ID A0A178DKE3_9PLEO Unreviewed; 1300 AA.
AC A0A178DKE3;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 28-JUN-2023, entry version 23.
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=IQ07DRAFT_685617 {ECO:0000313|EMBL:OAL43489.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL43489.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL43489.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL43489.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441667; OAL43489.1; -; Genomic_DNA.
DR STRING; 765867.A0A178DKE3; -.
DR InParanoid; A0A178DKE3; -.
DR OrthoDB; 927222at2759; -.
DR Proteomes; UP000077535; 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; 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; IPR007967; GSKIP_dom.
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; PF05303; GSKIP_dom; 1.
DR Pfam; PF13374; TPR_10; 2.
DR Pfam; PF13424; TPR_12; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF103107; Hypothetical protein c14orf129, hspc210; 1.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS51823; CLU; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03013};
KW Reference proteome {ECO:0000313|Proteomes:UP000077535};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03013}.
FT DOMAIN 329..573
FT /note="Clu"
FT /evidence="ECO:0000259|PROSITE:PS51823"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..698
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 927..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1233..1300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 626..641
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 642..659
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 660..696
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 927..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1263..1284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1300 AA; 144259 MW; 7AB06CF8AF3FF7CA CRC64;
MAANSNDASK SEASTTPSKD QKAAGQVDAA EDEGENVQQP ESIFQINIKL PHEPFEMQMT
ISTAEQVQDL RQSIIEMPHT FQYSCFHLEH DGQRINDYVE LSEVTGLKAD STLTLVEDPY
TEKEARLHVI RVRELIGAAG DRTDALHGIL AGLSLHDTVG VNESGKSTED GPEQSPLADY
DFKSAGAIKT LLPPAQEAAP KTIKAIAVSP WNPPPYHLRS KGHLLYLVVT TNENEQHHIT
AHASGFFVNK SSNASFDPFP RQAPKARHAH SLLTLLEELS PSFVSSFQQL LEHNAKKELL
TIFQLSNAIP ANPWLVPAPT SSLTVHQPDL ARTQESYLIA GVENTETLRD WNEEFQSTRE
MPKEAVHDRV FRERLTSKLF ADYNEAATRG AMLVARGEIA PLNPTEAKDA QIFVYNNIFY
SFGADGVGTF GTEGGDEAAR VAVGKDVFGV RAVNNLDIHN LFTSGTVVVD YLGKRIVGQS
IVPGIFKQRD PGEHQIDYGA VEGKEVVADD KSFVPLFEQL SKSLRVKKHP VWDKDNVRHE
LEGSVETKGL IGTDGRRYAL DLYRLTPLDV SWIEAYWSEP TKDGESKPKD KDYPHRMATL
RPELVESYGR LKLREYVKNE MEKKAKKAES AAQKAVKDEE SSSEEDSDDS EEDSDDSDSD
SDSEKKPKSK EVAKSKDDAE KKEEAEKKEE AEQDRVDISG FSFALNPDVF SGQNPQSEED
KKEWAQDENE VRAACDHLLS EVIPRLIQEL KDGDAGFPMD GQSLSSLLHK RGINIRYLGK
FAELADKPDP RLQALKRLVI QEMITRGFKH YANSKLRNVS APFTAPCVAH LLNCLLGAEV
SSKPVAEGDS NLKKMYPEVD FSYEKLTPDT LRKEVVAQVA LRYRYDLSQT WVEPGKQMQV
LREVSVKLGL QLVSKQYAFT KEALTSATAE TPAAPQTNGH STSSKKKNKK TSTPPRADSP
AVILPPQTFH ADDVLNIVPV IKEASPKSLL AEEALEAGRM SVAQDQKELG QELLLESLQL
HEQIYGVLHP EVARAYHTLS NLLFNLEDKA SALELAHKAV IVSERTLGVD HADTVLAYLN
VGLFEHASGN TKAALVYVRH ALELWKIIYG ADHPDSITTL NNAAVMLQAM KQYHESRIWF
EASLAICEEV SGKNSINTAT LLFQTAQALA LDKDMRGAVN RMRESYNIFK DVLGAEDRNT
KEAESWLEQL TQSAVSQAKQ LNDLAKGRIR RIQLTGKNPL RPAAATPSAS EAAASTQRSG
SSRVDQRKIE DLLKYIEGDS PKTPSKKRTQ TNPKKRTQKT
//
