ID A0A2U9BPE3_SCOMX Unreviewed; 702 AA.
AC A0A2U9BPE3;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Chromo domain-containing protein {ECO:0000259|PROSITE:PS50013};
GN ORFNames=SMAX5B_011568 {ECO:0000313|EMBL:AWP05232.1};
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:AWP05232.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP05232.1, 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 -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; CP026250; AWP05232.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9BPE3; -.
DR STRING; 52904.ENSSMAP00000034676; -.
DR Proteomes; UP000246464; Chromosome 8.
DR CDD; cd00152; PTX; 1.
DR Gene3D; 2.40.50.40; -; 1.
DR Gene3D; 2.60.120.200; -; 1.
DR InterPro; IPR033773; CBX7_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR001759; Pentraxin-related.
DR PANTHER; PTHR19277:SF94; NEURONAL PENTRAXIN RECEPTOR; 1.
DR PANTHER; PTHR19277; PENTRAXIN; 1.
DR Pfam; PF17218; CBX7_C; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00354; Pentaxin; 1.
DR PRINTS; PR00895; PENTAXIN.
DR SMART; SM00159; PTX; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
DR PROSITE; PS51828; PTX_2; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU01172};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT DOMAIN 1..44
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT REGION 35..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..109
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 240..272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 519..578
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01172"
SQ SEQUENCE 702 AA; 76634 MW; A1D275C6668430F5 CRC64;
MEFLVKWKGW AMKHSTWEPE ENILDDRLLL GFEQKERERE MNGPKKRGPK PKNFVGKARA
PKREPSSKAS GSRQTTPRSS SGRATPSSAA SARLLPSASS STIAPTPKLN SLAATHKLKK
DIHRCHRMSR RPLPRSDPMA STFSNPGGFP SRMHVSPFSE TVRILNRRVK PREVKRGRII
LNLKVIDKPG RGGARNITTG RHNIPSRNRI IGKKGEAPYR PFQPPLKMLG FPMYGKPTGA
RDSHTTSSQY QSPPSPSSSK TQKGQSAKHS APAPSSDAKA VGSASPFLPA SPSSSLEEEE
EEEGEEGALG RLVSSEGGRK NPRQRRARRP LPAALLSVSP GDQSPTPTEP RRVPAEGDPD
WHPEMAPSCK DVVVTDVTTN LVTVTIKEFP SPASAAAPGS RRPASPASPA APAAPKHPSK
NTPGRGKGTW RVEDLDGELE RKIKMLEKER QAMRKETQGQ HEKINQGLDT ANHRVTELEH
MLTEPSFPDG FVLSFPMRTN YMYGLVRKEI TEMYAFTACV WLKAKEGGIG TPFSYSVPGQ
PNELVLLQGV HNPVELLIND KVAQLPLSLP QDEWQHICVS WTLRDGVWKA YQGGKMKGRG
EGLAAWHPIK PGGVLILGQE QDTLGGRFDA SQALVGELSQ FNLWDRVLKP AEVAAVAECS
SPALGNIAPW TDLDVDVYGG ATKESLDPCH AGQQSNPSSP KQ
//