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Database: UniProt
Entry: E3KAD9_PUCGT
LinkDB: E3KAD9_PUCGT
Original site: E3KAD9_PUCGT 
ID   E3KAD9_PUCGT            Unreviewed;       957 AA.
AC   E3KAD9;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 2.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=DUF221-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=PGTG_06917 {ECO:0000313|EMBL:EFP81296.2};
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:EFP81296.2, 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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CSC1 (TC 1.A.17) family.
CC       {ECO:0000256|ARBA:ARBA00007779}.
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DR   EMBL; DS178278; EFP81296.2; -; Genomic_DNA.
DR   RefSeq; XP_003325715.2; XM_003325667.2.
DR   AlphaFoldDB; E3KAD9; -.
DR   EnsemblFungi; EFP81296; EFP81296; PGTG_06917.
DR   GeneID; 10536865; -.
DR   KEGG; pgr:PGTG_06917; -.
DR   VEuPathDB; FungiDB:PGTG_06917; -.
DR   eggNOG; KOG1134; Eukaryota.
DR   HOGENOM; CLU_009187_0_0_1; -.
DR   InParanoid; E3KAD9; -.
DR   OrthoDB; 1330110at2759; -.
DR   Proteomes; UP000008783; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0005227; F:calcium-activated cation channel activity; IBA:GO_Central.
DR   InterPro; IPR045122; Csc1-like.
DR   InterPro; IPR003864; CSC1/OSCA1-like_7TM.
DR   InterPro; IPR027815; CSC1/OSCA1-like_cyt.
DR   InterPro; IPR032880; Csc1/OSCA1-like_N.
DR   PANTHER; PTHR13018:SF154; DOMAIN PROTEIN, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G11660)-RELATED; 1.
DR   PANTHER; PTHR13018; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR   Pfam; PF14703; PHM7_cyt; 1.
DR   Pfam; PF02714; RSN1_7TM; 1.
DR   Pfam; PF13967; RSN1_TM; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008783};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        31..52
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..135
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        391..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        434..460
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        481..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        544..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        587..606
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        612..630
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        650..673
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..185
FT                   /note="CSC1/OSCA1-like N-terminal transmembrane"
FT                   /evidence="ECO:0000259|Pfam:PF13967"
FT   DOMAIN          210..374
FT                   /note="CSC1/OSCA1-like cytosolic"
FT                   /evidence="ECO:0000259|Pfam:PF14703"
FT   DOMAIN          386..668
FT                   /note="CSC1/OSCA1-like 7TM region"
FT                   /evidence="ECO:0000259|Pfam:PF02714"
FT   REGION          763..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          840..957
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        850..880
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        934..951
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   957 AA;  107512 MW;  2E5539B375813ED2 CRC64;
     MSSTDTAASS AASGLLSQYQ AKLTQVSTSS VLIQLVLMFC CSVGTVLAFS ILRPKNKIVY
     MPRYKYSAED KRPPKLEDGL FDWLKPLSKA TENELLAQIG LDAVVFLRFL RMCRWMCSLL
     AMLACALLIP CDVFYNLKIM DKSQQLSTSS NTLAMVSISN VRGSWLYVHV VYGYLVTFIV
     LYVIYVNYKT VVRLRWEWFR SPEYQNSIYS RSIMMTHVGS KHMSDSGLQN LLSQLQIPYP
     TTAVHIGRRV GMLAFLIERH NQTVRDLEQV LVTYLKGGKI SPNRPTIRIG KNFLGLGGRK
     VDAIDFYTAK IKQYELKIQA ARDAISGRKP ENYGFASFAA VAYAHIVAKK LGAKRIKGVA
     FSLAPPPQDI IWENLIKSDI VVFRQRVIGE AFMTVIATFY VIPLVALALL ANLASLTQYV
     GFLNSWSTAS PETFSAFAGI APPLLSTLLQ LALPVIMRAL ARFQAATTHQ KLDRAVFSRY
     FAFLTATQFL IFSLLSVVFS TVAEIVVEIG KKESFLRILQ NFNKLPDKIQ STYLQQSNYW
     LTWFPLRGFT SVLDLVQIVS LLLVFIRTKV WGRTPREIRE WTKPPEFDYP VYSANVLLML
     LVAFVYAPLA PLVPLLASAS FFASSWIYKY QLMYISITRC ESGGRLWRML INRVLFALCA
     MHAFLCLTIG LQLGWFKSIA TLPPFAIVIA FKFFLKSTFD SKFTWYIPTG AEFSQVHKHN
     ADARKNRLMK RFGHPSLHAE LFTPMIHKDH QLLLSEVYRG RIGDPSEDPK NPGAQQNYGQ
     ANYAGRSDDK APLSSGPQPV VGGLRFAAIA QHDLMYSQQQ FLRERGDDEM SLASTSLGNL
     GHAREHSNAP APQNDLNIQG YLENGPRPSF QYQEKGGTGS RSASPAPHEY PPEFGSNVRL
     PYHLPDDSYI PSPNPTHEES LEFDGYHPGI PASRHSTYGT SHSRSTSPLI TTRRPPA
//
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