PRH_PETCR
ID PRH_PETCR Reviewed; 1088 AA.
AC P48786;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Pathogenesis-related homeodomain protein;
DE Short=PRHP;
GN Name=PRH;
OS Petroselinum crispum (Parsley) (Petroselinum hortense).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; campanulids; Apiales; Apiaceae; Apioideae; apioid superclade;
OC Apieae; Petroselinum.
OX NCBI_TaxID=4043;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=7913642; DOI=10.2307/3869873;
RA Korfhage U., Trezzini G.F., Meier I., Hahlbrock K., Somssich I.E.;
RT "Plant homeodomain protein involved in transcriptional regulation of a
RT pathogen defense-related gene.";
RL Plant Cell 6:695-708(1994).
CC -!- FUNCTION: Specifically binds to the fungal elicitor-responsive DNA
CC element, 5'-CTAATTGTTTA-3', of the gene PR2 promoter.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- INDUCTION: By pathogen infection.
CC -!- SIMILARITY: Belongs to the PHD-associated homeobox family.
CC {ECO:0000305}.
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DR EMBL; L21975; AAA62237.1; -; mRNA.
DR PIR; T14917; T14917.
DR AlphaFoldDB; P48786; -.
DR SMR; P48786; -.
DR PRIDE; P48786; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR CDD; cd00086; homeodomain; 1.
DR CDD; cd15504; PHD_PRHA_like; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR017956; AT_hook_DNA-bd_motif.
DR InterPro; IPR000637; HMGI/Y_DNA-bd_CS.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR045876; PRHA-like_PHD-finger.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF02178; AT_hook; 4.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF00628; PHD; 1.
DR PRINTS; PR00929; ATHOOK.
DR SMART; SM00384; AT_hook; 4.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS00354; HMGI_Y; 2.
DR PROSITE; PS00027; HOMEOBOX_1; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS01359; ZF_PHD_1; 1.
DR PROSITE; PS50016; ZF_PHD_2; 1.
PE 2: Evidence at transcript level;
KW DNA-binding; Homeobox; Metal-binding; Nucleus; Plant defense; Repeat;
KW Transcription; Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1088
FT /note="Pathogenesis-related homeodomain protein"
FT /id="PRO_0000049265"
FT REPEAT 140..152
FT /note="1-1"
FT REPEAT 173..199
FT /note="2-1"
FT REPEAT 205..239
FT /note="3-1"
FT REPEAT 240..274
FT /note="3-2"
FT REPEAT 283..295
FT /note="1-2"
FT REPEAT 316..342
FT /note="2-2"
FT REPEAT 348..382
FT /note="3-3"
FT REPEAT 383..417
FT /note="3-4"
FT REPEAT 678..693
FT /note="4-1"
FT REPEAT 729..744
FT /note="4-2"
FT DNA_BIND 226..236
FT /note="A.T hook 1"
FT DNA_BIND 261..271
FT /note="A.T hook 2"
FT DNA_BIND 369..379
FT /note="A.T hook 3"
FT DNA_BIND 404..414
FT /note="A.T hook 4"
FT ZN_FING 578..635
FT /note="PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00146"
FT DNA_BIND 935..994
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 140..295
FT /note="2 X 13 AA repeats"
FT REGION 173..342
FT /note="2 X 27 AA approximate repeats"
FT REGION 205..274
FT /note="2 X 35 AA approximate tandem repeats (type C)"
FT REGION 220..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 348..417
FT /note="2 X 35 AA approximate tandem repeats (type C)"
FT REGION 363..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 667..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..744
FT /note="2 X 16 AA Asp/Glu-rich (acidic) repeats"
FT REGION 851..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..262
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..405
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 679..693
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..764
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 851..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 877..901
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1088 AA; 121014 MW; CD4AAA50D2F21201 CRC64;
MEEISDPKPN ALEQVLPTVP NGKCTAPVQM ESLAVDVQKV SGEAKVRICS CWCEIVRSPE
DLTKLVPCND FAEDIKLFDS DPMQQEAESS IGIPLIPKQV TMSHNHDHES GSEMVSNEVM
QENHVIATEN TYQKSDFDRI NMGQKETMPE EVIHKSFLES STSSIDILLN NHNSYQSGLP
PENAVTDCKQ VQLGHRSDDA IKNSGLVELV IGQKNVAKSP SQLVETGKRG RGRPRKVQTG
LEQLVIGQKT AAKSSSQLGD TGKRSRGRPR KVQNSPTSFL ENINMEQKET IPEQVTQNSI
LESLTIPTDN QSRTYNSDQS ELPPENAAKN CNHAQFGHQS DDTTKISGFK ELVIGQETVA
KSPSQLVDAG KRGRGRPRKV QTGLEQLVPV QETAAKSSSQ LGDTGKRSRG RPRKVQDSPT
SLGGNVKVVP EKGKDSQELS VNSSRSLRSR SQEKSIEPDV NNIVADEGAD REKPRKKRKK
RMEENRVDEF CRIRTHLRYL LHRIKYEKNF LDAYSGEGWK GQSLDKIKPE KELKRAKAEI
FGRKLKIRDL FQRLDLARSE GRLPEILFDS RGEIDSEDIF CAKCGSKDVT LSNDIILCDG
ACDRGFHQFC LDPPLLKEYI PPDDEGWLCP GCECKIDCIK LLNDSQETNI LLGDSWEKVF
AEEAAAAASG KNLDDNSGLP SDDSEDDDYD PGGPDLDEKV QGDDSSTDES DYQSESDDMQ
VIRQKNSRGL PSDDSEDDEY DPSGLVTDQM YKDSSCSDFT SDSEDFTGVF DDYKDTGKAQ
GPLASTPDHV RNNEEGCGHP EQGDTAPLYP RRQVESLDYK KLNDIEFSKM CDILDILSSQ
LDVIICTGNQ EEYGNTSSDS SDEDYMVTSS PDKNNSDKEA TAMERGRESG DLELDQKARE
STHNRRYIKK FAVEGTDSFL SRSCEDSAAP VAGSKSTSKT LHGEHATQRL LQSFKENQYP
QRAVKESLAA ELALSVRQVS NWFNNRRWSF RHSSRIGSDV AKFDSNDTPR QKSIDMSGPS
LKSVLDSATY SEIEKKEQDT ASLGLTEGCD RYMTLNMVAD EGNVHTPCIA ETREEKTEVG
IKPQQNPL
