GenomeNet

Database: UniProt
Entry: A0A176VUL8_MARPO
LinkDB: A0A176VUL8_MARPO
Original site: A0A176VUL8_MARPO 
ID   A0A176VUL8_MARPO        Unreviewed;       939 AA.
AC   A0A176VUL8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   03-MAY-2023, entry version 24.
DE   RecName: Full=BHLH domain-containing protein {ECO:0000259|PROSITE:PS50888};
GN   ORFNames=AXG93_1615s1540 {ECO:0000313|EMBL:OAE24500.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE24500.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE24500.1, ECO:0000313|Proteomes:UP000077202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Tak-1 and cv. Tak-2 {ECO:0000313|Proteomes:UP000077202};
RC   TISSUE=Whole gametophyte {ECO:0000313|EMBL:OAE24500.1};
RA   Honkanen S., Jones V.A., Morieri G., Champion C., Hetherington A.J.,
RA   Kelly S., Saint-Marcoux D., Proust H., Prescott H., Dolan L.;
RT   "Mechanisms controlling the formation of the plant cell surface in tip-
RT   growing cells are functionally conserved among land plants.";
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:OAE24500.1}.
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DR   EMBL; LVLJ01002594; OAE24500.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176VUL8; -.
DR   OrthoDB; 413453at2759; -.
DR   Proteomes; UP000077202; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   CDD; cd11445; bHLH_AtPIF_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   InterPro; IPR047265; PIF1-like_bHLH.
DR   InterPro; IPR044273; PIF3-like.
DR   PANTHER; PTHR46807; TRANSCRIPTION FACTOR PIF3; 1.
DR   PANTHER; PTHR46807:SF1; TRANSCRIPTION FACTOR PIF3; 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   Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015}.
FT   DOMAIN          713..762
FT                   /note="BHLH"
FT                   /evidence="ECO:0000259|PROSITE:PS50888"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          270..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          417..453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..726
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          904..939
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        507..540
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..583
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..649
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        651..668
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        669..684
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        711..726
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        904..928
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   939 AA;  101794 MW;  C39A4FF137E7035C CRC64;
     MKRAAGVREE KRVDGRKEGR KEGKWGGAMR EARSTRMWSS KDIILLDVAE DDQESNSSGC
     WRRDEGEEWR YVCLLDKLVL LVGHKLGFPS ARGTVSVGVR RASFPAQGTG FRIGNGLNTG
     RILSGCHYIP IRGEFSVGSL SRDRRAGDSY LLSVCVWSVY LSRNLPIPFP SLRNEEALKT
     MSHLVPDWDG NGGDLEAVLP TSDFSLPVKG KWDSLPHKRS HLSGLAFVPT HDAGETEWAE
     ESHIVAMQNQ SGKGNKAMWQ QMNFQNGWSS VPESEDAVTP VKPISSSSPG KEPVLVNEPA
     VDTHHSSALN MQEDEMVCWL QYPLDEHLER DYCSEFFGEL PNSNISNMQL MKDSFAGQNQ
     VAGRNNRNPG PVNVGSNSRM SSADAAMAMG AGRAAGLLPQ TGVEVFTKVR TTLQPYGGKW
     SPNQNNAGKT LGAMTSTLAP SPSRSPPMSG NLSTPMLPPK SQGLSFQPPR TSGPMNFSHF
     SRPAAVMKAN LQCLGMSHVA PPHGSGTNVR LKSQPYSGKP PVDASTSTGS SIAESTTTRQ
     RSGAFRKDTE CQVEGSEAQQ SLGTESSWPS MQNSLSGKDT DAVNSSVDGV DCDSKPGIAD
     VDNCRNSSIT GSGGLGTEKH QSQGAEVQEA PEPTITSSSG GSGNSADRGK EAASSGKRRT
     REGEESECQS EVSNLLQPQG SQVGAVAHRQ DGEDEMAQQK KPQQRGSTTK RSRAAEVHNL
     SERRRRDRIN EKMKALQELI PNSNKTDKAS MLDEAIEYLK MLQLQLQMMS MRSGMSIPSM
     VMPAGMQHLQ IPQLPQMGPM PPMGMGMGMG MGMGPMGMGM SMMDMGGGAP GRPMIPLPSH
     SGPSHSHNVS ATSPAVSMVD THDHRLQNPS VMESLNVFMA QHRQMQMAPQ PMSMDAFSAF
     MIHQHQQQHQ QQHQQHQLQH QHQHSLHHLP SSMGGGAPQ
//
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