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Database: UniProt
Entry: A0A401KJL4_ASPAW
LinkDB: A0A401KJL4_ASPAW
Original site: A0A401KJL4_ASPAW 
ID   A0A401KJL4_ASPAW        Unreviewed;      1827 AA.
AC   A0A401KJL4;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=NFX1-type zinc finger-containing protein 1 {ECO:0000313|EMBL:GCB19379.1};
GN   ORFNames=AAWM_02264 {ECO:0000313|EMBL:GCB19379.1};
OS   Aspergillus awamori (Black koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=105351 {ECO:0000313|EMBL:GCB19379.1, ECO:0000313|Proteomes:UP000286921};
RN   [1] {ECO:0000313|EMBL:GCB19379.1, ECO:0000313|Proteomes:UP000286921}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IFM 58123 {ECO:0000313|EMBL:GCB19379.1,
RC   ECO:0000313|Proteomes:UP000286921};
RA   Kusuya Y., Shimizu M., Takahashi H., Yaguchi T.;
RT   "Aspergillus awamori IFM 58123T.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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:GCB19379.1}.
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DR   EMBL; BDHI01000002; GCB19379.1; -; Genomic_DNA.
DR   STRING; 105351.A0A401KJL4; -.
DR   Proteomes; UP000286921; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd17936; EEXXEc_NFX1; 1.
DR   CDD; cd18808; SF1_C_Upf1; 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; IPR046439; ZF_RZ_dom.
DR   PANTHER; PTHR10887; DNA2/NAM7 HELICASE FAMILY; 1.
DR   PANTHER; PTHR10887:SF445; FINGER AND HELICASE DOMAIN PROTEIN, PUTATIVE-RELATED; 1.
DR   Pfam; PF13086; AAA_11; 1.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF20173; ZnF_RZ-type; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51981; ZF_RZ; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000286921};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          1742..1818
FT                   /note="RZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51981"
FT   REGION          1..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..79
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1827 AA;  203527 MW;  B6BC0687BB3701E8 CRC64;
     MAGAKETSNT PQRGRRASKG RRTTGPVAAG GNNGLAGKEN TLPHNNTGKR SQKGKSRGRG
     RDNIVRPEPA DRDSRAGKTS RSGYRPLPGT SRVSSSLAGA SDELSAAQMQ VFLEAGLAMI
     DESPDTRRTF IESLATESGL RKVRQIVETD FAISYSVLQP MFDPHCILFL RLVSHNELLS
     SLILEKAVGT IYNVIYGPGG RRAIGFFTKV TDYLTQFKSD GRSQAVVQHV ATPSEVLSLV
     SRVLLSTLTL NHEAAIQVDL KKIADRLYDC CHADNADARA GDDNLQLAYE NILKIQEIFS
     MGDSIPMSQK PDQVQKIKSN QQNSTRYIVD LPGELSDHGP RHDNDKTAIS DIQILPTKSE
     ILNADRPEFL PARCATGSAN MHHEWGIRRL LDSQFRLLRE DTSGVLREGI RLIIHAWELI
     VHGTDWRLKR KFLRDKMPTP VRVYSGVEIR QIKSEQFKGI EVNLEFDQLP RLKNVSPAKR
     KQWWFDSKAL KKGPTLLALL DAEDVDDTSA IYFLVSKRET SYVDKDKQGS VTGDRVSDVV
     SDGNRAMVTL GLVGPPNPPD LERLVLFSRS KPFPRPLILV EFPAIPYNSF EGILRCLQVL
     HQNPARMPFT AWLAPSTDNH ELCEALKGGS TDAGSISIQP PAYFHKDLLL DLSCLPGQGD
     IEDASQILSM SLSHDPRMLS ADLSRATDLD EGQANAFIWA LRRKIALIQG PPGTGKSYVG
     LQLARCLLHN KDVLDLGPIL CVCYTAHALD QFLDGLLRSS VTNIIRIGPR SASPHIERLS
     LDMRKQEPGP RIKGLPRLKD ESRVKLLSIS SRIDELLKQA QSGCHSLVLG ILKKRFPAQA
     SRITSESPGE TDTNALQAWV SGDAPGVWSE ANIERSIDRL LQEDVWTLKA SERTRLLNYW
     QEAALAEISQ QVLTLLEAHS AEKERYTSAF SLSDVQRLNN CQVVGVTTTQ LANNAELLRN
     LNAKVLICEE AAEVLESHVL TALIPSIQHA ILIGDHLQLR PRISNLRLSM DYERENPKYN
     LDESLFERLA NFRFGESTSS GTGGQNQQEY SFPVMQLSHQ RRMHPSISEL VRETLYPKLQ
     DHPTMTSYPL VPGIARRLFW LDHCNVEDPT DPTEPMQSKT NTWEIGMVTA LVRHLCQQGK
     YGPGELAVLT PYVGQLRMLR NVLEKEMTII ISTTDSDALD EAEGLQVSGP CMNEHGKWCG
     RQRAPQKGSL LDAIRLATVD NFQGEEASVV IVSLVRSNRS RNCGFLKMPN RINVLLSRAK
     HGMYIIGDAT QCLADIPVGG YAGSVDTQRA IPTTSIMAIA EAHAAGDSQL ARTAVAKHVI
     RPLCKDLQRI MPSMRRDMRM GLNVPCDLRC KKKLTSCGHQ CPGLCGERCP DSRLCRICGG
     PDILEHNVDL IELKAYKDIN VDEDPLVFLS CGHFYTASSL DGIMGMSEHY EVESSTGRIL
     GPKLNHRLFD SGRPKGCPQC RAPLRDIDRY NRIIKQAFLD EATKKFSTHA SIKFGHLVEE
     VEGYEKDIIG EKSKFVSDWY QETVETRSAD DVRRSVDVYR GRGNRLLNKI KEFTKSVAKS
     EQPFGRVSEM LASVAARKAG TPAAPFQYNE SDIQTGFQSR GHVLALRLTW VLFWNYDSIY
     SNKRIDPRIK VTLAQVVAKQ IGGLLSQCEA LTKYCQEAKF LQQEVETRTY HVLFSVLSLS
     NREARGNAVS GTTEAKIREK ALKELEACDA ICLRHSKILC YLREDIEKAR RLVNGGTFYS
     CVTSEERRQV YQAMAAQFNG TGHWYYCENN HPFAVGECGM PMEESRCPQC EAPVGGLNHE
     FAQGIRRADD MDVEFGGSLS LEAHTDL
//
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