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Database: UniProt
Entry: A0A3Q1CHD1_AMPOC
LinkDB: A0A3Q1CHD1_AMPOC
Original site: A0A3Q1CHD1_AMPOC 
ID   A0A3Q1CHD1_AMPOC        Unreviewed;       929 AA.
AC   A0A3Q1CHD1;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=NLR family CARD domain-containing protein 3-like {ECO:0000313|Ensembl:ENSAOCP00000027142.1};
OS   Amphiprion ocellaris (Clown anemonefish).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Pomacentridae; Amphiprion.
OX   NCBI_TaxID=80972 {ECO:0000313|Ensembl:ENSAOCP00000027142.1, ECO:0000313|Proteomes:UP000257160};
RN   [1] {ECO:0000313|Ensembl:ENSAOCP00000027142.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3Q1CHD1; -.
DR   Ensembl; ENSAOCT00000018960.1; ENSAOCP00000027142.1; ENSAOCG00000015853.1.
DR   GeneTree; ENSGT01070000253760; -.
DR   Proteomes; UP000257160; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
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; 3.
DR   Pfam; PF05729; NACHT; 1.
DR   Pfam; PF17776; NLRC4_HD2; 1.
DR   Pfam; PF17779; NOD2_WH; 1.
DR   Pfam; PF15227; zf-C3HC4_4; 1.
DR   SMART; SM01288; FISNA; 1.
DR   SMART; SM00368; LRR_RI; 5.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   SUPFAM; SSF52047; RNI-like; 1.
DR   PROSITE; PS51450; LRR; 2.
DR   PROSITE; PS50837; NACHT; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000257160};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          91..133
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          244..378
FT                   /note="NACHT"
FT                   /evidence="ECO:0000259|PROSITE:PS50837"
FT   REGION          1..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..40
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..81
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   929 AA;  105422 MW;  F281D8CF61A4E81B CRC64;
     MSVREEEEEF PASSCLSMKS DWSKGRPPEF SKEPEPSETK QRTESAASSC LSMKSDWSKG
     RPPEFSKEPE PSDTKVMKRR GVSVEEQPPC CASCQDVLKD PVSSSCGHWF CRQCITSNWD
     QSAPSGHSSC PQCGERSRTR GGLQTASQSS CGQSVGLQEV LQEHKMSLRR RCEHVTEGSD
     EAGGGTLLNR IYTELYITEG HSGEADVQHE VRQLETDSKN SLHDTPIRCQ DVFKALPEQQ
     RAIRVVLTNG VAGIGKTFSV LKFTLDWAEG GENQDVSVVV VLPFRELNLI RDEQHSLLTL
     LHLFHPTLQK VTAEQLAVCK LLFIFDGLDE SRLSLDFTNR EVVSDVSQKL SLDVLLVNLM
     EGNLLPSALI WITSRPAAAN QIPPTHVDRL TEVRGFTDGQ KEEYFRRRFS DEEPSSTIIS
     HMKTSRNLHI MCRLPVFCWI TATVLEHMLT TEQRGELPQS MTEMFSRFLL VQTQRKKNKY
     HEGPETSPQE LTKTDREVLL KLGRLAFEHL EKGNIMFYQE DLEQCGLDVT EASVFSGVCT
     QIFRRECEMF QKPVYCFVHL SIQEYLAAVY MFHCYTNGNT EVLEQFLGED WKDKKRHSLN
     MLLDRVMEKS LRSRNGHLDL FVRFLHGLCL ESNQRLLGGL LGQTENHPKM IQRIINNLKK
     LRSCEISPDR SINIFHCLME MKDLSVHQEI QEFLQSENRS EKFLSEIHCS ALAYMLQMSE
     EVLDELDLKK YNTSEEGKRR LIPAVRNCRK ARLSICELSE GHCEVVASAL KSNPSHLTEL
     EMSGNKNLEN SGVKHLSDGL QSPNCKLETL RLEHCGLSEI SCDSLVSALK SNPSHLKHLD
     LSRNKLQDSG VKHLSGFLEN PDCILKTLRL KDCRLSEISC DSLVSALKSN PSHLEHLDLS
     WNNLKDSGVK HLLDLVESPD CSLKTLRWK
//
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