ID A0A2K3Q9N3_9HYPO Unreviewed; 1118 AA.
AC A0A2K3Q9N3;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Uncharacterized protein RSN1 {ECO:0000313|EMBL:PNY24248.1};
GN ORFNames=TCAP_05804 {ECO:0000313|EMBL:PNY24248.1};
OS Tolypocladium capitatum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Tolypocladium.
OX NCBI_TaxID=45235 {ECO:0000313|EMBL:PNY24248.1, ECO:0000313|Proteomes:UP000236621};
RN [1] {ECO:0000313|EMBL:PNY24248.1, ECO:0000313|Proteomes:UP000236621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 113982 {ECO:0000313|EMBL:PNY24248.1,
RC ECO:0000313|Proteomes:UP000236621};
RA Quandt C.A., Patterson W., Spatafora J.W.;
RT "Harnessing the power of phylogenomics to disentangle the directionality
RT and signatures of interkingdom host jumping in the parasitic fungal genus
RT Tolypocladium.";
RL Submitted (AUG-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PNY24248.1}.
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DR EMBL; NRSZ01000931; PNY24248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3Q9N3; -.
DR STRING; 45235.A0A2K3Q9N3; -.
DR OrthoDB; 54187at2759; -.
DR Proteomes; UP000236621; 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; 3.
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:UP000236621};
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 63..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..170
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 532..558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 578..602
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 644..669
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 689..713
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 740..760
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 772..797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 818..838
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 844..864
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 63..211
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 234..518
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 530..604
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 621..762
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 769..838
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 1017..1109
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
FT REGION 36..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..58
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 328..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..408
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 886..904
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 923..948
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 124839 MW; 701CA4AEEED0C079 CRC64;
MPVPPDARHH HHRPAGGAML ERRGFLDIFG GQDPRVGSGR EDSSGGGTLS TTSNSKTSSL
GKLGSTFIPI VIYVAICLVI FTVLRRKCRR VYAPRTIPGL RAPELPSPAL PDGWVDWVVP
FFKIPDTFVL NHGSLDGFFF LRFLKVLRNI CLAGCLILWP VLFPLHATGG GGLSQLDMLT
IGNVKDPKKL YAHAFMAWVF FGFVLYTIVR ECIYYVNLRQ AYLSSPYYSQ RISSRTILLT
NVPKQYLDEH RLRKLYGDSV KRVRIPRTTK ALANLVKERE QTALRLEKAE VELIQKANKA
KQKRLKRAAK EAAKEAAKEP TPASKSQPRP PATATGSVAS QRDLGAVSGG GEDGDMVTRG
GCPVIELPAS LDLDPSEERP GSDGDPDETA KHNETVKEED DEYTHPYGLD PDLPDVRGSV
AAQWIPVQAR PYHRPLGNFG RRVDTIRWTR TRLRELNAQI FKMRRQVRRG DGNTLPAAFV
EFDTQENAQA ARQVLGHHRP LQMSSRILGI RPDEILWKTL RMPWWERIAR RFFILSLITA
AVIFWSLPSA AIGLVSNIDF LAEKIVVLFW IKKLPSVIVN FLQGFVPAIA LSLWMAAIPF
MLRCTFPPFA IRPFTNADAL QVCGAQAGIP SVTMVELFVQ QGYFAFQVVQ VFLVTTLTSA
ASAAFTDIIQ NPLSAKDVLS KNLPMASNFY LSYILIQCLA SSGTNLIQIF ALIRHCVLSR
FTTLPRAQFR TWRKLRPAKW GGIFPVFANM GVIGMFRSVA APAKQANTSL AALSYACIAP
LILIFAAGGM AVVRLVWRYN LIFVFDSDMD SKGLFYPRAL LHLTIGLYLA EVCLIGLFAL
HLSFVPLAMM IMFFIFTALV HLSLGDAIAP LLQNLPQTLT LEEEIQQEEK DAAERARERA
ATRAAEEAAG AGGAANSYYD TEQAFGEEED MNSDGRNEYD DEEEHTDDDD HGTVTNDRAI
EGASGVKSAL AEWLKMSTQS KVQAEAEKSG LGETLAKLRF WRGDKHGDKP PGFLARWLHP
EEYEDFLALR RLIPPDGQPN IAYPDEYYSK YCDYLPPEVW MPKPTLWIPR DEARVSRQEV
AHTKKFTPIS DRGASLDHKG RMVVHFEQAP FGEPRLIL
//
