ID A0A0V0XM12_TRIPS Unreviewed; 841 AA.
AC A0A0V0XM12;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=4-coumarate--CoA ligase-like 7 {ECO:0000313|EMBL:KRX88988.1};
DE Flags: Fragment;
GN Name=4CLL7 {ECO:0000313|EMBL:KRX88988.1};
GN ORFNames=T4E_1596 {ECO:0000313|EMBL:KRX88988.1};
OS Trichinella pseudospiralis (Parasitic roundworm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=6337 {ECO:0000313|EMBL:KRX88988.1, ECO:0000313|Proteomes:UP000054815};
RN [1] {ECO:0000313|EMBL:KRX88988.1, ECO:0000313|Proteomes:UP000054815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS141 {ECO:0000313|EMBL:KRX88988.1};
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 -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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:KRX88988.1}.
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DR EMBL; JYDU01000213; KRX88988.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0XM12; -.
DR STRING; 6337.A0A0V0XM12; -.
DR Proteomes; UP000054815; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR GO; GO:0004089; F:carbonate dehydratase activity; IEA:InterPro.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd00326; alpha_CA; 1.
DR CDD; cd05911; Firefly_Luc_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 3.10.200.10; Alpha carbonic anhydrase; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR001148; CA_dom.
DR InterPro; IPR036398; CA_dom_sf.
DR InterPro; IPR018338; Carbonic_anhydrase_a-class_CS.
DR PANTHER; PTHR24096:SF426; BCDNA.GH02901; 1.
DR PANTHER; PTHR24096; LONG-CHAIN-FATTY-ACID--COA LIGASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00194; Carb_anhydrase; 1.
DR SMART; SM01057; Carb_anhydrase; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF51069; Carbonic anhydrase; 1.
DR PROSITE; PS00162; ALPHA_CA_1; 1.
DR PROSITE; PS51144; ALPHA_CA_2; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 3: Inferred from homology;
KW Ligase {ECO:0000313|EMBL:KRX88988.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW Reference proteome {ECO:0000313|Proteomes:UP000054815};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 384..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..265
FT /note="Alpha-carbonic anhydrase"
FT /evidence="ECO:0000259|PROSITE:PS51144"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX88988.1"
SQ SEQUENCE 841 AA; 93607 MW; B3737E9D18635C20 CRC64;
LSMNPSWSYW EDGGPKFWAK SYPLANGSAQ SPVDIANYIT DNSLPENGPT IHYQMNDLTS
IFNTGTTWQL RCAADSKSCM HVVSKQLSAP YKLKQIHAHW GTNGTNGSEH TINGKGYAGE
IHLVHWNTNY NTIEEAVNRR DGVNVLAVLV EESSTENIAL QPLIKFMRKI PEKNDTYTIE
EPFDATALLP NVRNYFTYEG SLTTPPCNEC VIWTIFETPI AMSSSQLDAF RSLRTCCETL
DGKRNILCNV RPVQPLNGRE GEIAELNGDK LFTFVEKLLL KSANGASDPT ADSWITESFA
LLEGTMPICS TVGDVKIEKQ TLHECVLNAI VQYDEQTLLC INSETGKSYT CRDVVLIIQA
ITTWLDGKVK KGDVVVICAS NTPYFMFTLL AVLLHGAVVS AVSATLTSRE MGYQFKECQC
KFVVTESKNK NNVLEACEHL PDQIEHIFDM DDFSNLLLKE DGRSAETIVR ELLANFCFVT
ANDLAMMMFS SGTTGYPKAV MLTHSNVSSI VQILKCDAFQ LIPEQNKVIL GYLPFYHIYG
NVLFLLGIIS GCKIVTMEHF KLEIFLQLIE KFRVENLFVV PPILVMLLKH SKVDKHDISS
VKKIIVGAAP IGKDLFDEVT KKFTHIKSVV QGYGMTEVSG VSHITKPFSV KVQKGSCGRL
LPNYECKVID IESGEELPAG KSGEICLRSP TCTIGYFGNS SATEQLIDTN GWIHTGDIGY
YDEDGDFFIQ DRIKEMIKVK GFQLCPAELE ELLLSFPDIT DAAVVGIPDK YCGEVPFAFI
VKKPNSAISA LEIAKNIEKQ VASYKHLAEK HIAFVESIPK ASTGKILRRK LRELIQFQPK
I
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