ID A0A2U9BXQ7_SCOMX Unreviewed; 1187 AA.
AC A0A2U9BXQ7;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 22-FEB-2023, entry version 17.
DE SubName: Full=Putative myelin transcription factor 1-like {ECO:0000313|EMBL:AWP09095.1};
GN ORFNames=SMAX5B_015285 {ECO:0000313|EMBL:AWP09095.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP09095.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP09095.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
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 EMBL; CP026253; AWP09095.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BXQ7; -.
DR STRING; 52904.ENSSMAP00000001629; -.
DR Proteomes; UP000246464; Chromosome 11.
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; -; 6.
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; 6.
DR SUPFAM; SSF103637; CCHHC domain; 6.
DR PROSITE; PS51802; ZF_CCHHC; 6.
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:UP000246464};
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 649..897
FT /note="Myelin transcription factor 1"
FT /evidence="ECO:0000259|Pfam:PF08474"
FT REGION 62..230
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 607..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..719
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 765..826
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 846..867
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1058..1120
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 62..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..147
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..162
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..186
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..271
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..287
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 698..719
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 765..787
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..826
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1187 AA; 131532 MW; 9F9458CDB3EAEF16 CRC64;
MSIEGDDKRT RTRSKGIRVP IELVGQELSC PTPGCNGSGH ISGRYSRHRS ILGCPIARKR
RLEEAEAEQE QEETERPASK RKSHPLKLTL DEGFSAESDA SSEAEGEGEK DGENAGDAKE
EEEQEQEQEQ EEDREAVADE EGEGMTEDLM QESQTNGQEV EMQSQQKEEE GRTKEEDTHQ
KEENSVIADE EEECVIIEPE LRAAPPASEE SQSPSPSGEV AGNSFFHAGR VSDNTAPTVA
IQLPVAMETE VTVAAKWGED VKDKPEGDMK VKDEEEEEEE EGEEEEEMAV PAQHRQDTLA
LLEEDEERDE EDLRNHVLPL PDVPTVIRTI TSTAAAQGTH ITAEDHRAGP LEAYSLHRAS
PLDKCDSHGP SPLHSYKASP PLSYSSHRAS PLEDYFPNPR VENYKIHKAS SSASPDIIEV
RSDKSEEKDF EDVDGDDERD DEDSLSQRST VTDESEMFDM TRGNLGLLEQ AIALKAEQVR
PAGPRELLRA PDIHHQRYFT MEDRPKHLDI IRKSYFSKES SKPEKREIKC PTPGCDGTGH
VTGLYPHHRS LSGCPHKDRI PPEILAMHEN VLKCPTPGCT GQGHVNSNRN THRSLSGCPI
AAAEKLTKGH DKQHLSQPGS EHLKGSPNDR VLRPMCFVKQ LEVPAYGSYR PNMAPATPRA
NLAKELEKYS KVTFDYASFD AQVFGKRLLA PKMPTSETSP KAFKTKPSFP KSSSPSLSLH
GYGKSSTLAY DYSQDAEAAH MAATAILNLS TRCWEKPENL STKAQNKEMD IEVDENGTLD
LSMKKPFKRE GSLSATSPGV RSPDPSSSSA SSLHHGGSSG MTSPNLHAYK QEDWEGPLDY
TKPNRQREEE VDEMEHTGQS FVSSDPEDCD MMQECLEDRK YPGEVTTPSF KVKFQPKDSK
KELLSCPTPG CDGSGHITGN YASHRSISGC PRAKKSGIKT PTKDNQEDSE LLKCPVPGCD
SLGHISGKYA THRSAYGCPL AARRQKEGVL NGTPFNWKAF KTEGPTCPTP GCDGSGHANG
SFLTHRSLSG CPRALFAKKK AKFPTEEYLS TKFRASDVLD NDEDIKQLNK EINDLNESNN
EMEADMVNLQ TQISSMEKNL KSIEHENKMI EEQNEALFME LSGLSRALIR SLANIRLPHM
QEPLTEQNFD SYVSTLTDMY TNKDCFQSPE NKALLESINK AVKGIKV
//
