ID A0A395MWQ0_9HYPO Unreviewed; 1922 AA.
AC A0A395MWQ0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Zinc finger, ccch-type {ECO:0000313|EMBL:RFN51883.1};
GN ORFNames=FIE12Z_3844 {ECO:0000313|EMBL:RFN51883.1};
OS Fusarium flagelliforme.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium incarnatum-equiseti species complex.
OX NCBI_TaxID=2675880 {ECO:0000313|EMBL:RFN51883.1, ECO:0000313|Proteomes:UP000265631};
RN [1] {ECO:0000313|EMBL:RFN51883.1, ECO:0000313|Proteomes:UP000265631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 13405 {ECO:0000313|EMBL:RFN51883.1,
RC ECO:0000313|Proteomes:UP000265631};
RX PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA Busman M., Gutierrez S.;
RT "Evolution of structural diversity of trichothecenes, a family of toxins
RT produced by plant pathogenic and entomopathogenic fungi.";
RL PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFN51883.1}.
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DR EMBL; PXXK01000089; RFN51883.1; -; Genomic_DNA.
DR STRING; 2594813.A0A395MWQ0; -.
DR Proteomes; UP000265631; 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 Gene3D; 4.10.1000.10; Zinc finger, CCCH-type; 1.
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; IPR000571; Znf_CCCH.
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 SMART; SM00356; ZnF_C3H1; 1.
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}; Reference proteome {ECO:0000313|Proteomes:UP000265631};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PROSITE-ProRule:PRU00723};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00723}.
FT DOMAIN 35..62
FT /note="C3H1-type"
FT /evidence="ECO:0000259|PROSITE:PS50103"
FT DOMAIN 1841..1916
FT /note="RZ-type"
FT /evidence="ECO:0000259|PROSITE:PS51981"
FT ZN_FING 35..62
FT /note="C3H1-type"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00723"
FT REGION 493..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1771..1793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1771..1788
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1922 AA; 215532 MW; FE5AB7B41C957832 CRC64;
MADIQRQAFL LQNDSISTDA FRNAFRNAPR AFGTRNPTHP CFHFKQGTCK FGNRCRFLHD
ASTPLRTSQL NSPDPPGAAS DGKLRQWKRH LNLGDLGWNS SELTTAVVGR FFQLGLEMMD
GDIGAVQDVI KLLAKDAGLA FIRALADVHI PRVDNSRKTT LWETEVKPLF TLITHPRVVD
STVLEQQVAD IFNCILGVEG QRMARIFSFI IDLVTTSVPS TQPDSRMEVL ELSLSVLSKV
IDCNTRNIVN SECNRLVALF AQIVESDHGQ KDEFSRLQAS KYIDYMQQRL DTGKNIPDLD
PSRRVLLARE DFVIRHDLPG TLSADGPRHN NDHVDITKIK IMPTYDEIVS PRGEYLPTNN
PSSWHVKGIR GRLDREFRLI REDTVGQLRD AVRDVLELAR DPKHTKGRQS NTLRTYTYEN
PLTIDVNLHR VGGLEMSICC HQLPVVRKLN AKKRKDWWAQ SKRLQAGALV CLFDVAGSML
FCVVSDTTMR SKDDKEARRI YNDNDQDQAP NDQVRTLSDD QDFLFVNLKL VDPTTSEISL
ALKWYQNIKS YPPRYLVEFP GVLLDSFKHS LSALQKMHEK PNIPFANLLA PKDDSSSDAD
IGLPQYARKI GFTFDLSCLT NDNTPLTTDP RSPITPEALS LKSSLDPTQS AALLNTLTTG
LSLIQGPPGT GKSFTGEKII KVLLKSKQTA KLGPILCVCY TNHALDQLLE HLLDDGTKRI
IRIGSRSKSE RLQNLNLRAI VKGMSLTKSE KSSHWEAERD IREHVEDGKN LLKDLTDCQS
WKAIKFLLAW QYPRQHAELF GEDQDGWKTV IHQPEMVIDR WLQSGQHIAT NPRPLEHLKC
AQLNSLFNHE RILLHRHWIK AIRDPIIVQL ARLNQNYNDA VRRRDEIRGD VDMRCLNDAD
IVGVTTTGLA RNLNLLRKMR CKVMLCEEAG EVLEGHILTA LLPSIEHAIL IGDHLQLRPQ
IQNYDLQSTN PRGKQYSLDV SLFERLVHPP HDTDLRIPYS MLETQRRMHP SIAELVRSTL
YPSLNDAEAV AEYPEVVGMK RRLFWFHHDQ PENADENNSS LSTSRSNSFE VDMTAALVSH
LSQQGAYKPG DIAVLTPYLG QLQLLRRRME SMFEIYINDR DLDELDAAQD EDSRTNRPRG
VPLSKTTLLK SVRVATVDNF QGEEAKVVVI SLVRSNPQGE CGFLKTSNRI NVLLSRAKHG
MYIIGNSTSY KKVPMWAGVM KILASGNNLG TKLELHSLRK ADATLHVTRD CLVGILVLGD
ATQIHCIMLS SAWHPVSVPR KDAITLVLFD AEILVTTTAL SNLRMLFCSL AGTACLHLDV
GKPRIQQLSI AWKWSRRMCQ GASIKCASSV MKMSLLPITN VLLPVGIIAS VDIPVPVVAF
AATHVKTERS RNKTTVYATS AVAESTRPVN ITALRPVTVM HPVSRARNDA KYGAATRGAA
TYCGHQCPSL CGEVCPTSKF CQVCATDEVK SVCVDFLEMK EYKEIDLDQE PCIFPDCGHF
LTVSSMDGQM DMAAHYKLDT NGIPELILRS SEPFAMENED VKNCATCRGP LRSISRYGRI
VRRAMLDEAT KKFISWSNAE YHLLAAKLIT EQEILAAMQP TAIRDPKFEP VGNLTKGGTR
QRQLQCLKGY TDKRYDSMLK MRKDIASYTG KVQKEEQPFQ RVANLVRHAN LHHGGQNEFR
YEESVIQTKG SLLASTLLLK CDVLILSDFF RLLLDQKSDL TKPDVKLDLL PFMRDCYSLI
QGAKKAVYPR EEAQGHIFSA QLCAFSRSLV STPPSPSIPG SETPSTTPAH DPDILDKLRD
QGLDHIQQAR RIVMENHSAA ALKNDIDVAE EALRGGVYRP VTAEELRQVY AASMGELSGT
GHWYTCSNGH PFTINNCGMA MEEALCPECG ARIGGRNHVS VEGVRHAVEI EELAREFGGV
RL
//
