ID A0A182WDW0_9DIPT Unreviewed; 1454 AA.
AC A0A182WDW0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 22-FEB-2023, entry version 27.
DE RecName: Full=Clustered mitochondria protein homolog {ECO:0000256|HAMAP-Rule:MF_03013};
OS Anopheles minimus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=112268 {ECO:0000313|EnsemblMetazoa:AMIN008556-PA, ECO:0000313|Proteomes:UP000075920};
RN [1] {ECO:0000313|Proteomes:UP000075920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MINIMUS1 {ECO:0000313|Proteomes:UP000075920};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles minimus MINIMUS1.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:AMIN008556-PA}
RP IDENTIFICATION.
RC STRAIN=MINIMUS1 {ECO:0000313|EnsemblMetazoa:AMIN008556-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- FUNCTION: mRNA-binding protein involved in proper cytoplasmic
CC distribution of mitochondria. {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 STRING; 112268.A0A182WDW0; -.
DR EnsemblMetazoa; AMIN008556-RA; AMIN008556-PA; AMIN008556.
DR VEuPathDB; VectorBase:AMIN008556; -.
DR OrthoDB; 927222at2759; -.
DR Proteomes; UP000075920; 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 CDD; cd15466; CLU-central; 1.
DR Gene3D; 3.30.2280.10; Hypothetical protein (hspc210); 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
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 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; 1.
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.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_03013};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_03013}.
FT DOMAIN 408..650
FT /note="Clu"
FT /evidence="ECO:0000259|PROSITE:PS51823"
FT REGION 1..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 713..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 946..998
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1390..1454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..976
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..998
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1408
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1454 AA; 160928 MW; 481D7CC4EA376F11 CRC64;
MALETESVQS PDAATDTVST PGSDGIVSGG DSGGKKKGFA KNKKQNGKSS SPPGGGGEDK
ETIGNGHAEQ NGLNGHLSSE ESDAVTANDG GAEDKNAGVA GGGGTTDPSA TGDDDVMKLM
QETGFTVQVL SPGVEPLSIQ VSSMELVQEI HQLLMDREDT CHRTCFSLQL DGRTLDNFAE
LKNIDGLQEG SVIRVVEEPY TMREARIHVR HVRDLLKSLD PADAYNGVDC SSLTFLHTIT
MGDIMEKKKA RQESVDCTPP DFIMPGAKER PLLPLQPGSG KKGNPQPLKV LTTSAWNPPP
GPRKLHGDLM YLYVVTMEDK RLHISACSRG FYVNQSTDDT FNPQPANPSY LSHSLIDLLS
QISATFRRCF SQMQKKRTQR HPFERVATPY QVYTWTAPAL EHTIDAIRAE DTFSSKLGYE
EHIPGQTRDW NEELQTTREL PRATLPERLL RERAIFKVHS DFVTAATRGA MAVIDGNVMP
INPGEDAKTQ MFIWNNIFFS LGFDVRDHYK ELGGDAAAFV APRNDLHGVR VYSAVDVEGL
YTLGTVVIDY RGYRVTAQSI IPGILEREQD QSVVYGSIDF GKTVLSHPKY LELLNSAGKH
LRIQPHSVYN DKQEAIELCS SVECKGIIGN DGRHYILDLL RTFPPDVNFL VLPAEEEAVG
RDSQAMGFPI VHRHKLCCLR QELLEAFVEN RYLMFMKHAA VQLQQCVKKK QEQKAAQKSS
TDDTKPAAIE EGESEKAKEE KEPVKDASRP VPKADSDDAK KLVESLISSD QMNESKEVVK
RVCEAVGSLK EYEFDIRFNP DVYSPGIRHV DEDAGAACSL RRQKQLVKDA AEFLVKHQIP
TFVHECLDHS SAPMDGVTLT ELLHNRGINV RYLGKVVDQL SKIKQLEYLH TIAVSELIVR
AAKHIFTTYL QQTDVMSMAA AISHFLNCLL TVSTVGYQPV ANGNGGDGDG QLADEFGPKS
SSGGKNKQSK QSKRGGKGTN GGGGGRKTTF SVPSSDNNEW QSLTSKLLWS QIRQELKAYW
DFELTVEPSK EGKSTTTIDS IEPLIGAFKL QKISLLRAFC LKTGVQIMLQ EYAFEQRNRP
AFTDSDIVNV FPVVKHINPR ASDAYNFYTT GQTKIQQGYL QDGYGLISEA LNLLNNVYGA
MHPENAQCLR MLARLSYIMG DPQEALAIQQ RAVLMSERVN GVDHPYTISE YAHLALYCFA
NSQISTALKL LYRARYLATI VCGENHPDIA LMDSNISLIL HAVGEYELSL RFLEHALALN
IRYYGEKSLK VAVSYHLVAR TQSCMGDFRS ALVNEKETYA IYKQQLGESH EKTQESSECL
RHLTQQAVVL QKKMNYANGK LLSTGLPPIH IQPPSMGSVL DMLNAINGII FVQISSKEIA
NFKNEIEKRQ KEAGQSQGQQ TTPPVQANQE EVDRMLMETM QKTAAGIPFE EQDGEKKESA
LKEESASKVE VASS
//
