ID A0A1F5LBI1_9EURO Unreviewed; 1249 AA.
AC A0A1F5LBI1;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 22-FEB-2023, entry version 20.
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=PENARI_c016G08417 {ECO:0000313|EMBL:OGE50593.1};
OS Penicillium arizonense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=1835702 {ECO:0000313|EMBL:OGE50593.1, ECO:0000313|Proteomes:UP000177622};
RN [1] {ECO:0000313|EMBL:OGE50593.1, ECO:0000313|Proteomes:UP000177622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141311 {ECO:0000313|EMBL:OGE50593.1,
RC ECO:0000313|Proteomes:UP000177622};
RX PubMed=27739446; DOI=10.1038/srep35112;
RA Grijseels S., Nielsen J.C., Randelovic M., Nielsen J., Nielsen K.F.,
RA Workman M., Frisvad J.C.;
RT "Penicillium arizonense, a new, genome sequenced fungal species, reveals a
RT high chemical diversity in secreted metabolites.";
RL Sci. Rep. 6:35112-35112(2016).
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:OGE50593.1}.
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DR EMBL; LXJU01000016; OGE50593.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5LBI1; -.
DR STRING; 1835702.A0A1F5LBI1; -.
DR OrthoDB; 927222at2759; -.
DR Proteomes; UP000177622; 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:UP000177622};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03013};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}.
FT DOMAIN 324..568
FT /note="Clu"
FT /evidence="ECO:0000259|PROSITE:PS51823"
FT REPEAT 970..1003
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 610..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 874..891
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1249 AA; 138748 MW; 28B591F9B55604FC CRC64;
MAQTNGELEH SKEAPQASQE VTNGNAPEGV EEDNAGGLFQ ISVKLPHAPY KIQVMVSSQE
QVQDVRQSIV ELPGTFQYTC FHLEFNGSRI NDFVELSEVP DLQADSEIVL VEDPYTEKEA
RMHVVRIREL IGASGDRVDN LHGISAGLSL HDAISAEAVK ANASEKEHSL SKYDLTGVSS
LQTILPSAQA PLPKTVKSIS LSSWNPVPYN LRQKGHLLYL LVTTNEGEQF QITAHVSGFF
VNKCSNTRFD PFPKPMPKDK KGSAHSLLTL ISHISPSFNE SFEALQEYNN EKDLLTTFPF
QNAIPNSPWL ISPSTSSLNA HQPDITRSQE NYLISGVDNA ETLRDWNEEF QTTRELPRDT
VQDRVFRERL TSKLFADYNE AAARGAVLVA RGEVAPLNPT EARDAQIFVY NNIFYSFGAD
GVGTFTSEGG DEAARVAVGK DVLGIKAVNQ LDIDGLFTPG TVVVDYLGKR IVGQSIVPGI
FKQREPGEHQ IDYGGVEGKE VVATHSDFVP VFEKLSKALR IKSHPVWDKD NKRHDLEGSV
ETKGLLGTDG RKYVLDLYRV APMDAEWQQE DGSDVYPHRM SVLRLELVES YWRHKMSQYV
KAEVERRRAA AAETPKEEGK TEEENAADQE RVDISGFNLA LNPDVFSGQV PQTEEEKEQW
AQDEKEVREA CDHLRSKVIP DLLKDLHDGD VGFPMDGQSL TQLLHKRGIN LRYLGKLAQQ
SNEKGPRLQA LSTLLIQEMI TRAFKHVANR YLSNVPAPFV APCISHLLNC LLGSAVNATP
KAEIDESLRE IFTEGDFSFE KVTPESLRAE IEKQVTIRFR FSLENGWTNT LRHLQLLRDI
SIKLGLQLGA RDYPFSKDQV KEVVVPVPTS NGTNREEPKK KGNKKKGGDT KSPTRAPAPA
KPAVTFTADD ILNVVPLVRD AAPRSALAEE ALEAGRISLM QNQKQLGQEL ILESLSLHEQ
IYGILHPEVA KLYHQLSMLY YQTDEKEAAV ELARKAVIVT ERTMGVDSAD TILSYLNLSL
FEHASGNTKT ALVYIKHAMD IWKIIYGANH PDSITTMNNA AVMLQHLKQY NDSRKWFEAS
LSVCEDLFGK DSINTATILF QLAQALALDQ DSKAAVGKMR EAYNIFLAQL GPEDRNTKEA
ETWLEQLTQN AVSIAKHAKD IQARRLRRIN MNPRVSTMGT RVQPQVGQVA PDVTGAAQPS
ASGLDSRNID ELLKFIEGGD AGSSSRSKQK KRAATSNPKL RGSKQTPKA
//
