ID H6BLH2_EXODN Unreviewed; 963 AA.
AC H6BLH2;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
GN ORFNames=HMPREF1120_00088 {ECO:0000313|EMBL:EHY51865.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY51865.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY51865.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY51865.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JH226130; EHY51865.1; -; Genomic_DNA.
DR RefSeq; XP_009152326.1; XM_009154078.1.
DR AlphaFoldDB; H6BLH2; -.
DR STRING; 858893.H6BLH2; -.
DR MEROPS; M01.007; -.
DR GeneID; 20304727; -.
DR VEuPathDB; FungiDB:HMPREF1120_00088; -.
DR eggNOG; KOG1046; Eukaryota.
DR HOGENOM; CLU_003705_0_2_1; -.
DR InParanoid; H6BLH2; -.
DR OMA; MMEYVAI; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000007304; 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; 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:UP000007304};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT DOMAIN 104..290
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 325..542
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 617..936
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 398
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 397
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 401
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 483
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 963 AA; 108093 MW; 269DC57D3C0274C7 CRC64;
MKHYVRSLSR LAGSRPIQSP TCTLHHQCFR RSFSSRVQTT NTTTVRRAVP SLIRSRNLNP
SSSPFASRQA RASLFNPANM CRFMSDAPGA HNTQGRVILP DNVVPKHYDV TLEVDFDKFT
FEGTVVIDLD VPKDTTSIAL NTLELDIHST TVHADGSLVT SSPTLSYDAD TQTTTIELGK
TITKGQKVQL KHTYTGQLND KMAGFYRSKR RDGQYLAVTQ FEATDARRAL PCFDEPALKA
EFTVTLIADE DKTCLSNMDV ASTEIVDSKI TGGKRKAVKF NRSPRMSTYL LAFIIAELKS
ISTDKFRLPI KVWMTPEQNE EDGRFSLDVA AKTLAFYEKA FQAPYPLPKM DMVAIPDFAA
GAMENWGLVT YRVVDLLFDQ KSAGAATKER VAEVVQHELA HQWFGNLVTM DFWDGLWLNE
GFATWMSWYS CNEFYPEWKV WQTFVIDTLQ GALGLDGLRS SHPIEVPVHR AEDINQIFDA
ISYSKGSAVL RMISKYLGED VFIDGVRRYI KKHAWGNTKT SDLWDALGDA SGKDVAHVMD
IWTKNIGYPV VTVTENEKDS TITVKQNRFL RTGDVKPEED KVLYPVMLGL KTKDGVDESL
MLTEREQTYK IKGGLEFYKL NTDHSAFYRT SYTPERLTKL GEAAQKGGLL SVEDRAGMIA
DAGALAASGY GRTSGILSLL QSFNTETEFV VWNEILTRIN AIRNTWIFED ESTKKALKSF
QLNLCSAKAH ELGWEFSENE DHILSQFKSL MFGSAGLAGD KKIQAAAKEM FAKFLDGDFN
AIHPNLRASV LAMVLRDGGV KEWEAVLARY HTAPTADEKN TCLRSLGRAR SPELIKKTLD
LALSGEVKMQ DIYMPIGGLG TTSEGIEKRW EWMCNNWDVL VEKLPPSMTM LSSVVSICVA
GFTKEDQLAK VEHFFHDKDK KGFDRSLQQS LDSIRAKANW LKRDGDDVTG WLKENGYLEK
GRL
//
