ID A0A182NM80_9DIPT Unreviewed; 743 AA.
AC A0A182NM80;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Large ribosomal subunit protein mL50 {ECO:0000256|ARBA:ARBA00035183};
OS Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR008765-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
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 dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR008765-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR008765-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the mitochondrion-specific ribosomal protein
CC mL50 family. {ECO:0000256|ARBA:ARBA00008860}.
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DR AlphaFoldDB; A0A182NM80; -.
DR STRING; 7168.A0A182NM80; -.
DR EnsemblMetazoa; ADIR008765-RA; ADIR008765-PA; ADIR008765.
DR VEuPathDB; VectorBase:ADIR008765; -.
DR OrthoDB; 3078059at2759; -.
DR Proteomes; UP000075884; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.40.1800.20; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 4.
DR InterPro; IPR018305; Ribosomal_m50.
DR InterPro; IPR039970; TF_Grauzone.
DR InterPro; IPR012934; Znf_AD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR23225:SF2; AT09679P-RELATED; 1.
DR PANTHER; PTHR23225; ZINC FINGER PROTEIN; 1.
DR Pfam; PF10501; Ribosomal_L50; 1.
DR Pfam; PF07776; zf-AD; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 8.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 7.
PE 3: Inferred from homology;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 479..507
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 510..532
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 535..563
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 564..591
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 625..653
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 653..681
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 682..710
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 320..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 337..362
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 718..743
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 743 AA; 85720 MW; E48DB6352C506B66 CRC64;
MAGIFRSTVA ARNTALFLTN KTVDITTLRF ASANRVKRIK KPEITNRDAN QAKSAAMRAE
VEAQGTLYEG KRFESVAQSI SARGYLRALK PYTPPENASE QVLKLAKENG LNDSKQSFSG
TQQKFAFLSA CGKAFDHWVP NSMLHELQTI EDAIIFYQTP IDTRLPLDAI RTVELPENLH
IQQDYVRFHP ETDTMFGGKS AFPKSSTVVT GLKYKQKYRG HEAKNEKLKT LFTFPITTID
SFPSSVCLRC EEQVSVFHTY HELVKTNQEQ LWAVQHQKYF EVVKVEPTLH NEYDAFELPI
QGAEAGEKTV EPDACKVEIV DVPEDRKEHD AVESEPDEGN GQDDYDPASS EDNTSDDSDY
DEEENKSLAR VHTVPVQSAR PGQKRRGRPR KGEVRETKQS HTSPKRKYKS MDETNQRLRE
FYDMKCEICD EKLDSFTALK NHYYKQHQVQ GYIKCCERTF HSRYRLLEHL SKHVGASMVR
CEICDKNFSS RSYLLVHNSR MHGQAEDRPY KCTQCHQSYA MECHLKAHIV SHVRVNCPVC
GKELASSLSL RTHMINMHGN RENHICDSCG REFRSRQAFE RHVKLHLGLE VTEQVQCNVC
AKWLNSKRAL KMHTKLVHME AGQTFQCDLC TQQCPNSRAL ASHKQRVHVE ERFKCEECGK
LFKRQLYLKE HVAALHTRKP LYSCEVCGAT FNSNANKYSH RKNKHPVEWE ARRKQQEEQQ
QQQQMQQQQQ QQQHQQPQEE SSG
//