ID A0A178ZQT5_9EURO Unreviewed; 1264 AA.
AC A0A178ZQT5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Alpha/beta hydrolase fold-3 domain-containing protein {ECO:0000259|Pfam:PF07859};
GN ORFNames=AYL99_04215 {ECO:0000313|EMBL:OAP62012.1};
OS Fonsecaea erecta.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1367422 {ECO:0000313|EMBL:OAP62012.1, ECO:0000313|Proteomes:UP000078343};
RN [1] {ECO:0000313|EMBL:OAP62012.1, ECO:0000313|Proteomes:UP000078343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 125763 {ECO:0000313|EMBL:OAP62012.1,
RC ECO:0000313|Proteomes:UP000078343};
RA Weiss V.A., Vicente V.A., Raittz R.T., Moreno L.F., De Souza E.M.,
RA Pedrosa F.O., Steffens M.B., Faoro H., Tadra-Sfeir M.Z., Najafzadeh M.J.,
RA Felipe M.S., Teixeira M., Sun J., Xi L., Gomes R., De Azevedo C.M.,
RA Salgado C.G., Da Silva M.B., Nascimento M.F., Queiroz-Telles F.,
RA Attili D.S., Gorbushina A.;
RT "Draft genome of Fonsecaea erecta CBS 125763.";
RL Submitted (APR-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:OAP62012.1}.
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DR EMBL; LVYI01000003; OAP62012.1; -; Genomic_DNA.
DR RefSeq; XP_018695379.1; XM_018835729.1.
DR AlphaFoldDB; A0A178ZQT5; -.
DR STRING; 1367422.A0A178ZQT5; -.
DR GeneID; 30008384; -.
DR OrthoDB; 1943592at2759; -.
DR Proteomes; UP000078343; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140663; F:ATP-dependent FeS chaperone activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro.
DR CDD; cd02037; Mrp_NBP35; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_02040; Mrp_NBP35; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR013094; AB_hydrolase_3.
DR InterPro; IPR019591; Mrp/NBP35_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR PANTHER; PTHR48081; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR PANTHER; PTHR48081:SF35; AB HYDROLASE SUPERFAMILY PROTEIN C4A8.06C; 1.
DR Pfam; PF07859; Abhydrolase_3; 2.
DR Pfam; PF10609; ParA; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000078343}.
FT DOMAIN 147..260
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT DOMAIN 345..396
FT /note="Alpha/beta hydrolase fold-3"
FT /evidence="ECO:0000259|Pfam:PF07859"
FT REGION 301..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 481..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 661..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 827..862
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 883..924
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 962..995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 661..678
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 680..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 834..862
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1264 AA; 137497 MW; D5E43051CD99C296 CRC64;
MTINTLTAGA AVTPTVIKTC ISHYANRKPR RQKPTAHISY DEGLHLMRTF LLYASHHTVE
DLQSFTAQWV PSPSWVRTES VTITTDHVSK AAKTITAQLG PTGIEQVGGT QWWQWRPKGA
DLKAEWVEMR AHYNELKRQG TKSRRIMLYI HGGAYFFGSV DVHRYQLQRH ARKLKARVFA
PRYRLAPQFP FPCGLQDCLA AYFYLLSIHD PTEIILAGDS AGGGMVVSIL CILRDQGLPL
PAGAVLISPW VDLTHSFPSL SGSAEFDYIP PYGFMQKPST SWPPPNDEEL ATISRLAKGK
DVPLKNKEDG PSTSVPIKDD GNVEPGPQLP LSMELDGKRV VLRDQIQMYT TNQLLAHPLV
SPVLQPSLGG LPPVLILTGG GEILRDEQIY LAHKMANPSK FPLGSIYKAR YDPDGALLAK
YKPTPVQLQV WEDLCHVAPT LSFTRPAKFM YRSVAQFGAW VLAKAQKRAI EIMDDDNISV
ISSQTDNNSL PDTDADSSST GAAKAKLDLN KVTGSVGRAG DPIPPFENNM IRQRIDRHGK
IYPLAEPHEL PALQMHPDQV GVVKPGPVRK WLEAKQTWDT KYARVRTKVQ KERVAALSSG
KIKGFEAGEH PPPCALASRR TDKDLFVKKK RKSYGLAMWS MWGSKHDESV LKREEEAVQL
EKSEDKRLGR EREDGVTPTI VEGEQSSTRW RRSNSGGRSA SAKRQTSQSN TRGRRRTISV
TDRGQAEGRN VPPVVLPSDP ARSKELPATA GNEHSAQDGH IASPESSLLS AGFIPKFKTA
VHLRDDSGGQ HTPVLSDAAS TMTGRSGFVA DDASTRAVFA APGISKSVDS QEVEKAKPSS
PATNTRPGSP LANETRSFVS GSEEFNEGVA SIHLGSELGS VTAGRFHTGA HGNDTPRSQR
SLERLQSHQR DEGMGRLAPL RSPSSTAIVK AEGVVGVVED TEYSRKEGVE DYEMKEGMIE
KEKDINGVGL PRSSAPGSKG PPPTIPRAQR GLPQKRPLRH VRHTIAVSSA KGGVGKSTLA
ANLALSFSRH GLRTGILDTD IFGPSVPTLL GLADAGEPNL TPQNMLVPLT SYGLKSMSMG
YLLPSESAPV AWRGLMVMKA LQQLLHEVDW SPGLDVLVLD LPPGTGDVQL TIGQQVEMSG
AVIVSTPQDI ALKDAVKGVQ MFRKMNIDVL GMVQNMSVFV CPHCHQETKI FAANDTGLSG
AEAKAAELGV DFLGDVPLDA RICADADRGM PTVVAEEAAG VKVNSGYYEH IAEKVARKIG
LGWQ
//
