ID F2PKT3_TRIEC Unreviewed; 1237 AA.
AC F2PKT3;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=TEQG_01536 {ECO:0000313|EMBL:EGE02501.1};
OS Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN [1] {ECO:0000313|Proteomes:UP000009169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT "Comparative genome analysis of Trichophyton rubrum and related
RT dermatophytes reveals candidate genes involved in infection.";
RL MBio 3:E259-E259(2012).
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; DS995722; EGE02501.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PKT3; -.
DR VEuPathDB; FungiDB:TEQG_01536; -.
DR eggNOG; KOG1839; Eukaryota.
DR HOGENOM; CLU_003256_2_0_1; -.
DR Proteomes; UP000009169; 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; 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 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 317..561
FT /note="Clu"
FT /evidence="ECO:0000259|PROSITE:PS51823"
FT REPEAT 962..995
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 858..888
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..20
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1237 AA; 137470 MW; F11062E8D7A689A3 CRC64;
MDQQSKGPEH SKEVPEDTKP ENTSQELANG NKAEGEQDDN NNAGVLVVCL RHAVSSRAVR
MFASMSNCRV LSVHLLHLET EGNRINDYVE LSEVKGLKAD SEVVLIEDPY TEKEARMHVV
RIRELIGAAG NRVDTLHGLS AGLSLYDSVA AGEELPEEAK KTHALDGYDV NAPLDLATVL
PKDQSAVPKT VRSVSLSPWN PPPYHLRQKG HLLYLLVTTN EGEQHQITSH VSGFYVNKCS
NSKFDPFPRP APKNYSAHSL LTLISLISPS FNESFKALQE YNNKKDLLTT FPFQNSIPNN
PWLVPASQSQ ATAHISDATR SQENYLIAGI DNSETLRDWN EEFQTTRELP RENVQEKVFR
ERLTSKLFAD YNDAAVRGAI LVARGEVASL NPMEARDAQI FVYNNIFFSF GADGVGTFAA
EGGDEAARIA VGKDVMGVKT VNQLDIPGLF TPGTVVVDYL GKRIVGQSIV PGIFKHREPG
EHQIDYGGVE GKDVVAKNEA FTPVFEKLSK ALRVKKHAVW DKDGVRHELE GSVETKGLLG
TDGRKYVLDL YRITPLDISW TEDAEGHDEY PHRMPVLRHE LVEAYWRYKM GQYVKEEVEK
RRAAAKETKA VENGEGGDAE KKDNSDQDRV DISNFRLALN PDVFSGQVPQ TEEEKEEWAR
DEKEVRDACD HLRSKALPEL VKDLYNGEVG FPMDGQSLGQ LLHKRGINIR YLGKVAQLAQ
EKGSRLQSLV ALVVQDMVAR SFKHIANRYL RNLPPPFATT CIAHLLNCLL GTEVNSKPRA
EIDESLRAIY PEGDFSFEEV TPASLAADIE KQVKSRYRYT LEASWTGSLK HFQVLRDISL
KLGLQLVAKE YAFSKSQVKE QSPAGNGAHS DSQDEKKKKK KGSSAAAATP APAPALTFVP
DDIVNIVPIV KDASPRSALA EEAFEAGRIS LMQNQKELGQ ELILESLSLH EQIYGILHPE
VAKLYHQLSM VYYQTDEKDA AVELARKAVI VTERTMGVDS SDAILSYLNL SLFEHANGNT
QTALVYIRHA LELWKIVYGP SHPDSITTMN NAAVMLQHLK KYPDSRKWFE SSLAVCDELF
GRQSVNTATL LFQLAQALAL DQDSKSAVNR MREAYNIFLN ELGPEDRNTK EAESWLEQLT
QNAVSIAKRA KDIQARRRRL VNLPGRSSLT AQAQPSVGQT TSEMVAGVDG ANPSLDSRSI
DELLKFIEGG DAARSKPKKR TTRNPKLRGS KQTSVKP
//
