ID U5DAL1_AMBTC Unreviewed; 933 AA.
AC U5DAL1;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=DNA repair protein RAD16 {ECO:0008006|Google:ProtNLM};
GN ORFNames=AMTR_s00037p00235150 {ECO:0000313|EMBL:ERN17443.1};
OS Amborella trichopoda.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX NCBI_TaxID=13333 {ECO:0000313|EMBL:ERN17443.1, ECO:0000313|Proteomes:UP000017836};
RN [1] {ECO:0000313|Proteomes:UP000017836}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24357323;
RG Amborella Genome Project;
RT "The Amborella genome and the evolution of flowering plants.";
RL Science 342:1241089-1241089(2013).
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC {ECO:0000256|ARBA:ARBA00008438}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI392350; ERN17443.1; -; Genomic_DNA.
DR RefSeq; XP_006855976.1; XM_006855914.2.
DR AlphaFoldDB; U5DAL1; -.
DR STRING; 13333.U5DAL1; -.
DR EnsemblPlants; ERN17443; ERN17443; AMTR_s00037p00235150.
DR GeneID; 18445784; -.
DR Gramene; ERN17443; ERN17443; AMTR_s00037p00235150.
DR KEGG; atr:18445784; -.
DR eggNOG; KOG1002; Eukaryota.
DR HOGENOM; CLU_000315_2_10_1; -.
DR OMA; YFCKQCD; -.
DR OrthoDB; 11932at2759; -.
DR Proteomes; UP000017836; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IBA:GO_Central.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0140096; F:catalytic activity, acting on a protein; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
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; 2.
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; IPR027370; Znf-RING_euk.
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; 2.
DR Pfam; PF13445; zf-RING_UBOX; 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:UP000017836};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 212..507
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 679..719
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DOMAIN 759..923
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 933 AA; 105646 MW; B7FFD54A012B78FC CRC64;
MVRRKATTVR RSNRAKRQRN APTSDSEDSW QSDSGGDPTV SSDFSSSESD ESSVPKVQVR
RRTRSHVSAS VQEEASDPPE VNGVIVDALR DLNHGDIDDA LGGLNHDGGL NHDGVNEDMI
QRNHGVAAPR KRRKRNYRQT WNFPHKYHFP RLPWEKWEEE NIEWLVDSGK EDIELDSVAP
FYGGTPDSID PSSEILVPLL QFQREWLAWS MKQEESVMRG GILADEMGMG KTLQAISLVL
KARELRKPSL AKSQIPIDGA LPRVKGTLVV CPVVAIIQWA NEISRFTAQG SARVLIYHGA
KRFKDALQFS EYDFILTTYS IVEAEYRKNV MSPKAKCQWC GKSFYPKKLV IHQKYFCGPS
AMKTEKQSKQ VKKKTKIKVK AKNKSFEKDN EIETEIVVGK EKGKDKAMER TRQKTVRIQT
SDETRIPHGT SEASSATGGS ALGSSLLHSV KWERIILDEA HFIKDRRCNT AKAVFALESS
YKWALSGTPL QNRVGELYSL IRFLQIEPYS YYYCKDCDCK SLDHRYDEDG KRCQNCGHSP
LKHFCWWNKY VANPIMASSS ISEARQAMFL LKYKLLKSTV LRRTKKERAA DLALPPRVTI
LREDSLDNRE EDFYEALYTQ SQSQFNTYIA EGTLMNNYAH IFDLLTRLRQ AVDHPYLVVY
SDSQQSNNQI GPADAMQYCG ICHDPAEDSV VTSCGHTFCK ACVLDFTETS GQVMCPCSKP
LTVDLTTKEN SKDGSSKMAV KGCKRSRIMN QIKNLDDFQT STKIEALKEE IFLMHERDAA
AKAIVFSQFT SFLDLINFSV RKAGVRCVQL VGSMSLAARD EAIKTFTDDP DCRVFLMSLK
AGGVALNLTV ASHVFLMDPW WNPAVEQQAQ DRIHRIGQYK PIRIVRFVIA NSIEERILKL
QEKKKLVFEG TVGGSSEALG RLTQADLRFL FQT
//
