ID A0A094EP30_9PEZI Unreviewed; 1021 AA.
AC A0A094EP30;
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=V499_06481 {ECO:0000313|EMBL:KFY73425.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY73425.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY73425.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY73425.1,
RC ECO:0000313|Proteomes:UP000029295};
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:KFY73425.1}.
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DR EMBL; JPKB01001082; KFY73425.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094EP30; -.
DR HOGENOM; CLU_000315_2_1_1; -.
DR Proteomes; UP000029295; 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 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..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 191..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1021 AA; 114823 MW; 114C2B08A9673B0D CRC64;
MVALSTRRRT RSSMAATYDG AGDENDVDPL QVAESIDRTS MSSASTAHES SGYSTPATSA
VTTPAQVKDE PSTRNPRRRI ASSLAHEVSS ATATVVHRAK ALRNSEFALN PSSSRKRSHQ
VLDSEDDDDD EFEDNSRDAQ LARALQKEEN ERSELVSTER QTSLGTSRRG RPRRSVLPMT
DFVDEFSEGE DAYNPPSKRA KLSDGKGKAR ATVPDSDEQS EFTDGSSSAD ENDFPGFLNL
TDDEETQPPR RPVQARRPAQ ARGRFGNNPP QRRRSTFQQP SIPAMEPADY TAPIQQPHSA
GEEGSNDDSE IPAFSTMTPA QRREYKLESR ARAARQRLET HHPELLVMWK ELRDLPKIPP
TKAEQPTNIS RELKPFQLEG LNWMKMMEKT KWGGGLLGDE MGMGKTIQAV SLIMSDYPAK
NPSLVLIPPV ALMQWQQEIA QYTDGTLKTF VYHGTNSAAK GVTVATLRKY DVILMSYNSL
ESLYRFQEKG RKRKDEVAFQ KSPVHQIQFH RVILDEAHNI KQRTTGSAKA CFALKADHKW
CLSGTPLQNR IGEFFSLIRF LDVRPFASYF CKQCPCSQLE WAMDERNRCT KCSHNGMQHV
SVFNQELLNP IQKYGNYGPG KDAFAKLRLL TDRFMLRRVK TDHSAAMELP AKEIYVDRKF
FGDEENDFAG SIMNSGTRKF ETYVSQGVLL NNYANIFGLI MQMRQVADHP DLILKKDGAG
GQNILCCCIC DEPAEDAIRS ACKHDFCRTC VKNYIASSEE STGTPDCPRC HLLLAIDLEQ
PEMVQDESAV KKTSIINRIK MENWTSSSKI EALLYDLHLL RSKNSSTKSI IFSGFTTMLQ
LVEWRLRRAG ITTVMLDGSM TPAQRQASIN AFMTDPTIEC FLVSLKAGGV ALNLTEASHV
FIVDPWWNPA AEWQSADRCH RIGQCRPCSI TRLCIEDSVE SRMVMLQEKK SNMIRSTINN
DEAAMESLTA EDMQFLFRED GKFDDLEFKT KLEAELTTFH SMGPKAVMSL DPKQGEFCFK
A
//
