ID A0A0J6YC79_COCIT Unreviewed; 713 AA.
AC A0A0J6YC79;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Ubiquitin-like conjugating enzyme {ECO:0000313|EMBL:KMP04408.1};
GN ORFNames=CIRG_04099 {ECO:0000313|EMBL:KMP04408.1};
OS Coccidioides immitis RMSCC 2394.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX NCBI_TaxID=404692 {ECO:0000313|EMBL:KMP04408.1, ECO:0000313|Proteomes:UP000054565};
RN [1] {ECO:0000313|Proteomes:UP000054565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RMSCC 2394 {ECO:0000313|Proteomes:UP000054565};
RX PubMed=20516208; DOI=10.1101/gr.103911.109;
RA Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA Taylor J.W., Rounsley S.D.;
RT "Population genomic sequencing of Coccidioides fungi reveals recent
RT hybridization and transposon control.";
RL Genome Res. 20:938-946(2010).
CC -!- SUBCELLULAR LOCATION: Preautophagosomal structure
CC {ECO:0000256|ARBA:ARBA00004329}.
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DR EMBL; DS028094; KMP04408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J6YC79; -.
DR STRING; 404692.A0A0J6YC79; -.
DR Proteomes; UP000054565; Unassembled WGS sequence.
DR GO; GO:0000407; C:phagophore assembly site; IEA:UniProtKB-SubCell.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.140.100; Ubiquitin-like modifier-activating enzyme ATG7 C-terminal domain; 1.
DR Gene3D; 3.40.140.70; Ubiquitin-like modifier-activating enzyme ATG7 N-terminal domain; 1.
DR InterPro; IPR032197; Atg7_N.
DR InterPro; IPR042522; Atg7_N_1.
DR InterPro; IPR042523; Atg7_N_2.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF3; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME ATG7; 1.
DR Pfam; PF16420; ATG7_N; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 4: Predicted;
FT DOMAIN 1..362
FT /note="Ubiquitin-like modifier-activating enzyme Atg7 N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF16420"
FT DOMAIN 381..605
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
SQ SEQUENCE 713 AA; 79202 MW; 062215A74B50FA5D CRC64;
MQYTPFISDI EIPFFSSLAT LKLNHDKLDD SIHNILGFYE VRPSDPQEVS CRMQVPGNAL
VADKVPFGAF RAEGVIKNFN TAEEYRIVDK SAMLHDAGKR IWDAIMDGSV YSSPSLLASF
LMLSFADLKK YRFSYWFAFP AIHSNPPWVP SPVHHDSRDL DKSENAIHQS SFSLTNSDRD
ALVDAVLAWR STVEPRQHGF FLARRVRHLP SQPQLESNIP TDPGSNASPL QAPDYNKCNC
TWEVSSLSTY ENGFFGNAAA EDCFICFVDP SNYPDAPGWM LRNLLILIRH KWRLNKVQII
RYREIPSFAM GPQSTVMILK SDTSIDDSFS RSGSLVMPKL SGWERNANGK LSGRLINLTE
HMDPERIADQ SVDLNLKLMK WRITPSLNLD VIKRTKCLLL GAGTLGCYVA RNLLAWGVQT
INFVDNGSVS FSNPVRQPLF GFHDCLYGGA KKAVRAAEAL QEIYPGVCST GHVLSIPMVG
HPMVNNNAAK SDYEHLKNLI DQHDAIFLLM DSRESRWLPT VMGKAAGKMV MNAALGFDTF
VVMRHGTTAR RQESVLGCYF CNDIVAPANS TRVQTLDQQC TVTRPGVASM ASALLVELFV
SALQQFNTPP APDSSSHGNS SHPLGIVPHQ IRGFLSTFSN VVVTGQSYEF CSACSNNIVH
AYITDGWEFV QRAINENGYI EEVSGLKKVQ QSAEEAIASL ELEDPLDSEG EML
//
