ID A0A094BA41_9PEZI Unreviewed; 980 AA.
AC A0A094BA41;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=DNA repair protein RAD16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=V494_05025 {ECO:0000313|EMBL:KFY36493.1};
OS Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY36493.1, ECO:0000313|Proteomes:UP000029288};
RN [1] {ECO:0000313|EMBL:KFY36493.1, ECO:0000313|Proteomes:UP000029288}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
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 -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC {ECO:0000256|ARBA:ARBA00007025}.
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:KFY36493.1}.
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DR EMBL; JPJW01001722; KFY36493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094BA41; -.
DR STRING; 1420907.A0A094BA41; -.
DR HOGENOM; CLU_000315_2_1_1; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000029288; 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; IPR002464; DNA/RNA_helicase_DEAH_CS.
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; PS00690; DEAH_ATP_HELICASE; 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:UP000029288};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 386..564
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 727..771
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 809..969
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..89
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..215
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..277
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 980 AA; 109634 MW; E75A6E3D5C9F71D8 CRC64;
MVAPGTRRRT RSSMGTSYDG AGDDIDPLQI AESVGRTSVS SASTTHESSG YSTPATSAVT
TPAPVKDEAS ARGPRRRIAS SLAHEVSPAA ATVVHRAKAL RNSEFALNPS SSRKRTLIQD
SEDDDDEYED NSRDAQLARA LQNEENERSE LVSTEPQTSF GASRGGRGGR PRRSVVSMTD
YAVDLSEDDV YDPPSKKAKL SDRKGKGRAL TVPDSDEESE FTDVSSSAEE NDLRTFLDTV
DDEDTKPPRR PVQPRRRPGN NPAQRRGTFQ QPSIPAVEPT DDATPVEPTG DTAAVKGTGS
SDEEDSDQSE IPDFSTMTQT QRRAYRLESR AKASRRRLES HHPELMTMWK ELRDLPKIPP
TKAEQPTNIS RELKPFQLEG LNWMKMMEKT KWGGGLLGDE MGMGKTIQAV SLIMSDYPAK
NPSLVLIPPV ALMQWQQEIA QYTDGTLKTF VYHGTNSAAK GVTVATLRKY DVILMSYNSL
ESLYRFQEKG RKRKDEVAFQ KSPVHQIQFH RVILDEAHNI KQRTTGSAKA CFALKADHKW
CLSGTPLQNR IGEFFSLIRF LDVRPFASYF CKQCPCSQLE WAMDERNRCT KCNHNGMQHV
SVFNQELLNP IQKYGNFGPG KEAFAKLRLL TDRFMLRRVK TDHSAAMELP AKEIYVDRKF
FGDEENDFAG SIMNSGTRKF ETYVSQGVLL NNYANIFGLI MQMRQVADHP DLILKKDGAG
GQNILCCCIC DEPAEDAVRS ACKHDFCRTC VKNYIASSEE SAATPDCPRC HLPLAIDLEQ
PEMMQDESAV KKTSIINRIK MENWTSSSKI EALLYDLHLL RSKNSSTKSI IFSGFTTMLQ
LVEWRLRRAG ITTVMLDGSM TPAQRQASIN AFMTDPTIEC FLVSLKAGGV ALNLTEASHV
FIVDPWWNPA AEWQSADRCH RIGQCRPCSI TRLCIEDSVE SRMVMLQEKK SNMIRSTINN
DEAAMESLTP EDMQFLFRGT
//
