ID A0A176VF77_MARPO Unreviewed; 2073 AA.
AC A0A176VF77;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Homeobox domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AXG93_1923s1410 {ECO:0000313|EMBL:OAE18585.1};
OS Marchantia polymorpha subsp. ruderalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE18585.1, ECO:0000313|Proteomes:UP000077202};
RN [1] {ECO:0000313|EMBL:OAE18585.1, 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:OAE18585.1};
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 ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
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:OAE18585.1}.
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DR EMBL; LVLJ01004028; OAE18585.1; -; Genomic_DNA.
DR OrthoDB; 394285at2759; -.
DR Proteomes; UP000077202; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR CDD; cd00086; homeodomain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR InterPro; IPR007759; Asxl_HARE-HTH.
DR InterPro; IPR018501; DDT_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR044977; RLT1-3.
DR InterPro; IPR028942; WHIM1_dom.
DR InterPro; IPR028941; WHIM2_dom.
DR PANTHER; PTHR36968; HOMEOBOX-DDT DOMAIN PROTEIN RLT2; 1.
DR PANTHER; PTHR36968:SF5; HOMEOBOX-DDT DOMAIN PROTEIN RLT2; 1.
DR Pfam; PF02791; DDT; 1.
DR Pfam; PF05066; HARE-HTH; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF15612; WHIM1; 1.
DR Pfam; PF15613; WSD; 1.
DR SMART; SM00571; DDT; 1.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR PROSITE; PS50827; DDT; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS51913; HTH_HARE; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|PROSITE-ProRule:PRU00108,
KW ECO:0000256|RuleBase:RU000682};
KW Homeobox {ECO:0000256|PROSITE-ProRule:PRU00108,
KW ECO:0000256|RuleBase:RU000682};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000077202};
KW Transcription {ECO:0000256|ARBA:ARBA00023163}.
FT DOMAIN 200..260
FT /note="Homeobox"
FT /evidence="ECO:0000259|PROSITE:PS50071"
FT DOMAIN 821..880
FT /note="DDT"
FT /evidence="ECO:0000259|PROSITE:PS50827"
FT DOMAIN 1005..1074
FT /note="HTH HARE-type"
FT /evidence="ECO:0000259|PROSITE:PS51913"
FT DNA_BIND 202..261
FT /note="Homeobox"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT REGION 125..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 664..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1103..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1467..1515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1744..2073
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1105..1138
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1139..1167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1744..1762
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1779..1795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1815..1834
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1865..1889
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1890..1905
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1924..2073
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2073 AA; 230580 MW; F8DE66F3C707FB4F CRC64;
MEEGTKKKRR KDWRRNFAFF AFLRLLCFAL LWRQRAWRTR EMEDALLTSE ASMEEEGEVK
IARKRQRREK LAFSAGEVVV QWRDKENKME FMMAIGGPGG RPMLERHVVI CRPVRQSVGL
VGPSSCDYGG ARAAERETRG GRGESKARRG GPLGKRGRKD RREAIPNGRR TGGEDYGERK
APSNFVAMDS DGENRLSSPE EKNPKRRMKT PFQLEALERV YAEDRYPTEA VRAELSSQLN
LSDKQLQMWF CHRRLKDRKG KDDEIPGAAG RKKQKTDRPG GGVGASAGGG GGGGGLKAGY
PGAVLEPEMG EAAAVGRNGY NDELDFEEEE HGMGMLRGSA SAQPQHRKVA AQEAEPAPRR
RNQAPVGRVV DPRAAAENAA VSAVEAQLGE PVRENGPILG VEFDPLPPGA FGTPIDHKSE
QRVATAPPRV HSEDRAQERQ ESRPSKAGAF GLPPLPTTGV KRKAVGLSGQ QSFSAQQVPR
TPREFQFLPE QPTAREESQS HQRQIQLNLH PNAERFDLLP APRVRSLSPL GGFLPTNMHS
IPSGDGYGFP QERVQNVGIS LLPPGESRPS GLYAQNGLGL DDPQRRGLYH SFDVEGQMGF
RQTAIQAMAA NQSAVAPTES LALFHEHEQA RLEKKRKSEE LKVAKESEAN VKRMKREMER
QEIVRRKKEE QMRRELEKQD RDKRKEEERA VRERQREEER IQREHRREME RRERMLLKEN
KRIEKQRRKE EVRKAKEAAR LKAASERAAA KKLSKESMDT IDDEQLELME AATAQGLFSV
NGLDDGGAQV MDISKVLLKK FPPASVRMKL PLAIRPWNEL EHCMGHFFMV WRFLTTFADV
IGLWPFTLDE FAQSLHDFDP RLLGEIHIAL IKTMVKNIED AAQAATSGAG GSQNAIALAS
GGHPQLVEAA YEWGFDIKEW GQHVNPLTWP EILRQFALAA GYGPKWRKRN VEAPARPREE
VEEPVEEENA VSILRSGAAA ASAVALMQGK GVGHLRRCRY RLTPGTVKYA AFHVLSLEGS
KGLTILEVAD RIQKSGLRDL TTSKTPEASI AAALSRDTNL FERVAPSTYC VRPAFRKDPE
DAEEVLQAAR ERIRLFQSGF LDVEEAEKEN EEGEEVERDE EYDSDGQDVE DADADADADV
DTPIPKESEL KDESLQAEDA AKSESLAEEE MEIDESQVGE PWVQGLMEGE YAELSVEERL
VALVALINVV NEGNSIRLAL ESRMEAASAL KRQMWAEAQI ERRRHKEEQL LRLQPALLAA
AKNESGEMVD VGSVPVTVTG EKVVEPLVST KQETILELNL VPADSNMVSD GPGSVEHNPS
VAEKSITVQE KNGSMHEKNA PHEGSVTQEA VASGHVTERS RAQVKADIGV WAEELYVVRS
LPLGTDRRRN RYWQFVTCRG GQDPSCGRIF FESFSDGLWE VIDTEEALDA LMSSLDIRGT
REAALHAVLV RLESTLRPAM RLAAASSSSS VSHHDVKSEL GEAGKPTDSA GRGGASGASY
GTAVDGSPSS GLGVEIPARS GSISVDLGKT DAEKQRAFDR FKDFEHWTWT ENTRSLSALK
VAKTGRKREP DLLLCCSKCH ELYSAIDKHC QFCHATFPKT QTKHDFHARE CEDKMKKKDP
AWKLCGLSSV PPRIQILKAD ILYIETVIPS EAFKDPWDHQ ERKAWASLLK RAMTPSELLQ
CLTELESRIH REWLSSSYET TEELLSASAS SVTIANQVAP WVPQTSAAVA LRVMAFDAAL
SYSSEERKRR QKQEEEERKN LMHTSIGVFP SRTTPEVPVV EKPDVDEDDV VVDVASGRGR
GRGRGRGRGS RGGGRGSRSS RSAPPATTNS RATVKKGASK RKLQFQEEGA AEGKQGGKGG
GRGQGRSRGR PRGRGSGRPR GRGSRGGRRS VAVRRIDKLP KEKNPNELMS QEVVLRKGQV
AEPEDDHEEE EAESEEEDAF RSGEWDGSEE QMEDQQEDAE EEEEEDDEEE DLTGAMQEEE
DEDEDGEEGD EEEVQVEEGD DEGQAEDGDE NGQEEEGDEE DEDRQYDDDS YPQDGEGEDD
EEAVEPETDE DEEEEEVEEA DEGAESARES DED
//
