ID A0A0D2JG45_9EURO Unreviewed; 1280 AA.
AC A0A0D2JG45;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=DUF221 domain protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=Z518_02966 {ECO:0000313|EMBL:KIX08310.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX08310.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX08310.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX08310.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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; KN847476; KIX08310.1; -; Genomic_DNA.
DR RefSeq; XP_013275446.1; XM_013419992.1.
DR AlphaFoldDB; A0A0D2JG45; -.
DR GeneID; 25291037; -.
DR VEuPathDB; FungiDB:Z518_02966; -.
DR HOGENOM; CLU_002458_2_0_1; -.
DR OrthoDB; 54187at2759; -.
DR Proteomes; UP000053617; 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; PROBABLE MEMBRANE PROTEIN DUF221-RELATED; 1.
DR PANTHER; PTHR13018:SF20; SPORULATION-SPECIFIC PROTEIN 75; 1.
DR Pfam; PF14703; PHM7_cyt; 2.
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:UP000053617};
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 27..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 109..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 654..674
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 712..733
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..780
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 800..829
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 875..893
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 913..935
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 947..965
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..188
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 212..281
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 563..646
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 661..932
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 1199..1271
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
FT REGION 313..368
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..501
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1007..1029
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1015..1029
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1280 AA; 145192 MW; 00A5659208FB8A9E CRC64;
MSLNDTFNLG GNSTAAEQKN GLSAGQFAAS LVTAISIFGI EIVLFLLIKD RFARIYQPRT
YLVPERERTN PSPPGWWEWI KPVVATSNSE FVQKCGLDAY FFLRYLRTLL KVFVPAALVI
LPILIPMNTI DGRGAKFATG KYENETNVTG LDQLAWGNVA PEHTRRYWAH WVLALALITW
VCYVAFDELR NYIRMRQAYM TSPQHRLRAS ATTVLVSSIP RKWCNVEALD GLYDVFPGGL
RNIWINRNFD ELSEKIKQRD KLAATLEAAE TELIKKCFKK NDEDVAKAEK KAGKKLTKDE
RKLRATMKNE AGTNAAHGHG ISAGNPHQVN HNLHDAIDGH DGDSSFASSS DAKEEVEEPP
RNRRAIPIPV IGEGISAVTQ GLDRFGDRIM GGIRGVNREV HDTIDTTNGF VAADADHEEM
GRSSGEQSGP QNECSSSAPK TQNDPCQKRT TGAKDESAKG QPQPSNRGRS FEKSIRDEGP
LSPISQSSTM RDDKVRPEKS LTQFDKFKKA IGLGSEDKEP VEYPAAFEEE FEHEPDDAVW
RRYLSDKDRE TMRLPIFGWQ WMPSLPLIGQ KVDTIQYCRK EVARLNVEIE DDQAHPERFP
LMNSAFVQFN HQVAAHMACQ ALSHHIPKQM APRLVEIDPN DVIWDNMSIP WWSAYIRTGG
VITTVTGMII LWAIPVAFTS ALSQLETAAK TWTWLHWVLD IPPWFRSVLQ GVLPAALLGL
LMFLLPLILR FLVRLQGTQS GMLIELSVQK YYFCFLFVQL FLVVSIASAL TQFFALFTSV
DGWTSVPSLL GTNIPKASNY FFSYMLLQAL SVSAGALLQV GSLIGWFILA PLLDSTARSK
FKRHTQLSDV QWGTFFPVYT NLACIGLIYS VISPLILLFN IITFTLFWFT YRYNTLYVTR
FTRDTGGLLY PNAINYTFVG LYVMEIALIG MFFLVRDQNG DVACTGQAVG MIVIFILTAG
YQLLLNNAFS PLFRYLPITL EDDAVRRDEE FARAMQKRHG FIENEVEGED LEDQLERNEQ
QSIEEDRQEQ AYELQQIERD KQARLERQKS QKLPESEPYE SQNAEVKMNV DQENKGMRMV
QAAAHRTAET TKHIMPPTFS RRYDRKSWAD RGNVRNRRAS NFGEWESPLQ SQSLHRSESD
LQQRKSHKRV ISDPKDMLNR LNNFNPLMGN EKDVEAQRAA RNQLADALFS GINDELEDLT
PDERDKLVQR AFQHSALRAK RPVIWIPRDE LGVSDDEIHR MGRFSNHIWV SNVRQGLDSN
GRCVYSGAPP DFSEVDLIQL
//
