ID A0A163JAX8_ABSGL Unreviewed; 1155 AA.
AC A0A163JAX8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=BHLH domain-containing protein {ECO:0000259|PROSITE:PS50888};
GN Name=ABSGL_03669.1 scaffold 4609 {ECO:0000313|EMBL:SAL98142.1};
OS Absidia glauca (Pin mould).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Cunninghamellaceae; Absidia.
OX NCBI_TaxID=4829 {ECO:0000313|EMBL:SAL98142.1};
RN [1] {ECO:0000313|EMBL:SAL98142.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101.48 {ECO:0000313|EMBL:SAL98142.1};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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DR EMBL; LT552047; SAL98142.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163JAX8; -.
DR STRING; 4829.A0A163JAX8; -.
DR InParanoid; A0A163JAX8; -.
DR OMA; WACITEE; -.
DR OrthoDB; 1369766at2759; -.
DR Proteomes; UP000078561; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR CDD; cd22249; UDM1_RNF168_RNF169-like; 1.
DR Gene3D; 4.10.280.10; Helix-loop-helix DNA-binding domain; 1.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR PANTHER; PTHR47336; TRANSCRIPTION FACTOR HMS1-RELATED; 1.
DR PANTHER; PTHR47336:SF2; TRANSCRIPTION FACTOR HMS1-RELATED; 1.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; HLH, helix-loop-helix DNA-binding domain; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000078561};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT DOMAIN 279..373
FT /note="BHLH"
FT /evidence="ECO:0000259|PROSITE:PS50888"
FT REGION 118..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1054..1074
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 31..60
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 258..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 445..461
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1155 AA; 129080 MW; 31618D19674F4B74 CRC64;
MDTFIHRPDL NMYGNNDDSL FSLSQFDLEL QQQAQAAIQQ QQQQQQQYQL QQQLQQQQQQ
QYTLEQRPIQ DLWQDFDRYL PIDCQPFMMN EPVMNEPSAF NPSMPTLTAT MYDKGPAPFT
PSINSNPSPL YDPAAKPDNA DFSPPVDLNL TPVVLSQWNS TDMIKQEYPS PAEYSDSLSP
PQKSTPLMPS MSSPPQQTSN DTNDQPLVAS TSTSSSQSPP PTSSSMAPNV ADIIARMNWE
MSTLSNLDSN KVPIQRLKSS NDNGLATSPS NTLNGGTKQK KTAHNAIERR YRNNINDRIT
ELKNAVPALL HAKPKDKDRI AAGGGVAGKR GRLDDDDDDI GEDGEEYLDG VAVATKLNKA
TILCKATEYI NHLKRTGNDM KRENDALQNL LAQLPGGHEV LAHYQIQKVQ REEAMQRQMM
MERQLMKQEQ LERKRNTSKR KRAKRRQSNL DDDHDDGSLS SNSGDHPHTP PSDKNRVFMA
LFMAISFFSS SPLTTTAGSD QLNNHHHVSR TAAGQMDAAA SMATSNNSYY SSTPTNNQPG
TLWFSINDAW SILRWVVFVA CLTQLLFPYL KPYLFGHSFR VRRTSRLRHH RLVSVKTAKL
GLNSTKATTL AISPGDAKCM QMHQLLTKRL ITEHGDTTSR LSYKNKVVLF LALVKEMAQF
TLRHVFGFDV ATEGYSGGID GDDYDDDEME QHKLRRWGHV FKWIKLNECE CLGGNSVLSR
ATMLYHSVRM LNLVDSLEEE MDYYNDSDDE QETRQRQLSS MRARAYATAA IQMVMAIPYA
TMAMRAADYL WGIALMDATE EDTWACITEE DDDLETSMME ALSTKEPWIE TLDVVRTQLS
TWTKVSATAT ATPMGLSLSS NAPSLVPTAI LSNLYILDQM ASHLRNLIDG MIHPAGARSD
PLAFFAHISS ALDDDSQRLA GWFALVGITV EALWRHDTER AEQAMLTLVH RVPRAMIVPG
FSKKKTRQGE LDTMAKQQIA HTLAGATLLQ KQDSQEGIKE LEIASSLRQR KNKRALPTTN
ELEAMHIEGR VMALAEFAVL LVGLEAWVST WEQSSDDHTS KASETTSDDA PALETSNEQV
RLAALALRRM VCRPALAGLK TQQVIIDRLS KVGRIMDDGC DDEDDTDSAA CEHLADGNAQ
KDGRIEKVMA IIHGK
//