ID A0A178E0I5_9PLEO Unreviewed; 1249 AA.
AC A0A178E0I5;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=DUF221-domain-containing protein {ECO:0000313|EMBL:OAL48901.1};
GN ORFNames=IQ07DRAFT_680958 {ECO:0000313|EMBL:OAL48901.1};
OS Pyrenochaeta sp. DS3sAY3a.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Cucurbitariaceae;
OC Pyrenochaeta.
OX NCBI_TaxID=765867 {ECO:0000313|EMBL:OAL48901.1, ECO:0000313|Proteomes:UP000077535};
RN [1] {ECO:0000313|EMBL:OAL48901.1, ECO:0000313|Proteomes:UP000077535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS3sAY3a {ECO:0000313|EMBL:OAL48901.1,
RC ECO:0000313|Proteomes:UP000077535};
RG DOE Joint Genome Institute;
RA Zeiner C.A., Purvine S.O., Zink E.M., Wu S., Pasa-Tolic L., Chaput D.L.,
RA Haridas S., Grigoriev I.V., Santelli C.M., Hansel C.M.;
RT "Comparative analysis of secretome profiles of manganese(II)-oxidizing
RT ascomycete fungi.";
RL Submitted (MAY-2016) 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; KV441647; OAL48901.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A178E0I5; -.
DR InParanoid; A0A178E0I5; -.
DR OrthoDB; 54187at2759; -.
DR Proteomes; UP000077535; 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:UP000077535};
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 133..152
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 682..707
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 727..752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 773..797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 822..850
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 895..913
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 934..953
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 965..985
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 31..200
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 226..298
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 561..669
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 681..952
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 1168..1240
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 413..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1016..1128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..372
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..503
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1061
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1062..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1249 AA; 140586 MW; 522B1BF118A9AE42 CRC64;
MSDTAAASST PTPANNQGIG RNAENQSIEN FAASLSTAAV IFGVQISIFL ILSGNWKLHK
TKKSAASESS STERQSLFHK IYYYKTAFVP KAKRIAAPVT ALESFKNVFT ISDRELVRIA
GVDGYLFLQY LQLLLRIFVP MALVILPILL PINRVGDVDG VSGLDSFAWP NVGVPTKVYR
LWAHLILAVS VVLWVCFNFY LALRKFIRLR QTILTLPEHR IRASATTILV QSIPRKWLTV
PALDALYDVF PGGIKDIWIN RNFDNLMDKV NQRTKIARQL ESAETNLIIA CTKKHKKMQE
KAAKEAGEKK RSNKEKKREE QLQNEAIDLG MHDSGEDAGN PHQIEEQLQQ VLQEEGSASS
SSSSSRSSSP SRRKGLIPIP LVGQGFHAVG EGIRDVGQGV DRFNKKIFSG VKGAFGGKQH
HEHKDERDHY EPQLDGTVEV PGSSPTSADF AQRGASSDTY TPLAAPAKEK YGSEGTATEP
NSPKPAETVD PHEENEKPTK GGFRPWQKLK AAYFGQGDFA SPQPYRQQGE VLPMEIKDPE
KIKYQTIGLY DDSFAEDGEN AIWRTYLKPK DRETMRIPLF NVSWWPALPL VGKKVDTIYH
CRKELARLNA EIADDQAHPE RFPLMNSAFI QFNHQVAAHM ACQSISHHIP RQMAPRTVEV
NPNYVLWDNL TMKWWERYLR MLGVILIIAA LIVFWGIPVS FTGALSQVKT LTNKLPWLGW
INDLPEWAIS FIQGVLPPAF LAILFAVLPL VLRFLAGVTG TTTSGERELL VQNFYFAFVF
VQLFLVVSIS TGITTAIEDL VNDPISIPAT LAKNLPRSAN YFFSYMILQA LSISSGTLLQ
IGAVVVIVFL RFLDTTPRQK VSRVLSRPGI NWGTMIPVYT NFGAIGIIYS VVSPLILIMM
LITFCLFWFT YRYQMIYVSY AKAETNGLIF PKAVNQLFTG LYFLELCLIG LFFLQRDVNL
NVSCFPQAII MIVTLVFTVL YQIVLNRAFG PLFTYLPITF EDEAVMRDEE WQRAQASRWE
KDNEEHQSLT AEQTAMQTAE ERELAHLKDQ NRLDRKQRES SYGPSSYELD NLDSNQSTVN
GLSGGAERKS RPKSNWAEKS RNSSASRSRS RSHAHTSKKP KRKDPLDFVT DTLKRGLDDV
TRPVRDIEAQ ILPARNLFDD IDDELADIEP EARQKLIKRS FQHPATRALQ PAIWIPQDDL
GVAKDEIQRT SAYTKKIWIT SINARLDAGG NVIYRGLPPD RDPFENIEV
//
