ID A0A0V1CX01_TRIBR Unreviewed; 1413 AA.
AC A0A0V1CX01;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme ATG7 {ECO:0000256|ARBA:ARBA00017647};
DE EC=3.6.4.13 {ECO:0000256|ARBA:ARBA00012552};
DE AltName: Full=ATG12-activating enzyme E1 ATG7 {ECO:0000256|ARBA:ARBA00029897, ECO:0000256|ARBA:ARBA00032823};
DE AltName: Full=Autophagy-related protein 7 {ECO:0000256|ARBA:ARBA00030242};
DE AltName: Full=Ubiquitin-like modifier-activating enzyme atg7 {ECO:0000256|ARBA:ARBA00018730};
DE Flags: Fragment;
GN Name=Y67D2.6 {ECO:0000313|EMBL:KRY53718.1};
GN ORFNames=T03_11081 {ECO:0000313|EMBL:KRY53718.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY53718.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY53718.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY53718.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001556};
CC -!- SIMILARITY: Belongs to the ATG7 family.
CC {ECO:0000256|ARBA:ARBA00010931}.
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:KRY53718.1}.
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DR EMBL; JYDI01000081; KRY53718.1; -; Genomic_DNA.
DR STRING; 45882.A0A0V1CX01; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003724; F:RNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd18791; SF2_C_RHA; 1.
DR Gene3D; 1.20.120.1080; -; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
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; IPR006285; Atg7.
DR InterPro; IPR032197; Atg7_N.
DR InterPro; IPR042522; Atg7_N_1.
DR InterPro; IPR042523; Atg7_N_2.
DR InterPro; IPR011709; DEAD-box_helicase_OB_fold.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR048333; HA2_WH.
DR InterPro; IPR007502; Helicase-assoc_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR NCBIfam; TIGR01381; E1_like_apg7; 1.
DR PANTHER; PTHR18934; ATP-DEPENDENT RNA HELICASE; 1.
DR PANTHER; PTHR18934:SF136; ATP-DEPENDENT RNA HELICASE DHX35-RELATED; 1.
DR Pfam; PF16420; ATG7_N; 1.
DR Pfam; PF21010; HA2_C; 1.
DR Pfam; PF04408; HA2_N; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF07717; OB_NTP_bind; 1.
DR Pfam; PF00899; ThiF; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00847; HA2; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000313|EMBL:KRY53718.1};
KW Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Helicase {ECO:0000313|EMBL:KRY53718.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000313|EMBL:KRY53718.1};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 757..936
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 968..1143
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT ACT_SITE 564
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR606285-1"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRY53718.1"
SQ SEQUENCE 1413 AA; 159838 MW; FD34E0EAD8CCB821 CRC64;
LKAMATVETE EVKLLRFDPF KSTFHPAFWD AVTTKKLEEW KLDETPKDVV GYYQNTTRSV
LPSYFSLDFN SLDPAPKVAG NSFVVHGLLY ILNTLDKFAA VDKKELMTDI GKQREIWNNI
DTKVWLQNPS LLNRFILLVH IDAKKYLYDF MIGFPAFNVS DMFFASEPEQ FSKLDVDFMK
AIQRVCLEAQ RDLLPYFVIL KQDDEYVLKM LNDPICETVT EDKIFLAFAD PSASPKYAGW
PLRNFLKAWK VFRPDFTYVR VICWRYTSFN SIDQPTNSLL LHISMQCDKD AIATFLPVVG
WEKNSEGKVK SVHMDLSAQM DPNKIAQSAS KLNLHLMRWR IVPELNLGLH WQTSCLLFGA
GTLGCNIARC LGAWGFGRIT FVDNGRVSYS NPARQSLYSI KDCIGGRKWK CEAAASALKD
IYPDMEIAGE RITVPMPGHF VDIEGEKEQS FAEDVNRLER LVSSHDIIFL LFDTREARWL
PTLLSCLHNK IAITVALGFD SYLILRHGFG CGKKSASDDS DVHSPLQDVE STTSASGANL
ACYFCCDVTA PGNSTRDRTL DQQCTVTRPG VSMIASGLAC ELVTSLIQHP LQGQAPVEKP
DSGANRSCLG VIPHQIRGYV NRFDQWNLTV ERFASCIACS EPVIDQYKRG GFRFVADVCN
DPTLLETITG LDRLKDDAKD MLVIELAERM IRPDEKLLEN WKNQTTSSIK SVEDRLLLDE
VGVEVNTGIL YNTNLTAFSV QQQRVRLPIY KNRDVILYLI EKYQTLIIFG ETGCGKSTQI
PQVLSIDNFF TAYIVVTYLL EAGWAEKQKI CVSEPRRVAA VTLATRVAEE RASILGHEVG
YVVRFDDFTQ SDKTRIKFMT DGILVREIMK DPLLNQFSVV IVDEAHERNI NTDITLGLLR
KIIAKRPELR LIISSATLDA KEFHNFFNIN DSDDPSRNTS FILSVEGRTC PVDVFHLKRP
IPDYVKASVI TAINIHRTEP PGGDILIFLT GQDEVVNCCD MLKEESKKLK GYDRLWIVPI
YGALPFKEQI KVFDSSPSGT RKVTVATNIA EASITIPGVV YVIDCGFVKM RALHPDTGIE
SLMIVPISQA SAQQRSGRAG RIRPGKAFRL YPESEFDKLR TFTVPEIQRI HLAPALLQLK
ALGINNVLRF HYLSRPPAMS MSRGLELLLA LGGKFSFYHI VNLHGCHVFL YALAIDEDGK
LTSPLGVQMA ELPLPPMHAK ALLVSGSLHC SEELLSIMAM LQVQDIFVSP FGSKHKALKI
LFLFQEIMKR KFSVEDGDHL TMLNVYSCFT EAGKTQRWCA EHYVNYKGLC RATEIRAQLL
TFLRRFKIPI VRRLDAIDRI KQALVSGFFS CAAKLDHTGT YRTIRENFPL KISKGSALMY
RNEYPKWIIF NEVMQDSMRD ITAIDPEWLL MKY
//
