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Database: UniProt
Entry: A0A3Q3LLY8_9TELE
LinkDB: A0A3Q3LLY8_9TELE
Original site: A0A3Q3LLY8_9TELE 
ID   A0A3Q3LLY8_9TELE        Unreviewed;      1460 AA.
AC   A0A3Q3LLY8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Zinc finger protein 536 {ECO:0000313|Ensembl:ENSMAMP00000014217.1};
GN   Name=ZNF536 {ECO:0000313|Ensembl:ENSMAMP00000014217.1};
OS   Mastacembelus armatus (zig-zag eel).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Anabantaria; Synbranchiformes; Mastacembelidae; Mastacembelus.
OX   NCBI_TaxID=205130 {ECO:0000313|Ensembl:ENSMAMP00000014217.1, ECO:0000313|Proteomes:UP000261640};
RN   [1] {ECO:0000313|Ensembl:ENSMAMP00000014217.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC       family. {ECO:0000256|ARBA:ARBA00006991}.
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DR   Ensembl; ENSMAMT00000014604.2; ENSMAMP00000014217.1; ENSMAMG00000009628.2.
DR   GeneTree; ENSGT00940000156397; -.
DR   Proteomes; UP000261640; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 7.
DR   InterPro; IPR036236; Znf_C2H2_sf.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR45925; ZINC FINGER PROTEIN; 1.
DR   PANTHER; PTHR45925:SF2; ZINC FINGER PROTEIN 536; 1.
DR   Pfam; PF00096; zf-C2H2; 5.
DR   Pfam; PF16606; zf-C2H2_assoc; 1.
DR   Pfam; PF13909; zf-H2C2_5; 1.
DR   SMART; SM00355; ZnF_C2H2; 10.
DR   SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 4.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 6.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 8.
PE   3: Inferred from homology;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000261640};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          136..163
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          164..186
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          289..317
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          361..388
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          389..416
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          671..698
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          793..820
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   DOMAIN          821..848
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
FT   REGION          561..580
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          596..653
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          705..793
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          842..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          907..954
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          991..1046
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1107..1159
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1209..1328
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1435..1460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..622
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        628..642
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        718..762
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        915..931
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        932..954
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1009..1034
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1117..1131
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1260..1281
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1282..1306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1307..1328
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1460 AA;  158970 MW;  A127AFD9CAA01425 CRC64;
     MEDSSLCLGV SSAVPDADTH LSSAVLNGRY PISQKLHQLT AQLGHAFPDL HRPQQIPEEK
     AATPLDEKTH HTALASQPIS SQMALLANQL NRDIDAGALS GLNGRVDLQQ FLNGQNLGIM
     SQMNDIEDDA RKNRKYPCPL CGKRFRFNSI LSLHMRTHTG EKPFKCPYCD HRAAQKGNLK
     IHLRTHKLGN LGKGRGRVRE ENRLLHELEE RAILRDKQMR GSGSLLQTAQ TPHLGINSSS
     NTHQQQLGSA CGLLPHSGLS TPDTITQPSS SPKPAGIQDE QALNPTTGFR CTFCKGKFKK
     REELDRHIRI LHKPYKCTLC EFAASHEEEL ISHVEKAHIT AETTQGTGAG GGTGMQMATE
     FRCDVCGQVF SQAWFLKGHM RKHKDSFEHC CQICGRRFKE PWFLKNHMKV HLNKLAIKSK
     PPQSSEQDMA AINSMSNLAQ EAHANLYSRY ISCLQGGFLS PDKQGLSEQH QMLAKAGIAM
     KEKEMLGKLL GPMAGGIGHG LGENEKRSLL GCLNLVPPLK SSCMERLQAA AKVAEMDSLN
     SYQAWQIMAR GMTMDRAFMP KEPQQHPHHI PAGQEDEMGG AGALASFSKD KQDYSLISSN
     DSSKQKQLSE ALQGSKASSG TMISMKEDGR GFDSHRDLMS HHGSAEGPGA LAGLGSPNID
     YSLSGLKEKP SECPDCGRVF RTYHQMVVHS RIHGKDRRGI EEALQQQGLD ERRGSASDPE
     SQSISRSTTP GSSNVTEESG AGGGHSQTGS VQDDSPHPSS PSSDVGEDLG KAAGSIQPPL
     SQHRERSLGS SSKDCPYCGK SFRTSHHLKV HLRIHTGEKP YRCPHCDYAG TQSASLKYHL
     ERHHRERQNG STTSGTSSGH TASSDHKEDH GKTTGGIFAR PDVLRNVFKG MPSNLDFRAG
     QLLPHQWTSA GMMSPQDRDR ERGDRRFESA SSAENMKTAD VPSSLVSTST HSPASFSDLS
     RAYQSMMGNG VHFQGSLQAF MDSFVLSSMK KDMKDNQSPA QLPAQHYHDN GEPKAKRAIS
     ADQDREDKAD AKQNSEPVKP GSQYEPLDLS VSVRPESASG SLPGSSVTIH DNVAWHGCLF
     CSFSTSSLEL MALHLQANHL GKAQLQRSDA GKELHGEASP TTSTIHSSNA KISGVAIDKG
     GDRDGEKSQG GWNNHMDQPY NPFQSDFYRR FGDLYDGSSR TNQSLQGYLG PTEQSLDPSS
     QAFVGATSVG DDQIGESGSC GDAEEDQVGS DEEVVKAGVH SASETPSATP KRQQQPNNSD
     EEEEEAGVAE EEEERDVDGQ MDMEREEEGS PASERLLNHP KHLQDDSSMP TRSGAGLTTS
     SAMTPLSLVP RPQNQALPLE KQWQQGLSLL SPGGPQGLLK AEQQTHLEQQ MNMLSVLRAY
     SNDNLPTFNG LGSGAGGSST GGMKRPDVPV HLWVGEEDQP MTHDPALIHD TNHLNRDLNH
     PNNHNLGDPE GLDAHAVNKD
//
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