ID A0A0V1MY60_9BILA Unreviewed; 2644 AA.
AC A0A0V1MY60;
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=acylphosphatase {ECO:0000256|PROSITE-ProRule:PRU00520};
DE EC=3.6.1.7 {ECO:0000256|PROSITE-ProRule:PRU00520};
GN Name=rol-3 {ECO:0000313|EMBL:KRZ76711.1};
GN ORFNames=T10_11054 {ECO:0000313|EMBL:KRZ76711.1};
OS Trichinella papuae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ76711.1, ECO:0000313|Proteomes:UP000054843};
RN [1] {ECO:0000313|EMBL:KRZ76711.1, ECO:0000313|Proteomes:UP000054843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ76711.1};
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 + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001171};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an acyl phosphate + H2O = a carboxylate + H(+) + phosphate;
CC Xref=Rhea:RHEA:14965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:43474, ChEBI:CHEBI:59918; EC=3.6.1.7;
CC Evidence={ECO:0000256|PROSITE-ProRule:PRU00520};
CC -!- SIMILARITY: Belongs to the acylphosphatase family.
CC {ECO:0000256|RuleBase:RU004168}.
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:KRZ76711.1}.
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DR EMBL; JYDO01000026; KRZ76711.1; -; Genomic_DNA.
DR STRING; 268474.A0A0V1MY60; -.
DR Proteomes; UP000054843; Unassembled WGS sequence.
DR GO; GO:0071944; C:cell periphery; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003998; F:acylphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004714; F:transmembrane receptor protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IEA:InterPro.
DR CDD; cd00063; FN3; 3.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR InterPro; IPR020456; Acylphosphatase.
DR InterPro; IPR001792; Acylphosphatase-like_dom.
DR InterPro; IPR036046; Acylphosphatase-like_dom_sf.
DR InterPro; IPR017968; Acylphosphatase_CS.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR InterPro; IPR020635; Tyr_kinase_cat_dom.
DR InterPro; IPR002011; Tyr_kinase_rcpt_2_CS.
DR PANTHER; PTHR24416:SF527; PROTO-ONCOGENE TYROSINE-PROTEIN KINASE ROS; 1.
DR PANTHER; PTHR24416; TYROSINE-PROTEIN KINASE RECEPTOR; 1.
DR Pfam; PF00708; Acylphosphatase; 1.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00112; ACYLPHPHTASE.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00060; FN3; 5.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF54975; Acylphosphatase/BLUF domain-like; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 3.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR SUPFAM; SSF101908; Putative isomerase YbhE; 1.
DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1.
DR PROSITE; PS00151; ACYLPHOSPHATASE_2; 1.
DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1.
DR PROSITE; PS50853; FN3; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00239; RECEPTOR_TYR_KIN_II; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|PROSITE-ProRule:PRU00520};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU10141};
KW Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1934..1958
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 253..346
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 645..743
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1120..1223
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 1621..1718
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000259|PROSITE:PS50853"
FT DOMAIN 2006..2278
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT DOMAIN 2553..2643
