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Database: UniProt
Entry: A0A2S4VPD9_9BASI
LinkDB: A0A2S4VPD9_9BASI
Original site: A0A2S4VPD9_9BASI 
ID   A0A2S4VPD9_9BASI        Unreviewed;      1385 AA.
AC   A0A2S4VPD9;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   08-NOV-2023, entry version 22.
DE   RecName: Full=Peptidase M12B domain-containing protein {ECO:0008006|Google:ProtNLM};
DE   Flags: Fragment;
GN   ORFNames=PSTT_05334 {ECO:0000313|EMBL:POW11353.1};
OS   Puccinia striiformis.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=27350 {ECO:0000313|EMBL:POW11353.1, ECO:0000313|Proteomes:UP000239156};
RN   [1] {ECO:0000313|EMBL:POW11353.1, ECO:0000313|Proteomes:UP000239156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-210 {ECO:0000313|EMBL:POW11353.1,
RC   ECO:0000313|Proteomes:UP000239156};
RA   Xia C.;
RT   "Gene loss provides genomic basis for host adaptation in cereal stripe rust
RT   fungi.";
RL   Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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:POW11353.1}.
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DR   EMBL; PKSL01000039; POW11353.1; -; Genomic_DNA.
DR   VEuPathDB; FungiDB:PSHT_02328; -.
DR   VEuPathDB; FungiDB:PSTT_05334; -.
DR   Proteomes; UP000239156; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 4.10.70.10; Disintegrin domain; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR001762; Disintegrin_dom.
DR   InterPro; IPR036436; Disintegrin_dom_sf.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR002885; Pentatricopeptide_rpt.
DR   InterPro; IPR001590; Peptidase_M12B.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   NCBIfam; TIGR00756; PPR; 1.
DR   PANTHER; PTHR11905; ADAM A DISINTEGRIN AND METALLOPROTEASE DOMAIN; 1.
DR   PANTHER; PTHR11905:SF159; ADAM METALLOPROTEASE; 1.
DR   Pfam; PF01535; PPR; 2.
DR   Pfam; PF13041; PPR_2; 1.
DR   Pfam; PF13688; Reprolysin_5; 1.
DR   SMART; SM00050; DISIN; 1.
DR   SUPFAM; SSF57552; Blood coagulation inhibitor (disintegrin); 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS50215; ADAM_MEPRO; 1.
DR   PROSITE; PS50214; DISINTEGRIN_2; 1.
DR   PROSITE; PS51375; PPR; 3.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00276};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239156};
KW   Signal {ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00276}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1385
FT                   /note="Peptidase M12B domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015701483"
FT   DOMAIN          330..553
FT                   /note="Peptidase M12B"
FT                   /evidence="ECO:0000259|PROSITE:PS50215"
FT   DOMAIN          581..657
FT                   /note="Disintegrin"
FT                   /evidence="ECO:0000259|PROSITE:PS50214"
FT   REPEAT          1143..1178
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT   REPEAT          1179..1216
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT   REPEAT          1287..1317
FT                   /note="PPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00708"
FT   REGION          133..154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..416
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          924..946
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1242..1266
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        495
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         494
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         498
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   BINDING         504
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
FT   NON_TER         1385
FT                   /evidence="ECO:0000313|EMBL:POW11353.1"
SQ   SEQUENCE   1385 AA;  153383 MW;  8761F2A0F085E90A CRC64;
     MVSFIHLSIL VRVLSMCMIM SKVRGSSERT KPIKKVFHPS DLRIKVLKSA ASSSSVNQAQ
     EIRFQGDLVD QDQEEGSLIC SGDPILLQFS IPHQYSHQSP KQNDDGLKTR FSLYLEPSSH
     SFLHPNAMIT YNSMNGTSSQ ESMTPGSSSP SSFSSQAIKA DEVLAYSGTV VEDNINTRPA
     KKAHPSWANI LIHHPYGSKC LHIQDSRHVV LEGALYVNGV LWHIKSVDSY RKIKGHKDLN
     IDIHHGLDDP KLVIWTYSNL ASKMTMINNN FNQTVTLENE EYHRKSSSEQ EYHIFSKRQS
     ISNDIAGLTG EKVDYSSTIG IVEGCPKSAK MVYIGIAVDC TYLRKHEYSM DSVRLSILNN
     MNLVSGLYSR SFNISLGIVE INLPASSGGQ CPDRASRDRP WDADCPSGSS TDDPNGLDIN
     QRLNKFSQWR SDKGGSDGAG LWHLLTDCPN GSQVGVSWLG ALCKVGAEQG VNGGTTSGTG
     VTASTPNEWE TMAHEIGHNF GAVHDCISGC SMGDACCPAS RTSCENPDQN IMAPSSSGDG
     SSGRFSPCSI GNICSSLKTG GPSKMETSCV GELGQHYTTS LNQCGNGILE PGEECDPGQV
     ASPCCQWGVC KFTPGSRCMP SSQSPCCSDT CQYSPASTPC NSSSFSSTCS GDSPTCPSSD
     SGLAIHSSQH HPIIHHPSST NNQEPFLSAV IKGFNQILLL ETGLEHSQSR EVMEILMRIV
     RQKLSSSLDQ QDHQIWNASK QVIIHSALRP RMSSVGEWAW EEIGRGNYAR LIQVWTGILE
     IVDRRHGKLV PDGLPTTIGL DQAFFSALVV VSSTLSNGPS LSVLVKSLVD RIWSRVIPAD
     QLKLDKLPQP DRARYFLRAV ELGLLWRRPV EDEQEHSDGL VEQDERIVHL IRREFLTQQP
     QSLQYCHDLS SRIQEAVDGT GHEPGWLTVD WSQPPPQTEE KKSPSNIKRD IVLTQKVIGT
     LFNGFAENGM IDQVEQLIKF SRKLGGMSRY LWSALLRGLN KFNNKSQAGL WMKEFVGRME
     SEDNLDLDFN MRCILISGSI ATDLDGALDS LDKLLLSTTK ASSSKKSEKL LPIDAINSII
     SALLRHKMIE RAESLLSQLS DRLEVNTTTL NHFLNYYSKL QYPELDQVLK TLKSFEDKLV
     KPDVVSFTIL LNVLMKLGSG KETINQLLKM MESVGIQPNA ITYGSIIHHL CRTGTVDDVQ
     VALKLLDEIE QRGIATTDIT YTALIQGFLR AHIQEYESTN AGFQTNNNSQ TNHLSTSTKQ
     PESRPQTKLE IATDLIGRLK NRGGRLNQVI YNSLLNALFS TGQFDSGLQV FKLMKSELKS
     NPNGTGGFEL YGNGWIDSYG IIFRRLIQFG NLDLFHIIYF HHFKFEMFTF VPNWIEKLID
     RFEKS
//
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