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Database: UniProt
Entry: A0A2S4Q161_9PEZI
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Original site: A0A2S4Q161_9PEZI 
ID   A0A2S4Q161_9PEZI        Unreviewed;      1275 AA.
AC   A0A2S4Q161;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   22-FEB-2023, entry version 16.
DE   RecName: Full=Clustered mitochondria protein homolog {ECO:0000256|HAMAP-Rule:MF_03013};
DE   AltName: Full=Protein TIF31 homolog {ECO:0000256|HAMAP-Rule:MF_03013};
GN   Name=CLU1 {ECO:0000256|HAMAP-Rule:MF_03013};
GN   Synonyms=TIF31 {ECO:0000256|HAMAP-Rule:MF_03013};
GN   ORFNames=EPUL_001242 {ECO:0000313|EMBL:POS88022.1};
OS   Erysiphe pulchra.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Erysiphales; Erysiphaceae; Erysiphe.
OX   NCBI_TaxID=225359 {ECO:0000313|EMBL:POS88022.1, ECO:0000313|Proteomes:UP000237438};
RN   [1] {ECO:0000313|EMBL:POS88022.1, ECO:0000313|Proteomes:UP000237438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Cflorida {ECO:0000313|EMBL:POS88022.1};
RA   Wadl P.A., Mack B.M., Moore G., Beltz S.B.;
RT   "Development of genomic resources for the powdery mildew, Erysiphe
RT   pulchra.";
RL   Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: mRNA-binding protein involved in proper cytoplasmic
CC       distribution of mitochondria. {ECO:0000256|HAMAP-Rule:MF_03013}.
CC   -!- SUBUNIT: May associate with the eukaryotic translation initiation
CC       factor 3 (eIF-3) complex. {ECO:0000256|HAMAP-Rule:MF_03013}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03013}.
CC   -!- SIMILARITY: Belongs to the CLU family. {ECO:0000256|HAMAP-
CC       Rule:MF_03013}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:POS88022.1}.
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DR   EMBL; PEDP01000041; POS88022.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2S4Q161; -.
DR   STRING; 225359.A0A2S4Q161; -.
DR   OrthoDB; 927222at2759; -.
DR   Proteomes; UP000237438; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007005; P:mitochondrion organization; IEA:UniProtKB-UniRule.
DR   GO; GO:0051640; P:organelle localization; IEA:UniProt.
DR   CDD; cd15466; CLU-central; 1.
DR   Gene3D; 3.30.2280.10; Hypothetical protein (hspc210); 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR   HAMAP; MF_03013; CLU; 1.
DR   InterPro; IPR033646; CLU-central.
DR   InterPro; IPR025697; CLU_dom.
DR   InterPro; IPR028275; CLU_N.
DR   InterPro; IPR027523; CLU_prot.
DR   InterPro; IPR007967; GSKIP_dom.
DR   InterPro; IPR023231; GSKIP_dom_sf.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR12601:SF6; CLUSTERED MITOCHONDRIA PROTEIN HOMOLOG; 1.
DR   PANTHER; PTHR12601; EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT EIF-3; 1.
DR   Pfam; PF13236; CLU; 1.
DR   Pfam; PF15044; CLU_N; 1.
DR   Pfam; PF12807; eIF3_p135; 1.
DR   Pfam; PF05303; GSKIP_dom; 1.
DR   Pfam; PF13374; TPR_10; 2.
DR   Pfam; PF13424; TPR_12; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF103107; Hypothetical protein c14orf129, hspc210; 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS51823; CLU; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03013};
KW   Reference proteome {ECO:0000313|Proteomes:UP000237438};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_03013}.
FT   DOMAIN          336..580
FT                   /note="Clu"
FT                   /evidence="ECO:0000259|PROSITE:PS51823"
FT   REGION          913..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1244..1275
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1275 AA;  142991 MW;  9D94739FDE2EF15D CRC64;
     MAGLEKVANV SKSAVNSLEN IHETKLKSES PIMMIGEQPE TENGERNIEM MFELTVHLPN
     FPRSVTVMVS NQEAIHDVHQ LVTEQPGTFQ YSCFHLEHKG KQVNDFTLIS EIDNITSEPE
     LTLIEDPYTE KEARIHFVRI RELIGAAGDR TDTLHGVLSG LTLYDSVTPR TTQGKKEVNT
     VQYLVDYDFK ATGSLSKLLP HVQEPPPKTV KSLSLSPWHP PPYHLRQKGH LLYLLLTTNE
     GEQYQITSCV SGFYINKSSN MKFDPFARGA PRAHSAHSLL TLLADVSPSF SSCFEKLLEY
     NNSKEPLATF QISNTVPANP WIVPSSNSPN VSHQPDITRT QESYLISGLE NAETLRDWNE
     EFQSTRELPK ENIQNRVFRE RVVSKLCADF TEAAARGAIL VARGEITPLN PTESKEAQIF
     VYNNIFFSFG ADGVGTFAME GGDEAARVAT GKDVLGVRMV NQLEIEDLYT AGTVIVDYLG
     KRIVAQSIVP GIFKQRGPGE NQIDYGAVDG RDVIAADERF STVFEKLSKA LKVKKHRLWD
     KNGKEFDLHG SVETKGLLGT DGRKYVLDLY RITPFDIAWM EEYDTIIFDP EKSSNINSNS
     YPHRMTVLRP ELVDTFWKFK MREWVDKEIK KRRQMSTNTS QPIETPTTKI LEISEAVDIN
     TQSISDTTSS KADPISDLDK IDITDFDFSL NPDAFFGQEP QTDEEKKKLA EDEADVRDAC
     QYLRSSVIPE LVNDLKEGDV GFPMDGQSLS RLLHKRGINI RYIGKIASLS QEKKLEPLKI
     LSIQEMISRA FKHVSSRYLK HLPIPLSSSC ISHLLNCFLG FDLNPKPIPS INKDMASLYR
     GADLAFQTVT PQSLQKEIEL NVVKRFQYTL KDDWISEMKK LQMLREVSLK IGLQLEAKDY
     IFQPLPISKQ PVSTNGHLIE PTKKTSSSKK SKKATSRSHS PAVIALNTFT PDDIINIVPI
     IKDAAPRSTL AQEALEAGRI SILQNQKKLG QELLLESLSL HEQIYGIIHP EVARVYNNLS
     MLYYQLEEKE AAVELALKAV IVSERTLGVD NPETLLSYLN LGLFSHAAGE TVQALTYITH
     ALDIWRIIYG NFHPDSITTL NNAAVMLQHL KCYHSSRLWF EASLDICSSI YGPNSINAAT
     LLFQLAQALA LDNDSKQAVL RMKSSYNIFL AALGPEDKNT REAECWLDSL TQNAVNIAKH
     AQAKDIQARR LQAAIQVGVG QATPGREKIS TQMDKSSIDE LLKFIEGKDA RNKPKRRQPN
     GGRKNPKSRV SNGIA
//
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