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Database: UniProt
Entry: K5WVL5_PHACS
LinkDB: K5WVL5_PHACS
Original site: K5WVL5_PHACS 
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).
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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
//
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