ID A0A094HMT1_9PEZI Unreviewed; 1883 AA.
AC A0A094HMT1;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=PHD-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=V502_05225 {ECO:0000313|EMBL:KFZ16182.1};
OS Pseudogymnoascus sp. VKM F-4520 (FW-2644).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420915 {ECO:0000313|EMBL:KFZ16182.1, ECO:0000313|Proteomes:UP000029308};
RN [1] {ECO:0000313|EMBL:KFZ16182.1, ECO:0000313|Proteomes:UP000029308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4520 (FW-2644) {ECO:0000313|Proteomes:UP000029308};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
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:KFZ16182.1}.
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DR EMBL; JPKE01002032; KFZ16182.1; -; Genomic_DNA.
DR STRING; 1420915.A0A094HMT1; -.
DR HOGENOM; CLU_000315_18_3_1; -.
DR OrthoDB; 1384108at2759; -.
DR Proteomes; UP000029308; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
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 GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd17919; DEXHc_Snf; 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; 1.
DR InterPro; IPR016197; Chromo-like_dom_sf.
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 InterPro; IPR040934; Znf-CCCH_6.
DR InterPro; IPR041684; Znf-PHD-like.
DR InterPro; IPR001965; Znf_PHD.
DR PANTHER; PTHR45623:SF17; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED; 1.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF18585; zf-CCCH_6; 1.
DR Pfam; PF15446; zf-PHD-like; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00249; PHD; 1.
DR SUPFAM; SSF54160; Chromo domain-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000029308};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771}.
FT DOMAIN 793..965
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 1100..1252
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 32..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 497..516
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1383..1596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1626..1650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1793..1883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1383..1411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1436..1488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1850..1873
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1883 AA; 208774 MW; 617EA13E6A2DF411 CRC64;
MASSGDDGED SVDELQSFQG LSPLKSADAL SVTALQHRPR MSSPVDADHG IGMGEDGRAD
GASKDTIEDD GDFSFEIRLP PAINSEEYTW IPGESDEGYV DCVESEVEDE ENVSYHIRYD
DGGDDIVPFE RLLQLCNGQN ALDVFHNPDE VEELDIPRRT EKSRGLSTRQ ASILSYTRKR
TSTRGHPRGH NASDEDEFSI NQSDSRRRRA ASPRRSLRSR TDSHAPRNKR YAGMTSPDEE
SSSDELASRS LSRRSLGARS SSGHGHRARG RLTRQSKNDY DSDDMTGAVD SDASGIVVKR
STGRPSRGRG RGKAKGGMSK KSGMFGRRKK DFEDSSSEAP EPTRKSGRST KVSKNMRDRL
EDEELYAEEV SDNGETGPKI ISVREIFQPL AANNHFRVIH NRRCDICSGL NTASNKGPSP
LIQCQGCTTS IHKVCLGYRG PREHLVTKVG EGDFVLQCRR CIGLARKKDK NAPDLGACQE
CKQPGLACAP FSTKKTSKQE EKLREENGGT DPITPVSPDL LNNHAILLFR CVSCRRGFHF
EHLPPLNDSA YTPDDVADLQ EARFSEYEPR WNCKECIEVP GKPQQLVAWR PANLETYAPG
TTLESLAEDE KEYLVKWQGM SYFSCAWVPG AWAWGITAAT MRNAFARRCV EQNNGLPIMT
ESDAIPEEFL RIEIVLDVKY SSRVSTHTEE IDKARIKEVE EVLVKFTGLG YDEIAWESPP
PPTETERYAD YHAAYLEFVA GKYFKQHNSK VKERLIQYRQ SNFERNVLLE GQPAALTGGK
LMEYQMEGMN WLLYNFHREK NVILADEMGL GKTIQVIAAL TALIKEKPKC WPFLIVVPNS
TCPNWRREIK QWAPSLRVVT YYGSREARET AMKYELFPEG RSELAAHIVV TSYEAPVDEN
SRAFFRKTKW AGLIVDEGQR LKNDKNLLYG ALTALKVPFR VLLTGTPLQN NKKELFTLLQ
FLDSDINATT LDEKYEELTN ENLPELHDLI RPYFLRRTKA MVLKFLPPMA QVIIPVKMST
VQKKLYKSIL SKSPELLRSI FGKDQAQLKP SERGSLNNIL MQLRKCLCHP FVYSEAIEER
SNNRAVLHRN LVDASSKLQL LEIMLVKLQE RGHRVLIFSQ FLKQLDIIED FLDGLGLQFQ
RLDGTIGTLE KQKRIDAFNA PDSPLFAFLL STRAGGVGIN LATADTVIIM DPDFNPHQDL
QALSRAHRIG QKNKVLVFQL MTKDSVEEKI VQIGRKKMAL DHALIEAMDE DDDAGVDLQS
ILQHGATALF EDDDQNDIRY DSASVDKLLD RTQMETTNTG DDKSAESQFS YARIWANDSG
ALQDDVGDPD SEEPMPNTDF WEKILKEREA EAAREELAKQ KQFGRGKRAR QVIAGYTDVV
NEEVTPRKSK KLRVMGESDG EFTRQSTDAE EEESDAGLVD ANELAAAKAR SGGRGMTQIS
PASKSPAKTL PLKNEKKTSS VPMKTSKRVV QANATPKKTV RQTQPPKKAV KPNQPPKNAV
KPDQPPKKLG QPPKDAVKQD PSPGSPIVKK PTMASSVPGS AGNPVLLDKK SDTARGAPRK
PKVMATAGRA PSNGSQVQAP SSETVSQKQA PNKRNTSVRI VTVAPKVPGP QANPLGDAIS
GKAPSLAKSA PKVMQRTTPM SNAVTGKRPR PVEPIDAFQR ARIVRDVPNM SDDPDFMRTF
GNTAAIYNRQ CLACDSIHAV GQCPSKRSGP EHCGLCGMAH YGFTQSGSQA ACPHLSSETQ
VRLMLDALKM STEPRDIIEP ARTYLRGVIG NLVNKKKREM REMELHAARS RPILPPILPP
SRPGATQRRW HADPQVTGGN GVYGGGLIRG GRPALGQPFD GGPSQDPWLL NKSAVASNAG
LSSATSNPPQ ATPSAEEMAD IHA
//