ID A0A6M3ZA73_9ADEN Unreviewed; 828 AA. AC A0A6M3ZA73; DT 07-OCT-2020, integrated into UniProtKB/TrEMBL. DT 07-OCT-2020, sequence version 1. DT 14-DEC-2022, entry version 7. DE SubName: Full=ORF19A {ECO:0000313|EMBL:QJP03699.1}; OS Fowl aviadenovirus 5. OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes; OC Rowavirales; Adenoviridae; Aviadenovirus; Fowl aviadenovirus B. OX NCBI_TaxID=172861 {ECO:0000313|EMBL:QJP03699.1, ECO:0000313|Proteomes:UP000503087}; RN [1] {ECO:0000313|EMBL:QJP03699.1, ECO:0000313|Proteomes:UP000503087} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LYG {ECO:0000313|EMBL:QJP03699.1}; RA Chen H.; RT "Genomic characteristics of fowl adenovirus 5 from ducks related with egg- RT drop syndrome in China."; RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}. CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. Lipase family. CC {ECO:0000256|ARBA:ARBA00010701}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; MK757473; QJP03699.1; -; Genomic_DNA. DR Proteomes; UP000503087; Genome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW. DR GO; GO:0016298; F:lipase activity; IEA:InterPro. DR Gene3D; 3.40.50.1820; -; 1. DR InterPro; IPR029058; AB_hydrolase. DR InterPro; IPR018247; EF_Hand_1_Ca_BS. DR InterPro; IPR013818; Lipase. DR InterPro; IPR000734; TAG_lipase. DR PANTHER; PTHR11610; LIPASE; 1. DR Pfam; PF00151; Lipase; 1. DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1. DR PROSITE; PS00018; EF_HAND_1; 1. PE 3: Inferred from homology; KW Membrane {ECO:0000256|SAM:Phobius}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 780..800 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 23..169 FT /note="Lipase" FT /evidence="ECO:0000259|Pfam:PF00151" FT REGION 570..616 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 707..743 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 579..613 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 722..740 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 828 AA; 92816 MW; D01F1FA777AE5D1C CRC64; MPCKPGVYRR MWDHGILRQG RESNIIFLVH GWHGVQSSFK MFFPMLRFHQ KLTPNAAVIL VDWGVQGSDQ LVLAHAATSS VQLNITDFLI DIDPNKSKVH CIGHSLGGHA CGAICRRYIN LHQTKCDRIV GLDPASVPFK HNSPYPYLID RSVSKHDADY VAVFLTNSNF MGLHDFVGDE YITANVYGYY SYDCPFMGKW WGGVCAQNYL GMKVCENMDV GTMFNSGIIP HTLDSCSHMM ALLVFMKSLD VRTGFSLLRF EGNPPKSHHK GHLPSVWNGY VVSKDYRYDT FFNSETIVYS THLDTYGIQL KPAYSVTALI SRGCQPQLDK AYHEQVINYG SKYQIISGFM PYNAHDGSTP FMEKIWFSYE PCTLYAVRRM TQEGFVMNMT YGVRDGIPMP GHTIENLWCS KYNSPSSLYY GLFYCKNTYQ YWHTNAYRSM MSGLAKNSSL PSPAVPPTQG CLFDNTNSTD LLRTYLGSRH LKTNQRINIK ITETDWQFSL IRVTLWDPSD RKVHTLMTYW DSCKTSTPVN MRLDRTTQSV TIYFTKPGEY WMSFFFEWEE VNLRFKVTAL PTPKPPTTTP TTTTTTTTPT PTTTTPTTTT SASRATPSSE SSLPELCDED EDEDCWFASI GGNIYTPVPY EVPSGSNGDD DTDGEVDYSD FVIIGEDSNY KEGTANPNPT TTIPEEITIT ISPGTREPMT TEEELMYTRM TSSTPSPSEK APKSDVEPEL GNRIPEGIEE DPSEAPFITV LDNEIRAGAR VGEERDESSS ALSNPQTTPL VAAAIVGAVA LVAIAVMVAF RKGRTTKKTP PRAIYIAVPQ PDVELPNV //