ID F4WDH3_ACREC Unreviewed; 1867 AA.
AC F4WDH3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Ovalbumin-related protein Y {ECO:0000313|EMBL:EGI67753.1};
GN ORFNames=G5I_03626 {ECO:0000313|EMBL:EGI67753.1};
OS Acromyrmex echinatior (Panamanian leafcutter ant) (Acromyrmex octospinosus
OS echinatior).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Acromyrmex.
OX NCBI_TaxID=103372 {ECO:0000313|Proteomes:UP000007755};
RN [1] {ECO:0000313|EMBL:EGI67753.1}
RP NUCLEOTIDE SEQUENCE.
RA Nygaard S., Zhang G.;
RT "The genome of the leaf-cutting ant Acromyrmex echinatior suggests key
RT adaptations to social evolution and fungus farming.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the serpin family.
CC {ECO:0000256|RuleBase:RU000411}.
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DR EMBL; GL888087; EGI67753.1; -; Genomic_DNA.
DR STRING; 103372.F4WDH3; -.
DR EnsemblMetazoa; XM_011052501.1; XP_011050803.1; LOC105143919.
DR eggNOG; KOG2392; Eukaryota.
DR InParanoid; F4WDH3; -.
DR Proteomes; UP000007755; 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:UP000007755};
KW Serine protease inhibitor {ECO:0000256|ARBA:ARBA00022900}.
FT DOMAIN 1425..1863
FT /note="Serpin"
FT /evidence="ECO:0000259|SMART:SM00093"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..284
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 809..831
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1149..1387
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1149..1172
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1181..1263
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1272..1289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1294..1313
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1345..1367
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1867 AA; 203061 MW; FB932BF9FBE86182 CRC64;
MENESRPNGE RARMSRIGFS SPSNRTGTRF YPYRMASLPG IPDDLGRLVV AGDMHANGVQ
TAESRIIMSQ RLRWLLPALI VSWMSLQLGV TLPAHNEHSH VSADTFDPST ATSTIIHQNH
DGRAHHPPNG KNETQSSHKL VASPAGLLRP DKFQFYTYDD KGDMITRQMT AQEIQGLIAS
GGTDHIAMDR QEPQKADDVL TGGKKVMDVV QKVQNVLKSA LDKPPTLTGS IPKIPEHANV
EWSNILPSIL SGETDSIPPN SDSSQLSHKL TTEKVEAESI SEHPTKKPAT LDVQTNTYAG
FTNNVQGKPH QGHHSQQTVV TEKPMIPVPV ITLTEQKLST LQSAVTESPV FQIVSVIPVE
SAGTKESQTD PSTADSSAAS STIQLSAQTE ESQTEQYVEL TLSEVPEETT FPQLTSLDTY
PVSITKQTTT SSKVSQGMKT SGTYSTTTPG VSTHLSPTKQ TATHGGSSEL TTDKISPSNT
SYILILSKNN TKVSDDSSFA SSVTKESQTN GIYNDIIIPQ TDTLATLVPI SHASPKPEEA
SNALHSPSTL ASVTRIKDPT VSTLHHYLNE GSSTVTKESS SPVTSTYFNP LPTDIQSSAP
IEPLPTQLID SFSSVINQVS EVKPPVLPLS NEMPEIPIMN INYEQRRNVS EVNEKNVRPI
PINTQTYETF TTEIPLRDAT KFDYSITYQP VNIVDRESST SSIYENSRIK ATTSTASIRV
GTTSNRIASN NLPTTPAGLK STQIHEEVLG STAASSFVQL EKTHATSASL PASQTESPAT
LGSITERIMS EKTSTTSFLN LTDTKAVASD ATKTQSTTAS IDTNLSSNKS TTNENFDNTL
ANLNLSDPVS AIDKVISIVS LPSSTPTIKP IDLPDNISNF VGEIAGDIAS GLIAGFPTTN
IPNLSTIEKE KIENATKLHE TERNVTQSTQ EILTDPVRNN TLIYGTSTQT KESNDTLEPI
KLLSNNERID DSTKASLSSP ANKFTSVNDE SKVAIKQPLY NATTVGIVNV IPEQTTTTTT
IDVGIRSPGV NKTTFNTNNN QKKTEIKEKI KTTEALIVRT DLSPELSNQL SVKVANDTKN
SGHVESSPKI ELLNEKNDSF ANVSSITKET IVIHSINDSS SESSSQAYND VTTDISVLNI
TSDAIVSNRN STDSTLSQNP NHVTTTAGYK NKDNIQNKED NKNNESSSVP LSIKEHTNSS
IKITQDSTND ANGNKGNISR PDNPINNTSS QIDKNVTQTT STVNASIQND EYSNNTENKT
ASLKHSESSP EPDVIRLQAS TSPSSVPVRP TSRPDYKPSE KPDVTKTDAD VNAEDKWTLI
SQQASPAISK LPKPPKLPKP LQRKPVNHAQ TSLPPSSSNS NDSTHVRSPG VEAPAHQQEQ
SQSSTQSFLP LDASQSAIGL DATIRHTSAD IVNFAKLCNE LAFNFWVATN KGLSTARSLA
LSPFGMTSLL AMIFLGARGP TSDQMNEVLG LDDVATFNPH LVFQNITDAV GLARGQGIAN
AAFVRELFAD KMKVRKLMPF YKEQAQQFYE GLVTEVNFAT ISDLVRRRTN LLVRKQTGGR
IKDFVKTNTV PLRSPLAALS ANVFQTDCNS SLTSSVGRDG ELYFAVSPAV RQRKLVPVPA
TTWRSGVLAG YEPSIDATAI GLGGSDKLVS TIFVLPGQQG HTAPGDTLDR LEQRLVRSAF
RDGAWNKLLK ALIPRHGLEL QVPKFSHRSV VNATAALKRM GLDELFSGNA DFKGINGIGH
RLHLADVLQM NLFSTCGDEN ILNGRHHVET YPASPLRRNV ERRTEDDNFG NTAEENTMRY
GTLPQEDNID SYADQSRTIL YGFYREEKQL SLERPRLKLD RPFLYFVRHN PSGIILHMGR
FNPRLLP
//
