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Database: UniProt
Entry: A0A3B4A971_9GOBI
LinkDB: A0A3B4A971_9GOBI
Original site: A0A3B4A971_9GOBI 
ID   A0A3B4A971_9GOBI        Unreviewed;      1028 AA.
AC   A0A3B4A971;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Myelin transcription factor 1 domain-containing protein {ECO:0000259|Pfam:PF08474};
OS   Periophthalmus magnuspinnatus.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Gobiaria; Gobiiformes; Gobioidei; Gobiidae; Oxudercinae; Periophthalmus.
OX   NCBI_TaxID=409849 {ECO:0000313|Ensembl:ENSPMGP00000013051.1, ECO:0000313|Proteomes:UP000261520};
RN   [1] {ECO:0000313|Ensembl:ENSPMGP00000013051.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the MYT1 family.
CC       {ECO:0000256|ARBA:ARBA00010194}.
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DR   AlphaFoldDB; A0A3B4A971; -.
DR   STRING; 409849.ENSPMGP00000013051; -.
DR   Ensembl; ENSPMGT00000013928.1; ENSPMGP00000013051.1; ENSPMGG00000010757.1.
DR   Proteomes; UP000261520; Unplaced.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   Gene3D; 4.10.320.30; -; 7.
DR   InterPro; IPR013681; Myelin_TF.
DR   InterPro; IPR002515; Znf_C2H2C.
DR   InterPro; IPR036060; Znf_C2H2C_sf.
DR   PANTHER; PTHR10816:SF15; MYELIN TRANSCRIPTION FACTOR 1-LIKE; 1.
DR   PANTHER; PTHR10816; MYELIN TRANSCRIPTION FACTOR 1-RELATED; 1.
DR   Pfam; PF08474; MYT1; 2.
DR   Pfam; PF01530; zf-C2HC; 7.
DR   SUPFAM; SSF103637; CCHHC domain; 7.
DR   PROSITE; PS51802; ZF_CCHHC; 7.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
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|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU01143}.
FT   DOMAIN          502..555
FT                   /note="Myelin transcription factor 1"
FT                   /evidence="ECO:0000259|Pfam:PF08474"
FT   DOMAIN          555..695
FT                   /note="Myelin transcription factor 1"
FT                   /evidence="ECO:0000259|Pfam:PF08474"
FT   REGION          42..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          205..266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          291..321
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          575..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          900..962
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        42..67
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        85..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..121
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..219
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        224..261
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        578..604
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        610..624
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        629..655
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1028 AA;  114518 MW;  F97DFEEA903DC380 CRC64;
     MSLTLLFISC PTPGCNGTGH ISGRYARHRS VLGCPIARKR RLEEAEAEQE TESERPASKR
     KSHPLKLALD EGFSADSDGS SEAEGELDKE EKVEKDGEER GEREEREEEE DKAEEGETQE
     VTEDVKENGQ TNGKEEEKEE EEEEEQKDEG TNKNVIILFQ MTSPQESVTM ECEPVVAPPA
     VASEEQCPHS AEEVANSLLH LGQVQEPKHN QNNATAPTAI LEPETMETEE EEVPAATEEE
     EKEEEEREEE EREEEEETTE QSLQNEQVRT YKISSWFRSD VDLVWSWSNP GLSENEDGDD
     EDSLSQRSAM TEDEEEETFD MTRGNLGLLE QAIALKAEQV KPLLRAPEIL HTHRPYYTME
     DRPKHLEALR KSYFKSSSRP EKKEVKCPTP GCDGTGHVTG LYPHHRSLSG CPHKDRIPPE
     ILAMHENVLK CPTPGCTGQG HVNSNRNTHR SLSGCPIAAA EKLSKSQDKQ HLPQADLKGS
     NERVLRPMCF VKQLDTATFG AYRHSAPPTT PRANLAKELE KYSKVSFDYA SFDAQVFGKR
     TLAPKILTSE SSPKAAHMAA TAILNLSTRC WEKPENLSTK NQNKDMEIEV DENGTLDLSM
     KKPIKRESPA PSANQASNSG MTSPPLGHAY KHEEWEGPLD YTKPHRQRDE DMDEMEQAAQ
     SYVSSDEDDI MEGLEDRKYP GEVTTPTFKL KFHPKDAKKE LLSCPTPGCD GSGHITGNYA
     SHRSLSGCPL ADKSLRSLMA ANTPELKCPT PGCDGSGHIT GNYASHRSLS GCPRAKKSGI
     KTPTKDNQED SELLKCPVPG CDSLGHISGK YATHRSAYGC PLAARRQKEG LLNGTPFNWK
     AFKSEGPTCP TPGCDGSGHA NGSFLTHRSL SGCPRALFAK KKAKYSAEEY LSSKFRAGDV
     LDNDEDIKQL NKEINDLNES NNEMEADMVN LQTQITSMEK NLKNIEHENK MIEEQNEALF
     MELSGLSRAL IRSLANIRLP HMEPITEQNF DRYVSTLTDM YTNKECFQSP ENKALLETIN
     KAVKGIKV
//
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