ID G0SB63_CHATD Unreviewed; 719 AA.
AC G0SB63;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=DUF676 domain-containing protein {ECO:0000259|Pfam:PF05057};
GN ORFNames=CTHT_0049040 {ECO:0000313|EMBL:EGS19443.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS19443.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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; GL988044; EGS19443.1; -; Genomic_DNA.
DR RefSeq; XP_006695265.1; XM_006695202.1.
DR AlphaFoldDB; G0SB63; -.
DR GeneID; 18258942; -.
DR KEGG; cthr:CTHT_0049040; -.
DR eggNOG; KOG2029; Eukaryota.
DR HOGENOM; CLU_014564_0_0_1; -.
DR OMA; EICATHI; -.
DR OrthoDB; 2331935at2759; -.
DR Proteomes; UP000008066; 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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR007751; DUF676_lipase-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR48182; PROTEIN SERAC1; 1.
DR PANTHER; PTHR48182:SF2; PROTEIN SERAC1; 1.
DR Pfam; PF05057; DUF676; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
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:UP000008066};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 88..224
FT /note="DUF676"
FT /evidence="ECO:0000259|Pfam:PF05057"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 719 AA; 81776 MW; 49978B8F4A385523 CRC64;
MDKPSSLSFL RKKEKSKGRL SVNHVSRRQS FDPEELEKIR ALTASDTAVE AQSNDSDLEH
AEEFDPINPE GITLLHMPED PQTHKVDIIF IHGLGGGSYR TWSYKTKPDK FWPKLWLPRE
VPEARIFTFG YDANVNVLRK GDDVSILDFA KTFLQRVKHY QEGTTQRFGQ VPIIVVAHSM
GGLVFKQAFV LGHMDPAFHD IIPMFRAVLF LATPHRGSDL AKVLSLFLSS GRTYVEELIR
KSTTTDQLRE SFRHLAPKLR IISFYETKPT PIALGISTMI VEKDNAILDY PGEESMMLAA
DHHQVCKFKS TNDNNYRIVI EKIRSVVMQL SSVPAQADTA NVPHGDLQQN LDAELEEIAY
MLGVEHHIGT PKADPDLLCR ISERTDGTCI NFLHDTRVEN WLNTGKTEIL WAYAPAGSGK
SMTCAFFTDY LFQNYQHCSF FFFKYGQRAR QSPQDMLLSL AYQTARQLPE YRRALLNLAK
SGSSRARTLA SLDWMAIRRQ LFTGFLAPLK TAADLYWVVD GVDEGLSRDQ IMRALTEVAA
DFKGPVKVHI LVSSRPLEDI RQVIRVAKAR EDKKKDGIII DEMPFPDNRD DIRRTVDNEL
DYLPCDEEEH PTLKRDIVER IVDRADGNFL WARLISEKIV QECADYADIE HVLDTTPSGM
SEFYDRMMGA IQKLNNNKDK TMAQASSTCD ISSPNFVVNL SSLITKDESL WFIILLENI
//