ID A0A0G4KUV8_9PEZI Unreviewed; 1268 AA.
AC A0A0G4KUV8;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 22-FEB-2023, entry version 27.
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=BN1708_010872 {ECO:0000313|EMBL:CRK13579.1};
OS Verticillium longisporum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK13579.1, ECO:0000313|Proteomes:UP000044602};
RN [1] {ECO:0000313|EMBL:CRK13579.1, ECO:0000313|Proteomes:UP000044602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VL1 {ECO:0000313|EMBL:CRK13579.1};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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}.
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DR EMBL; CVQH01004780; CRK13579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G4KUV8; -.
DR STRING; 100787.A0A0G4KUV8; -.
DR OrthoDB; 927222at2759; -.
DR Proteomes; UP000044602; 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; 2.
DR Pfam; PF13424; TPR_12; 1.
DR SUPFAM; SSF103107; Hypothetical protein c14orf129, hspc210; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
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 Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03013};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 337..581
FT /note="Clu"
FT /evidence="ECO:0000259|PROSITE:PS51823"
FT REPEAT 999..1032
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 167..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 622..660
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1198..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1213..1235
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1268 AA; 140273 MW; 0CAAE7DBA9220F5F CRC64;
MSSEKNEVPA GSVPAAEEVA AQDSAGQEAA IAENDIDQEE HAAEALINLT IGLPQEPHSM
TILVSPQEQV HEVRQSIIDL PAAFRYTCFH LEHNGERVND FIPMSEVPGI AENPNVTLVE
DPYTEKEARI HLVRIRELIG GAGDRADVVQ GVLPGLSLLD SIDVTAKHGS ERNEDQPPAE
QPEPVGESTF SSPASISHLL PPPPEDAPKT IKTITLSSWN PPPCHLKQRG HLLYLIITTN
EGEQFQVTAH VGGFYVNKSS NSKFDPLPRP APKGQSAHSL LSLLELISPS FEPSFKALQE
FNNRKDPLAT FQIANAIPAA PWIVPSTTSP HCTHLSDPTR SQETYLIAGV DNTDTLRDWN
EEFQSAKELP KETVQDRVFR ERLLSKLFAD YNDAATRGAV LVARGEIPPL NPTECKDAQI
FVYNNVFFSF GADGVGTFTS EGGDEAARVA TGKDVAGVRL VNQLDVDGLF TTATVVVDYL
GKRIVGQSIV PGIFKPREPG ENQIDYGAVE GKDIVAADDR FVSVFEKLSR ALRVKKHPVW
DKESKRIDLE ASVETKGLMG TDGRKYVLDL YRVTPLDVAW LEASAEEGEF PEYPHRMTVL
RPELVESFGR KKMKEWVDEQ LAQRAQSKQE STEDTTKQAS TADSTGESTE AQATSEKEKD
RIDLSQFQFA LNPDAFSGQL PQTPDEKAEL KADEKDVRVA CEYLTDRVIP DLVRELQDCD
ISFPMDGQAL SRLLHKRGIN VRYLGRIASL STDPRLQCLR DIAIQDMVAR SFKHVISSFL
RETPSPLASS CVAHLLNCLL GAELNPKPVA DVDPTMKALY SDLDTSYESV TPQTLRARIS
EETHRRYRFK LDDEWYKSIK PLQTLREISL KLGLQLQAKE YLFSKTDSTE APTEAKPADA
TANGQLNGES KKKNKKKNRD ASPAAVATTG APCTFSADDV INIVPVVKHS CPRSALAEEA
LEAGRISIMQ SQKKLGQELL LESLSLHEQI YGILHPEVAR VYNTLSMLYY QLDEKEAAVE
LSRKAIVVSE RTVGVDSAET LLNYLNLSLF LHQTGDSQGA LSYAKHALQL WKIIYGPDHP
DSITTINNGA VMLQHLKAYH ESRLWFEESL RVCEKVFGKS SINAATLLFQ LAQALALDQD
SKGAVKRMRE SYNIFLSELG ADDKNTKEAE SWLEQLTQNA VSIAKHAKDM QTRRLRTGIK
FSPRGAPFEA DAPSSVASTS RQTQLDGSSQ MDSRSIDELI KFIEGNDQQT NKSSKRPSRG
NPKRRGKA
//
