CLU_CANGA
ID CLU_CANGA Reviewed; 1267 AA.
AC Q6FJB0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Clustered mitochondria protein homolog {ECO:0000255|HAMAP-Rule:MF_03013};
DE AltName: Full=Protein TIF31 homolog {ECO:0000255|HAMAP-Rule:MF_03013};
GN Name=CLU1 {ECO:0000255|HAMAP-Rule:MF_03013};
GN Synonyms=TIF31 {ECO:0000255|HAMAP-Rule:MF_03013};
GN OrderedLocusNames=CAGL0M07722g;
OS Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS Y-65) (Yeast) (Torulopsis glabrata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC Nakaseomyces/Candida clade.
OX NCBI_TaxID=284593;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
CC -!- FUNCTION: mRNA-binding protein involved in proper cytoplasmic
CC distribution of mitochondria. {ECO:0000255|HAMAP-Rule:MF_03013}.
CC -!- SUBUNIT: May associate with the eukaryotic translation initiation
CC factor 3 (eIF-3) complex. {ECO:0000255|HAMAP-Rule:MF_03013}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03013}.
CC -!- SIMILARITY: Belongs to the CLU family. {ECO:0000255|HAMAP-
CC Rule:MF_03013}.
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DR EMBL; CR380959; CAG62660.1; -; Genomic_DNA.
DR RefSeq; XP_449684.1; XM_449684.1.
DR AlphaFoldDB; Q6FJB0; -.
DR SMR; Q6FJB0; -.
DR STRING; 5478.XP_449684.1; -.
DR PRIDE; Q6FJB0; -.
DR EnsemblFungi; CAG62660; CAG62660; CAGL0M07722g.
DR GeneID; 2891734; -.
DR KEGG; cgr:CAGL0M07722g; -.
DR CGD; CAL0136551; CAGL0M07722g.
DR VEuPathDB; FungiDB:CAGL0M07722g; -.
DR eggNOG; KOG1839; Eukaryota.
DR HOGENOM; CLU_003256_2_0_1; -.
DR InParanoid; Q6FJB0; -.
DR OMA; VSGFYVN; -.
DR Proteomes; UP000002428; Chromosome M.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:EnsemblFungi.
DR GO; GO:0007005; P:mitochondrion organization; IEA:UniProtKB-UniRule.
DR CDD; cd15466; CLU-central; 1.
DR Gene3D; 1.25.40.10; -; 1.
DR Gene3D; 3.30.2280.10; -; 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; IPR023231; GSKIP_dom_sf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR12601; PTHR12601; 1.
DR Pfam; PF13236; CLU; 1.
DR Pfam; PF15044; CLU_N; 1.
DR Pfam; PF12807; eIF3_p135; 1.
DR SUPFAM; SSF103107; SSF103107; 1.
DR PROSITE; PS51823; CLU; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..1267
FT /note="Clustered mitochondria protein homolog"
FT /id="PRO_0000366401"
FT REPEAT 64..102
FT /note="TPR 1"
FT DOMAIN 329..586
FT /note="Clu"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01167"
FT REPEAT 420..453
FT /note="TPR 2"
FT REPEAT 716..749
FT /note="TPR 3"
FT REPEAT 795..830
FT /note="TPR 4"
FT REPEAT 904..939
FT /note="TPR 5"
FT REPEAT 1010..1043
FT /note="TPR 6"
FT REPEAT 1138..1171
FT /note="TPR 7"
FT REGION 1203..1267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1203..1218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1220..1256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1267 AA; 143838 MW; 6FF5FAAB74C26B8C CRC64;
MSQPSDIVKV IVALPTLSKK PQQGKKKKSK ELEEITLQFR KDSKLQNVLD FLSIAPATKY
FTNYNLKNST GDLLLSSEEK TLRELCSDKD EYKVALELKP YNQYQALKHV LTSRDFFGFA
SETEDGLSNV AVSTGSKFYK LPLKEIKEKS PENEDKDTEN KKPTSMNVTD EEKVEFNHMV
HGLFETLKKE KKVLLKDLMN TDTSVVTPCL RSINFSPYNP VPAFYRTKGH LFYLQIVTLE
GESLQVTAIP SGFYINKSTT SKFDPSPKEN DGHVDTVHYT LYDLLASSSK NFVTHISSLE
KKFDDLESVT YVRPACTTLN KPWLIPAIPT NGPDYLRTQI DSFNFEPERN FNDEFQSIKE
IPTNTLQARI ESERIFAKLT HEFTINATKG AMDILYGNGT AMNPDSPLEE QIFLKNNIFY
SFVGDLNQTY ADKGGDEAAI ASANQDLRTL NMLTRLNLPN IHHLLTTIVD FGGKRILAQT
PVPGLLSPMG VKITTNEETK EETVSELSSD ICVKYGLDEN EKKVVFNEEF DEILNDQFAK
SFHLKKHTIQ GTELVFSSQS KGIVGSDKRH YILDLANTYP LDVEFAKENF DDVKEASKKY
PHRQTLIRPE LVEKWWATKI ENDKVELVKA YEENLYSYNP DAYQVPGVED ETVVEISKYL
NEEIIPNVVQ DYLNGNIISP YNGEHLADTF HKNGVNMRYL GKFANLVKEE LRKQEEAHEA
KLAQVIVDNK EYEEWEKSYL QKIETMIKER QAKINKLVQE GKEVPKELTE DLKLDDNEIK
KPSTEKPVVV SYDELVPLIK TAELEIISRS LKHILRKYSR SLPPIVIPAL ISFVFNLLFG
TTYNPAPAVE SVDPLYPVDQ YEFKNLTHDT LLKEIEQEAV VRYRYELEGD WFAEHELYPF
TLIRSICNKF GVQLLNKDYF FSTEQLEEYK QSLDKKSRAK YVAPLTTFSV SDLTVIPKIK
AIDYSSPISE ELWSQGASII NENQKDGLTL LAQSIGFKEE VNSILHSSVA EKYLTLSTIY
NKLGLNAEAI AFCRKSCAIY ERVCGVDSFE LLRALTNLAT LEFANESPYN VALIYQRIIQ
TVSGYGLDKI HHPIFTNIFN YLEQLSLGVQ DAKLAVEVLK SLGDFLVSID GTESLPYAYI
KSKLGNLLAA DNRFSDALNQ IKVAERIFTK ELGTNHGSTA QARQWVDGLT NLIKDVNQKK
QLQQDQTAAS GLKQQPQKSK SGHNKKETTN PDLADKSVDE LLSFIEGEDG KSSKTTKKSK
SKGKNKK
