ID A0A0G2HMW5_9PEZI Unreviewed; 938 AA.
AC A0A0G2HMW5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=Putative dna repair protein rad16 {ECO:0000313|EMBL:KKY36298.1};
GN ORFNames=UCDDA912_g03742 {ECO:0000313|EMBL:KKY36298.1};
OS Diaporthe ampelina.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Diaporthales; Diaporthaceae; Diaporthe.
OX NCBI_TaxID=1214573 {ECO:0000313|EMBL:KKY36298.1, ECO:0000313|Proteomes:UP000034680};
RN [1] {ECO:0000313|EMBL:KKY36298.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY36298.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY36298.1, ECO:0000313|Proteomes:UP000034680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DA912 {ECO:0000313|EMBL:KKY36298.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) 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:KKY36298.1}.
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DR EMBL; LCUC01000133; KKY36298.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2HMW5; -.
DR STRING; 1214573.A0A0G2HMW5; -.
DR OrthoDB; 200191at2759; -.
DR Proteomes; UP000034680; 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; cd16567; RING-HC_RAD16-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; 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:UP000034680};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 423..601
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 764..804
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 845..938
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..146
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..171
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 938 AA; 104012 MW; 2CE031E2C16CB0A5 CRC64;
MARTRRSLAG AAGETGESSQ AIRNNSSPSV SAPAASDSLP VKRGRGRPSK ASLVAAAAAA
NSESLSSLGT STYSSADSVS GYSTPLTSNV TTPAPVDNAK PASTRSTRSS NLEVAIPAAK
SRGSGNKSNL KADNQSMDTS SKVTRRNRLI AVHDSEDDVL TDDSPNARRI RYDEEVARSL
QNELNREVEG LPFDLEDGPE DDLEELLGIE SESEDYAATD PKGKGKAVAT RKASGTPAAA
KKRVVQDSDV EDDDDDSDFA DLSPPAKKQK TAVRSRGKKA SVKGKRVVAP LMSDSDDDLP
SLDTTPGLEE AISDGSGLSD VDSADFHTDS EDDSDDADPS AATNDPTRIQ AISRGRRGFG
AYANRKRIRT GRLQLEEHHP TLKTMWDRLR DMPVLKAGKA EQPKSISRLL KPFQLEGLAW
MKAMEKTEWK GGLLGDEMGL GKTIQAVSLI MSDYPAKQPS LVLVPPVALM QWVSEIESYT
DGTLKTLVYH GTNAQVKGKT VKELKKYDVI IMSYNSLESI YRKQEKGFKR KNGLHKERSL
IHSIQFHRVL LDEAHCIKTR TTMTAKACFA LKVDYRWCLT GTPLQNRIGE FFSLIRFLNI
RPFASYFCKN CPCESLEWTM DEDHRCTQCK HNGMQHVSVF NQELLNPIQR YGNLGPGAEA
FRKLRLMTDR IMLRRLKKDH TNSMELPVKE IYVDRQFFGE AENDFANSIM TNGQRDFDTY
VAHGVLLNNY ANIFGLIMQM RQVADHPDLI LKKNAEGGQN ILVCCICDEP AEEAIRSRCK
HDFCRSCAKS YLSSQDQPDC PQCHIPLSID LEQPEIEQDE AFVKKSSIIN RIKMENWTSS
SKIELLVHEL HKLRSDKTSH KSIIFSQFTT MLQLIEWRLR RAGITTVMLD GSMTPAQRAA
SIDHFMKNTE VECFLVSLKA GGVALNLTEA SRVFIVDP
//
