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Database: UniProt
Entry: A0A109FAS4_9BASI
LinkDB: A0A109FAS4_9BASI
Original site: A0A109FAS4_9BASI 
ID   A0A109FAS4_9BASI        Unreviewed;       790 AA.
AC   A0A109FAS4;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=AFG1-like ATPase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=RHOSPDRAFT_23715 {ECO:0000313|EMBL:KWU41050.1};
OS   Rhodotorula sp. JG-1b.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=1305733 {ECO:0000313|EMBL:KWU41050.1, ECO:0000313|Proteomes:UP000062823};
RN   [1] {ECO:0000313|EMBL:KWU41050.1, ECO:0000313|Proteomes:UP000062823}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JG-1b {ECO:0000313|EMBL:KWU41050.1,
RC   ECO:0000313|Proteomes:UP000062823};
RG   DOE Joint Genome Institute;
RA   Goordial J., Raymond-Bouchard I., Riley R., Ronholm J., Shapiro N.,
RA   Woyke T., Grigoriev I.V., Labutti K.M., Greer C., Whyte L., Bakermans C.;
RT   "Draft genome of eurypsychrophile Rhodotorula sp. JG1b isolated from
RT   permafrost in the hyper-arid Upper Elevation McMurdo Dry Valleys,
RT   Antarctica.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the AFG1 ATPase family.
CC       {ECO:0000256|ARBA:ARBA00010322}.
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DR   EMBL; KQ954567; KWU41050.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109FAS4; -.
DR   OrthoDB; 1617at2759; -.
DR   Proteomes; UP000062823; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR005654; ATPase_AFG1-like.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; NF040713; ZapE; 1.
DR   PANTHER; PTHR12169:SF2; AFG1P; 1.
DR   PANTHER; PTHR12169; ATPASE N2B; 1.
DR   Pfam; PF03969; AFG1_ATPase; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000062823}.
FT   REGION          104..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          532..563
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          737..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          598..632
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        104..124
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..558
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   790 AA;  86944 MW;  021A2EE1A547288D CRC64;
     MLVARRRLPL LARSLASPAS SWITRTTCAT RRTASTAASP ASETGIQVAD PLLLYFSLVA
     QGKIKKDEEQ LRALVQIRKL HADLLDYQPP VQLVTLLDSI RSLPSNSKSE SNARSALSNL
     GEGLSESEEQ ERQRLLALSD KEKTTQLVKA LKAHEGLEDL DTPKGFLLTG PPGTGKSLLM
     DLFFQSLPVA SKTRHHYHAF LLWIYQGVHR ALEKQRLENE AEEKAMNELY QANGNKGYPW
     SRREEMKARA ISQGWQSVFA GGRSAHDPAL NTREFVLAQV ALDLIKTQGW LLAFDEIQLV
     DIAGAGLVSR VMSWYWRLGG VVVGTSNRVP EDLYKQGIQR STLSPFLTAL SHRAPVIDLT
     SPTDYRLVSR AEHGLTPETD AAEPGDFGSV DAWKRWGTRS RGWFVKGEID DEAWNEALRW
     IAGDVKGEAT TLSVYGRQVK VPWAAGGVAR FSFKDLCEQP LGPADYISIG SAFHTIIIDD
     VPVLPLSAKN EARRLITLLD ALYESKTRLL ARADAPIDSL FFPDAVNAAA SAPQNTPLDD
     LPTTFSEHEG SQAPGTSAQD AAGEVADSLV EEMLGDVQQD LDAPYRPNVS SYDQSAGVQA
     YERDRARAVE RAEQEEQVAR QLRARREQEG RAPIHPSAAT PSFQSLAIFT GEEERFAFKR
     AVSRVHEMSS TEYLVTAQHS PLPSSIRTWE QTIAQSLAPL TPNTAPAPSL HVMGEKSPLS
     STDRLSGVLD PADLRAKWPE GMPTGDKQVD VRGSQKPVLR EEHVWGVRDD WGKKAGRWGK
     GAKAYSAGED
//
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