ID A0A061H0Y0_9BASI Unreviewed; 1154 AA.
AC A0A061H0Y0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=RAD16-nucleotide excision repair protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PFL1_06538 {ECO:0000313|EMBL:EPQ25863.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ25863.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ25863.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ25863.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
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; KE361649; EPQ25863.1; -; Genomic_DNA.
DR RefSeq; XP_007882272.1; XM_007884081.1.
DR AlphaFoldDB; A0A061H0Y0; -.
DR GeneID; 19320611; -.
DR KEGG; pfp:PFL1_06538; -.
DR eggNOG; KOG1002; Eukaryota.
DR HOGENOM; CLU_000315_2_1_1; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000053664; 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 Reference proteome {ECO:0000313|Proteomes:UP000053664};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 548..721
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 893..938
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 987..1137
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..249
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..292
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 423..437
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..490
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1154 AA; 127408 MW; 0C0C825010D1113E CRC64;
MAPPPGPRRS SRQSISRGQG SAASGSDGRD ELDMLGDDAR TATTPSPELG RGSQRASFAS
SAGSTTPATI ASNISSARAS GTVTPATSID DAEEVLLPVP ASKASASRTG PVKGAFSPTN
QPPAVKFEAG HAFVEIPSHT SSQRSTRAST RASVPTRSAL KRSTSAAGDA AAAPSTKSTG
KRKIEAIVIS SSSDDEAEKQ RQPQPPLRPA KRSRTSIGGS SSMRKFDEDK YKDGDDINDD
EDDETEDETE WYMAAKFTPK AAKGKGQTKA MAKGKGKIVK GVDEDPHEDA DVKAAPPATQ
QRSALQRTSR RSTAAAAAAA APAMKGDSDG DEELVALSLE LASEGVSDVP EPASVATKSK
GRRAAANAAS IKTKAKAALD EYQVDDDNSG SDSDFEPVGY SKRASRSARQ ARLKRDIDID
SDASSLDGSD DSELSDEDAP LAAGSSAGPS TGLAAGSMRE EQQYETAKQR AARLRSERRQ
ARLKNKNVRS QYEKNKRALV AHHPELKDVW EKLRDGVAVI KPEQAEQPAG LNIKLLPFQR
EGLDWLKRQE AGPWKGGMLA DEMGMGKTIQ MISLMLSDRQ KPCLVLAPTV AIMQWRNEIE
QYTEPRLKVE LWHGANRTQD ADRLRRADVV LTSYAVLESC YRKQETGFQR KKMRVKEDSV
LHAIHWRRII LDEAHNIKER ATNTAKGAFA LKGDFRWCLS GTPLQNRVGE LYSMIRFLGG
DPYAFYFCKK CPCKSLHWQF SDRRNCDSCG HTPMHHTCFW NNEILKPIQK NGAEQGEGKD
AFGRLRLLLE RMMLRRTKLE RADDMGLPPR TIEVRRDLFN EEEEDLYTSL YSDTTRKFST
YLDQGTVLNN YSNIFTLLTR MRQIANHPDL VLRSQSGVSN RLLGEQQDEH HVCKICADVA
EDAIMSRCRH VFCRECVRQY LETDLPPDAG APDCPYCHAT LSIDLEGEAL EPPQPLNNAS
DGGRSGRQGI LSRLDMDQWR SSTKIEALVE ELTQLRAEDK TIKSLVFSQF VNFLDLIAFR
LQRAGFQICR LEGNMSPEAR NKTIKHFMEN PNVTVFLVSL KAGGVALNLT EASRVYLMDP
WWNPSVEVQA MDRIHRLGQH RPIIVKRMII ENSIESRIIE LQNKKSAMIE AAIGKDESAM
GRLSVADLRF LFTL
//
