ID A0A3Q1K471_ANATE Unreviewed; 1115 AA.
AC A0A3Q1K471;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Regulator of nonsense transcripts 1-like {ECO:0000313|Ensembl:ENSATEP00000025816.1};
OS Anabas testudineus (Climbing perch) (Anthias testudineus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Anabantaria; Anabantiformes; Anabantoidei; Anabantidae; Anabas.
OX NCBI_TaxID=64144 {ECO:0000313|Ensembl:ENSATEP00000025816.1, ECO:0000313|Proteomes:UP000265040};
RN [1] {ECO:0000313|Ensembl:ENSATEP00000025816.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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 AlphaFoldDB; A0A3Q1K471; -.
DR STRING; 64144.ENSATEP00000025816; -.
DR Ensembl; ENSATET00000026234.2; ENSATEP00000025816.1; ENSATEG00000017867.2.
DR GeneTree; ENSGT00940000157413; -.
DR InParanoid; A0A3Q1K471; -.
DR OMA; TDRGQHG; -.
DR OrthoDB; 170190at2759; -.
DR Proteomes; UP000265040; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR006935; Helicase/UvrB_N.
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; PF04851; ResIII; 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}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000265040};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU01341};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU01341}.
FT DOMAIN 94..251
FT /note="Upf1"
FT /evidence="ECO:0000259|PROSITE:PS51997"
FT REGION 44..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 102..134
FT /note="C3H"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 116..144
FT /note="CC/SHH/C"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 162..192
FT /note="C4"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01341"
FT REGION 979..1082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 44..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1032..1082
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1115 AA; 123288 MW; 5FE241001C2AE36D CRC64;
MSVEAYGPSS QTLTFLDTEE TELLGADTQG SEFDFTDFTL PSQTQTQGQT QSQLDSQVNG
PDGVLQNGDD PVVKASQLLA ELNFEEDEED TYYTKDLPVH ACSYCGIHDP ACVVYCNTSK
KWFCNGRGNT SGSHIVNHLV RAKSKEVTLH KDGPLGETVL ECYNCGCRNV FLLGFIPAKA
DSVVVLLCRQ PCASQSSLKD INWDSSQWQP LIQDRCFLSW LVKIPSEQEQ LRARQITAQQ
INKLEELWKE NPTATLEDLE KPGVDEEPQH VLLRYEDAYQ YQNIFGPLVK LEADYDKKLK
ESQTQDNITV RWDLGLNKKR IAYFTLPKTD SDMRLMQGDE ICLRYKGDLA PPWKGIGHVI
KVPDNYGDEI AIELRSSAGA PIEIPHNFQV DFVWKSTSFD RMQSALKTFA VDETSVSGYI
YHKLLGHEVE DVVIKCQLPK RFTAQGLPDL NHSQVYAVKT VLQRPLSLIQ GPPGTGKTVT
SATIVYHLAR QGNGPVLVCA PSNIAVDQLT EKIHQTGLKV VRLCAKSREA IDSPVSFLAL
HNQTRNMDSM PELQKLQQLK DETGELSSSD EKRYRALRRT AERELLMNAD VICCTCVGAG
DPRLAKMQFR SILIDESTQA TEPECMVPVV LGAKQLILVG DHCQLGPVVM CKKAAKAGLS
QSLFERLVVL GIRPIRLQVQ YRMHPALSAF PSNIFYEGSL QNGVTAADRV KKGFDFQWPQ
PDKPMFFYVT QGQEEIASSG TSYLNRTEAA NVEKITTRLL KAGAKPDQIG IITPYEGQRS
YLVQYMQFSG SLHTKLYQEV EIASVDAFQG REKDFIILSC VRANEHQGIG FLNDPRRLNV
ALTRARYGVI IVGNPKALSK QPLWNHLLNY YKEQKVLVEG PLNNLRESLM QFSKPRKLVN
TINPGGRFMS TAMYDAREAL IPGSVYDCSS NGRTSNMYFQ THDQIGMIGT GSSPMTSMNI
PIPFNLVMPP IPPPGYMGQV NGPSAGRGGG MKGKAGTGGG SGNRGGRQRN RGNTGNHGGG
NGGMDRGHGG HMSGSQASQD LVSQPFSQGP LTQGYINMSQ PSQMSQPGLS QPELSQDSYL
GDEFKSQIDV ALSQDSTYQG ERAYQHGGVT GLSQY
//
