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Database: UniProt
Entry: A0A0J6YRA0_COCIT
LinkDB: A0A0J6YRA0_COCIT
Original site: A0A0J6YRA0_COCIT 
ID   A0A0J6YRA0_COCIT        Unreviewed;      1056 AA.
AC   A0A0J6YRA0;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=TPR repeat {ECO:0000313|EMBL:KMP09794.1};
GN   ORFNames=CIRG_09027 {ECO:0000313|EMBL:KMP09794.1};
OS   Coccidioides immitis RMSCC 2394.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP09794.1, ECO:0000313|Proteomes:UP000054565};
RN   [1] {ECO:0000313|Proteomes:UP000054565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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DR   EMBL; DS028100; KMP09794.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J6YRA0; -.
DR   STRING; 404692.A0A0J6YRA0; -.
DR   Proteomes; UP000054565; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043531; F:ADP binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046486; P:glycerolipid metabolic process; IEA:UniProt.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07216; Pat17_PNPLA8_PNPLA9_like3; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR002182; NB-ARC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR002641; PNPLA_dom.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR46082:SF6; AAA+ ATPASE DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR46082; ATP/GTP-BINDING PROTEIN-RELATED; 1.
DR   Pfam; PF00931; NB-ARC; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   Pfam; PF13374; TPR_10; 2.
DR   Pfam; PF13424; TPR_12; 3.
DR   PRINTS; PR00364; DISEASERSIST.
DR   SMART; SM00028; TPR; 7.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48452; TPR-like; 3.
DR   PROSITE; PS51635; PNPLA; 1.
DR   PROSITE; PS50005; TPR; 1.
PE   4: Predicted;
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   DOMAIN          1..182
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000259|PROSITE:PS51635"
FT   REPEAT          813..846
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   REGION          1037..1056
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1056 AA;  119252 MW;  369DA3BCF477D4A1 CRC64;
     MSRLNYERHQ EGKPPAKPCE IFDLIGGTST GGLMAIMLGR LEMDVDECIS KFSQISEEIF
     RERSSWFLLD RKARIKGRFD SKNLERAVRA VLKERNVAEN EMLDDGVSRG CKVFVCATSK
     DTKEVKRLRS YTIPDELNIK PTIVEAALAT SAATSFFDPV TIGFRTFVDG GVGANNPVNQ
     VEQEASNIWC PKSGDLKPLV KCFVSIGTGN TGKVALDYNA AKFAQALVDL TTDTEFTAKD
     FIARWRGHYE EGRYFRFSVD HGIENLDLAE YRAQGLIEAA ADDYIHHQEQ KFKIQSCVQN
     LLKKEINAGK DIENAIQRFQ QSSPLPEAEP LDSEFTVPFD LTGIRYTAQF IGRVSELAQL
     RELLLSNEFN RRKVVVLQGL GGIGKTQLAI EFARRYQESF SSIFWISGKT REMLLHSLAS
     VTRRLASDQN DEAIVEDMKD SKGIEKRAKE ALNWFALKGN NKWLIIFDNV DKDPSGEVED
     DEAFPVEDFF PGADQGAIII TTRLRQLQEL GDFIHLRTMA QDDALELLAA SGKSSVFKDE
     NDDWNSETLE LIKKLDGLPL AIVLAGSYIS RTGMKVAREI ARTDQLAATL LLFLSSFDNQ
     DIWYGLLEHG KSGWDAPEWF EEIVSDEVNF YTVIGTLSDY SFVEKKENAE GYSMHPVVQQ
     WCQGYLKSAK NCKSIYIAAF ACICNAIPST NEQKFWILQQ RLLPHANRLL PFFQENFSVL
     ECLNDSKILE VVSRLGQLYT EQGKLAQAEV VLRRTLEKQE KILGADHLST LDTVRYLAQL
     YWDLTKLAEA EAMILRALKG KEKVLDQSDT EILRLMNSLG AVLYLQERFD EAEVMYQRVI
     EANDNRKSGQ DDIAAVKATN NLGGIRSTQG RVEDAKKLFR KSHEMARKTL GPDHTLTLKS
     LFNLAVIYHR EKNLDEAEKI HQQVYDGYVK AFGANHLYTM DSLQKLANVL RDQGKLATSE
     QMYLHVLEER EKGGPAEALQ ELGLNYKAQG RLEDADTTLL RALKSQEKAM GPTHDETLEI
     VEQLSLLYLE QGRHEEAEAM KGRVHQPPAS EARENP
//
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