ID A0A1E3QRR2_9ASCO Unreviewed; 1012 AA.
AC A0A1E3QRR2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Aminopeptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BABINDRAFT_49119 {ECO:0000313|EMBL:ODQ79732.1};
OS Babjeviella inositovora NRRL Y-12698.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; CUG-Ser1 clade incertae sedis; Babjeviella.
OX NCBI_TaxID=984486 {ECO:0000313|EMBL:ODQ79732.1, ECO:0000313|Proteomes:UP000094336};
RN [1] {ECO:0000313|Proteomes:UP000094336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL Y-12698 {ECO:0000313|Proteomes:UP000094336};
RG DOE Joint Genome Institute;
RA Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goker M.,
RA Salamov A., Wisecaver J., Long T.M., Aerts A.L., Barry K., Choi C.,
RA Clum A., Coughlan A.Y., Deshpande S., Douglass A.P., Hanson S.J.,
RA Klenk H.-P., Labutti K., Lapidus A., Lindquist E., Lipzen A.,
RA Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J., Peng Y.,
RA Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C., Stielow J.B.,
RA Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V., Jeffries T.W.;
RT "Comparative genomics of biotechnologically important yeasts.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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DR EMBL; KV454431; ODQ79732.1; -; Genomic_DNA.
DR RefSeq; XP_018985060.1; XM_019132146.1.
DR AlphaFoldDB; A0A1E3QRR2; -.
DR STRING; 984486.A0A1E3QRR2; -.
DR GeneID; 30149999; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000094336; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR Gene3D; 1.25.50.20; -; 1.
DR Gene3D; 2.60.40.1910; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR034016; M1_APN-typ.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000094336};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 168..347
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 381..598
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 670..988
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 97..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 454
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 453
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 457
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 476
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 539
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 1012 AA; 113206 MW; F9918E4970426627 CRC64;
MKYIAPRSLG LSLTRARFST LCATLPGGLT PSGRGTQTSW LSGKLKLDIN TPSPTFSSLT
THSFSSLQHR YYCQMCRHAT TGGSSTMYVS TFCRNETNTG SKNASQNRSK RHRDSNCSPK
RANSYRGNCM LFFLWPFLVF PQWTLAGNST QLILSVPSDR QVLPTNVKPT KYDVTMEPNF
STFKFDGSIK IDLDVKEDTH TVTVNSLEIE IHSAKIAGQD AASTTFDEDK QSATFTFAEE
LKAGTTAQLE LTFTGVLNDK MAGFYRSTYQ ENGETKYLAT TQMEPTDCRR AFPCFDEPAL
KAVFDITLIS DEKLTCLSNM DVKSEKKLAG GKKAVSFNST PLMSTYLVAF VIGELNYIET
DAYRVPIRVY TTPGLEEQGR FSLDLAAKTL AFFDKTFGID YPLPKMDMIA IHDFSAGAME
NWGLVTYRVV DLLLDPKTSS LSTQQRVAEV VQHELAHQWF GNLVTMDWWE GLWLNEGFAT
WMSWYSCNQF YPDWKVWEQY VTDSLQSALS LDALRASHPI EVPVKRADEI NQIFDAISYA
KGSSLLKMIS RWLGEEVFIK GVANYLKKHK YSNTQTGDLW KALSEASGKD VVKVMDVWTK
KIGYPVVSVT EKDNELTVKQ NRYLTTGDVK PEEDETIYPV FLGLRTAAGI DESVVLDSRE
KTLTLDDASF FKINGDQAGV YRTNYTPERW VKLGEAGRQG LLSVEDRAGL VADAGALCVS
GYSSTTNLLS LVSGWKQEQS FVVWDEIITR ITSLRAAFLF EDVETRDALK ALTRALISEK
AHVLGWEFKE TDGFLEQQLK ALVFAAAVGA KDEELVAVAQ DLFQKYVAGD KSAVHPNIRA
SVFSTVAATG GAEEYDQIYH IYHNAISVDE KITALRTLGR FEQPELIQKT LNILLDSSIV
KAQDVYIPMQ GLRSHSAGIE ALWTWMQANW DEIYKLLPPG LSMLGSVVQI CTSGFSSEEK
KEEIRAYFAT KSTKGFDQGL TQSLDSIQSK ANWIKRDSAS IKEWLTTNGY KK
//
