ID A0A0V0X1B6_9BILA Unreviewed; 1643 AA.
AC A0A0V0X1B6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=peptidylprolyl isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
DE EC=5.2.1.8 {ECO:0000256|PROSITE-ProRule:PRU00277};
GN Name=Adsl {ECO:0000313|EMBL:KRX81753.1};
GN ORFNames=T06_12761 {ECO:0000313|EMBL:KRX81753.1};
OS Trichinella sp. T6.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=92179 {ECO:0000313|EMBL:KRX81753.1, ECO:0000313|Proteomes:UP000054673};
RN [1] {ECO:0000313|EMBL:KRX81753.1, ECO:0000313|Proteomes:UP000054673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS34 {ECO:0000313|EMBL:KRX81753.1};
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=[protein]-peptidylproline (omega=180) = [protein]-
CC peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000256|PROSITE-
CC ProRule:PRU00277};
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:KRX81753.1}.
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DR EMBL; JYDK01000028; KRX81753.1; -; Genomic_DNA.
DR STRING; 92179.A0A0V0X1B6; -.
DR Proteomes; UP000054673; Unassembled WGS sequence.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:InterPro.
DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0007420; P:brain development; IEA:InterPro.
DR GO; GO:0009152; P:purine ribonucleotide biosynthetic process; IEA:InterPro.
DR GO; GO:0032012; P:regulation of ARF protein signal transduction; IEA:InterPro.
DR CDD; cd03302; Adenylsuccinate_lyase_2; 1.
DR CDD; cd08833; ArfGap_GIT; 1.
DR Gene3D; 1.10.275.60; -; 1.
DR Gene3D; 3.10.50.40; -; 2.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR Gene3D; 1.10.220.150; Arf GTPase activating protein; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR019468; AdenyloSucc_lyase_C.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR037278; ARFGAP/RecO.
DR InterPro; IPR001164; ArfGAP_dom.
DR InterPro; IPR038508; ArfGAP_dom_sf.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR047161; GIT-like.
DR InterPro; IPR022018; GIT1_C.
DR InterPro; IPR013724; GIT_SHD.
DR InterPro; IPR008948; L-Aspartase-like.
DR InterPro; IPR046357; PPIase_dom_sf.
DR InterPro; IPR001179; PPIase_FKBP_dom.
DR InterPro; IPR004769; Pur_lyase.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR001440; TPR_1.
DR InterPro; IPR019734; TPR_repeat.
DR NCBIfam; TIGR00928; purB; 1.
DR PANTHER; PTHR46097:SF3; ARF GTPASE-ACTIVATING PROTEIN GIT; 1.
DR PANTHER; PTHR46097; G PROTEIN-COUPLED RECEPTOR KINASE INTERACTING ARFGAP; 1.
DR Pfam; PF10397; ADSL_C; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF01412; ArfGap; 1.
DR Pfam; PF00254; FKBP_C; 2.
DR Pfam; PF12205; GIT1_C; 1.
DR Pfam; PF08518; GIT_SHD; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR Pfam; PF00515; TPR_1; 1.
DR PRINTS; PR00405; REVINTRACTNG.
DR SMART; SM00998; ADSL_C; 1.
DR SMART; SM00105; ArfGap; 1.
DR SMART; SM00555; GIT; 2.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR SUPFAM; SSF57863; ArfGap/RecO-like zinc finger; 1.
DR SUPFAM; SSF54534; FKBP-like; 2.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
DR PROSITE; PS50115; ARFGAP; 1.
DR PROSITE; PS50059; FKBP_PPIASE; 2.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 4: Predicted;
KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW Isomerase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW Lyase {ECO:0000313|EMBL:KRX81753.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000054673};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Rotamase {ECO:0000256|PROSITE-ProRule:PRU00277};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00288}.
