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Database: UniProt
Entry: A0A0M9A942_9HYME
LinkDB: A0A0M9A942_9HYME
Original site: A0A0M9A942_9HYME 
ID   A0A0M9A942_9HYME        Unreviewed;      1577 AA.
AC   A0A0M9A942;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Ovalbumin-related protein Y {ECO:0000313|EMBL:KOX79755.1};
GN   ORFNames=WN51_11365 {ECO:0000313|EMBL:KOX79755.1};
OS   Melipona quadrifasciata.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC   Anthophila; Apidae; Melipona.
OX   NCBI_TaxID=166423 {ECO:0000313|EMBL:KOX79755.1, ECO:0000313|Proteomes:UP000053105};
RN   [1] {ECO:0000313|EMBL:KOX79755.1, ECO:0000313|Proteomes:UP000053105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=0111107301 {ECO:0000313|EMBL:KOX79755.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KOX79755.1};
RA   Pan H., Kapheim K.;
RT   "The genome of Melipona quadrifasciata.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the serpin family.
CC       {ECO:0000256|RuleBase:RU000411}.
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DR   EMBL; KQ435710; KOX79755.1; -; Genomic_DNA.
DR   STRING; 166423.A0A0M9A942; -.
DR   OrthoDB; 3182479at2759; -.
DR   Proteomes; UP000053105; Unassembled WGS sequence.
DR   GO; GO:0005615; C:extracellular space; IEA:InterPro.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.39.10; Alpha-1-antitrypsin, domain 1; 2.
DR   Gene3D; 3.30.497.10; Antithrombin, subunit I, domain 2; 1.
DR   InterPro; IPR023795; Serpin_CS.
DR   InterPro; IPR023796; Serpin_dom.
DR   InterPro; IPR000215; Serpin_fam.
DR   InterPro; IPR036186; Serpin_sf.
DR   InterPro; IPR042178; Serpin_sf_1.
DR   InterPro; IPR042185; Serpin_sf_2.
DR   PANTHER; PTHR11461; SERINE PROTEASE INHIBITOR, SERPIN; 1.
DR   PANTHER; PTHR11461:SF387; SERPIN DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00079; Serpin; 1.
DR   SMART; SM00093; SERPIN; 1.
DR   SUPFAM; SSF56574; Serpins; 1.
DR   PROSITE; PS00284; SERPIN; 1.
PE   3: Inferred from homology;
KW   Protease inhibitor {ECO:0000256|ARBA:ARBA00022690};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053105};
KW   Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1577
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5005831088"
FT   DOMAIN          1158..1574
FT                   /note="Serpin"
FT                   /evidence="ECO:0000259|SMART:SM00093"
FT   REGION          463..491
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..756
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          916..940
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          968..1009
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1022..1053
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1082..1114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        968..992
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1029..1053
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1577 AA;  172008 MW;  D6E3EB531F056B07 CRC64;
     MSTGLFHAAL TTVVFWTCLS FSVGSERPVS ETATTVLLPM KYTKSRATTY QEISGIREPE
     GARNEAVRAT QANNRSPSPA GVNFYRLPPS PANLLKPDGF QFYTYNERGD MITKQMTMQE
     IQALIASGGP DHSNVEVQEP QKAEDILTGG KKVMDVVEKV QNVLKSAMDK PLSALSGSHP
     MIPEKVNVEW SNILPAILAG DKYGNKVEES HHVERPTSKP MSKPASTYYV AHNQNDSTLD
     SLESNASETV PSEGLENVKV EKNGTQPTIA TKPTTVSYTE KLMIPVPVIT TERNAESIGN
     SQFTTQSPTF HKLTEATPLL ENTTYGSYDR DDENLTSVNP VTKSTTTGVS LLASTLQLDE
     STKSSYDNAD LVSEILHPEK NNSHVDETVT DSLVTQTKIK PVIIGTSSTE DDEVLMKTQT
     PPVVEANQVQ TVITNEPFSK LPLQYSVSVP ATTNKHKITS VTEQLTTTQQ DTVTKPSDRL
     SGSVEPSISS PSMELVSSLS NVISQISDDT VSPVLSSSFG FQSTFSGNEN KRNNGSEIIA
     TYSSTINGDR PENVNATSDE ERIQESFTDT TVKFKTDRER ISLTAATTPI ISTNVTELDK
     TTNHNVSTVS TKFDGITSVH PVSNVTEAPM SINETSATTF NSFQPIALID SILYTASPET
     NTPVTESITL PSDLSENLLA NTLASSLIAN PSNLKINKTQ TVLDETTTSY SEKLNSTDTV
     ALNSKLPISI NKDIMNDTMK KDPTNENEVS RTSTTKEHLF TEQQKIESSQ LQNELSVTSE
     STTTSSFITA DSVLKNAVET DGISGTLFAN NTLNEQTSNP IYETTISSNE ASTTSTNTRV
     IVPNVENVTE EASQNSDMIS TISLDETTEI SSSERDKPPA HHTVDKLTTN WTAVANLSNA
     EEHPAQNVTD KIALQRPLKK TEEQSRNDTV HTTATQHEIN AVSSTTATSF NDTKSFVAST
     TPESITAALN SSTKESNEIK GTTSATNSDE MNSTDYKTKK PAEPYLHASN STGMELLEIV
     DKSSHSNESK LNDSASSTLQ SKTNDTHANS EHTWQRISLH QATPSLSMEL TTTPTMYSNE
     ISTSTSASTL ANTSSTKLPS NSQPIPANGT ESTVSLDASK SVGGLDTSTR NASVDIVNFS
     RLCNELAIKF WIAANNGLSI GRSFALSPFG MTSLLAMIFL GARGSTSDQM NEILGLDNVA
     TFNPHLIFQN VTDTVSLARH QGIANAAFVR ELFADKAKVR KLLPFYKEQA QQFYEGLVAE
     VNFATISDLA RRRTNLLIRK QTGGRIKDFV KSNTVPLRSP LAAISANVFQ TDCNTSYASA
     TGRDGELYFA VSAAHRLRKL IPVPATVWRS NVLAGYEPSL DATASAIGSA DKLVSTIFLV
     PGQQGHAAPG DTLDRLEQRL VKGAFQDGTW NKLLKVLIPR PGLELQIPKF SHRSVVNATA
     ALKRMGLDQL FSTQADFKGI NGIGNRLFLS DVLQMNLFST CGDENIASGR HHVEIYPASA
     SLRNSRRVEE QTFRRIRRTV DTKSENYRTV SLKERIRNVE RSEEKPRLRL DQPFLYFVRH
     NPTGLILHIG RFNPRLI
//
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