ID A0A0A1V1Z3_9HYPO Unreviewed; 1248 AA.
AC A0A0A1V1Z3;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=X797_003373 {ECO:0000313|EMBL:EXV03573.1};
OS Metarhizium robertsii.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=568076 {ECO:0000313|EMBL:EXV03573.1, ECO:0000313|Proteomes:UP000030151};
RN [1] {ECO:0000313|EMBL:EXV03573.1, ECO:0000313|Proteomes:UP000030151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2575 {ECO:0000313|EMBL:EXV03573.1,
RC ECO:0000313|Proteomes:UP000030151};
RA Giuliano Garisto Donzelli B., Roe B.A., Macmil S.L., Krasnoff S.B.,
RA Gibson D.M.;
RT "The genome sequence of the entomopathogenic fungus Metarhizium robertsii
RT ARSEF 2575.";
RL Submitted (FEB-2014) 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:EXV03573.1}.
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DR EMBL; JELW01000003; EXV03573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1V1Z3; -.
DR eggNOG; KOG1839; Eukaryota.
DR HOGENOM; CLU_003256_2_0_1; -.
DR OrthoDB; 927222at2759; -.
DR Proteomes; UP000030151; 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; 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; PF13374; TPR_10; 1.
DR Pfam; PF13424; TPR_12; 2.
DR SMART; SM00028; TPR; 2.
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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_03013};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 330..574
FT /note="Clu"
FT /evidence="ECO:0000259|PROSITE:PS51823"
FT REPEAT 983..1016
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 624..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..679
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 871..907
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1179..1248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 871..889
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1193..1210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1214..1231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1248 AA; 138842 MW; 2A7CD170B5193200 CRC64;
MAAPEQVPNP TAAGAEAAQK SANPMAVGTE SDLDAEAENG AEALINLSIV LPDSNATRMQ
IMVSSQEQVH EVRQSIIDLP AAFRYTCFHL EYQGNKVNDF ISIAEIPNLE PEPEFRLIED
PYTEKEARIH LVRIRELIGA AGDRVDVYQG VLPGLSLFES VARQTQKISG AAQDASPLKD
YDFQSAPSLN NLVPDFFEPG PKTVKSVALS SWNPPPCHLR QRGHLLYIVV STNEGEQFQI
TSHVSGFFVN KSSNAKFDPY PRASPKGYSA HSLLELITLI SPSFSDTFQQ LLEYNNQRDP
LATFQITNTV PSAPWAVPSP TSALCAHVAD PTRPQETLLL SGVENTDTLR DWNEEFQSAK
ELPKETVQDR VFRERLISKL FADYNDAATK GAVMVARGEI APLNPTEGRD AQIFVYNNIF
FSFGADGVGT FTSEGGDEAA RVATGKDVAG VRLVNQLDIE GLFAPATVVV DYLGKRIVGQ
SIVPGIFKQR EPGENQIDYG AVDGKDIVAD DERFAASFAQ LSKALKVKKH PVWDKDGKRF
DLEASVETKG LMGTDGRKYV LDLYRITPYD INWLEDTKLQ AEKGHSKAYP HRMTVLRPEL
VDSFARFKMK QWVDAELALR DRTKADEDVN NESKEASDEG KSKTQLDLSD FKFSLNPDAF
SGQVPQSDEE KVQLEEDEKE VREAGNYLRN QVIPDLLREL SDSDISSPMD GQSLSRLLHK
RGINVRYLGA VASRATDGRL RCLQEICIQD MVARSFKHAA AVYLRDLPVP FTASCISHLL
NCLLGYEMNA KPKAEVDTSL KSLYSDSDLS FELVTPGELR VSIEEQVLKR FRYKLEDGWL
NTIRKFQLLR EICLKIGIQI QAKDYSFDER TKPSYQSTET VSKQSNGQQN GESKDKKKKK
KGQETSTVAA TLSTVNTTFS PEDVVDVVPV IKHSAPRSSL AEEALEAGRL SIIQNQKKLG
QELLLESLSL HEQIYGILHP EVARVYNSLS MLYYQLDDKE AAVELARKAI VVAERTVGID
SAETLLNYLN LSLFLHQVGD SRGALAYSKH ALVLWKIIYG PGHPDSITTI NNAAVMLQHL
KQYHESRLWF EESLRVCESV FGKQSINSAT LLFQLAQALA LDHDSKGAVN RMRESYNIFL
SELGPDDKNT KEAESWLEQL TQNAVSIAKH AKDVESRRIR SGIRFPATVP PEQQPGARSQ
RMTQPSQIDA RSIDELIKFI EGGDQKSKAS KKRPGRGNPK RRGQSTSA
//
