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
//