ID A0A0D1Y3D1_9EURO Unreviewed; 1427 AA.
AC A0A0D1Y3D1;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=NACHT domain-containing protein {ECO:0000259|PROSITE:PS50837};
GN ORFNames=PV11_09152 {ECO:0000313|EMBL:KIV77352.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV77352.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV77352.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV77352.1,
RC ECO:0000313|Proteomes:UP000053599};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala sideris CBS121828.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the putative lipase ROG1 family.
CC {ECO:0000256|ARBA:ARBA00007920}.
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DR EMBL; KN846954; KIV77352.1; -; Genomic_DNA.
DR HOGENOM; CLU_000288_34_1_1; -.
DR OrthoDB; 2615795at2759; -.
DR Proteomes; UP000053599; Unassembled WGS sequence.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 3.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR007751; DUF676_lipase-like.
DR InterPro; IPR007111; NACHT_NTPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48182; PROTEIN SERAC1; 1.
DR PANTHER; PTHR48182:SF2; PROTEIN SERAC1; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF05057; DUF676; 1.
DR Pfam; PF05729; NACHT; 1.
DR SMART; SM00248; ANK; 8.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS50837; NACHT; 1.
PE 3: Inferred from homology;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000053599};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 336..512
FT /note="NACHT"
FT /evidence="ECO:0000259|PROSITE:PS50837"
FT REPEAT 1087..1119
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1120..1145
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1188..1221
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 1222..1255
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REGION 1366..1427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1388..1409
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1427 AA; 160146 MW; 34E66AF0DCFCAC96 CRC64;
MFSTSSRQPT TAGEKERHGL FVLHPSKKNA PWDVDIVVIH GLGGDAYTTW TADNKQMWPR
DFIPHIMPTA RVMTFGYDSK PAFSRSIADI EDCARILLNS LRNKRWSAEE MNNPIIFICH
SLGGIVCKKA LLLAQSEPKY TNIFEKTSAI IFFGCPHRGS RVANWGTVFA NVINASTFHR
SARDDLLAAL SLGSKILADI STAFKEIASD IDIKTFYETA IMLPLKGPVV EKDSAILGLP
TEQIIPIAAN HREMVRFADI NSQKFDPVKY ALIETMEGKP LDLKSIRDSM LYLADELNVA
DYDQQLVRIP TRWPGTCEWI SNHPSFSSWY EEPGSGLLWL RGYAGVGKSV LTKYIIAELL
QASYIGSKNP PSTEEDQAKS RGDFLAYFFC SERNRHLQSE RNILRSLLHQ MLLAAPLEVT
KALQQFRRRS VDFAFLAGTS ALWDAIEAAF LATSWQNIYL VFDGLDEMAP ESLDSFARGL
KKLVESVAPQ MEPRQAKLLL ASRPTASLEE RLKCPSISIR SERDVRCFVQ GSADELADRF
TLTPQLKDNI VKRICDKAKG MFLWAVLAWH ELCRNANKPE DFATNLSRAQ RLPDSLDLLY
ASILDRVPPS SRDLCLGVIE LLALSARPLH SLELRFAIAL DQENGNYQQI LNKMISENRL
KSLFPALISV GEDGYVQFAH SSIKDFFLSS KPAPPYRLDA VKIHSRISIL SLDMLHMPGF
DATGVLYSLV SRPVNEPRDM VDLPRQYYFL SYATTNWHYH AALAGKDIRV WQAFQNFLVA
PQSVKLWLLL SRYDGSFMAQ RGWHMSQGFY EMLGKVNPMP PPIHVALLAN NMYFASKLVG
SGVDINALNR FWKNSAPKYR QPHMSPGGTV LDNELDLQTL DTLLRLGADV NAHDSYGQGA
IARAIKDHDD GRALRLLSFA RGVRDRLPPL GYEPQLLAQA ASMTMQKVVA EMLDDPLMDL
CQESVLQEST SIVGTFIATP LEHACLFGQA TMATIMMSHP RMVEAQQRME REWRGRSPAS
VALLTTLQGW SELTLLALQH FEIDLARERD INKRTILIHA VMEEWHDVLE HCLEHLTGLD
LNVHDQHGMT ALHHAGKVRN WYAAKRLLEA GADAYVEDNS GQTPAHSAAE AGSERVLWIM
LEKGVVSTVS LDHNNRNILH YVATWNLNTI AERLIELEAD QVKTEDQLGR TPVHLAALFG
STAVLAQLLA TGLVDVNAQD HRGRTALHLA VEGRVESCID ELLSRETTDL NIMDRNLRAP
LDMTNSFKDL DQAAVIRGLL EAAGCKPGLW RPRRSYGNVV EQAVASGEEM AGFYEAHWQI
VLALPGEAKL RERERKVEEA VDQAWKAGVA YDRDEIIERI LADEAREKDV RSSPPLPESP
AHYGPQEDLD WKISDRQPRE SEIPKQSRRG YVKKSSKRAS GRGERAL
//
