ID A0A421JK67_9ASCO Unreviewed; 2216 AA.
AC A0A421JK67;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=ATP-dependent DNA helicase RRM3 {ECO:0000256|HAMAP-Rule:MF_03177};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_03177};
DE AltName: Full=rDNA recombination mutation protein 3 {ECO:0000256|HAMAP-Rule:MF_03177};
GN Name=RRM3 {ECO:0000256|HAMAP-Rule:MF_03177};
GN ORFNames=JA1_004270 {ECO:0000313|EMBL:RLV90878.1};
OS Spathaspora sp. JA1.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX NCBI_TaxID=2028339 {ECO:0000313|EMBL:RLV90878.1, ECO:0000313|Proteomes:UP000285775};
RN [1] {ECO:0000313|EMBL:RLV90878.1, ECO:0000313|Proteomes:UP000285775}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA1 {ECO:0000313|EMBL:RLV90878.1,
RC ECO:0000313|Proteomes:UP000285775};
RA Formighieri E.F., Steindorff A.S., Trichez D., Almeida J.R.;
RT "Physiological and comparative genomic analysis of newly identified yeasts
RT Spathaspora sp. JA1 and Meyerozyma sp. JA9 reveals insights into xylitol
RT production.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: 5' to 3' DNA replicative helicase recruited to paused
CC replisomes to promote fork progression throughout nonhistone protein-
CC DNA complexes, naturally occurring impediments that are encountered in
CC each S phase where replication forks pauses. Required for timely
CC replication of the telomere and subtelomeric DNA and for wild-type
CC levels of telomeric silencing. Involved in DNA repair during stalled
CC replication fork, regulation of fragile sites expression and essential
CC for genome stability. Plays also a role in mtDNA replication. Has G-
CC quadruplex (G4) unwinding activity and can suppress G4-induced genome
CC instability when PIF1 levels are low. {ECO:0000256|HAMAP-
CC Rule:MF_03177}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03177};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000256|ARBA:ARBA00000900};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC {ECO:0000256|ARBA:ARBA00004514}. Nucleus {ECO:0000256|HAMAP-
CC Rule:MF_03177}. Chromosome, telomere {ECO:0000256|HAMAP-Rule:MF_03177}.
CC -!- SIMILARITY: Belongs to the LTN1 family.
CC {ECO:0000256|ARBA:ARBA00007997}.
CC -!- SIMILARITY: Belongs to the helicase family. PIF1 subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_03177}.
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:RLV90878.1}.
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DR EMBL; NSGQ01000044; RLV90878.1; -; Genomic_DNA.
DR STRING; 2028339.A0A421JK67; -.
DR Proteomes; UP000285775; Unassembled WGS sequence.
DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005657; C:replication fork; IEA:UniProtKB-UniRule.
DR GO; GO:1990112; C:RQC complex; IEA:InterPro.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051880; F:G-quadruplex DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR GO; GO:0000002; P:mitochondrial genome maintenance; IEA:UniProtKB-UniRule.
DR GO; GO:1990116; P:ribosome-associated ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
DR CDD; cd18037; DEXSc_Pif1_like; 1.
DR CDD; cd16491; RING-CH-C4HC3_LTN1; 1.
DR CDD; cd18809; SF1_C_RecD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR HAMAP; MF_03176; PIF1; 1.
DR HAMAP; MF_03177; RRM3; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR010285; DNA_helicase_pif1-like.
DR InterPro; IPR039795; LTN1/Rkr1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049163; Pif1-like_2B_dom.
DR InterPro; IPR048293; PIF1_RRM3_pfh1.
DR InterPro; IPR039804; RING-CH-C4HC3_LTN1.
DR InterPro; IPR028880; Rrm3.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12389:SF0; E3 UBIQUITIN-PROTEIN LIGASE LISTERIN; 1.
DR PANTHER; PTHR12389; ZINC FINGER PROTEIN 294; 1.
DR Pfam; PF05970; PIF1; 1.
DR Pfam; PF21530; Pif1_2B_dom; 1.
