ID A0A0V1P279_9BILA Unreviewed; 992 AA.
AC A0A0V1P279;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 22-FEB-2023, entry version 26.
DE SubName: Full=Suppressor of hairless protein {ECO:0000313|EMBL:KRZ90298.1};
GN Name=Su(H) {ECO:0000313|EMBL:KRZ90298.1};
GN ORFNames=T08_2922 {ECO:0000313|EMBL:KRZ90298.1};
OS Trichinella sp. T8.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92180 {ECO:0000313|EMBL:KRZ90298.1, ECO:0000313|Proteomes:UP000054924};
RN [1] {ECO:0000313|EMBL:KRZ90298.1, ECO:0000313|Proteomes:UP000054924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS272 {ECO:0000313|EMBL:KRZ90298.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the Su(H) family.
CC {ECO:0000256|ARBA:ARBA00009704}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ90298.1}.
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DR EMBL; JYDM01000058; KRZ90298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1P279; -.
DR STRING; 92180.A0A0V1P279; -.
DR Proteomes; UP000054924; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:InterPro.
DR Gene3D; 2.80.10.50; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.60.40.1450; LAG1, DNA binding domain; 1.
DR InterPro; IPR015350; Beta-trefoil_DNA-bd_dom.
DR InterPro; IPR036358; BTD_sf.
DR InterPro; IPR040159; CLS_fam.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR008967; p53-like_TF_DNA-bd_sf.
DR InterPro; IPR015351; RBP-J/Cbf11/Cbf12_DNA-bd.
DR InterPro; IPR037095; RBP-J/Cbf11_DNA-bd_sf.
DR InterPro; IPR038007; RBP-Jkappa_IPT.
DR PANTHER; PTHR10665; RECOMBINING BINDING PROTEIN SUPPRESSOR OF HAIRLESS; 1.
DR PANTHER; PTHR10665:SF0; SUPPRESSOR OF HAIRLESS PROTEIN; 1.
DR Pfam; PF09270; BTD; 1.
DR Pfam; PF09271; LAG1-DNAbind; 1.
DR Pfam; PF20144; TIG_SUH; 1.
DR SMART; SM01268; BTD; 1.
DR SMART; SM01267; LAG1_DNAbind; 1.
DR SUPFAM; SSF110217; DNA-binding protein LAG-1 (CSL); 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF49417; p53-like transcription factors; 2.
PE 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054924};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 509..696
FT /note="RBP-J/Cbf11/Cbf12 DNA binding"
FT /evidence="ECO:0000259|SMART:SM01267"
FT DOMAIN 700..848
FT /note="Beta-trefoil DNA-binding"
FT /evidence="ECO:0000259|SMART:SM01268"
FT REGION 190..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 562..584
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..261
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 992 AA; 109336 MW; 7D9BF4AE34665851 CRC64;
MLCSPSGMQV AQAHEMHTTK ADLIKNLHFM NCTIRIDVPT QPALSRPDLL FSPFLWPNSV
LVNSGSGIVA GGQPFHGSTA SGLSSTVFSE PSSSSATLNA SVSTASSLLK VAISTLPYLL
PVQAAGPLLN STAAAYTLAS AYLATNAHWL NVLERSQREA MVMLSPMDPP SRHSSPQSVE
QQLPIQTFPV TTIANQQSAN PATVAGSRKR RRSKEPKSDA SPVNTAAAAA AASSSSLASG
EEEDEEEDEE EEEDVDDYDD DGDELLNRRQ DRPASGLLLS NYDAAAPHPA SADTHPLMAA
FMHSQQQHHY LQNQHYHSVN VLDSLSSFNV KQRRIAAESS KMPGDSKGNP SGGAQMNNHH
HCRHGQQQRR HNGALSLDNF SSSFQSFDVG FWNCPNSGGD GGGTYADRSQ PLCASYYYYY
PNIPNRPVEF GGDVRSEPIE ISPAVATVQP FLSSSMVKND DHNNSLNRLP IGTTAATTLP
FPRSQLVTGV QSLTKEAMLR YLQDDTQCIL TIFHAKVAQK SYGSEKRFFC PPPCVYLFGS
GWKQKKRQVS FLYRQMMQVR RVNSSSAVEE DPPLSVKANE EEDSPLLERS AGNLQQLYDT
DPTNCSTMND ASAGDLVACI GIDQSEQEKQ PLDFSCGKNY CSAKTLFISD TDKRKYFELH
VQLAYACGHE LGVFSSQRIK VISKPSKKKQ SMKNTDCKYL CIASGTKVAL FNRLRSQTIS
TRYLHVENGN FQASSVQWGA FTIHLLEDGA AESEEFDVRD GFIHYGSTVK LVDSVSGIAL
PRLIIRKVEK QVALLDSDEP VSQLHKCAFF MKGTDFMYLC LSQERIIQYR AQPDSNPKRH
VITDGAAWTI ISTEKAEYRF YEAMGPVRCP VSPVPTVRDL SVNCMSQLTL SGSHFTPALK
VWFAEVEAET IFHNSEVLIC TIPDIDEFHL TASPWEKHVV PLSLVRFDGV IYHTGVTFTY
TRKKDEKTTK SESNSAANFV IQAENKCEMA RL
//
