ID A0A158PP69_ANISI Unreviewed; 1623 AA.
AC A0A158PP69;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 08-NOV-2023, entry version 32.
DE SubName: Full=Major sperm protein (inferred by orthology to a C. elegans protein) {ECO:0000313|WBParaSite:ASIM_0001379501-mRNA-1};
GN ORFNames=ASIM_LOCUS13223 {ECO:0000313|EMBL:VDK49226.1};
OS Anisakis simplex (Herring worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Ascaridomorpha; Ascaridoidea; Anisakidae; Anisakis;
OC Anisakis simplex complex.
OX NCBI_TaxID=6269 {ECO:0000313|Proteomes:UP000036680, ECO:0000313|WBParaSite:ASIM_0001379501-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:ASIM_0001379501-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (APR-2016) to UniProtKB.
RN [2] {ECO:0000313|EMBL:VDK49226.1, ECO:0000313|Proteomes:UP000267096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG Pathogen Informatics;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase A1 family.
CC {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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; UYRR01031341; VDK49226.1; -; Genomic_DNA.
DR WBParaSite; ASIM_0001379501-mRNA-1; ASIM_0001379501-mRNA-1; ASIM_0001379501.
DR Proteomes; UP000036680; Unplaced.
DR Proteomes; UP000267096; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05471; pepsin_like; 4.
DR Gene3D; 2.40.70.10; Acid Proteases; 8.
DR InterPro; IPR001461; Aspartic_peptidase_A1.
DR InterPro; IPR001969; Aspartic_peptidase_AS.
DR InterPro; IPR034164; Pepsin-like_dom.
DR InterPro; IPR033121; PEPTIDASE_A1.
DR InterPro; IPR021109; Peptidase_aspartic_dom_sf.
DR PANTHER; PTHR47966; BETA-SITE APP-CLEAVING ENZYME, ISOFORM A-RELATED; 1.
DR PANTHER; PTHR47966:SF45; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00026; Asp; 6.
DR PRINTS; PR00792; PEPSIN.
DR SUPFAM; SSF50630; Acid proteases; 4.
DR PROSITE; PS00141; ASP_PROTEASE; 3.
DR PROSITE; PS51767; PEPTIDASE_A1; 4.
PE 3: Inferred from homology;
KW Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR601461-2};
KW Hydrolase {ECO:0000256|RuleBase:RU000454};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|RuleBase:RU000454};
KW Reference proteome {ECO:0000313|Proteomes:UP000267096};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..278
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 354..691
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 862..1179
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT DOMAIN 1253..1604
FT /note="Peptidase A1"
FT /evidence="ECO:0000259|PROSITE:PS51767"
FT ACT_SITE 372
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT ACT_SITE 561
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT DISULFID 385..390
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
FT DISULFID 599..637
FT /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ SEQUENCE 1623 AA; 181513 MW; 97CED5989640F147 CRC64;
MQRTLMNLSL ATQSVFLLPC PFAWQPSINA NNKVIQQREC FEIRQKFALV DLLKGFNSDP
ADGVLGLAFA ISASKHLTPP FLNGVPQNVF DQPITTIWMK RHEPQKNVFG GYAVLGGYDD
EKCGAIIYGL GWEVVADTGT SLILGPPHVI EEMVNAIGGE VSNEQMIYVR SSLHLAHRNF
DEVEEFCLHN IDHYDDNYYI ECDLMDKLPP IHFAVRDTSI VIHPQNYVTH MTWDTEACLL
ALGVTGTSSY DPAWIFGNPL YRALCIVEMR NVLIILLLFV SLAIAAVTRV PLTRIQSKRE
RLMSQGKWGE YQRAKNVRRL EIARRMQSKD VVAERVSGHL NFYSNLNDYD DLQYVSKFAI
GTPPQEFNLV MDTGSSDLWV AGATCLSTSC RTKNLYNSKQ SSTFESTDGR FRTGYGDGSG
ASGSIAKDTV HFLGPNGTLV SVREQEFGVA DSLNGFDDDT VDGILGLGFA VLANTHATPP
FLKGVQQHAF DKPIMTIWMK TDGPRDNVFG GYMVLGGYDD EKCGSIMGYK DLSMASYWQF
QMEKVAVHNF NSELGWNVIA DTGTSFIIGP SYVIRKMTDA IGGANVRYDS DNDIYTVSCY
YANRLPQIHF SVGGMSIVIH SQNYVVRFQT TSGADVCVLA LGEMDTDRVG ILQSSSEKSE
AGAPFYEILL YPSLPYPFAV FLRLRKLINV QDSMSIIPLT MSLPRWIVFS SEDSYSRPQY
AIVTIKNVES FPVVYRIRTK DRSFPRFSRC HGYLSKGASE EITIMIPSSE HWPRDPIEFA
GKLLIIRRLQ MTPNREIFIA LLLTCARVFI INAQIFRTPF TYLHAAAAAE ILPEYSHQDV
MSAQNGQLTQ QQVLNNYGNT VIVANITIGT DPSQTFLLVV DTGAADTTVA DITCQSKACH
RKRRFNSTLS KTYSTDHLAW KTKYQNGGSL KGFVGQDVFT LRGSGQSQIR IEKQLFAQIT
EWNHDEKAPA DGTLGLAYRA KAQYHNPTPM DNMASQLAES IFTIWIPRKG TSAEGSSDGL
ITHGGLDLDH CGKMIGYRYL SSARHWQFRM DSVSVGSYTN QKGWEVASET GYAFIGVPKY
VMNHIVKELN LAPAMVNNAY FTNCKQLPSL PTLKFGIGSN IYEMDTNTLF HQRSGMCLSV
LMAIESFGYG NEATWALGVP FAFNFCQTFD FGKQRIGVMQ LIALVVLLNG ISAEVIRYPL
REIDSVRVQL MRSGEWHQRL KAKEILRTTP ISHDIVRQSK NHLQMNDYDD LEYFGVIAIG
TPDPQPFIVI PDTGSSKLWI PDVSCDTAYC AKKHLFNQSL SQTYVADERI WAIGYGDGSG
AFGVTGRDTI TLGDADGEHI RVHNQTFGQA IILIGFTAEP IDGIVGLAFA ELGHDGDIPL
VINAVNQGLL DEPIFTVWMQ HRVRIRYFFS NEFVQFSLLQ ITCKCKHYYQ RSLMKIFQLS
NETLFGGQIT YGGFDRVNCG ELIAYENLTS ATFWQFRMRR IASGNYSNAN GWEVISDTGT
SFIGGPTNVI KKLADEINGT YDQLNDVYMV DCDAKSDGIS LQIGSIDYFI DLSNLIIKVD
EEFCILSLFG FEFDGYGPSW ILGDPFIRQY CHIHDVSNKR IGFAESINDY STNANANFTL
FDY
//