ID H3B2T1_LATCH Unreviewed; 940 AA.
AC H3B2T1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN Name=LOC102347142 {ECO:0000313|Ensembl:ENSLACP00000016202.1};
OS Latimeria chalumnae (Coelacanth).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Coelacanthiformes; Coelacanthidae; Latimeria.
OX NCBI_TaxID=7897 {ECO:0000313|Ensembl:ENSLACP00000016202.1, ECO:0000313|Proteomes:UP000008672};
RN [1] {ECO:0000313|Proteomes:UP000008672}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Wild caught {ECO:0000313|Proteomes:UP000008672};
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lander E., Lindblad-Toh K.;
RT "The draft genome of Latimeria chalumnae.";
RL Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLACP00000016202.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR634016-3,
CC ECO:0000256|RuleBase:RU364040};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136, ECO:0000256|RuleBase:RU364040}.
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DR EMBL; AFYH01021231; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01021232; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01021233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01021234; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AFYH01021235; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 7897.ENSLACP00000016202; -.
DR Ensembl; ENSLACT00000016314.1; ENSLACP00000016202.1; ENSLACG00000014273.1.
DR eggNOG; KOG1046; Eukaryota.
DR GeneTree; ENSGT00940000157902; -.
DR HOGENOM; CLU_003705_2_0_1; -.
DR InParanoid; H3B2T1; -.
DR OMA; FLWQIPF; -.
DR TreeFam; TF300395; -.
DR Proteomes; UP000008672; 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:UniProtKB-UniRule.
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:SF156; ENDOPLASMIC RETICULUM AMINOPEPTIDASE 1; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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|RuleBase:RU364040};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000008672};
KW Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..940
FT /note="Aminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003580106"
FT DOMAIN 62..249
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 307..495
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 595..915
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 355
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 354
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 358
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 377
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 440
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 940 AA; 107761 MW; 492DB3B09AF9B03C CRC64;
LVQCPAAMHV GTVLLLMAAI GGSLYQRGKS QQATERDISI PSGHSGRLFP WQSSRLPTNV
TPEHYHLTLH PDFHTQAFRG WTKILLYVHK ATSSIVLNSK ELHITGARLE QLPKSNQQKN
LILQTLQSLK NEQVAFVASE TLEAGRRYEL AIEYSAVLAS GFLGFYKASY RTLNGETRML
AATQFEPTSA RKAFPCFDEP SFKSTFTLTI IRDRKHNAIS NMPKRVSIER KDGLVEDHFL
HSVKMSTYLV AFVVSDFVSI NSTSARGTKI TAPXVKEQVS GVRRYPSETL IDSVGQVRQC
HSLTCPLDLV AIPDFEAGAM ENWGLITFRK TALLYDPRTS TLQDKLWVTM VITHELAHQW
FGNLVTMEWW NDIWLNEGFA TYMEYFACEH LAPSWSVEDE MLLFSFYKAL GRDAFRSSHP
VSVPVKGSQH IREMFDVVSY SKGASILRML KTFLTEPLFS SGVKSYLKKH SYGNAHKDHL
WEALTQTCNT NVTQYLSASL GVPRCHSALA AGCRINVKAM MDTWTVQKGY PLVSVRVNGA
KLKVTQEIFT LYPQNSTGFL WQIPFTYYTS NSSTTTTHLL KQREESITIP HPVIWIKANS
NSTGFYRVNY DAPTFNALQK QLEDNHSVFS RSDRASLIDD TFYLASHGTL SFKSPLSLTL
YLRHETEYLP IRLALHHIFK LVSRFVFADD LCTAKLIKKH ILVLFGNLMR IQRWNDSGTL
PQQNLRILLL SLATGFQNLP AERRAWRLFQ RWMETDGKAQ LPNSLRNLIF RTGIRKGNNK
HWRFLLTKYF ESGSSADKIH ILSALAQTRN AAKKIWLLKA ALRNRQIKSQ DLLIIIWQVS
SSPRGSELAW KFMKQHWSKL VKEYSLGSSY LSQIVLTITS RFDSKRKYNK VRKFFQAQKE
TADLTFVKQA LENIQVNIRW LKKNKEEIQR WMQERYPKEY
//
