ID A0A319DY00_9EURO Unreviewed; 1901 AA.
AC A0A319DY00;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:PYH83782.1};
GN ORFNames=BO82DRAFT_331031 {ECO:0000313|EMBL:PYH83782.1};
OS Aspergillus uvarum CBS 121591.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1448315 {ECO:0000313|EMBL:PYH83782.1, ECO:0000313|Proteomes:UP000248340};
RN [1] {ECO:0000313|EMBL:PYH83782.1, ECO:0000313|Proteomes:UP000248340}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121591 {ECO:0000313|EMBL:PYH83782.1,
RC ECO:0000313|Proteomes:UP000248340};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; KZ821687; PYH83782.1; -; Genomic_DNA.
DR STRING; 1448315.A0A319DY00; -.
DR VEuPathDB; FungiDB:BO82DRAFT_331031; -.
DR OrthoDB; 2971338at2759; -.
DR Proteomes; UP000248340; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR CDD; cd17936; EEXXEc_NFX1; 1.
DR CDD; cd06008; NF-X1-zinc-finger; 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 InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR000967; Znf_NFX1.
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; PF18044; zf-CCCH_4; 1.
DR Pfam; PF20173; ZnF_RZ-type; 1.
DR SMART; SM00356; ZnF_C3H1; 1.
DR SMART; SM00438; ZnF_NFX; 4.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS50103; ZF_C3H1; 1.
DR PROSITE; PS51981; ZF_RZ; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|PROSITE-
KW ProRule:PRU00723}; mRNA processing {ECO:0000256|ARBA:ARBA00022664};
KW Reference proteome {ECO:0000313|Proteomes:UP000248340};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00723}.
FT DOMAIN 14..41
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 1827..1901
FT /note="RZ-type"
FT /evidence="ECO:0000259|PROSITE:PS51981"
FT ZN_FING 14..41
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
SQ SEQUENCE 1901 AA; 213353 MW; CA1B41F957479D5B CRC64;
MSNRGRPNSF RKRNQSETSC VHFQRGRCHY GERCRFSHDL NKAADFKSNP AAYHPTTHDL
DTRNQYFDWK RLLRNGILGS GSSPREHEEI VQFWNGALEI LESDSRENHQ FLAKDLVDDN
LHGYEFILAT ADTDNPEKVR LIPSYDEPFL KVITHTSLLN CLSVDSFVGT LYTSFGGTNG
DRAIRYLRNV CRTLMSKGEE INENVPVISL DMMKLLLNTL YQLLSRVRLA RFHDEIPALL
DLIREVGSQV ETCSKADIDG FESRIEVMQS LIACANRSLF TPRAHEENHQ KRVSAHSSFP
LDMQTPGGRH DNDLAEISQV QILPTHGEIV SGNSEYLPST NFLQPHFLPD PLQRYIDSTF
RLLRHDIFGS AKDALRDLLQ QDDLTRFSHF SSKDNGTHIY LGAQVPQIFI NEKNELEATV
SFATPPQVRK KTSNEQCRWW QDSNRLEEGS LVCFLTSQGT HGRLIFLEVT VKNASKDRAH
QNKSSLASDK FPPSITVKLA ACLQQELLLL CQLYSKKLTG ILVDFHGLIP ATFAPILKNL
QRIQREGELA FKKWILPGRK DSEDGHSIPP PAYARKPGFV FPLTSITNVG AEKVALNPNT
PEAIDLLRLQ TQTGLDHGQC QGLIAALTRE YALIQGPPGT GKSYLGVKLV QVLLEIKKKA
NLGPILVICY TNHALDQFLK HLFDVGIQKI IRIGGRSQAT ELEGKNLRVV SKHIGKTRIE
SQTLGMSYGR LEDCMKSAGY AMKPLHQSQK GLSWTAIQHF LHRKWPIIHE QLARPDTEGF
TTKDQNEKRR ILAMSWFKQW QEIETASLFE ALDRAANLRG DINAVHEEVN RRALIQADVV
GITTTALARH IETLRRVGTK VVICEEAAEV MEAHVISALM PGVEHFIQIG DHRQLRPQIQ
NHSLSLETST GKTWQLDRSQ FERRAVGEPG LKPAPVAQLN VQRRMRPEIS QLIRSVYPKL
EDHESVTNLP NVVGMRNNLF WLDHRYDEDS RDDGSRVKSH SNQWEVDMAT ALVRHLVRQG
EYKSTDIALL TPYTGQLRKL KASLSKDFEI CLSERDLETL AADGLEKFED EYPESNGRKS
LEKKTLLQTL RLATVDNFQG EEAKVIVVSL VRSNSKRKVG FLRTENRINV LLSRAQHGMY
LIGNTETYLN VPMWAGVHSQ LASANAVGTE LALCCPRHSD TPILCYEPHD FERKSPEGGC
SLPCIRRLDP CGHQCQAKCH SAVMHDSFAC GKPCPRIRST CEHACPKLCG EDCGPCMAKI
QDVELPCGHI KKVIFCHQMP NLKVIKCDVK VEKTVPKCGH TIQVGCFKDV TSPTFRCPKP
CTDILSCGHN CSDCCGNCLE EVHDGRRVFK HPKCTKRCDR PHGVCNHRCP KICHNEESCG
YCEAKCEVRC SHSACDLTCG KACAPCIEKC TWSCKHQGSC SMPCAAICDR LPCNERCTKI
LKCGHQCPSL CGEDCPNNLC QECGDKGDAR VDFLEWKTYS EINLDETPII VLGCGHFFTS
ESVDGFVGLD EVYTRDENGT FDGLQDISSS LASAIPSCPD CKQPIRQFVT KRYNRVINRA
VMDETCKRFL IKGRTDLEGL ESRLNDIEDK LNSEPAVLSV GDTKLQLNAR YAACERLGTE
ASTLSKAMEA ENQPMKRLMD AIAIHQKSPR DEIASLSARM EAMDIATRES NNQITLGARL
IYIKSKEVML SDAFRAVDSS GKSATRPRLR FTKPALPLIQ VLKDCQDLIT QANEGNFSRI
VITATISFAK IAQLDRWYHR SHPGETTSDL HLKEKTGLEK LEDRYQTAHN LLAVALKLCD
ELGNCPELQQ KIQEMVRLYE GARYETVTLE ELQSIKTAMV SGRGGLATHS GHWYNCVNGH
PFAIGECGMP MEQARCPECG APIGGQNHTA VEGVSRAREM E
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