ID K5WVL5_PHACS Unreviewed; 1433 AA.
AC K5WVL5;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Transcription regulator {ECO:0008006|Google:ProtNLM};
GN ORFNames=PHACADRAFT_258377 {ECO:0000313|EMBL:EKM54497.1};
OS Phanerochaete carnosa (strain HHB-10118-sp) (White-rot fungus) (Peniophora
OS carnosa).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerochaete.
OX NCBI_TaxID=650164 {ECO:0000313|EMBL:EKM54497.1, ECO:0000313|Proteomes:UP000008370};
RN [1] {ECO:0000313|EMBL:EKM54497.1, ECO:0000313|Proteomes:UP000008370}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HHB-10118-sp {ECO:0000313|EMBL:EKM54497.1,
RC ECO:0000313|Proteomes:UP000008370};
RX PubMed=22937793; DOI=10.1186/1471-2164-13-444;
RA Suzuki H., MacDonald J., Syed K., Salamov A., Hori C., Aerts A.,
RA Henrissat B., Wiebenga A., vanKuyk P.A., Barry K., Lindquist E.,
RA LaButti K., Lapidus A., Lucas S., Coutinho P., Gong Y., Samejima M.,
RA Mahadevan R., Abou-Zaid M., de Vries R.P., Igarashi K., Yadav J.S.,
RA Grigoriev I.V., Master E.R.;
RT "Comparative genomics of the white-rot fungi, Phanerochaete carnosa and P.
RT chrysosporium, to elucidate the genetic basis of the distinct wood types
RT they colonize.";
RL BMC Genomics 13:444-444(2012).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH930473; EKM54497.1; -; Genomic_DNA.
DR RefSeq; XP_007397188.1; XM_007397126.1.
DR STRING; 650164.K5WVL5; -.
DR GeneID; 18917097; -.
DR KEGG; pco:PHACADRAFT_258377; -.
DR HOGENOM; CLU_000315_29_2_1; -.
DR InParanoid; K5WVL5; -.
DR OrthoDB; 5482994at2759; -.
DR Proteomes; UP000008370; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd18659; CD2_tandem; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.40.50.40; -; 2.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR025260; CHD1-like_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623:SF14; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 1; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF13907; CHD1-like_C; 1.
DR Pfam; PF00385; Chromo; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00298; CHROMO; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM01176; DUF4208; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50013; CHROMO_2; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000008370};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 189..261
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 288..349
FT /note="Chromo"
FT /evidence="ECO:0000259|PROSITE:PS50013"
FT DOMAIN 390..559
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 687..843
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1231..1301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1387..1433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 20..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..94
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..148
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 945..976
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1231..1259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1261..1281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1393..1433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1433 AA; 162838 MW; 04E00D891E22F621 CRC64;
MMASDHSPVN PTSGSSDESD DHNMQVDSDV DVPKDVDIDA DGEYDDDDEL EDTAQVTHTV
PSSSAYLSKR AVKDEEDSDD PEPASDDDED ASYADEEYGV AKKKAPKKKK QPSKPRVTVR
HSPSDSDSDY GARSKKKKKP RIPSDEIRVS SRGTKVPNYI DDVQDFEQFD DDEIDAGTYG
GPQVVKEEDE IEMVLGHTRD EQHLSDPEDN WYTNTRFHIK WKNFSHLHNT DEMYEFLKRF
KGVKRVDNYI KAYKLYLERV NAPGLSREDK EALLLDKERE KEEFETYKTV ERIIAQRENA
ENHVEYFVKW NNLNYDHCTW ELQDEIRPIA KEQIDAFRTR EAEAKFPYKS AMYAKNSRPA
FKKITEDPQY LVKTGGELKD FQLTGLNWLA YLWSNGENGI LADEMGLGKT VQSVSFLAYL
FHEMRQFGPF LVIVPLSTIT AWQSQFATWG PDLNVITYIG NANAREVIRT FEFGPSNKKL
KMNVLLTTYE LTLRDARELS DIKWQVLAVD EAHRLKNSES QLYEALRAFS AASKVLITGT
PLQNNVKELL SLMHFLMPEK FHLSNEFDLT DVDHEEKIKE LHKQLEALML RRLKKDVLTS
LPTKSERILR VEMSALQTHL YKNILTKNFQ GLIKSANGNT NISLLNIAME LKKAANHPYL
FEGVEPESAT SEELLKGLVM NSGKIVLLDK LLARLRQDSH RVLIFSQMVR MLDLLSEYMQ
LRGYQFQRLD GMVSSEARKK SIAHFNAPGS PDFAFLLSTR AGGLGINLET ADTVIIFDSD
WNPQNDLQAM ARAHRIGQKS HVSVYRFVSK DTMEEDVLER AKKKMVLEYA IINQMDTSQA
HLSSKAGATK ENTKPNDLSK DELHAVLKYG AQKIFDKDDS QQNQKLDEMD LDDILKTAEQ
HETMAANNEG ASLGGEGFLA QFANVSDVKN DMSWEDIIPV EERQKFEEEE AKRKAEELAA
QERESKDRKR SHAPVSYEGM DVEQPAPTPA PKKPKHPAPQ RKTASQKAME LKERDVRVLI
RSLQRWGDIR QRYDVIVQEA KLQDKNRGMI IDTSDDIVEL CAHAVSQANQ EKRTRMEAGE
QLTNAQKSKA VLVTYRNVGN INAETVLSRH RDLQVLFKYL SELDDPYQWT IPIDNIRPTL
NWSGRWGPQD DAMLLVGAYL YGFGNWEAMQ KDPRLGLEGK FFLEEGKKGE DTSTRPIPNA
IHLVRRGDYL LGILREHDEK IRAIESTLQR KSSGGYKTSL SPPPPAASTS YSSSVRRRAE
SEAVASVEEG STKKRKRRPT PTFTDSSSSD ECPSMDEAAT KEELRPVKKQ LKNLKLSGGD
MPRDDKVAIL KESLAAIGKR IEYVLEQKAK SGEDAKRWKR HLWTFVTLFW PKKVKAAKLE
EIHAKMVMKE SSSAPRAGSS DPTATKKPRL SSTGAPSRSN GPSSSSHVNG KYR
//