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Database: UniProt
Entry: A0A022RT14_ERYGU
LinkDB: A0A022RT14_ERYGU
Original site: A0A022RT14_ERYGU 
ID   A0A022RT14_ERYGU        Unreviewed;       885 AA.
AC   A0A022RT14;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   RecName: Full=RING-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=MIMGU_mgv1a001113mg {ECO:0000313|EMBL:EYU42055.1};
OS   Erythranthe guttata (Yellow monkey flower) (Mimulus guttatus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Phrymaceae; Erythranthe.
OX   NCBI_TaxID=4155 {ECO:0000313|EMBL:EYU42055.1, ECO:0000313|Proteomes:UP000030748};
RN   [1] {ECO:0000313|EMBL:EYU42055.1, ECO:0000313|Proteomes:UP000030748}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DUN x IM62 {ECO:0000313|Proteomes:UP000030748};
RX   PubMed=24225854; DOI=10.1073/pnas.1319032110;
RA   Hellsten U., Wright K.M., Jenkins J., Shu S., Yuan Y., Wessler S.R.,
RA   Schmutz J., Willis J.H., Rokhsar D.S.;
RT   "Fine-scale variation in meiotic recombination in Mimulus inferred from
RT   population shotgun sequencing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:19478-19482(2013).
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RAD16 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008438}.
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DR   EMBL; KI630319; EYU42055.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A022RT14; -.
DR   STRING; 4155.A0A022RT14; -.
DR   eggNOG; KOG1001; Eukaryota.
DR   Proteomes; UP000030748; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA 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; 3.
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; IPR001841; Znf_RING.
DR   InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR   InterPro; IPR017907; Znf_RING_CS.
DR   PANTHER; PTHR45626:SF24; ATP-DEPENDENT HELICASE ULS1; 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; PF13923; zf-C3HC4_2; 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:UP000030748};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00175}.
FT   DOMAIN          163..436
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   DOMAIN          590..626
FT                   /note="RING-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50089"
FT   DOMAIN          701..874
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS51194"
FT   REGION          1..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..29
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   885 AA;  98250 MW;  2EE6F2A8E3842B81 CRC64;
     MHSSHQPLKR ALPPSLQPST SNFRPNNLLE NVGPSEIRDP YGKSHESSAW SNSSNGNNSM
     KENFISGSGN DSSLYEKRGN RLLPPSMMPG KHSSSTPYSG SNDSFHHTGV GEERPAGADE
     RFVFQAAVQD LHQPKVEARL PEGLLSVSLL RHQKIALAWM LNKESSGLCL GGILADDQGL
     GKTVSMIALM QMQKVLEAKS KPKDSPNTVI EALNLDDDDG SSGCVAVGDA NQQIKESDDF
     AINTIKDFRS RRPTAGTLIV CPASVLRQWA RELDEKVTKE ARISTLIYHG GSRTKDAAKL
     ARYDAVLTTY AIVANEVPKQ PLVDEDGTEQ KDGDQFGLSS AFSMEKKRKK SSVNNKSKKG
     KKEIDMSAFD SNCGTLARVK WSRVILDESQ TIKNHRTQVA RACCSLRAKR RWCLSGTPIQ
     NSIDELFSYF RFLRYDPYDK YKTFGSSIKA LISRDSVKGY KKLQVVLRNI MLRRTKGTLL
     DGEPIINLPP KRVHLTRVEF SLEERAFYSK LEADSRKQFK AYAAAGTVNQ NYANILLMLL
     RLRQACDHPL LVKGLSSDPV GKVSSQMAQM LPRELLVNLL KQLETSLAIC LVCRDPPENA
     VVTMCGHVFC YQCVADHLTG EDNTCPAPEC KEQLGADVVY SRSTLLRCMS DDIDGDTAAP
     YELSDKSTVL QRDYISSKIK SALEIIKTHC ISKSLSSESC DLVKYDGDAS SSAGPCLNSE
     NKEPEKAIVF SQWTSMLDLV EMSLKNSRIR YRRLDGTMSI AARDKAVKDF NTDPEVDVML
     MSLKAGNLGL NMVAACRVIL LDLWWNPTTE DQAVDRAHRI GQTRPVTVSR LTIKDTVEDR
     ILALQEDKRK MVASAFGEDP SGGHVTRLTM EDIRFLFEGS DARRH
//
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