FT /note="Acylphosphatase-like"
FT /evidence="ECO:0000259|PROSITE:PS51160"
FT REGION 2333..2387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2438..2468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2438..2452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 2568
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT ACT_SITE 2586
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00520"
FT BINDING 2041
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 2644 AA; 299418 MW; E385CBF2AB5CE051 CRC64;
MVSPDLNAAN LARVVSTVVA LSPCRLTCLS ISVFLALFGY GALFCPSADQ WTRASTLLQQ
HCFEDCNLTL MVLPGVFHTS GDYKKKNTFE DLTNECKFGC TYWNPERKKS CLISCEGSAP
YCRGCLNAEQ RWQSCVQQSA SSIRLETAHL PSHEGVQVQW LDRIALDTVY EIVWRLQIRP
FGRYPNLPVH WSDVDTDIQR LSGNVRIAFI SYEKLRSFVD YQLRLVAMHH DRLLARTVPV
QLSHISKTDL SSALLNLHLV TVKETQAYVS WNPNLIKQVP KLKFQVELRT RATNELLIYE
TVNFSYYMFS NLIPGHAYEC TVRGVVSEKT NSVGLSESVV FETHSLVDTL SSDLMKPMLL
YASQSTVSMI KNVDDFLLKT NPTPIFEDKT FKVAALAYGE GDVFIASHDG QIVKFSITDH
SAAIQRAVLL FSLLTHIQSI GYDFTKQQLF VLSNTQIILC KLNSKRCQIV LRTAEIMDNI
VVDSINGFLY GNSGWKIFRA PLADVEALSE IDIPSGMRQS FDNKLKLSID YPAQLLVIHV
NGSVMAYSLT SGRLENIRLN KLHPDSKRSY DSFVKFQSWQ KRLFWISSPC VDALNPADGS
CIYSEEHNPN NGLLSIHNYL LPVNHGKLVD LVLLVPVMRY SLLPSPSNLS AFFTSNSVRM
IWNIGKPFPF QAQLEWREFN FEIEITDNDQ MVYRQAGVDQ LSFVYNGLSA GRRYLLRVRA
CLSVGHCSNW AELSGTTYSS WPDDNDQHQQ QQFSLFSRDQ TVLRFDLSGN VRDSMQPPEQ
PIQFITMADR AGGIFTVGDS VVRRLPRNEL VTRLQSEEPI SAIAYEPFGQ EMYWTSKSGM
FRQSLKESNL LKISSDGLIQ WFHLLPNQGL VVLGSCDHVY TLYLTGMFHR RYFSCDNVDC
QILGVSVSED ADSAVVYYLV EQGDSVVLNS VDVKNEKTNT LAKADAFSSR PNVWTAIKIF
YVVNNNKLVI LSRNGQLMLV EPDLQSVSVY PFEQVVHIIR VLNSWPYNIT WSPPCCLTVD
LKLGDPNEPR PFLQWNDTNS DNLPSDVPFV KYYNLSMLAG EKNNEKLVSA TITEDNEIAI
GADVLEKKDF NVQLMEIALW RRAHVSKTFT APDMFPLPPA QTALNVVHIK SPFNITADVI
FSWTPVVWNG KPKFYKIYCW RFDGDSKNRT YLVKGKEIDW RSTRYDISKI SQNWTIYCSV
SAVNANKGES KLTVPISVVT SENSPPSIIL IVTSSGLYQY HVDFERVLDS TISGPYKAAT
YGKDFIYAIR NQSEGDYLMK FHSYGLAVIE QLPLSKYLSS ATLLTFDWIG ERVLLVGRSR
QHGHIQGDSI YVISLDNEAE PRSLFTTHPG YEILNIAYNP MDRYSTLVFI RKKHQIYFVE
SFGGKYSLKS WLSGSDQLLT FECVPSSPVF SMNFLNPAAV EPSSFMITGN GIADSKNCTI
IIDASHLYGV EMNEVVSLSH DVNHFYLVER ESLHILNRKR LEIVELSFTG VRQVLSTSPQ
YQPLPDIECM KLPSTVKSFT VTSLSNTGVL ITCVISDKPS DCGNVTDLPI NYELKLTPQT
KKNFEDIRQS LIKESRSVTF HVEGLVPGIE YMVKVKWWNR FTKPTTYKPG PLSFYTSYLI
PVQNLDAFTI APDKVQLLWI PFIDADSNQP IPVDYRIVMQ NYENNTLQEV VSCSTNPCQY
LFKNLDPLTL YFVQAYAIDL PKQSNMVDEQ HKMVTSSTIN VTTFDLPVRY DEKDFTSSHT
SIAFQLAENT SPSLQQITVE YQLADETVWH VIEASWVEKE KRGYRIDNLK QNQAFLFRAH
AKYSTNRIYM GTLRSFADTF NQQLPPITTK GQAVQMSMKV ELVQLNGKKH LKWKILNNAD
NFIVQNFIVS YRANSNVDWV KFEVLPATTY STLVPEPVSN EDRDMQFRVE AVADDNVIMS
GYWQPDTEDS LSPAVIATVV FISILLTALI FVIVICTIRR KKLSRHMSRR MPEEKKQTFV
PNTPEVLDQL PAEDLNSLPH IPRSCISIVR ELGRGAFGEV YEGLAYNLPK FGPKSLPVAV
KTLRPGSTYA EKVRFIKEAI LMSHFDHPNI VALRGVCFET EPHWIILELM EAGDLLKYLR
SVRATNSMPS QVSLKDLLCI TIDVARGCTY LEEIHHVHRD LAARNCLITS RNPTMRVVKI
GDFGMTRDVY EEDYYRVEGH GLLPVRWMAP ESMIDGVFTT KTDVWSFAVL LWEVMTLGKQ
PYSGRSNWDV LNYVRIGGRL EKPPSCPIEM FEIMLACWAF EAKDRPAFSA LLYRLMSLSD
LPEYNSDQPF PQFNGISPMR HSTDLTSGSL NSYSDDKVKV CATRSSARFF RGKNSSSVAE
KTKSRGSSFR SLRKKKKEHA PPLPSKEEVN MPPEMRLSTG RPASQVSSSG TESIVLFGSD
AYEIPLIRNL SKSARSELKK LNASEPQYHQ NFALDIGETS PSEQSSYGPT VVSRLPEGSF
PPVPSVQAPR RTKKLNKEIP VEENSKTAAQ FDDTYENVRD DVEVPKLHFM PSRNQKFASK
LMRCCAVLKT VLISSILYSR SVSTLEMSKS LLSVDFEVFG KVQGVFFRKC TVEKAKDLGL
VGWCQNTKTG TVVGQVEGPK NEVNEMKIWL ENVGSPSSRI DKAVFKNEKE ISTLNFNSFD
VKRA
//
