ID A0A3N2Q0D3_9PEZI Unreviewed; 1268 AA.
AC A0A3N2Q0D3;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
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=SODALDRAFT_290096 {ECO:0000313|EMBL:ROT40146.1};
OS Sodiomyces alkalinus F11.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT40146.1, ECO:0000313|Proteomes:UP000272025};
RN [1] {ECO:0000313|EMBL:ROT40146.1, ECO:0000313|Proteomes:UP000272025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11 {ECO:0000313|EMBL:ROT40146.1,
RC ECO:0000313|Proteomes:UP000272025};
RX PubMed=30368956; DOI=10.1111/mec.14912;
RA Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA Grigoriev I.V., Debets A.J.M.;
RT "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT shifted to a protein diet.";
RL Mol. Ecol. 27:4808-4819(2018).
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; ML119052; ROT40146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2Q0D3; -.
DR STRING; 1314773.A0A3N2Q0D3; -.
DR OrthoDB; 927222at2759; -.
DR Proteomes; UP000272025; 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; 3.30.2280.10; Hypothetical protein (hspc210); 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 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 Initiation factor {ECO:0000313|EMBL:ROT40146.1};
KW Protein biosynthesis {ECO:0000313|EMBL:ROT40146.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000272025};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03013};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT DOMAIN 329..573
FT /note="Clu"
FT /evidence="ECO:0000259|PROSITE:PS51823"
FT REPEAT 997..1030
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..659
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1190..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 907..921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1268 AA; 141052 MW; 1575536E63BC85B2 CRC64;
MATVSDEALG STTCQNNAAT ANPTPETPSH HSEAVVQDGE QAHEALINLT IHLPHEPRSM
NILVSPHEQV HEVRQSVIDL PAAFRYTCFH LEYQGSRVND FLPVSEVISP DQPHVTLVQD
PYTEKEARIH LVRIRELIGA SGDRTDLVQG ISPGLSLLDT LNTKGDEAVQ DNREDDLKQY
EFRASASVTK LLPPEAQEAP KTVKSICLSS WNPPPCHLRQ RGHLLYLVVA TLEGEQHHIT
SHVGGFYVNK SSNGKFDPQP KPPPKGHAAH SLLHLLSFLS PSFEAAFRAL QQFNTQRDPL
ATIQIANALP AAPWVVPPTV SLLSSHVSDP TRSQETYLLA GGDNTDTLRD WNEELQSARE
LPKETVQDRV FRERLISKLF ADYNDAATRG AIMVARGEIQ PLNPTECEDA QIFVYNNIFF
SFGADGVGTF TSEGGDEAAR VATAKDVSGV RLVNQLDIDG LYTTATVVVD YLGKRIVAQS
IVPGIFKPRE PGENQIDYGA VEGKDVVAAD ERFIAVFEKL SRDLKVKQHP VWNKDGQRVD
LETSVETKGL MGTDGRKYVL DLYRVTPLDV GWLEISTKEG DFAEYPHRMT VLRPELINSF
CRKKMKEWVD AELARRGRGP KASPSRSEKA VGALPDVENP STAATDETSG SSGAEKDDDH
IDLSKFSFSL NPDVFSGQDP QTDEDRRQLE ADEKDVRLAC HYLTDEVIPE LLRELKECET
SFPMDGQALS RLLHKRGINI RYLGRVASLS TDPSLQCLRN ICVQDMIARS FKHIASAYLR
QTPAPLTSSC VAHLLNCLLG VQLNPAPVPD IDPSLKALYL ESDFSFETVT PYSLRSQVVD
ETWRRFRYRL EDLHRDIKPL QLLRDISLKL GLQLQAKDYV FAQIATDPPA APEAKDQSGT
PNSQTNGESK KKKKKNRDMS PMPGRNTEAR CTFWSDDIVN IVPIVKHSSP RSALAEEALE
AGRISILQSQ RKLGQELLLE SLSLHEQIYG VLHPEVARVY NTLSMLYYQL DEKEAAVELA
RKAIIVSERT VGIDSAETLL NYLNLSLFLH QTGDSKGALM FAKHALDLWN IIYGPDHPDS
ITTINNGAVM LQHLKAYHHS RLWFEESLRV CEQVFGKGSI NAATLLFQLA QALALDQDSK
GAVNRMRESY SIFLSKLGPE DKNTKEAENW LEQLTQNAVS IAKHAKDVQN RRLRPGVRFP
GEGPFNTASH SQASPSTFQK SPLTTTPNID SRSIDDLIKF IEGNDQANMT SKRPSRGNPK
RRGEARAV
//