FT DOMAIN 483..626
FT /note="Arf-GAP"
FT /evidence="ECO:0000259|PROSITE:PS50115"
FT REPEAT 671..703
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 1272..1360
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT DOMAIN 1389..1475
FT /note="PPIase FKBP-type"
FT /evidence="ECO:0000259|PROSITE:PS50059"
FT REPEAT 1542..1575
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 1576..1609
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
SQ SEQUENCE 1643 AA; 183384 MW; 647AD01103F4CB5D CRC64;
METNVHETYQ SVLSGRYASK QMQTLFSDEH RIARWRKLWI WLAQAEMELG LPMIHPEQID
DMQAHINDID WSMIKTFEKQ LRHDVMAHVH AFELAAPKAK GIVHLGATSA YVQDNADILI
MRDGLQLILE KTATCLHVLS NFAILHKSLP TIGRTHYQPA SLTTVGKRAV QWAQDLLIAF
QHVNFSKSSL LFRGAKGATG TQNSFLTLFG NDINKVRKLD RRICELAGFF DSETEKGCFT
ITGQTYSRMQ DCSVICSLAM LGAAVHKICM DIRMLQCFDE LMEPFESSQV GSSAMPYKRN
PMRSERCCGL ARFLINMPPN AFHTEAIHGF ERTLDDSSNR RLVLPESFLT ADALLLTFQN
ILEGLRVNHA EIARHVDHEM PFLVLEAILM HMTLRGADRQ VAHEKIRLLA LKAHAIREQS
GEYGSEMLQL LKEDCFFEPV WPFLNDLLLP ERHIGLSPMQ VEEFCSRQLF PIIQPYKSKL
LSPSILESIR VEIEMSKTKM TVTSQADILC ADCSAPGPSW ASVNRGVFIC TECCSVHRTL
GRHFSQVRSL SKSYWHSHQL ELVRTLHANG ANNIWEHHLL NPLTGASASK VSRKPKPKDP
LYPVKAEFIR AKYQDLAFSL RRSKDETMPM DLQLDDLNRQ LNSCVRTNHV ETTLRLLVLG
ADPSGFMDPD SGATPVHVAA REGQSLQVEL LFLYGADPAQ PNFDGQTPSA LAEAAGHAEL
ARRLEELEYE ATDRLSFYLC GRMPDHQTGM HFLIPEVATG QLEQNRAVKL RLQRLTDRAL
EKLVQDVYDE TDRRETDSAW AACAKMDQSS ERYVVPFLPV NADLAAPRNQ RRQKLAKFNG
REFTGLQIML LNECKRRLQN RPDVALSDPT SGSEGKKLEC EPLLSVTSVP NSADGPVYDE
VPLESAEMLA DVQAGGGADD FRTLRRCLAT MNRKFDELSL QNKLFQAEIL YLKKSYEQLS
EELKSLKTSE QCYNAESNVP FTTGRMGPAA SRGFEPLNSG QLSTTAGGHH YYWRHRQTAP
KATSRSASMF LGDRTTALNG RLAGMLTTAH RSSLELPVGT TTASSVVVCG AGASGTLGVE
EGGGDNDDDD GQFPSNLVFL TESLTKEIHH ILAAAQAQQH HRFAPLVVRV QSIVDSMVNS
VPPRLRKGTM AQSLDAIVDA CLMLTVHCAG SPGEQDPTEE QFSMNIVKAS YEVAKAAKQL
MYALYVISVS QSSCACAGRL IVSHSVRAMS ESANSTEMKN DSSAEDLTPD HDGGVMKEII
KHGVGSFHPS KGNMVFVHYV GTLTDGTKFD SSRDRGKEFS FNVGREQVIK AWDIAVPTMK
QGEICKITCS PKYAYGEAGA PPKIPENATL IFEIELLRWE GEDISPSRNK TILRSVQVAG
EKRGMPKDES VVDIHIVGIY KGQLFLEKDI SYTLGECEDQ DLPSGVDEAL RHFSKGEKSM
VTLKENWGYG ASGMPAFNIP PNADVEFMIT LNSFTTVKEA WSMSDAEMLE HAENLKEKGS
AFLKDGKVKM AIHKYNLVKN MLEQNTAVEE DALKEKRMNL IKAVFLNLAL AYLKEDDNLQ
ALHSCNKVLT HDPSNVKALY RRGQAHQNRR DYEDAMADFE KVISLEPKNA AALANIAFCK
KQLQNERQRQ RNLYANMLSI SKA
//
