ID A0A0V0U877_9BILA Unreviewed; 1409 AA.
AC A0A0V0U877;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Sphingosine-1-phosphate lyase 1 {ECO:0000313|EMBL:KRX47339.1};
DE Flags: Fragment;
GN Name=SGPL1 {ECO:0000313|EMBL:KRX47339.1};
GN ORFNames=T05_11862 {ECO:0000313|EMBL:KRX47339.1};
OS Trichinella murrelli.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=144512 {ECO:0000313|EMBL:KRX47339.1, ECO:0000313|Proteomes:UP000055048};
RN [1] {ECO:0000313|EMBL:KRX47339.1, ECO:0000313|Proteomes:UP000055048}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS417 {ECO:0000313|EMBL:KRX47339.1};
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50};
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:KRX47339.1}.
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DR EMBL; JYDJ01000044; KRX47339.1; -; Genomic_DNA.
DR Proteomes; UP000055048; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IEA:InterPro.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:2000431; P:regulation of cytokinesis, actomyosin contractile ring assembly; IEA:InterPro.
DR CDD; cd17733; BRCT_Ect2_rpt1; 1.
DR CDD; cd06450; DOPA_deC_like; 1.
DR CDD; cd01229; PH_Ect2; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 6.10.140.2150; -; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.50.10190; BRCT domain; 3.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR001357; BRCT_dom.
DR InterPro; IPR036420; BRCT_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR026817; Ect2.
DR InterPro; IPR049396; ECT2_BRCT0.
DR InterPro; IPR049395; ECT2_PH.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR PANTHER; PTHR16777; PROTEIN ECT2; 1.
DR PANTHER; PTHR16777:SF2; PROTEIN ECT2; 1.
DR Pfam; PF21243; ECT2_BRCT0; 1.
DR Pfam; PF21242; ECT2_PH; 1.
DR Pfam; PF12738; PTCB-BRCT; 1.
DR Pfam; PF00282; Pyridoxal_deC; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00292; BRCT; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF52113; BRCT domain; 2.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS50172; BRCT; 2.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
PE 4: Predicted;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:KRX47339.1};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000055048}.
FT DOMAIN 129..203
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 223..311
FT /note="BRCT"
FT /evidence="ECO:0000259|PROSITE:PS50172"
FT DOMAIN 389..579
FT /note="DH"
FT /evidence="ECO:0000259|PROSITE:PS50010"
FT MOD_RES 1195
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRX47339.1"
SQ SEQUENCE 1409 AA; 160496 MW; 5C508AD5438DA2CF CRC64;
LFWQTFPMLT NDEHIACSVL ESEQIENDEK TIKGINQTED EIRAICLVGS VAHDDKLKEV
LKTVFNLLVY ESEKGVEYIS QKDVAFVLEN FSGPDFNYLY HAGRRIFGPT IIFESSQSSA
KLPIKSRPLY CNAMKEVTVC FAGLHDKKVL SNVVDLVHHM GGSVRKNFTM SVTHVVTNTT
QSSKYRLAVG MGKAVMHVDW IFKMWERRSN AHVSALSPDW SCFKLKPFFA LKLYFRGFLP
NEENHMKELA IQNGAVVTDC NACTHFVVDP SVRYEDLTDS DRNLQCRFVT AEWFWLSIQL
DICANEDMYT LMDKDQKCRK RSKSPAVFEN KRHAKRLSEF HGSGDLNPFS SHCSSLDVSS
DYSSMLGDQM FSSEDLDNLM KSPKKGMSKR QQIAVEMLQT EFKYVQVLHT IITIYKEPLE
SPDSTVGGHL LDSAEMKLIF GNLPPIYVIH QKLHKELANL IAHWSEDRCI GNVWLQHADE
LVKAYPPFVN FYERTKETLN KCDKSKPRFH AFLKARQNRP ESNRESLQEL IIRPVQRLPS
VILLLSELLK NTDKANKDYQ CIAKAIDALK RVLTHINEDK RKTEGQVKLF DIVNEIENCP
PYLLSSQRQF ITSISVTSLS HGFVKKGSQC VFYLFNDCLE VAKSRQKTNG REETRTLHAT
LKPYKHAELL FLSNIRRVID VTCFEEASNI FCLTIRNNMG DTNYPFQLVD ETANEARRMF
LEKLCDQVLK TVGRVDFCLQ SLQSADADGD SDLALTIQKA IKHLKYGGRR LSRAFSFNKT
QTSLRRAVSQ IAVNVGGHLR RMSSREKRSL NRQVPSRQLF DGICFCMEKL YNDIRMFVFS
CFLASIHLID WCRRLYNVTF GELEPWQISA YTFCAFSVFL WLDKFFHCEE AFVVRLEKTL
FRTARRLPWV KRKISVQLSK TRQSVQMELQ KNDPDPEFIR HLPDRGFDQN DIIAKAERYQ
KAVSNCQHVM RVMCLKRTFD FSKGKVSGAV YNANVELLSL NAEIMKLFCW SNPLHPDIFP
GIRKMEAEIV RMVCNMFNGG NNACGTVTSG GTESLILACL AYRNRAYGRG NKDPEIVVPI
SAHGAFDKAA QMLRLRIRHV PLEAGTFKVD LDKMKQMITK STCMLVASAP NFPYGIIDPI
EQVAALGEKF GIPVHVDCCL GGFLLPFMER ADYPLDEEFD FRIRGVTSIS CDTHKYGFST
KGTSVLMYRN KLYQRYQYFC QPNWPGGIYA TATVAGSRNG ANSASCWATM LHFGIHGYVQ
CTRKIIRTAR YIERKLREVK GIYIFGHPRV SVVAFTSYVF DIYAFASQMG DRGWSLNLLQ
LPPAVHFCIT MNQTLEGVAH SFIEDATAVA EALLEDPSKS NDISGAAALY GSSQTLPDRT
LVNEIACAYL DACYATETKC DPDDLDGLI
//
