ID E9E9S1_METAQ Unreviewed; 1077 AA.
AC E9E9S1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=DUF221 domain-containing protein {ECO:0000313|EMBL:EFY87384.1};
GN ORFNames=MAC_06619 {ECO:0000313|EMBL:EFY87384.1};
OS Metarhizium acridum (strain CQMa 102).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN [1] {ECO:0000313|EMBL:EFY87384.1, ECO:0000313|Proteomes:UP000002499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY87384.1,
RC ECO:0000313|Proteomes:UP000002499};
RX PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA Wang C.;
RT "Genome sequencing and comparative transcriptomics of the model
RT entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL PLoS Genet. 7:E1001264-E1001264(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; GL698528; EFY87384.1; -; Genomic_DNA.
DR RefSeq; XP_007812959.1; XM_007814768.1.
DR AlphaFoldDB; E9E9S1; -.
DR GeneID; 19250930; -.
DR KEGG; maw:MAC_06619; -.
DR eggNOG; KOG1134; Eukaryota.
DR HOGENOM; CLU_002458_2_1_1; -.
DR InParanoid; E9E9S1; -.
DR OMA; RWGGIFP; -.
DR OrthoDB; 54187at2759; -.
DR Proteomes; UP000002499; Unassembled WGS sequence.
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 InterPro; IPR022257; PHM7_ext.
DR PANTHER; PTHR13018:SF53; DOMAIN PROTEIN, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR13018; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR Pfam; PF14703; PHM7_cyt; 1.
DR Pfam; PF12621; PHM7_ext; 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:UP000002499};
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 68..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 531..557
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 577..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 622..650
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 670..694
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 740..762
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 782..803
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 810..827
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 65..214
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 237..517
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 529..801
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 978..1069
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
FT REGION 31..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 889..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 365..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 889..909
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1077 AA; 120855 MW; B82A7A1D2E3AC613 CRC64;
MALDSAPHLT DAAISHLWHF IETRGLDLDV GGSQDPRQGS ARNDSSGGGT LSQTAGSKGS
SLGKLGTTFI PVSIFTAVCL VIFTVLRRFC KRVYAPRTIP ELRSPDSVPS PALPGGWLDW
IVPFFKTPDT IVLNHGSLDG FFFLRFLKIL RNICLAGCLI TFPVLFPIHA TGGSGLTQLE
MLTIGNVKDP QKLLAHVFVA WAFFGFVLYM IVRECIYYVN LRQAYLSSPY YADRISSRTI
LLTCVPKEYL DERRLRKLYG DSLRRVFIPR TSKALVKMVK EREQTAERLE KAEIALIRIA
NLARQKKLAK DPKLADSSTA AASTTESAGS KQDLVVIPSD STANATCRGD PDEAESPGSI
TCLESLRRDP DKDSHTSQHE GTKLNNITAD ENEKLDQVDD EYEHPYGLSM DLPDVRGSVA
AQWIPVERRP YHRPIGNFGR RVDTIRWTRS RLRDLNLQIF KMRRQVRRGD GITLPSVFIE
FYTQEAAQAA HQVLTHHRPL QMSSRLLGIR PDEIIWSCLR MPWWELIIRR FGILTLVTAA
IIFWAVPSAF IGTISNIDSL TQKIEFLSFL NKLPGVILNF IQSFMPAVVL SLWMAAVPWM
LRFCGAQSGI PTITRVELFV QNVYFAFQVV QVFLITTLTS AASSALGKIL SNPLGTKDLL
AENIPKASNF YLSYIMIQCL MSGGMRLIQV FGLIRHYIVG RVSEVPRTRY KRWCKLESAY
WGGVYPVYTN MGVIALSYSC IAPLVLLFAA GGLFATQVVW KYNLLYVLDS DMDTKGLFYP
RALIHLTIGL YLAEICLIGL FALKGAFAPL ALMVLFFIFT GLVQFSLSDA IAPLLLNLPQ
TLPLEGEIQE EEKAKALREK ELATARLEGE SGVAGAANDY YDSEQVFGDE EQMEQSDTEE
EEEEEESGDE HGPVTGTRAV EGAASIGSTL KEWAKATTQA KVNKTINSPD VQEFLARIQF
WKHDKHANDK PPGFLARWLH PEEYEDFVAL RNTIPGDQLR HVEYPSEFRK RCYLPPEMWA
PKPTLWIPRD EARVSRQEVA HTKKYTPISD KGAELDEKGG VVVYFDKAPI KKDRMLL
//