DR Pfam; PF13639; zf-RING_2; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM01197; FANCL_C; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_03177};
KW Chromosome {ECO:0000256|HAMAP-Rule:MF_03177};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW DNA damage {ECO:0000256|HAMAP-Rule:MF_03177};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW DNA repair {ECO:0000256|HAMAP-Rule:MF_03177};
KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_03177};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_03177, ECO:0000313|EMBL:RLV90878.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_03177};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_03177};
KW Nucleus {ECO:0000256|HAMAP-Rule:MF_03177};
KW Reference proteome {ECO:0000313|Proteomes:UP000285775};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Telomere {ECO:0000256|HAMAP-Rule:MF_03177};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 2160..2206
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT DNA_BIND 631..650
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03177"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2052..2079
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 197..204
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03177"
SQ SEQUENCE 2216 AA; 252343 MW; A30C5075BCCE69C8 CRC64;
MTTTQGKPRP TLSSKSQSKI SSFFTSSRSV NANTSKTGTI PRGKSISGSL TRSDSFLSKA
MTSTSGFDDP ASSDTSFDTS TEINNFRNVA ISKSFNGRYG QTTTTNNDRK PEVIEISDVE
DEDVRPTQSF GLTQLKRSNT SDFLDNLSGQ ARKVPKLSRN NSSSTTTVDY GSAILSEEQN
SVVQSVVYQK QNVFYTGSAG TGKSVVLREL VRKLKEIYRD NVGITASTGM AACNIQGQTL
HKYLGIGLGA GSPFEISKRI KKHQPNLRKW QTVKVLIIDE ISMIDGVLFD KLEEVARLVR
GNSKPFGGIQ IVCTGDFFQL PPVSKDGKAS FCFQAKSWNN VIKKTILLRK VFRQKGDNEL
IDMLNALRFG KLQPETIQKF MRLSRRVSYQ DGIEPTELFP TRNEVKRANF ARLNQLNSKA
YVFVADDNVV NPELKKQLDN LMCEQTLTLK EGAQVMNLKN MDDQLVNGSI GTVIFFSTTR
LHLKVLEHYG PLESFTEEML QEMKLLSTRI GGSASLTPEE TSFIENMPAE RKPIFQLLCH
AAGQESADSI LPVVNFKING LDHIVLVERE EFKIELNTRK TLSSQAQGTP EALIRTQLPL
LLSWAISIHK AQGQTIDRLR IDLGKSFEKG QVYVALSRAT TKDHLEIRNF HPSKVMTSEI
TPNMGEEEED RPTGDLGYSG FEVSLNYFTS LPDVASIASS ELTVIFKSLL KKDPKTKEKA
LSDFLTYLES DENVAYTSDY LTIMAWIQTY PKLAIENSRS IRVLAHQVQA NYLQKVGGKA
FSKYLKSSLP VWLLGVFDTD KSVCSTAYSG LLESFQNDKS KVDEKIWILF ADAIVNLIGN
IVLIESPETM SDKRYTSESE LNLKYERALS CSLNMLMRLI SLANDDKISL ESESTRIEYI
LNSEVLWDRL GSSIKEKTMN LPLFKTLLML ISKVFDMTKA NIFITQVTDV KLIYKTVSKK
FFKIKLVNDT KSSSGNIIYS NIILQFWSTI ITLTDFTLRD VKKFKLKKNF WELGGSKGVS
RFYEYLRVGS CNSDPIYYQL VSRLFDVFAK LSVSSEPTTV VDFVSEDEFE YTTGLLLKQF
NSNQPKFKAP SLDCHFRIVE TFKLPDSSKS GVIYETLVNV VNNLTTIRAQ NFNDQIITTV
ASHFESNSDY LNESLTKLNS TIQNNIVDGN LASEFSLTVP EKNFVQKYFD LLQRLNKKEL
IEDIIKRIIQ ELEENSDTNL KLLLSVIKIY VETEDNFSQS VADFIEVLPA YVEEGFIDVP
IDLFHTAISR QYIKTESQLV EIINDFYLKL TMVSPSSLND FLYSLKGLVD IQPEQFEDLY
SYVLDLSQSK DLNDQLIETI LSITTQEEVL NNIISRARVD DKGSIHFIEL VNRYNLLPKL
LKTHGSKEFD RVLLTAWKNL KFQACKDFLV SLKEDQATFI NSFHTFLTSC TINDDIPEIA
KFISSGPVPI SVLVEELKTI SNQINVNAVA ISNPLESAIY LCKKPKATNT SEFGPILGKF
LVSLEPDCIT DEVIILGLIV KEYISDYVFI QNSKAFDFVQ VSEILNKLDV FLTDALKGVS
FKDVVNTLNE NSSSIITKLF SILEGNDTYA FYVARAVKKV IEATLENESL SQFESYEINY
TKLIKFPFKF ISVITGISRF LTSKKLDRVR QYVFSEILGV RKESDILNQG LKWITFSLLF
YNIEDKADFL PIVKFTMVLN QISSWFDSSI AYDSEFIDVR IQVTRFLGFV LSKQLTIPDN
YWDLTNRVLK DNLEVIQTEP DRIDLKYYTF KLYNLINKTR KESWDDLYED LLEIFLSKDT
FEVDNQATIL TQQISQRALE ESTIPTKVLI GEKMKLVSTF TTSNLISAQR VTASYLRRVI
LKEQEDFVVE YQLSKSKLSE DDQDKVEAKI LDEFVAAVKD HKYAISELEE FDFTKYLWSW
YLIFTYFEDS TFKIRSDYIG QLSKHNELRA LFEFIAEHMD FSDRFFGTLV FKQDDDTQEN
RIPNYDLIKT ARTEDLGYEI KYLIVHVFYK CLNYCGSEVQ YWFKEIRDKQ LKGKIEKCSS
KYVSSILITS IMNQVLQEKD KIQGKEENLN IKVNQITNEI RTTYVIDEQK MEMVIKIPQE
YPLANVTVEG PLRLGVKENQ WKAWLLASQR VISLTNGSII DSIELFCKNV NLHFSGFEDC
AICYSILHQD LSLPSKTCPT CSNKFHAACL YKWFKSSGSS TCPLCRSAFA FRVGRS
//
