ID A0A364MTN8_9PLEO Unreviewed; 2870 AA.
AC A0A364MTN8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Autophagy-related protein 1 {ECO:0000256|ARBA:ARBA00030237};
GN ORFNames=DDE83_008338 {ECO:0000313|EMBL:RAR03110.1};
OS Stemphylium lycopersici.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Stemphylium.
OX NCBI_TaxID=183478 {ECO:0000313|EMBL:RAR03110.1, ECO:0000313|Proteomes:UP000249619};
RN [1] {ECO:0000313|Proteomes:UP000249619}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIDEFI 213 {ECO:0000313|Proteomes:UP000249619};
RA Medina R., Franco M.E.E., Lucentini C.G., Saparrat M.C.N., Balatti P.A.;
RT "Draft genome sequence of Stemphylium lycopersici strain CIDEFI 213.";
RL Submitted (MAY-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RAR03110.1}.
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DR EMBL; QGDH01000191; RAR03110.1; -; Genomic_DNA.
DR STRING; 183478.A0A364MTN8; -.
DR OrthoDB; 3085317at2759; -.
DR Proteomes; UP000249619; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09601; M1_APN-Q_like; 1.
DR CDD; cd14009; STKc_ATG1_ULK_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; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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; IPR048941; ATG1-like_MIT2.
DR InterPro; IPR022708; Atg1-like_tMIT.
DR InterPro; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR PANTHER; PTHR11533:SF174; PUROMYCIN-SENSITIVE AMINOPEPTIDASE-RELATED; 1.
DR Pfam; PF12063; ATG1-like_MIT1; 1.
DR Pfam; PF21127; ATG1-like_MIT2; 1.
DR Pfam; PF11838; ERAP1_C; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR Pfam; PF00069; Pkinase; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Autophagy {ECO:0000256|ARBA:ARBA00023006};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Isomerase {ECO:0000313|EMBL:RAR03110.1};
KW Kinase {ECO:0000313|EMBL:RAR03110.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR634016-3};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927};
KW Reference proteome {ECO:0000313|Proteomes:UP000249619};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022927};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR634016-3}.
FT TRANSMEM 1332..1353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1514..1534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1546..1563
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1607..1631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1651..1676
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1705..1725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1745..1764
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1785..1806
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1919..2230
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 48..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1433..1475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1887..1913
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2253..2394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2439..2494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2712..2734
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2798..2818
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2835..2870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1042
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1072
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1444..1469
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2300..2325
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2326..2343
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2369..2394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2458..2494
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2715..2734
