ID E9E828_METAQ Unreviewed; 1097 AA.
AC E9E828;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=DNA repair protein RAD16 {ECO:0000313|EMBL:EFY87899.1};
GN ORFNames=MAC_06026 {ECO:0000313|EMBL:EFY87899.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY87899.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY87899.1,
RC ECO:0000313|Proteomes:UP000002499};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(2011).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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DR EMBL; GL698519; EFY87899.1; -; Genomic_DNA.
DR RefSeq; XP_007812366.1; XM_007814175.1.
DR AlphaFoldDB; E9E828; -.
DR STRING; 655827.E9E828; -.
DR GeneID; 19250337; -.
DR KEGG; maw:MAC_06026; -.
DR eggNOG; KOG1002; Eukaryota.
DR HOGENOM; CLU_000315_2_1_1; -.
DR InParanoid; E9E828; -.
DR OMA; RNDACKV; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000002499; Unassembled WGS sequence.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 1.
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:SF12; DNA REPAIR PROTEIN RAD16; 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 Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000002499};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 507..685
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 848..888
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 929..1083
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 36..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..73
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..252
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..334
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 413..428
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1097 AA; 122017 MW; DD2FC11838B0B858 CRC64;
MPRGRRPLQA GGMPLLKVPG KHLVLSDLGL IPFLTGDIES PDVNGTRRTR SVSSRPANGD
EIVISSDSTQ PVRRPRGRPS RASLLSAVTT SATSSPSYDN GVNPRRGRAS VIGSTSVSSA
ATPLELSSDA EYSTPATSKY PTPLAAEGSV SAEASKSLPS LEVRLPARSR ADDSDSERAL
RNSIYSMKAN RKLTEIVNSD EEDDDSSDTG RDARIARKLQ DEEFAKADEG ALRSSSLCGS
NRAVTATTSP LPNRGIAKRG RASTRSSMQL APPAKKNRVI PDSDDPPTSD FDMDAEIAAA
AALDSELSEG EATFTDSDES DEAEADEDGS TSDAFSDDEP LSAKKKGKRP EKPRTLSSKA
KIPTRRGRPS TAATGSKPNL ALRLHRAQDV VQDSDDDDVA EVVSIASDMC TVSSVSAGPG
SSNSSDAEEG VSELRRIAAN RRAYRSGNRR RLKKERDRLE YHHPEIVTMW EDLEKMPILK
AGMAPQPQSI SRQLKPFQLE GLAWMKEMEK REWKGGLLGD EMGLGKTIQA VSLIMSDYPA
KQPSLVLVPP VALMQWQSEI KSYTDGTLKT FVFHGTNQKA KTITAKELKT YDVIMMSYNS
LESMYRKQEK GFKRKNGIHK EKSVIHSIHF HRAILDEAHS IKTRTTMTAK ACFALQTTYR
WCLTGTPLQN RIGELFSLIR FLNIRPFALY LCKQCPCSTL EWAMDEDSRC SHCNHAGMQH
VSVFNQELLN PIQKFGNLGP GREAFRKLRL MTERIMLRRL KKDHTNSMEL PVKEIYVERQ
FFGEEENDFA NSIMTNGQRN FDTYVAQGVL LNNYANIFGL IMQMRQVADH PDLILKKNAD
GGQNILICSI CDEPAEDTIR SRCKHDFCRA CVSSYIGSTD SPDCPRCHIP LSIDLEQPEI
EQDENLVKKN SIINRIKMEN WTSSSKIELL VHELHKLRSD NASHKSIIFS QFTTMLQLIE
WRLRRAGITT VMLDGSMTPS QRQASIEHFM NNVDVECFLV SLKAGGVALN LTEASRVFIV
DPWWNPAAEW QSADRCHRIG QTRPCTITRL CIEDSVESRM VLIQEKKTNM IHSTVNADDK
AMESLSPEDM QFLFRGT
//
