ID A0A0V1CUU2_TRIBR Unreviewed; 903 AA.
AC A0A0V1CUU2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Aldehyde dehydrogenase, mitochondrial {ECO:0000313|EMBL:KRY52914.1};
GN Name=ALDH2 {ECO:0000313|EMBL:KRY52914.1};
GN ORFNames=T03_15680 {ECO:0000313|EMBL:KRY52914.1};
OS Trichinella britovi (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=45882 {ECO:0000313|EMBL:KRY52914.1, ECO:0000313|Proteomes:UP000054653};
RN [1] {ECO:0000313|EMBL:KRY52914.1, ECO:0000313|Proteomes:UP000054653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS120 {ECO:0000313|EMBL:KRY52914.1};
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 -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000256|RuleBase:RU003345}.
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:KRY52914.1}.
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DR EMBL; JYDI01000096; KRY52914.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1CUU2; -.
DR STRING; 45882.A0A0V1CUU2; -.
DR Proteomes; UP000054653; Unassembled WGS sequence.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:InterPro.
DR GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd07141; ALDH_F1AB_F2_RALDH1; 1.
DR CDD; cd02620; Peptidase_C1A_CathepsinB; 1.
DR Gene3D; 3.90.70.10; Cysteine proteinases; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR025660; Pept_his_AS.
DR InterPro; IPR000668; Peptidase_C1A_C.
DR PANTHER; PTHR11699:SF302; ALDEHYDE DEHYDROGENASE; 1.
DR PANTHER; PTHR11699; ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF00112; Peptidase_C1; 1.
DR SMART; SM00645; Pept_C1; 1.
DR SUPFAM; SSF53720; ALDH-like; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
DR PROSITE; PS00639; THIOL_PROTEASE_HIS; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW Reference proteome {ECO:0000313|Proteomes:UP000054653}.
FT DOMAIN 654..901
FT /note="Peptidase C1A papain C-terminal"
FT /evidence="ECO:0000259|SMART:SM00645"
FT ACT_SITE 299
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007"
SQ SEQUENCE 903 AA; 101042 MW; 2FED45E753FCA4A1 CRC64;
MAFSRQVINK FRLFVAPVQY YCSVAAAAEI PNPFPVWKVE PKYTKLFISN EWIDSADGKT
FKTINPTTGE VICEVQEAKE VDVDKAVGAA KLAFQPGSAW RKTEPYQRSK LLHRLADLLE
RDRVYLASLE TLDNGKPYVE SYTDDMEMVI RCIRYYAGWA DKIHGKTLPT GKENMFLDGN
FFAYTRHEPV GVCGQIIPWN YPLLMFAWKL GPALACGNTV VLKPAEQTPL TALHVGSLIA
EAGFPPGVVN IVPGYGPVAG HALACHSNVD KVAFTGSTEI GRKIMSNSAN SNLKRITLEL
GGKSPNIVFA DADFEHAVKQ AHSGLFSNQG QICCASSRIF VEGKVYDKFV ELSVQMAKRR
RLGNPFDPNT DQGPQIDQNH RERILNFIEK GKQEGAKLAC GGRAAGEKGY FVEPTVFADV
QDPMVIAQEE IFGPVMQIMR FDSMEDLIEK ANNTIYGLAA AVFTKDIDKA LHVANNMRAG
VVWVNCYGIF DSTAPFGGYK MSGFGRELGE YGLEAYTEVK TVCICESEDH VEMTKIVYTI
FFLLKVVQNF STEFLKMIVA VLLFTLFLQH SYSAYYEDRF GTFLDNVHKL KNKFETDWQF
GLNEYFKGMS KEDIRIRVDG LSKELAKFKF ANRRENAIRN QQNYTDAKSE SLPLEEHFDA
REKWPECKYI GFIKDQSTCS CCWAMSSASV MTDRTCIAYK GEQQPFLSDE ELTSCCTSCG
YGCNGGFPLL AFKYWNEIGV PTGGPYGSKS GCKPFSIAPP TSSSTAAQTP LCQLKCISDY
KRKLDKDRYY GESYYLITSS NQPVKTIQRE ITDHGPVVAA MEIFESFLYY KSGVYSASKH
NDDPSLGLHA VKLIGWGEQK RIPYWLAVNS WNTTFGEQGL FKIRRGTNEC GIENLHVTAG
LAE
//
