ID A0A194SAK6_RHOGW Unreviewed; 781 AA.
AC A0A194SAK6;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aminopeptidase {ECO:0000256|RuleBase:RU364040};
DE EC=3.4.11.- {ECO:0000256|RuleBase:RU364040};
DE Flags: Fragment;
GN ORFNames=RHOBADRAFT_3200 {ECO:0000313|EMBL:KPV76431.1};
OS Rhodotorula graminis (strain WP1).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX NCBI_TaxID=578459 {ECO:0000313|EMBL:KPV76431.1, ECO:0000313|Proteomes:UP000053890};
RN [1] {ECO:0000313|EMBL:KPV76431.1, ECO:0000313|Proteomes:UP000053890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP1 {ECO:0000313|EMBL:KPV76431.1,
RC ECO:0000313|Proteomes:UP000053890};
RX PubMed=26441909; DOI=10.3389/fmicb.2015.00978;
RA Firrincieli A., Otillar R., Salamov A., Schmutz J., Khan Z., Redman R.S.,
RA Fleck N.D., Lindquist E., Grigoriev I.V., Doty S.L.;
RT "Genome sequence of the plant growth promoting endophytic yeast Rhodotorula
RT graminis WP1.";
RL Front. Microbiol. 6:978-978(2015).
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; KQ474076; KPV76431.1; -; Genomic_DNA.
DR RefSeq; XP_018272480.1; XM_018413009.1.
DR AlphaFoldDB; A0A194SAK6; -.
DR STRING; 578459.A0A194SAK6; -.
DR GeneID; 28973458; -.
DR OMA; VTYREND; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000053890; 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; 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 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|RuleBase:RU364040};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR634016-3,
KW ECO:0000256|RuleBase:RU364040};
KW Metalloprotease {ECO:0000256|RuleBase:RU364040};
KW Protease {ECO:0000256|RuleBase:RU364040};
KW Reference proteome {ECO:0000313|Proteomes:UP000053890};
KW Zinc {ECO:0000256|PIRSR:PIRSR634016-3, ECO:0000256|RuleBase:RU364040}.
FT DOMAIN 2..50
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 148..365
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 439..757
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT ACT_SITE 220
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 223
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT SITE 306
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KPV76431.1"
FT NON_TER 781
FT /evidence="ECO:0000313|EMBL:KPV76431.1"
SQ SEQUENCE 781 AA; 85371 MW; EE30A4BE11E81456 CRC64;
HYAVTQFQPT SARKAFPCFD HPAKKATFST SLISPVGLTS LSNTPELSRA PSSGAFEPTD
VATAAFLAGE EGKLAEPSSD TACETVEWEL VTFEDTPPMS TYLAAWAVGR FDSTASSYVS
PLTGKTVPLT AYAAKAFQHI ERGQARRALD TLAQVMPVYE KMFDLPYELG KLDLLVVDDF
EAGAMENWGL ITGRKSTLLY DDKVGGEGPL RRVVTTVSHE AAHMWFGNST TLSSWDELWL
NESFATLIGE VVAINVIEPS WNVHSSFIKF HRSDALKLDA LRSSHPIHLV CNHESEVPQT
FDHISYEKGS AVLKMLVEVI SESRFLAGTA AYLKEHQHAC ATSRDLWRAL SATSGFDVEN
MMDTWVEKVG FPVISVEEDG EQLKLRQNRF LSTGDPSAEE DETTWTIPLF VKDAASSELP
SVTIMSTREL VIPKPGSLYF LNAESRSTVR IAYPAPHVAK LADAAKSSSS RLCLTDRVGL
IEDLLLLSEA GYTSTVPTLD FLATFAPAEP DHLVWAEVAS SFKRFADAWW EQPTEELDAL
RAFARTLFRP VVDRLGLQHA PDDSHDTRRF RTLVVAAAAA VEDPDILTWV KHAFAGFLSG
AVDPLAADLA PFVVSCAVKH GGQAEYDAAL ALFGAAPSPQ YQMAAILGLT SSRDPQLLQK
TAAMMTSGAA SAQDLPIFLH GLAANPSSRR LVWALLQQAW PMLEQQYKGS MLLGKIAATA
VEVFSSEADA ASVEAFFADK DTTAYVQPLQ QALDTVRSKA RWLAREKDAV RAWLKKEGHF
A
//
