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Database: UniProt
Entry: U3JKI2_FICAL
LinkDB: U3JKI2_FICAL
Original site: U3JKI2_FICAL 
ID   U3JKI2_FICAL            Unreviewed;       418 AA.
AC   U3JKI2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   29-SEP-2021, sequence version 2.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Peptidase A1 domain-containing protein {ECO:0000259|PROSITE:PS51767};
OS   Ficedula albicollis (Collared flycatcher) (Muscicapa albicollis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Passeriformes; Muscicapidae; Ficedula.
OX   NCBI_TaxID=59894 {ECO:0000313|Ensembl:ENSFALP00000003286.2, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000003286.2, ECO:0000313|Proteomes:UP000016665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23103876; DOI=10.1038/nature11584;
RA   Ellegren H., Smeds L., Burri R., Olason P.I., Backstrom N., Kawakami T.,
RA   Kunstner A., Makinen H., Nadachowska-Brzyska K., Qvarnstrom A., Uebbing S.,
RA   Wolf J.B.;
RT   "The genomic landscape of species divergence in Ficedula flycatchers.";
RL   Nature 491:756-760(2012).
RN   [2] {ECO:0000313|Ensembl:ENSFALP00000003286.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the peptidase A1 family.
CC       {ECO:0000256|ARBA:ARBA00007447, ECO:0000256|RuleBase:RU000454}.
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DR   AlphaFoldDB; U3JKI2; -.
DR   STRING; 59894.ENSFALP00000003286; -.
DR   Ensembl; ENSFALT00000003299.2; ENSFALP00000003286.2; ENSFALG00000003135.2.
DR   eggNOG; KOG1339; Eukaryota.
DR   GeneTree; ENSGT00940000163644; -.
DR   HOGENOM; CLU_013253_3_0_1; -.
DR   Proteomes; UP000016665; Chromosome 26.
DR   GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.1960; -; 1.
DR   Gene3D; 6.10.140.60; -; 1.
DR   Gene3D; 2.40.70.10; Acid Proteases; 2.
DR   InterPro; IPR001461; Aspartic_peptidase_A1.
DR   InterPro; IPR001969; Aspartic_peptidase_AS.
DR   InterPro; IPR012848; Aspartic_peptidase_N.
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:SF70; PEPTIDASE A1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF07966; A1_Propeptide; 1.
DR   Pfam; PF00026; Asp; 1.
DR   PRINTS; PR00792; PEPSIN.
DR   SUPFAM; SSF50630; Acid proteases; 1.
DR   PROSITE; PS00141; ASP_PROTEASE; 1.
DR   PROSITE; PS51767; PEPTIDASE_A1; 1.
PE   3: Inferred from homology;
KW   Aspartyl protease {ECO:0000256|RuleBase:RU000454};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601461-2};
KW   Hydrolase {ECO:0000256|RuleBase:RU000454};
KW   Protease {ECO:0000256|RuleBase:RU000454};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT   DOMAIN          103..415
FT                   /note="Peptidase A1"
FT                   /evidence="ECO:0000259|PROSITE:PS51767"
FT   ACT_SITE        121
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   ACT_SITE        307
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-1"
FT   DISULFID        134..139
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601461-2"
SQ   SEQUENCE   418 AA;  46060 MW;  D522705CFE432F67 CRC64;
     MESSSWDMES SSWDRRAAGH GAQRTEPLKM PNYSYSPLCA VVFCLSLCRI SLKKGLSIRD
     KMRTAGVLDD FLKHIKYDPV KKYQPSQGSV VRQPITNHLD SSYFGEISIG EPPQKFLVLF
     DTGSSNLWVP SMDCKSPACF NHAKFQPNDS VTFSPSDRSH TVSYGSGSVT IALGYDTLRI
     QSITVTNQEF GLSQDEPTQP FYFADFDGIL GMAYPSLAVG GMATALEGML EQDQLAEPIF
     SFYFSRQPTY EYGGELILGG IDPRLFQGDI TWAPVAQKLY WQVALEEFAI GQSVTSWCSQ
     GCQAIVDTGT FLLTVPQEYI ESILQAVGAQ ETSYGFAVDC NDTQSLPPIT FGIGGAQLPL
     SPSTYVLNSN GYCTLGIEVT YLPSEDGQPL WILGDVFLKE YYTIFDMANN RVGFALSV
//
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