ID E7A131_SPORE Unreviewed; 1882 AA.
AC E7A131;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=DUF221-domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=sr13848 {ECO:0000313|EMBL:CBQ73188.1};
OS Sporisorium reilianum (strain SRZ2) (Maize head smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Sporisorium.
OX NCBI_TaxID=999809 {ECO:0000313|EMBL:CBQ73188.1, ECO:0000313|Proteomes:UP000008867};
RN [1] {ECO:0000313|EMBL:CBQ73188.1, ECO:0000313|Proteomes:UP000008867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRZ2 {ECO:0000313|Proteomes:UP000008867};
RX PubMed=21148393; DOI=10.1126/science.1195330;
RA Schirawski J., Mannhaupt G., Muench K., Brefort T., Schipper K.,
RA Doehlemann G., Di Stasio M., Roessel N., Mendoza-Mendoza A., Pester D.,
RA Mueller O., Winterberg B., Meyer E., Ghareeb H., Wollenberg T.,
RA Muensterkoetter M., Wong P., Walter M., Stukenbrock E., Gueldener U.,
RA Kahmann R.;
RT "Pathogenicity determinants in smut fungi revealed by genome comparison.";
RL Science 330:1546-1548(2010).
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; FQ311471; CBQ73188.1; -; Genomic_DNA.
DR EnsemblFungi; CBQ73188; CBQ73188; sr13848.
DR VEuPathDB; FungiDB:sr13848; -.
DR eggNOG; KOG1134; Eukaryota.
DR HOGENOM; CLU_002081_0_0_1; -.
DR OrthoDB; 1703463at2759; -.
DR Proteomes; UP000008867; Chromosome 6.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005227; F:calcium-activated cation channel activity; IEA:InterPro.
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:SF146; EXPRESSED PROTEIN; 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 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 12..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..160
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..226
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 689..719
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 739..759
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 787..811
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 823..844
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 884..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 908..926
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 946..967
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 85..224
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 394..678
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 692..963
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT REGION 252..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 323..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..518
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1136..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1239..1353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1420..1455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1512..1681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1706..1803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1855..1882
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 351..377
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 464..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1271..1285
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1447
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1522..1587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1647..1665
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1787..1803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1865..1882
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1882 AA; 209039 MW; 4922ED0A2AD1B966 CRC64;
MADLNERTIN SSFQGLVSTC VIFAVVGSIS AITYESLRQL RRLPRTRFTK FWHKDARLRH
PPGGVQDNPA HARDKDTCED WEMGHFYLSR VFHASTPSPM LPRWPFAWVK RAISFTDEWY
ADHTGMDTVV YVRFLRACLW WVLLQGLTTA PILLSIHITF SRGVSTTDMA RASLSYLVST
PEPGCTEERV DKCPTVPNEK GRSLLWIHLV LLWYLSITWV LALWWIGTGS LKVRKAQIQK
TRDKVIKAKA EARTAAANNT ATATATTSPL HRDAHHNLTT AQGLSSDNSD GWRQRTLMVM
NLPGTMRDEA SIRRYFEEFL RPDDDDTSSD DGHSNDAAFP ASRSDRQTRD MDAQQTSGSD
SDHRSTLGEQ QHATPPAVFS AHSDGPSGPQ PDLHPDRYLK SPVQTVVLVR KMNELASMLS
RRQEVLTQLE AAHVKLAQEV LVAVGRRTLK MRQQERKKAA DGSSQPNNDD QERSSSSSFF
ERFAASLGRP FRSRKRSKHA QAASGSHSGS ETPSEALDPD IEKLGSAQHP AGKALEEELA
RRLARFSPTN RGMHAKQTQA IDANDDGTGE HEMGETVWEA LNELPRELLD PFQPATRLSA
LFRGQTVPTI DYLLTKLNLL TALVTEMRSR PPTSYEPTST AFVTFRDPRQ ARMVWRELKD
QIVVKVRLAP EVKDLDWDRL MKTSFTVDVV RGFGVSVVTW GFTIFWVIII NTIVLGIFSV
DKLKQIPGLG NFFNDNPKVT GFVTITLPPL LVSLASMSVP ELIFQVSKRA QGFVTFSALY
DMCLIRYWKF VICNVVIFFS VGSAVIVTVL TKVGNTGSIL TTVASAFPSA APFFVSYLIL
QLALQSGFEH MGFMIALLQH WGARKAATPR VRAIKTLPRN FNRYYWLPLH INIMAIVFIF
ALLNPLVIPF ALVYLSLALV IFKKNFAYHY YRRFNEMEGA VYFLRLLRYS LDAIVVMQAV
LLIFFSVLRK RPVYIGMSAL LIPLTVITKL IATRLWKSQC RALDDEEAEA LCGIDSRPLW
QKMQRSDLGP STADEGSDSR TPLDALASGR YPSVVPPPPT NSAFQRVWQR LHDSFNANGL
DGQSYLATAY AKGKAPANAV GLGAKGIART PRYLVKETAK HAFHYRHAAK NSLGINNLVE
SPRPSRERAS GDRRRAISGL PPTSQLHVHS FRNSHDSPAV EEGQQQQQHM DGEVPNDPSA
ALQRRTAIRK QHVVHRRRGS SRSEDRPFLS AFDAVSAHAP LPSEDDYDLS FEDGDAPYLE
HDEEGHLLRH SSRRSRSRGS RHFGTLRKKP SQLATVADEE LPQSPGGFEM HDTAEGTSST
DPLYQQGASK HATGNTDQGW AKSSQQSHYE DYDESLKGRE LVRPHPPVRW DDTPNNTARY
NNPFYNQEMD DFLWLPRNPL APVDLFDTIE WYGPALVSSQ GGGGIVGEWD EEQDDDEYDD
DEEDEKHGDE IPLGGEAATL MRPRDLMLDG NEEIVLPDHL ARHLEETQEV EEVVDPAASI
PKNMMEDYKR ALRRRERAGS DASASGSPQS PSSLLRRRGS NLSSPSRQGP GFLGGTSLLQ
VPSYGSWRSG EGSQAPASPT SMRGSRRPGT GDSEPLASVA EGGVMVPRRS SSRRKRSKDR
DDAEDPAASA TENDQTLEAS PTKRRDAASA GVERNVSRRT YRRDASGALS RASGFSGGTA
QKTVTLQAAL RAEALEEERR LTLKERLAAS KNRKKRNASA HLDGLEEAAN AEDDDEEQDG
GAARRRGNLS SIMSRYEAQH RRREAQASEF GQLTPRKMGR DVSAGSQLDE FSPSSQLDRS
SSRRFRSAAM GVLSFSRSQK VAAGGATTVA MQELHPKTGG GGGMSRVETE AVLPAEASRT
SGLVENVEVP ASSSAQQEER ST
//