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2845..2859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 420
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-1"
FT BINDING 419
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 423
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 442
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-3"
FT BINDING 1953
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
FT SITE 505
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR634016-4"
SQ SEQUENCE 2870 AA; 317850 MW; C4CE022853493830 CRC64;
MHCFRHNGAS ALQNGRVLPS RPAIAVTTVT ATSFRSRLRP RRNLLLHTLS SPTTSSRYPA
THAQLRHATP RPSPPPPPPR HSLAAPVRYC SHRRNMCKHF GVDGHSSIDI TKGREVLPTN
VKPMHYDLTL EPDFEKFTYN GTVVIDLDVV DDTTSISLNT NELRIHSTKV AAGEQLLTHS
PNVTTDDDAQ ITKVSFDHTI PSGTKAKLTM TFSGILNDTM AGFYRSSFKS EDGSTTYMAT
TQMEPTDARR AFPCFDEPAL KATFTVTLIA DDKMTCLSNM DVASEKQVES AITGSKRKAV
TFNPTPLMST YLLCFIVGEL NFIETNNFRV PVRVYAPKDR DIEHGRFSLE LAAKTLEFYE
KTFNSPFPLP KMDMVAIPDF SAGAMENWGL VTYRVVDVLI DEKASGAATK QRVAETVQHE
LAHQWFGNLV TMDFWDGLWL NEGFATWMSW YSCNVFYPDW KVWEGYVTDN LASALSLDSL
RSSHPIEMPV KRADEINQIF DAISYSKGSS VIRMISKWVG EDTFMEGIRR YLKKHAYGNT
ETGDLWAALT DASGKDVGKV MDIWTKKVGY PVVAVTEGTD SIHLKQNRFL RTADVKPEED
QTLYPVFLGL RTKDGVDEDL TLFDREADFK LKDLDFFKLN ADHSGLYRTS YTPERLRKLG
IAAKEGLLTV EDRAGMIADA GSLAASGYQK TSGILSLLDS FKHEAEFVVW GEILARIGTL
RAAWMFEDQK TRDALKKFQL ELSADKAHEL GWTFSEQDGH IEQQFKGLMF GAAGMAGDEK
ITQACFDMFA KFKAGDKSAI HPNIRGSVYA IVLNNGGEEE YNAIVNEARN AVTSDERNSA
LRSLGRAKSP QLMQRTLDMA LSEEVKGQDI YLPIGALRTH PAGCHALWNW VKENWAELER
RLPPSLSMLS SVVAITTSCF THREHIEDIE AFFNDKSTKG FDMALSQSLD SINAKAAWVA
RDSQDVDGWL EDHNRARASI PRWHTEIEEK LTQRAMSQDA TQPDSPALAP APAPADVDHV
QLFRRSPHPY LRHRDEIRGQ SPERTADVAS QAQLPHHAVH DRDGRKRRKP ASQSPSESGT
EADDEGCSLV KALPAPPLRP HKGLRESRPL ETGEWASPLL TPTQIDDEAK NFSADFFDGT
KKNQPKGSVF HVDDETRAAR QKYMQRRRNE LHHSNLKLRR RIHLPAAFDP ATILYPPLLP
VLIAISLFAS SPKPLLPNIL LGLAALPARL IPSNSSPGYS SLHWLISIIP LIAAENTDIP
SRLSAEKPYK LKLPSSHRGM DPELLVCLFP LHQALLPPLY YLTTTSLLPT ELHLLSGGLI
NLFLFSESPQ SVILAVLLWF GGLGVFIFCG RILKWGVALA RIPRWRLRHA GRVIRARQNF
LQILNNSLGS RHNRGGGAVD GSDSDADEDD VASGTLYKTK SLKAGMVSFG NRSETPSRVA
ELHSAAEMSK ESPQKQHDVA EEPRSAGRKR RNTLPVLAAE NHTAQHRYSH RKRSRSIAHS
YLSLTPTQAW MRKWLYAAYV YVVVVILILG PIRYAIGEYA LHHHEPFGWA IGYLFGNIAS
LRWKVFEWDL EWWVPLPARL DADDLAGQLP VALRLSQDTL GEANMRILLC IYCGGTILAG
LISVFSLSAL VEVDTRRKVF HGTMVAMLLP TIYIDPCFVA LALSLVLAVF ILLDLIRASQ
LPPLSKPIAR FLTPYVDGRD LRGPVVVSHI FLLIGCAIPL WLSLAGVERT GDEPWRDWGV
KKRDVSMVSG VVCVGMGDAA ASLIGRRYGR RRWPWAGGKS LEGSLAFAVA VTIGLVMGRA
WLYIGWGSNH VMEKEAEGRA MAAGVTIGKA AVCAMGASLN EAVLTGGNDN VIVPVVLWIL
VRGVGLHPVP ASALGIGLGC SAGAASMASS PPSSHAPRRS GASPSSSATS GSEQIIGKFK
RMHHIGKGSF AEVYRGIHIK PPPQEKRQSV AIKSVNMNKL NKKLKDNLVS EITILRSLHH
PHIVSLIDCQ EAPSRMHIIM EFCELGDLSA FIKKRTDLVN HPQTQRMIEK YPNPSVGGLN
EVVVRHFAKQ MASALEFLRS KNYIHRDLKP QNLLLNPSSI FYSQSGTLER MPLAASANSL
IPATGIASLP MLKIADFGFA RILPTTSLAE TLCGSPLYMA PEILRYEKYD AKADLWSVGT
VLFEMMCARP PFRANNHVEL LRKIEERKDQ VRFPEGLICS RAMKTLIRAL LKRKPTERMS
YESFFADSVI RDEIPDMVDE DLPGSMQASE RLQASALEPP AEPSRQIQRV PVDMDRQVAE
NPYVPSPRDR VGVGMTPPSR PSSRPVSGNY SSTAPHPASR RSSNTPIEPN EDRISHREHR
RPMLTNAATA PGRPLSLHDQ PATGNSTSHR RRYSRDDQAP APTGLKEHLD RERIPQRAEA
NVLREAVERA AQDNALDEGF VFVEKRRVEI DALADEIANS PQTQRDRPIH RESAMKRRST
TQGSPTSITG AVPSKAIQIQ QKPTITHQRT GSYSRRQYRP SFETATSALS KAMNMVNIRG
LGLSPPVMKG VSPPPPQGYS AFPAYPTAQS SMLLVGDSGK TMGKDEDILA VRRIEDLAQL
SHVVYGFAEV KYSQLVPVAP SDPALGGGPT GVARKPNNDI VEYDDEDDDE LTPDTILLIS
EEALVLFVKT LAMLNKAMDL TGSYWNRARR NSGPDGTSRT NAKLGQVVSW MRDRFNECCV
KSEIVARKLK QAQQQLPVDH PSHPQNQSAA SGSATAVGSA ENILLTTGVT AEKLLYDRSL
EMSRQAAIDE LTGHNLGDCD INYWTAITML QAVLEEEEDL PGTKSEAEEI NGLDGEDRRS
IQKLLEQMRS RQRALKKKLD ALKTQKRSSI TSAPAPHSIG RSSPSPAAVK
//
