ID A0A182KA93_9DIPT Unreviewed; 736 AA.
AC A0A182KA93;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Large ribosomal subunit protein mL50 {ECO:0000256|ARBA:ARBA00035183};
OS Anopheles christyi.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=43041 {ECO:0000313|EnsemblMetazoa:ACHR007680-PA, ECO:0000313|Proteomes:UP000075881};
RN [1] {ECO:0000313|Proteomes:UP000075881}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACHKN1017 {ECO:0000313|Proteomes:UP000075881};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Besansky N., 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 christyi ACHKN1017.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ACHR007680-PA}
RP IDENTIFICATION.
RC STRAIN=ACHKN1017 {ECO:0000313|EnsemblMetazoa:ACHR007680-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; A0A182KA93; -.
DR STRING; 43041.A0A182KA93; -.
DR EnsemblMetazoa; ACHR007680-RA; ACHR007680-PA; ACHR007680.
DR VEuPathDB; VectorBase:ACHR007680; -.
DR OrthoDB; 3078059at2759; -.
DR Proteomes; UP000075881; 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:UniProtKB-UniRule.
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 Pfam; PF13912; zf-C2H2_6; 2.
DR SMART; SM00868; zf-AD; 1.
DR SMART; SM00355; ZnF_C2H2; 10.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS51915; ZAD; 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:PRU01263};
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:PRU01263};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 199..272
FT /note="ZAD"
FT /evidence="ECO:0000259|PROSITE:PS51915"
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 301..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 695..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 354..369
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..414
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..715
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..736
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 204
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 248
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
SQ SEQUENCE 736 AA; 85617 MW; 051191BF3431ED60 CRC64;
DLTCFRYGSS NRVKRIKKPE ITNRDANQAK AAAMRAEVEE QSALYEGKRF ESVAQSLSAR
GYLRAIKPYT PPENVAEQVL KLAKENGLTD TKQPFSGIEK KFAFLSACGN TFGHWVPNSM
LHEVQTVDDA TVFYQTPIDT RLPLDAIRSV ELPENLHIQQ DYVRFHPETD TMFGGKSAFP
KSSTVVTGLK YKKKYQMDEK CRLCFIQLKY HQSKTTIEED GFSEKLKTLF SFPITSIETF
PSSVCLQCVE KVTDFHNYHE QVKNNQDQLW STQHQKYFEE VKIEPTPDDV YDVLELPFEE
AEPVEITPTE SCKNETDPKC QEEDQRDVES ELDDETKYEE EYNPSSSATS NNKSDDSEYE
EEKPLRGLKG TAKSEQTRIA QKRRGRPRKS ETGKKSNNEW KSPSERRGKS KDETNQQLRE
FYDMKCELCG EKLESFTALK NHYYRQHQTH GYIKCCGRTF HSRYRLLEHL SYHVGASMVR
CEVCNKTFSS RSYLLVHKSR IHGQAEDRPY KCTQCHQSYA MECHLKAHIV SHVRVNCTIC
GKELASALSL RTHMINMHGN RENHICDSCG REFRSRQAFE RHVKLHLGLE VTEQVQCGEC
LKWLNSKRAL KMHVKLVHME AGQTFQCDIC TQQCPNSRAL ANHKQRVHVE ERFKCEECGK
LFKRQLYLKE HVAALHTRKP LYSCEVCGAT FNSNANKYSH RKNKHPVEWE ARRKQQQEQQ
QQQQQQQEQQ QEMELE
//