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Database: UniProt
Entry: E3JRN0_PUCGT
LinkDB: E3JRN0_PUCGT
Original site: E3JRN0_PUCGT 
ID   E3JRN0_PUCGT            Unreviewed;      1130 AA.
AC   E3JRN0;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   27-MAR-2024, entry version 69.
DE   RecName: Full=alpha-mannosidase {ECO:0000256|ARBA:ARBA00012752};
DE            EC=3.2.1.24 {ECO:0000256|ARBA:ARBA00012752};
GN   ORFNames=PGTG_00725 {ECO:0000313|EMBL:EFP74769.2};
OS   Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS   (Black stem rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX   NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP74769.2, ECO:0000313|Proteomes:UP000008783};
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=CRL 75-36-700-3;
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA   Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA   Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA   Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA   Schein J.;
RT   "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT   700-3.";
RL   Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000008783}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CRL 75-36-700-3 / race SCCL
RC   {ECO:0000313|Proteomes:UP000008783};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 38 family.
CC       {ECO:0000256|ARBA:ARBA00009792}.
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DR   EMBL; DS178262; EFP74769.2; -; Genomic_DNA.
DR   RefSeq; XP_003307775.2; XM_003307727.2.
DR   AlphaFoldDB; E3JRN0; -.
DR   STRING; 418459.E3JRN0; -.
DR   EnsemblFungi; EFP74769; EFP74769; PGTG_00725.
DR   GeneID; 10546625; -.
DR   KEGG; pgr:PGTG_00725; -.
DR   VEuPathDB; FungiDB:PGTG_00725; -.
DR   eggNOG; KOG4342; Eukaryota.
DR   HOGENOM; CLU_003442_0_1_1; -.
DR   InParanoid; E3JRN0; -.
DR   OrthoDB; 2786490at2759; -.
DR   Proteomes; UP000008783; Unassembled WGS sequence.
DR   GO; GO:0034270; C:Cvt complex; IEA:EnsemblFungi.
DR   GO; GO:0000328; C:fungal-type vacuole lumen; IEA:EnsemblFungi.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IBA:GO_Central.
DR   GO; GO:0004559; F:alpha-mannosidase activity; IBA:GO_Central.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019309; P:mannose catabolic process; IEA:EnsemblFungi.
DR   GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR   CDD; cd10812; GH38N_AMII_ScAms1_like; 1.
DR   Gene3D; 3.20.110.10; Glycoside hydrolase 38, N terminal domain; 1.
DR   Gene3D; 1.20.1270.50; Glycoside hydrolase family 38, central domain; 1.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR041147; GH38_C.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR011682; Glyco_hydro_38_C.
DR   InterPro; IPR015341; Glyco_hydro_38_cen.
DR   InterPro; IPR037094; Glyco_hydro_38_cen_sf.
DR   InterPro; IPR000602; Glyco_hydro_38_N.
DR   InterPro; IPR027291; Glyco_hydro_38_N_sf.
DR   InterPro; IPR028995; Glyco_hydro_57/38_cen_sf.
DR   PANTHER; PTHR46017; ALPHA-MANNOSIDASE 2C1; 1.
DR   PANTHER; PTHR46017:SF1; ALPHA-MANNOSIDASE 2C1; 1.
DR   Pfam; PF09261; Alpha-mann_mid; 1.
DR   Pfam; PF17677; Glyco_hydro38C2; 1.
DR   Pfam; PF07748; Glyco_hydro_38C; 1.
DR   Pfam; PF01074; Glyco_hydro_38N; 1.
DR   SMART; SM00872; Alpha-mann_mid; 1.
DR   SUPFAM; SSF88688; Families 57/38 glycoside transferase middle domain; 1.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 1.
DR   SUPFAM; SSF88713; Glycoside hydrolase/deacetylase; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008783}.
FT   DOMAIN          560..641
FT                   /note="Glycoside hydrolase family 38 central"
FT                   /evidence="ECO:0000259|SMART:SM00872"
SQ   SEQUENCE   1130 AA;  127786 MW;  45823AF53FCC2EBC CRC64;
     MPSTRDEDYP LMENMPRANR FRNVTLGHLK NFIGGDYGSQ NLSSVLYEAR DGSESAVKLE
     VWSAPDLSKP SFAEAVRQKY KKISKGFKFG PSWSNHWVKA TLTVPKQYQD RERVLFEFDP
     GCEALIFTSE GLPLQGITGG TDSAKRIDFI IPKQSRAFPF QIYIEVSANA LFGVPDEGQL
     EVHDDVFFEL AMADIAIPRM DAWHLMWDFQ VISDLTKSVP VTSPICLKAQ TVAMEIMNTF
     KPDNLETISA CRKIAEKILG AEWTQKPIYD PKSDWDLEGD SEGVPVFAIG HCHIDTAWEW
     PFSVTQQKVA RSWATQVDLI QRYPEYRFVA STAQQYKWLE ELYPQLFSKV RREVENGKFF
     VTGGSWVEND TNMPSGEALC RQFLYGQRYF KSRFGKYTDI FWLPDSFGYA SQIPQICRQS
     GIPYFFTQKM SWSEFNKFPH STFNWIGIDG TQVLVHMTPV DTYNAQANVD EVLKAITNHK
     DLEWSDKTLL VYGNGDGGGG PLAPMIEKLR RIRSASNNSS NSGVPKVTTG PSVSDFYKML
     LNKTRNGKDL PTWRGELYLE YHRGTYTSHG SIKRHNRKSE ILMREIEYFA TLASLFREDT
     GYEYPKDELD HLWEIVLLCQ FHDVLPGSAI AKVYEDAEKL YAEVAQKGTA LLEAARQSAL
     YGSQAVDVVT ASSNRGGNVV GLNTLSFPRQ EILRVPLEIY DGRSAFSASK TDEDSVFVIA
     KDATGNGLIE LESLSHLQEH IQLATASVGR DVKTGEVCYF LANKALTVQI SSQGRIVSIV
     DTELGRELIL SGQSSGFVMY QDQPLTYDAW NADIFHLDTK EIIDAINVKV VEPKGLRASI
     VVECATISLD AVPGSLKKDA LSLVRFETTI DWHEQHKFLK FEVPLDINSD QATYEIQYGV
     LQRPTHKNTT WDAAKFEVCG HRFADLSEFG YGVALLNDCK YGYACEGSYL RLSLLRASTS
     PDPRQDQGMH KMRFGILPHR GHFLESDVPQ VAMAFNNPIH LRYAPRNISS RNLLAPVTEI
     FKLDGLGARN VILDTVKRGE DDTFGFHSRK PVRTVIVRLY EAFGGRANVH LVTLVKAQEV
     FIVDVLEREL EKVELKNHQQ SITDDQEPYK QVVELNFKPF QFISLKFILS
//
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