GenomeNet

Database: UniProt
Entry: A0A176WAB8_MARPO
LinkDB: A0A176WAB8_MARPO
Original site: A0A176WAB8_MARPO 
ID   A0A176WAB8_MARPO        Unreviewed;       946 AA.
AC   A0A176WAB8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   22-FEB-2023, entry version 25.
DE   RecName: Full=Homeobox domain-containing protein {ECO:0000259|PROSITE:PS50071};
GN   ORFNames=AXG93_4486s1020 {ECO:0000313|EMBL:OAE29531.1};
OS   Marchantia polymorpha subsp. ruderalis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Marchantiophyta;
OC   Marchantiopsida; Marchantiidae; Marchantiales; Marchantiaceae; Marchantia.
OX   NCBI_TaxID=1480154 {ECO:0000313|EMBL:OAE29531.1, ECO:0000313|Proteomes:UP000077202};
RN   [1] {ECO:0000313|EMBL:OAE29531.1, 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:OAE29531.1};
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}.
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:OAE29531.1}.
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DR   EMBL; LVLJ01001453; OAE29531.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A176WAB8; -.
DR   OrthoDB; 468484at2759; -.
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:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR   CDD; cd00086; homeodomain; 2.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017970; Homeobox_CS.
DR   InterPro; IPR001356; Homeobox_dom.
DR   InterPro; IPR008422; Homeobox_KN_domain.
DR   PANTHER; PTHR11850:SF102; HOMEOBOX DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11850; HOMEOBOX PROTEIN TRANSCRIPTION FACTORS; 1.
DR   Pfam; PF05920; Homeobox_KN; 2.
DR   SMART; SM00389; HOX; 2.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   PROSITE; PS00027; HOMEOBOX_1; 1.
DR   PROSITE; PS50071; HOMEOBOX_2; 2.
PE   4: Predicted;
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PROSITE-
KW   ProRule:PRU00108};
KW   Homeobox {ECO:0000256|ARBA:ARBA00023155, ECO:0000256|PROSITE-
KW   ProRule:PRU00108};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PROSITE-
KW   ProRule:PRU00108}; Reference proteome {ECO:0000313|Proteomes:UP000077202}.
FT   DOMAIN          837..872
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000259|PROSITE:PS50071"
FT   DOMAIN          873..936
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000259|PROSITE:PS50071"
FT   DNA_BIND        839..873
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT   DNA_BIND        875..937
FT                   /note="Homeobox"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00108"
FT   REGION          10..34
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          799..824
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          866..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        16..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        801..819
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        866..880
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   946 AA;  105046 MW;  3E429EB77DBC0CE3 CRC64;
     MGEFLDWVDS LFSDPSEQAD GRTSGTNDGD KSMQIGARAH VLVVSSSEEC RPDGASGDQV
     DRGNADVVAG HNSFEDGQLY APRTPGGFIM DSFSGEMEPT NSITSSPFLE APTTFVSLRQ
     ARTSNGYATS ESLASAYGFM SDYCCPTEAM QSTPYVQIGD YCRTVVPPPF TGADATFYSG
     DHRQLWLDPS TSESSEFINS ATTSSGFGTQ QPIEFDCSTL DSSWLMESET TYGFVPPYQA
     QVRCNNLQSS AFAYDCNTVE VSHIMRMATT GEYSSDHQNA DDCTTIKSAK HTTEATTYTD
     NHELHSPTVD ELWTYLSTFG MCVPEDQPRD EFSQSGNVAL ADHMDFGHHL NAPPKITPQS
     PVCFDYRDTG QKSVHPEVWG STSHVDSRIV TAFHHQELGH RQEAPTIACP LQQEVLDDHI
     AQESVYCNAS TSNDEASTFV FDIDYMAYGH GLEEPTTTCT SQREGLVAFT AEESVGIKTS
     GVILNMDTRL VSDNQHLEFD QQFEAPTTCK PQPGMLLDSS AGDDASNLER RFASDSEHME
     FSHRLKAPSM CTPQAQAILD NTAQKASHAE DMQQVIEVPL CQRDTHHEFE QGNHWVVGQQ
     YLLQVLSSLG HASSTNVKLL VEDVFNQIFP FDKASNDSMD YEARHSQEVL SPVPYPQTYV
     EEVLATLACC SQRPELPLVP SGDNDNLNAV RGCEAEDPQE VCVSASSPPG CVEEVLDKDM
     DMDSSSDQLA WAPVPSPDDE IVTEMRACEP CNRGEEFASA PISQGSMREV LESNHPTCSQ
     QLEFTPRPAP VDDHVKATNS ILDTNDDSST GSLTSSRRKE LEGTGSRTWW EKNELIPYPS
     QREVYEMSRR TNLTLQQISD WFKNERSRKW RDDPRKKKAN RLPPRATRLL STWASEHLSH
     PNPSREQRED LAKESGVTYV QVSNWFMNFR KRSKARIRKA KASNIP
//
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