ID E1QSC1_VULDI Unreviewed; 779 AA.
AC E1QSC1;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN OrderedLocusNames=Vdis_0100 {ECO:0000313|EMBL:ADN49514.1};
OS Vulcanisaeta distributa (strain DSM 14429 / JCM 11212 / NBRC 100878 /
OS IC-017).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=572478 {ECO:0000313|EMBL:ADN49514.1, ECO:0000313|Proteomes:UP000006681};
RN [1] {ECO:0000313|EMBL:ADN49514.1, ECO:0000313|Proteomes:UP000006681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017
RC {ECO:0000313|Proteomes:UP000006681};
RX PubMed=21304741;
RA Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., Lucas S.,
RA Nolan M., Glavina Del Rio T., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S.,
RA Goker M., Wirth R., Woyke T., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Vulcanisaeta distributa type strain (IC-
RT 017).";
RL Stand. Genomic Sci. 3:117-125(2010).
RN [2] {ECO:0000313|Proteomes:UP000006681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14429 / JCM 11212 / NBRC 100878 / IC-017
RC {ECO:0000313|Proteomes:UP000006681};
RX DOI=10.4056/sigs.1113067;
RA Mavromatis K., Sikorski J., Pabst E., Teshima H., Lapidus A., Lucas S.,
RA Nolan M., Glavina Del Rio T., Cheng J., Bruce D., Goodwin L., Pitluck S.,
RA Liolios K., Ivanova N., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y., Jeffries C., Rohde M., Spring S., Goker M.,
RA Wirth R., Woyke T., Bristow J., Eisen J., Markowitz V., Hugenholtz P.,
RA Klenk H., Kyrpides N.;
RT "Complete genome sequence of Vulcanisaeta distributa type strain (IC-
RT 017T).";
RL Stand. Genomic Sci. 3:117-125(2010).
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; CP002100; ADN49514.1; -; Genomic_DNA.
DR RefSeq; WP_013335239.1; NC_014537.1.
DR AlphaFoldDB; E1QSC1; -.
DR STRING; 572478.Vdis_0100; -.
DR MEROPS; M01.021; -.
DR GeneID; 9751015; -.
DR KEGG; vdi:Vdis_0100; -.
DR eggNOG; arCOG02969; Archaea.
DR HOGENOM; CLU_003705_0_1_2; -.
DR OrthoDB; 139771at2157; -.
DR Proteomes; UP000006681; Chromosome.
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; 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 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:UP000006681};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 8..166
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 201..417
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 484..770
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 273
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 272
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 276
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 295
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 358
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 779 AA; 88396 MW; 55FE0F9ECFF752D2 CRC64;
MSLGVELYVV ELRFRFGDLT YEGVVDVHVS SVGDLLLNAV DLGIRSVEVD GRPVDYSYDG
RVLRVRGPIS GVVRVLFNGR VGDRLLGIYR APYRDGYMIT TQFEPTGARY FIPCVDNPAA
KARFRVRVLV DGDYDVIFNT PPVRVYWDGP WKVFEFAETP RISTYLLYLG IGRFFESRDR
VGNVDVIFAT PLKDRVEDGR FALDVAKGVL EFYSGYFGIP YPLPKLHLIH VPEFAAGAME
NWGAITFRET ALLVGRGSTE LTRRRVAEVV AHEIAHQWFG NLVTMRWWDD LWLNESFATF
MSYKAMDRLF PGWGVWYRFL ADETVGSMLR DSLVSTHPVH VPISSEEEAF EIFDDISYGK
GASLLRMLEN YVGEEEFRKG LSNYLRKYAY SNATEDDLWS SIEEVSGKPV TKVMKAWVDK
PGHPVIVVEE PGKGITLRQS RFILSGNTAD TWPIPIVYRF NGAVNTVLME HDTLTLSVSS
ASLFLNVNGS GYYRVRYTDW SRALSNASNH FERWSVINDA YAHLLQGSIS LSEYLSLVRS
VSDIVNYLIT TTVITQLGTL YSIKPSAVKE VFTEYLRAQS TLLEGVSGMD DVRELVLSRR
ALVDEDYAMS IAGLIRDYQG LSPVMRQAVV NAYAVVGERP FETLRGLYRT LVSDEDRNRV
LAAMLSVTDR DEYRKSLDFL MSGEVKRQDL QFFTVGSRNP YVRDINLGWL MNNYKRFIEA
YGDPGVLSRV FTYSIPFIGL GQEDEVERFL LGLNIQGIEM GVKAGLELMR VYSRLLHSI
//
