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Database: UniProt
Entry: A0A1J1J3T3_9DIPT
LinkDB: A0A1J1J3T3_9DIPT
Original site: A0A1J1J3T3_9DIPT 
ID   A0A1J1J3T3_9DIPT        Unreviewed;       937 AA.
AC   A0A1J1J3T3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=CLUMA_CG019499, isoform A {ECO:0000313|EMBL:CRL06618.1};
GN   ORFNames=CLUMA_CG019499 {ECO:0000313|EMBL:CRL06618.1};
OS   Clunio marinus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Chironomoidea; Chironomidae;
OC   Clunio.
OX   NCBI_TaxID=568069 {ECO:0000313|EMBL:CRL06618.1, ECO:0000313|Proteomes:UP000183832};
RN   [1] {ECO:0000313|EMBL:CRL06618.1, ECO:0000313|Proteomes:UP000183832}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Syromyatnikov M.Y., Popov V.N.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR   EMBL; CVRI01000067; CRL06618.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J1J3T3; -.
DR   Proteomes; UP000183832; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR   GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0048869; P:cellular developmental process; IEA:InterPro.
DR   CDD; cd19187; PR-SET_PRDM1; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 5.
DR   Gene3D; 2.170.270.10; SET domain; 1.
DR   InterPro; IPR016608; PRDM1.
DR   InterPro; IPR044413; PRDM1_PR-SET.
DR   InterPro; IPR001214; SET_dom.
DR   InterPro; IPR046341; SET_dom_sf.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR16515; PR DOMAIN ZINC FINGER PROTEIN; 1.
DR   PANTHER; PTHR16515:SF26; PR DOMAIN ZINC FINGER PROTEIN 1; 1.
DR   Pfam; PF21549; PRDM2_PR; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   PIRSF; PIRSF013212; PRDM1; 2.
DR   SMART; SM00317; SET; 1.
DR   SMART; SM00355; ZnF_C2H2; 5.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 3.
DR   SUPFAM; SSF82199; SET domain; 1.
DR   PROSITE; PS50280; SET; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 4.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183832};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          63..175
FT                   /note="SET"
FT                   /evidence="ECO:0000259|PROSITE:PS50280"
FT   DOMAIN          726..753
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          754..781
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          782..809
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          810..837
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          231..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          486..550
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          611..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          673..715
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          897..937
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        235..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        320..341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..550
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        673..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        900..931
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   937 AA;  105783 MW;  D6AF17873E5A193C CRC64;
     MTETSLSRGE SPTNSMNQDY DITRMREDDF ERLAVYIVPD VPCERGIPGR AEKTLPRSLT
     LKPSVVLSTP PQPIEGVWST GVIPKGTRFG PFEGHRTPSY PSDKSSWRYF WRIFKDSDFY
     YLDGSDNSHA NWMRFVASAY NMKVMNLVAC QHQEHIYFYT IRDIMPNEEL MVWYCRDFAK
     RMGYDIDPER ATYSICKEET LKKAAYAMPK TKISPEIAYN HMKYVMGLHI PASRRPQSPT
     ASTTTNSPPR HQATHQTVLN LRESHEERDR SPIRIMIHEN GVTRVEETAK PVKEEASPKL
     VVYEHQLTPN DGSVRSDEGY HSNGYHDEFT PPEDSSDSES EHNYVLDCSQ KTIEPKETVV
     VAKANGECVD GKNDYRKVKM KMPLKYEFKN KNMTKDCEAE VADVAMTDVN EEEMTVVQTK
     PATSTVIVLE SAPQNTPTIV PLTKSYYEAE TSSPPPQHHH HHHTSAAFMR YTPPTSSILE
     TILTGNRLDQ DSSRRQPNAT PPPTSPTEMA YSYKKSQRYG NACSPDSSSN PQQPNCTSTS
     NSHPLSPPQI LVPSRNVQQV VENSSNNNQA PTPPTLIYVN QSQFPPYESQ RTSPSYTYSI
     YSNGNLVTAN SNNHSTSSTS STSSYSPPLN NGQYERLTSS TSSGAAMLPF TNGNQLPLSH
     PLLTPLAPLQ HISTSRESPH SPPCSLSPDG ESYSRSGSPL SPGSPGSRGY KSLPYPLKKR
     DGKMHYECNV CCKTFGQLSN LKVHLRTHSG ERPFRCNVCT KSFTQLAHLQ KHHLVHTGEK
     PHQCDICKKR FSSTSNLKTH LRLHSGQKPY ECDLCPQKFT QFVHLKLHKR LHTNDRPYVC
     QGCDKKYISA SGLRTHWKTT SCKPNNLEEE MALAAAATNE YLGDKEHADM ERERELYEYQ
     HQQQQQSPQL HQQTTQNGGE TRPSVIESNQ PMIIECT
//
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