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Database: UniProt
Entry: V7CPJ6_PHAVU
LinkDB: V7CPJ6_PHAVU
Original site: V7CPJ6_PHAVU 
ID   V7CPJ6_PHAVU            Unreviewed;      1304 AA.
AC   V7CPJ6;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Helicase-like transcription factor CHR28 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PHAVU_002G224600g {ECO:0000313|EMBL:ESW31273.1};
OS   Phaseolus vulgaris (Kidney bean) (French bean).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Phaseolus.
OX   NCBI_TaxID=3885 {ECO:0000313|EMBL:ESW31273.1, ECO:0000313|Proteomes:UP000000226};
RN   [1] {ECO:0000313|Proteomes:UP000000226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. G19833 {ECO:0000313|Proteomes:UP000000226};
RX   PubMed=24908249; DOI=10.1038/ng.3008;
RA   Schmutz J., McClean P.E., Mamidi S., Wu G.A., Cannon S.B., Grimwood J.,
RA   Jenkins J., Shu S., Song Q., Chavarro C., Torres-Torres M., Geffroy V.,
RA   Moghaddam S.M., Gao D., Abernathy B., Barry K., Blair M., Brick M.A.,
RA   Chovatia M., Gepts P., Goodstein D.M., Gonzales M., Hellsten U.,
RA   Hyten D.L., Jia G., Kelly J.D., Kudrna D., Lee R., Richard M.M.,
RA   Miklas P.N., Osorno J.M., Rodrigues J., Thareau V., Urrea C.A., Wang M.,
RA   Yu Y., Zhang M., Wing R.A., Cregan P.B., Rokhsar D.S., Jackson S.A.;
RT   "A reference genome for common bean and genome-wide analysis of dual
RT   domestications.";
RL   Nat. Genet. 46:707-713(2014).
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008438}.
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DR   EMBL; CM002289; ESW31273.1; -; Genomic_DNA.
DR   RefSeq; XP_007159279.1; XM_007159217.1.
DR   STRING; 3885.V7CPJ6; -.
DR   EnsemblPlants; ESW31273; ESW31273; PHAVU_002G224600g.
DR   GeneID; 18638785; -.
DR   Gramene; ESW31273; ESW31273; PHAVU_002G224600g.
DR   KEGG; pvu:PHAVU_002G224600g; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   OMA; YQNNFHN; -.
DR   OrthoDB; 11932at2759; -.
DR   Proteomes; UP000000226; Chromosome 2.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd18008; DEXDc_SHPRH-like; 1.
DR   CDD; cd18793; SF2_C_SNF; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 3.
DR   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
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; IPR049730; SNF2/RAD54-like_C.
DR   InterPro; IPR000330; SNF2_N.
DR   InterPro; IPR018957; Znf_C3HC4_RING-type.
DR   InterPro; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45626:SF16; SNF2 DOMAIN-CONTAINING PROTEIN _ HELICASE DOMAIN-CONTAINING PROTEIN _ ZINC FINGER PROTEIN-LIKE PROTEIN; 1.
DR   PANTHER; PTHR45626; TRANSCRIPTION TERMINATION FACTOR 2-RELATED; 1.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF00176; SNF2-rel_dom; 1.
DR   Pfam; PF00097; zf-C3HC4; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SMART; SM00184; RING; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF57850; RING/U-box; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS00518; ZF_RING_1; 1.
DR   PROSITE; PS50089; ZF_RING_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000226};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          565..833
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          987..1026
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          1140..1299
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          42..64
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          119..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          722..766
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1094..1130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        48..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        724..745
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1304 AA;  144187 MW;  A191047CEEDE7847 CRC64;
     MADEEVDFSK LFPGDDGDDD MFYIDIHTVQ KVLDEDDDCD FLEKFPEDSS SKNVSPSESG
     THDTFQIQNG SQVLEEPQFS RLGFTDSVTS FSPFCSDASD SGVRGSVGVS DSVANSWLDC
     EPENQGPRSQ ACSSPNAFPG NLSNSLSQGE SDEVFCTEKT RVSKHEVPAC SAESSLPEAQ
     SKNISICGDN LNPSPWNGEN EIQFKYLRED VEFENTSISS IVDNDDVNIE GYVEDTIGGV
     SGQQENDSCT SFEAFMDADI SLHVATSSDS TIGQDDEMMN NMKAKNVDLN ADITCMSSGM
     PSNTTGWMSF LDLSDNVYPS FHSSKGNFDD MSSLSLSACD SYMPYGDHYQ NNFHCEDAKF
     NVGQSVKQTP GIFSSVGCQA YQFFEIEDNY AVIPGISNQN QDSNGGIASF QGNVDNLNLQ
     AANISLPHAH ALITSEKQFG SVKREGGVQH KLVDSHLSKG KIKNFHVEED PDVCIIEDIS
     HPAPTSRSTI TGNFSSISQS SGYANPQSYM VGSTKLKACD ERNILRVALQ DLSQPKSELN
     LPEGLLAVPL LRHQRIALSW MVQKEASSLY CSGGILADDQ GLGKTVSTIA LILKERPPLL
     NGCTNAHKSE LDLNLDVDDD VLPQNGRVKE ESNICEDKSS RYPVKSMNLL NQAKGRPSAG
     TLIVCPTSVL RQWAEELRSK VTSQTNLSVL VYHGSNRTKD PYEVAKYDVV LTTYSIVSME
     VPKQPSADKD DEEKGNVEDQ AVSSRKRKCP SNSSKGGKKR SDGTVPEANA RPLAKVAWFR
     VVLDEAQSIK NHKTQVARAC WGLRAKRRWC LSGTPIQNAI DDLYSYFRFL RYDPYDVYIS
     FCSKIKNPIS RNPTNGYRKL QAVLKTIMLR RTKGTLLDGE PIISLPPKYI ELKKVDFSME
     ERDFYYKLEA DSRAQFQEYA DAGTVKQNYV NILLMLLRLR QACDHPLLVK RYNSNSLWRS
     SVEMAKTLPQ EKQISLLQCL EASLALCSIC NDPPEDAFVS VCGHVFCNQC ICEHLTGDDN
     QCPAANCKNP LSTSRVFSKA TLNSCLSDQG CDNSPGCSGS EAEEFEPWSQ SQPYESSKTK
     AALEVLKSLC KPQSYTSKSS SEHSTFRKDN DCPGNPSNAD NGKSFIDSHE HQNLSDDNRC
     HGDSVTVVGD KAIVFSQWTR MLDLLEACLK KSSINYRRLD GTMSVVARDK AVKDFNTLPE
     VSVIIMSLKA ASLGLNLVVA SHVLMLDLWW NPTTEDQAID RAHRIGQTRP VSVLRLTVKD
     TVEDRILALQ QKKRMMVASA FGEDGTGDRQ SRLTVDDLKY LFMM
//
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