ID A0A367KT88_RHIST Unreviewed; 824 AA.
AC A0A367KT88;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=DNA repair protein rad16 {ECO:0000313|EMBL:RCI05424.1};
GN Name=RAD16 {ECO:0000313|EMBL:RCI05424.1};
GN ORFNames=CU098_010543 {ECO:0000313|EMBL:RCI05424.1};
OS Rhizopus stolonifer (Rhizopus nigricans).
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Rhizopodaceae; Rhizopus.
OX NCBI_TaxID=4846 {ECO:0000313|EMBL:RCI05424.1, ECO:0000313|Proteomes:UP000253551};
RN [1] {ECO:0000313|EMBL:RCI05424.1, ECO:0000313|Proteomes:UP000253551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSU 92-RS-03 {ECO:0000313|EMBL:RCI05424.1,
RC ECO:0000313|Proteomes:UP000253551};
RX PubMed=29674435; DOI=10.1534/g3.118.200235;
RA Gryganskyi A.P., Golan J., Dolatabadi S., Mondo S., Robb S., Idnurm A.,
RA Muszewska A., Steczkiewicz K., Masonjones S., Liao H.L., Gajdeczka M.T.,
RA Anike F., Vuek A., Anishchenko I.M., Voigt K., de Hoog G.S., Smith M.E.,
RA Heitman J., Vilgalys R., Stajich J.E.;
RT "Phylogenetic and Phylogenomic Definition of Rhizopus Species.";
RL G3 (Bethesda) 8:2007-2018(2018).
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:RCI05424.1}.
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DR EMBL; PJQM01000392; RCI05424.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367KT88; -.
DR STRING; 4846.A0A367KT88; -.
DR EnsemblFungi; RCI05424; RCI05424; CU098_010543.
DR Proteomes; UP000253551; 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:InterPro.
DR CDD; cd18008; DEXDc_SHPRH-like; 1.
DR CDD; cd23142; RING-HC_CHR27-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 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; 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|PROSITE-ProRule:PRU00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000253551};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00175};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00175}.
FT DOMAIN 234..409
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 570..615
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 662..811
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 46..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..151
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 94792 MW; 0BD3AB9866033FE3 CRC64;
MAPRRTSQRL LKKPKLESSP SDLMDVDILR DDSDDFQPLS VVVRRTRKEK GKQPVRLVVS
DSESEAASDV PSPFSKSSKS SGTSLTTNDN SKEVSAVNSP EAEPNSDSQQ KPSDEEEFVH
NDNSDNEEEE EEEEEEEEEE EEEEENSASS SEEEEVVQIR RPARTRRSVN NQPRLRSYER
TQLKILAHHK ELTTIWKDLE EVEPEAVVPI EQPPELTLQL LPFQRYGVGW MRRQENMDTF
KGGILADEMG MGKTIQTIAL LLSDRKKPNL VIAPTVAILQ WKDEIERHTN NALSVYVFHG
NKRTSSVEDL KKYDVVLSTY SIMESSFRRQ ESGVHNKATR SIRKEKSVLH KIKWHRIILD
EAHNIKDRSS NTARSVFNIS GAYKWSLTGT PLQNRVGELY SLIRFMQADP FSYYYCKQCP
CKEITWRFSN KRNCDSCGHT PMNHTCWWNN EVLKPIQYHG YLEEGREAMK KLGILLDKIM
LRRTKIQCAD DLGLPPRTVI VRRDMFTEEE EDVYTSLYSD VQRTFTTYVE EGTVLNNYAN
IFELLMKMRQ CADHPDLVTK KSSDNKQLVC MLCNDPPEDA IAAACKHVFC RECCVQYYDS
FDSNDNYEKP RCPSCYAEFS VDLSQPAIEV EGGHGLNANY SKSSIVNRIN MSTWRSSTKI
EALVEELSKL RQEDKTIKSI VFSQFVNFLD LVYWRLSRAG FECIRLDGTM TPDQRNAAIN
SFMTKPTVTV FLISLKAGGV ALNLTEASRV FICDPWLQNA MDRIHRLGQH RPIRITRLII
ENSIESRIIQ LQEKKTALVE STVDKNQKAL DKLTVEDLRF LFVM
//
