ID S3CDT9_OPHP1 Unreviewed; 1302 AA.
AC S3CDT9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 43.
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=F503_05276 {ECO:0000313|EMBL:EPE10181.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE10181.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE10181.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE10181.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
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}.
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DR EMBL; KE148146; EPE10181.1; -; Genomic_DNA.
DR STRING; 1262450.S3CDT9; -.
DR VEuPathDB; FungiDB:F503_05276; -.
DR eggNOG; KOG1839; Eukaryota.
DR HOGENOM; CLU_003256_2_0_1; -.
DR OMA; HPVWDKD; -.
DR OrthoDB; 927222at2759; -.
DR Proteomes; UP000016923; 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:0003743; F:translation initiation factor activity; 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; 1.25.40.10; Tetratricopeptide repeat domain; 2.
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; 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; PF13424; TPR_12; 2.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF103107; Hypothetical protein c14orf129, hspc210; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS51823; CLU; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03013};
KW Initiation factor {ECO:0000313|EMBL:EPE10181.1};
KW Protein biosynthesis {ECO:0000313|EMBL:EPE10181.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000016923};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03013};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 320..569
FT /note="Clu"
FT /evidence="ECO:0000259|PROSITE:PS51823"
FT REPEAT 1035..1068
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 641..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..966
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1277..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 652..682
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..944
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1302 AA; 143006 MW; 891169463AE5A156 CRC64;
MATSEDQTKA PPAEETSKAE NAVATQVEGV EDDEPAVEES LVNFTIVLPN SSETLAVTIP
SHEQFSEVRQ VINESPAAQE YSCFHIEYDG KRINEYGLVS EIPDLTPQAE IRVVLDPYTE
KEARLHVIRI RDLIGAAASR PDAVQGVLPG LSIYDSVNAD ATAAAAAAAP AEYDFAAPID
PSIILPRLSA DEVNAPKTVK AIQISPWNPP PANLRQKGHL LYLIITTNEG EQVQVTAHVG
GFYVNKSSNA KFDPLPRPAP KNQSAHSLLS LIRQLSPSFD DSFVKLQEFN SKRDPLSTYQ
INNSLPAAPW LVPSQSSPSC AHTADITRTQ EAYLISGTDS VDNLRDWNEE LQSARELPRE
TVQDRIFRER LVSKVFADYI DAATRGALLV ASGEINPLNP TEGRDAQIFV YNNIFFSFGA
DGVGTFTSEG GDEAARVATG KDVAGVRRVN QLDIENLYCP GTVVVDYLGK RIVGQSLVPG
IFKQREPGEN QIDYGAVDGK EVVAADKRFA EPFAKLSQSL NVKPHTVWDG EGKAFKLEAS
VETKGLMGTD GRKYVLDLYR ITPLDIQWQE ENDEAEKAGE SAYPHRMTVL RPELIEAYSR
FKLREWLDSE LAKRTKVKEE AEAVKTAKAA KKATKEAAKA AKAAKKESSD SEDSDDSEES
SDSDDSEESD SDEDEEDDEK KEEKPELDDR IDVSKFKFSL NPDAFSGQVP QTDEEKEEMT
ADEKDVRAVG DHLRATVIPG LIRELSESEI SFPMDGRSLT QLLHKAGINI RYLGRIAKAC
EGEKRLVCLQ TIAVREMISR AFKHVSAKYL RYLPLPLTSA CISHLLNCLL GAAANANPSS
EVDPALRELY SNADLAFEKV TPESLREDIE AETVRRFRFT LPTDWHSALT GHLQLLREVS
LKLGIQVLSK KFAFTAEQLS AVAATTTEAA QNGKSNGTTN GASKKKNKKV ARDASPAVDS
QRVASRAPHT FAAEDIVNVV PIVKNSAPRS TLSEEAMEAG RISLQQNQVK IGQELLLESL
SLHEQIYGIL HPEVARAYST LATIYYQLDE KEAAIELSRK AVIVSERVVG VDSSETIQSY
LNLGLFVHSQ GDSALALGYL KHAFKLWQIV YGLDHPDSIT TMNNAAVMLQ NLKAFHESRR
WFEESLRLSS TVFGEASINS ATLLFQLAQS LALDNDSKGS VVRMRECYNI FLSELGAEDK
NTKEAEHWLN QLTSNAVNIA KHTKDAEARR IRAGISFPTR APMTGLVDPA VNTKAVGSSS
SVNDGVDSRS IDELMRYIEG SEGKKKSASK KQSNPKKRGG KA
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