGID
VTEASEYSAL CTEMFKDECG LYQDKVFSFV HLSIQEFLAA LYALESWLGK SENVFDESFK
CDKLSDLHMS AVDKALQSKN GHLDLFLRFL LGLSLESSQN LLKGLLTRRG GQTPSIEETF
KYLSDKIKME SSPERIINLF HCLNELGDNS VVEEIQTSLR SGTLSETKLQ PHQCSALAFV
LMMSEGVLDE FHLKTYNTSV EGRLRLLPVV KTCKKASLAG CDLTYTSCRT LASALQTPNC
PLTELDLSYN DLGDRGVKLL CAGLHNIQTL ILGPCGLTEG CCLHLASVLR APNSQLKQLE
LRYNNLQDSG VTLLCAGLKD PNCKLQTLGL SQCGLTEGCC SDLASVLCST NSQLKQLELR
DNDLQDSGVT LLSDGLADPN CKLQKLGLGQ CGLTEGCCSD LASVLRAPNS QLKQLELRDN
DLQDSGVTLL SDGLADPNCE LQTLGLSGCE VTEEGCAALA SALRSNPSHL RELDLSYNHP
GDSAGGLLSA GQGDPTCKLM KLSVDHGAEC RLVSGLRKYA CQLTMDPNTA NTHLLLSEEN
RKVTRVDKEQ HYEDHPDRFK WHPQVLCGEG LSGSRYYWEV MWDSGEPDIG VTYKGMSRMG
WGSDSWIGQN TKSWSLNCAG KGYYYFYNAG ENITFIRGPV LHRVGVYLDW PAGTLSFYSV
SFGKQKHLHT FYTTFTEPLY PGFWIYPDSS LSTCNRCEMA S
//
