ID A0A1E3PYD9_LIPST Unreviewed; 1067 AA.
AC A0A1E3PYD9;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Upf1 domain-containing protein {ECO:0000259|PROSITE:PS51997};
GN ORFNames=LIPSTDRAFT_65451 {ECO:0000313|EMBL:ODQ70350.1};
OS Lipomyces starkeyi NRRL Y-11557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Lipomycetaceae; Lipomyces.
OX NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ70350.1, ECO:0000313|Proteomes:UP000094385};
RN [1] {ECO:0000313|EMBL:ODQ70350.1, ECO:0000313|Proteomes:UP000094385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ70350.1,
RC ECO:0000313|Proteomes:UP000094385};
RX PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC {ECO:0000256|ARBA:ARBA00007913}.
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DR EMBL; KV454300; ODQ70350.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E3PYD9; -.
DR STRING; 675824.A0A1E3PYD9; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000094385; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IEA:InterPro.
DR CDD; cd21407; 1B_UPF1-like; 1.
DR CDD; cd18039; DEXXQc_UPF1; 1.
DR CDD; cd18808; SF1_C_Upf1; 1.
DR CDD; cd21400; ZBD_UPF1-like; 1.
DR Gene3D; 2.40.30.230; -; 1.
DR Gene3D; 6.10.140.1240; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR047187; SF1_C_Upf1.
DR InterPro; IPR040812; UPF1_1B_dom.
DR InterPro; IPR018999; UPF1_CH/ZBD.
DR PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR PANTHER; PTHR10887:SF364; REGULATOR OF NONSENSE TRANSCRIPTS 1; 1.
DR Pfam; PF13086; AAA_11; 1.
DR Pfam; PF13087; AAA_12; 1.
DR Pfam; PF18141; UPF1_1B_dom; 1.
DR Pfam; PF09416; UPF1_Zn_bind; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51997; UPF1_CH_RICH; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU01341}; Reference proteome {ECO:0000313|Proteomes:UP000094385};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01341};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU01341}.
FT DOMAIN 93..250
FT /note="Upf1"
FT /evidence="ECO:0000259|PROSITE:PS51997"
FT REGION 27..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 73..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..133
FT /note="C3H"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 115..143
FT /note="CC/SHH/C"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 161..191
FT /note="C4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 904..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 905..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1067 AA; 117896 MW; D8DB8A0C309FDEBE CRC64;
MDAFTHLGQQ FDSASYVDTS SVISDMAPYR RRRQHNKRRA ANDDSGANTS DSGEDDDIES
TIDGTLSLAS VPIDDGHLRR TTDEEDEGED DEVKELPDYA CAYCGIHSPS SVVRCAQCDK
WFCNSRGNTS SSHIVNHLVR ARHKEVCLHA ESDLGATTLE CYNCGCKNVF LLGFIPAKSD
TIVVVLCRQP CASASSSKDM TWDTSQWQPL IEDRSFLSWL ITVPTEAEQV KARNPTAAQI
AKLEEIWKNN SNATINDLEN SAPDDEPVPV LLRYEDAYQY QRCFGPLVKI EADYDKKLKE
SQSQDQLVVK WDIGLNNKHL ASFVLPKMDM GDVKLAVGDE MRLRYNGDIR SKWEGVGYVI
KIANNISDEI TLELRRNDKS VPSDCTLGFS VDYVWKATSF DRMQLALKTF AINEMSVSGY
IYHKLLGHEV APVVLKTAMP KQFAAPNLPD LNVSQVHAVK SVLQKHISII QGPPGTGKTV
TSATIVYHLA KMNPGQVLVT APSNVAVDQL TEKIHRTGLK TVRLTAKSRE DIESSVSFLA
LHEQVRLNDT NIELQKLTQL KQELGELSSQ DEKKFKKLTR QAEREILTNA DVICCTCVGA
GDPRLSKLKF RTVLIDESTQ AAEPECMIPL VMGCKQAVLV GDHKQLGPVI MNKKAARAGL
HQSLFERLVL LGLAPIRLNV QYRMHPCLSE FPSNMFYEGS LQNGVTTDER LRKNVDFPWP
IADTPMMFWS NLGQEEISAS GTSYLNRTEA SNVEKLVTRF FKAGIQPSQI GIITPYEGQR
SYIVSSMQTN GSLRKELYKE VEVASVDAFQ GREKDYIILS CVRSNEHQGI GFLSDPRRLN
VALTRAKYGL VVIGNPKVLS KQPMWHHLLM HYKEKGCLVE GPLNNLQVSM IQFAKPRMPY
RGSPSSAGSY YQQQRQPPMS MRYGDLSRQQ QPDFDTGSVL GYIPDDVASL SGMPSSNYQA
IFANGFNVMN HWPSLPGSSS VPGPHGSVPP GDITNGNASN GKFGAIGAGP AGGKSIGLSQ
SDRLKQYVED DSASVYGGLG SVYSAIDDDA RSVSTAFASQ IGIGPYD
//