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Database: UniProt
Entry: A0A3Q3B539_KRYMA
LinkDB: A0A3Q3B539_KRYMA
Original site: A0A3Q3B539_KRYMA 
ID   A0A3Q3B539_KRYMA        Unreviewed;      1189 AA.
AC   A0A3Q3B539;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Myelin transcription factor 1-like {ECO:0000313|Ensembl:ENSKMAP00000024141.1};
OS   Kryptolebias marmoratus (Mangrove killifish) (Rivulus marmoratus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Atherinomorphae; Cyprinodontiformes; Rivulidae; Kryptolebias.
OX   NCBI_TaxID=37003 {ECO:0000313|Ensembl:ENSKMAP00000024141.1, ECO:0000313|Proteomes:UP000264800};
RN   [1] {ECO:0000313|Ensembl:ENSKMAP00000024141.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-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   RefSeq; XP_017265159.1; XM_017409670.1.
DR   RefSeq; XP_017265160.1; XM_017409671.1.
DR   AlphaFoldDB; A0A3Q3B539; -.
DR   Ensembl; ENSKMAT00000024446.1; ENSKMAP00000024141.1; ENSKMAG00000017881.1.
DR   GeneID; 108232093; -.
DR   KEGG; kmr:108232093; -.
DR   GeneTree; ENSGT00940000156364; -.
DR   OrthoDB; 3091993at2759; -.
DR   Proteomes; UP000264800; 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:SF10; MYELIN TRANSCRIPTION FACTOR 1; 1.
DR   PANTHER; PTHR10816; MYELIN TRANSCRIPTION FACTOR 1-RELATED; 1.
DR   Pfam; PF08474; MYT1; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000264800};
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          616..854
FT                   /note="Myelin transcription factor 1"
FT                   /evidence="ECO:0000259|Pfam:PF08474"
FT   REGION          1..54
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          452..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          664..687
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          728..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          1060..1122
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..90
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        155..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        207..226
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..248
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..306
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..321
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..352
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        353..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        385..419
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..484
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        738..765
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        766..798
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..815
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1189 AA;  132931 MW;  1E0A8E2CECFC0DFA CRC64;
     MSQDTETRTR TRSKAVRVTA DQVGQDMKLE LSSCPTPGCD GKGHVSGRYS RHRSALGCPI
     VKKRKLEKAE AEENQCAPKR RNQASKQAEE DSDSAEEEEQ KEDGAEDKDL IKDQKNNKEK
     ILTELITSDS LVTTEDIERL GPLAEDTMNR SINSEMDVKP ERENSNEVKT DDDPHQDQTP
     TKDEDTQPLE EYQPSELPLE ETAVIHQEET NDEDDEEPEE GTEEQEQQER QENFDEEREV
     RRQIMRQENS DHQYSSGDYN LQAKESQEEE EEEEEEEEEE EEVEEQKEEE EEEEQKDEEE
     EEETEVSTPF NMSPTTQEYE ATVSLREEKV RTLVTEEEED EEQEEEKEEE EDVRQEKEVS
     VVVEEEEEDR DSSKTSLSTV VIEVRSEEDD DEEEEEEEEE EEEDEDEEDE DEEEGEELDH
     VSEGSGITDD SENWDMTRGN LGLLEQAIAL KAEEVQGGQD SRSSPDYQPY SSSVKSSEST
     SAARRTSHCS KDKKEVKCPT PGCDGTGHVT GLYPHHRSLS GCPHKDRIPP EILAMHENVL
     KCPTPGCTGQ GHVNSNRNTH RSLSGCPIAA AAKLNKNQDK QVHLQAAATE PSSNSDRVLR
     PMCFVKQLEI PQYGSYRPNT VTTTPRANLA KELEKYSKVS FDYASFDVQV FGKRMIIPKT
     PSTANTSPKA FKSKSFPKAP SPSHCVSGSF PKPTLSSSGY DYSQDAEAAH MAATAILNLS
     TRCWERPETL STQPREPCTK ESDIEVDENG TLDLSMKKTK REDMQSPDPS SSSSSSSQHV
     GAMLSQVHTQ SDWDSPLDFT KSSEVKEEDH EEMEYTAPSY TSSDGEEDDQ ENLEDRKYPG
     EVTTSSFKVK FQPKDSKKDI LVCPTPGCDG SGHITGNYAS HRSLSGCPLA DKSLRTLMAA
     HTAELKCPTP GCDGSGHITG NYASHRSLSG CPRAKKGGVK TTPTKDDKED SELLKCPVPG
     CDSLGHISGK YATHRSAYGC PLAAKRQREG LLNGAPFSWK AFKTEGPTCP TPGCDGSGHA
     NGSFLTHRSL SGCPRASGNK KKAKLPGDEY ITAKFRASDV LDNDEDIKQL NKEINELSES
     NSEMEADMIN LHTQISSMEK NLKNIEEENK QIEKRNEALF LELSGLSQAL IRSLANIRLP
     TMQEPVSEQN FDSYVDTLTH MFTNKDCYQN PENRALLESI NQAVKGIEV
//
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