ID A0A1B0G9J4_GLOMM Unreviewed; 1473 AA.
AC A0A1B0G9J4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 13-SEP-2023, entry version 34.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblMetazoa:GMOY009981-PA};
OS Glossina morsitans morsitans (Savannah tsetse fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Hippoboscoidea;
OC Glossinidae; Glossina.
OX NCBI_TaxID=37546 {ECO:0000313|EnsemblMetazoa:GMOY009981-PA, ECO:0000313|Proteomes:UP000092444};
RN [1] {ECO:0000313|Proteomes:UP000092444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yale {ECO:0000313|Proteomes:UP000092444};
RA Lawson D.;
RT "Genome Sequence of the Tsetse Fly (Glossina morsitans): Vector of African
RT Trypanosomiasis.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Yale {ECO:0000313|Proteomes:UP000092444};
RG International Glossina Genome Initiative W.H.O.;
RA Lawson D.;
RT "Genome Sequence of the Tsetse Fly (Glossina morsitans): Vector of African
RT Trypanosomiasis.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblMetazoa:GMOY009981-PA}
RP IDENTIFICATION.
RC STRAIN=Yale {ECO:0000313|EnsemblMetazoa:GMOY009981-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
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DR EMBL; CCAG010015406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 37546.A0A1B0G9J4; -.
DR EnsemblMetazoa; GMOY009981-RA; GMOY009981-PA; GMOY009981.
DR VEuPathDB; VectorBase:GMOY009981; -.
DR PhylomeDB; A0A1B0G9J4; -.
DR Proteomes; UP000092444; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:InterPro.
DR GO; GO:0043484; P:regulation of RNA splicing; IEA:InterPro.
DR Gene3D; 3.40.1800.20; -; 1.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 7.
DR InterPro; IPR000467; G_patch_dom.
DR InterPro; IPR032922; SON.
DR InterPro; IPR012934; Znf_AD.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR46528; PROTEIN SON; 1.
DR PANTHER; PTHR46528:SF1; PROTEIN SON; 1.
DR Pfam; PF01585; G-patch; 1.
DR Pfam; PF07776; zf-AD; 1.
DR Pfam; PF00096; zf-C2H2; 2.
DR Pfam; PF13912; zf-C2H2_6; 3.
DR SMART; SM00443; G_patch; 1.
DR SMART; SM00868; zf-AD; 1.
DR SMART; SM00355; ZnF_C2H2; 11.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 6.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR PROSITE; PS50174; G_PATCH; 1.
DR PROSITE; PS51915; ZAD; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE 4: Predicted;
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU01263};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01263};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 755..801
FT /note="G-patch"
FT /evidence="ECO:0000259|PROSITE:PS50174"
FT DOMAIN 841..922
FT /note="ZAD"
FT /evidence="ECO:0000259|PROSITE:PS51915"
FT DOMAIN 1156..1180
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1184..1211
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1212..1239
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1241..1269
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1303..1331
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1354..1381
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1383..1410
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 1411..1438
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 39..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 122..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..106
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..186
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..393
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..409
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 843
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 846
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 895
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
FT BINDING 898
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01263"
SQ SEQUENCE 1473 AA; 169572 MW; D5440B4153A788F9 CRC64;
MANEMDPTDQ VVKFKEERSD PEIERRIQLL TAASTTAIIK EEPLDSNNGI VKVNKNINDN
DRVNNANSDV DESVDDDDDD DVSQDTQTSS EKHQNEDDDK KSVEPVKSSN EILTELFKVF
NVAPPDELLD DKNLINKVKK HKKDKKKKHK KNKSADEQSD SESGISKGKR KHKKKKKHKH
KHKDGDKVKE KGKGKDKEKG KTKDVHRDST EKKKSREGDK CKEEDRPKHK EVSKHLPLNK
NSKDCKTSSD HKRRRDKSEN ANNAKKKRSE VFNDFYKDFR EKDSQRGKKH SSRGRELKIK
KENLERVTSD SSKSEGEISD TTLSDEETYL REREPVRETS SPHHSKNRSH NSFYAGLKRT
RSRDRVDDRD RDCARSRDKY RDRGRERSKY SSNSRRYSRR SRSRSRTRSR SRYHDLGIDK
KRLLEIARKN AISMFKRGNL PGCDNMTQEV KDKVLLKMRY GGRTVEDLTE FCKKISNGEH
LSDLSSDEDS DVDKSGNAKA FHHPFQIKER EPIVMHIRNC KPIVPVVVKT DDQTKAITMQ
FPVSSGQQHR LTESWILVEA KDKGASLSAL STSNPAANIF KNSMPKNVLG KSLPAEEEQE
PAFKSVPPTA ATAAESATSA DVNVIKTEDA LTEPINGVAT ASVETPRVDF VPDVPIPSST
DTVFTQNEGP PLDVSSIISK RLNAMRRLQE NPMDSEALKM MYSSQREMTS WASSKHLPGQ
FTGSTGANIL KPSELNSGPQ VWARRDQLTS SKPVTGGVGM QLLQKMGWKP GEGLGRDKNG
ALQPLLLDVK LDKRGLVAQD DCNGFASRKL NPPKKRPVSG KAQAQLNIQD RHPRRKAKTM
ETCRTCAKCD FDNESQWMDL FNPQYRQTEI ESIRIEFNIW KLKISPNDGL PQKICHDCFN
KFLTISSFRL QCSEAQIKLN NIFDKIDNQS IKDVENFDNF TTEQENENNN EGTVKGTAVE
AKNTISANVK VSKKTIKNYT TRTAVIKTHN QNSSEIINNN NNNSNSNNNI IIPTIVVNNA
NNRKSIHCDD TNMMSDNGII EELHDVVKSV NWNTNESENY PNNVNFNNEK KKSSFSHYNE
NDLTNDNISI TFECKYCYKS RHRPIEMFQT QRDLLTHITV YHNSENPYNC PFCEMGFQDA
ASRTMHLKDQ HCQKMFTCET CGKKYADRFN LRNHIEKYHT EIDYDCTLCQ KSFLSRKSLN
YHMKWHKPEY QLKCAYCERL FINQRHLKCH EETHTGLRNQ EVCSFCGKCF IHLKTLRWHI
YRQHDGEKPY KCGNCSEVFA SYAKKRLHML DYHLDNLTVL EKTECMLCHK RYENEIDLKK
HMLEDHNEEK CSIKITNNKR VIMNKKQKQF TGLFQCEVCD KRFNMKSALE RHQAVHSIEG
RPHACPQCPK RFKRSQDMNW HLKTHSEEKP NICDVCGKGF ALKYVLTQHR RSHEGHMSKM
HDAEDVAATA NINFNTNYEK ELPLDDLVNF VIT
//
