ID   U3JLK7_FICAL            Unreviewed;       829 AA.
AC   U3JLK7;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 61.
DE   SubName: Full=Aminopeptidase O (putative) {ECO:0000313|Ensembl:ENSFALP00000003661.1};
GN   Name=AOPEP {ECO:0000313|Ensembl:ENSFALP00000003661.1};
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:ENSFALP00000003661.1, ECO:0000313|Proteomes:UP000016665};
RN   [1] {ECO:0000313|Ensembl:ENSFALP00000003661.1, 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:ENSFALP00000003661.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M1 family.
CC       {ECO:0000256|ARBA:ARBA00010136}.
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DR   RefSeq; XP_016160261.1; XM_016304775.1.
DR   RefSeq; XP_016160262.1; XM_016304776.1.
DR   AlphaFoldDB; U3JLK7; -.
DR   STRING; 59894.ENSFALP00000003661; -.
DR   Ensembl; ENSFALT00000003675.2; ENSFALP00000003661.1; ENSFALG00000003512.2.
DR   GeneID; 101818082; -.
DR   KEGG; fab:101818082; -.
DR   CTD; 84909; -.
DR   eggNOG; KOG1047; Eukaryota.
DR   GeneTree; ENSGT00940000155211; -.
DR   HOGENOM; CLU_022467_0_0_1; -.
DR   OMA; FARCSQA; -.
DR   OrthoDB; 3108672at2759; -.
DR   Proteomes; UP000016665; Chromosome Z.
DR   GO; GO:0005730; C:nucleolus; IEA:Ensembl.
DR   GO; GO:0070006; F:metalloaminopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   Gene3D; 3.30.2010.30; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   Gene3D; 1.25.40.320; Peptidase M1, leukotriene A4 hydrolase/aminopeptidase C-terminal domain; 1.
DR   Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR   InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR   InterPro; IPR033577; AOPep.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR038502; M1_LTA-4_hydro/amino_C_sf.
DR   InterPro; IPR015211; Peptidase_M1_C.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR46627; AMINOPEPTIDASE O; 1.
DR   PANTHER; PTHR46627:SF1; AMINOPEPTIDASE O; 1.
DR   Pfam; PF09127; Leuk-A4-hydro_C; 1.
DR   Pfam; PF01433; Peptidase_M1; 1.
DR   SMART; SM01263; Leuk-A4-hydro_C; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016665}.
FT   DOMAIN          679..828
FT                   /note="Peptidase M1 leukotriene A4 hydrolase/aminopeptidase
FT                   C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01263"
FT   REGION          102..126
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   829 AA;  93882 MW;  3CEEA243608BE5E8 CRC64;
     METQLDPMKD DLPLMANTSY MLVKHYVLDL DVDFKSKVIE GSIVLFFETG SQYKKTSSAG
     KESCQSQFDE TCKMRASEPC HIPMINVSTC SSKTEYNDFA VSGTEEEATS DENSNHSNNE
     QASGISSSKD CCDIENHGNK DFLLILDCCD LSVLKVEEVD VAAVSGIEKF TRPVKLTGAS
     KELENLRNQI VHELVTLPAD RWKEQLYYFT HCSQAPGCGE LLFSTGTWSL EIRKSGIQTP
     ADFPHAIRIW YKTKPEGRSV TWTTDQSGRP CVYTMGSPIN NRALFPCQEP PIALSTWQAS
     VRTAAGFVVL MSGENSAEPV QLREGILNWY YYVSMPMPAS TFTIAVGCWQ EVKQQSFKQT
     AAIETNTVCS LPSSQTDSRW HEGVCGHVEY PCRFQNPAAR LQAVIPYRVF APWCLMESCE
     EYLLQLIPQC LSAAYATLGT HPFSRLDVLI VPSNFSSLGM ASPHIIFLSQ SVLPGGSHLC
     GTRLCHEIAH AWFGLAIGAR DWTEEWISEG FATFLEDIFW ARAQQLSHDE IKGQQELKAL
     LRWRRLRDEV QNSEEELQVL RPKKESTGEL SESGASVVKY GLKAEKIFMQ VHYLKGYFLL
     RSLARTIGEV SYLASLRKFV VKFHGQLVLS QDFLSMLLED IPKQKGSGLT VESIFQNWLD
     TSGIPKPLLE EGETWKECQL VQQVSGEVTK WIQTNRRIRK SSKKKMKQDE VVFQQLLPDQ
     LVLLLESLLE EKTLCPKLLQ CLERTYRLRE QDAEVRHRWC ELVIKHKYEP GYGDIERFLR
     EDQAMGVYLY GELMVNEDAK QQELARKCFA AAQEHMDASS AKVVAEMLF
//