ID A0A177E3R7_ALTAL Unreviewed; 2081 AA.
AC A0A177E3R7;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 03-MAY-2023, entry version 22.
DE SubName: Full=DUF221-domain-containing protein {ECO:0000313|EMBL:OAG26428.1};
GN ORFNames=CC77DRAFT_1004379 {ECO:0000313|EMBL:OAG26428.1};
OS Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC Alternaria sect. Alternaria; Alternaria alternata complex.
OX NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG26428.1, ECO:0000313|Proteomes:UP000077248};
RN [1] {ECO:0000313|EMBL:OAG26428.1, ECO:0000313|Proteomes:UP000077248}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG26428.1,
RC ECO:0000313|Proteomes:UP000077248};
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.
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DR EMBL; KV441469; OAG26428.1; -; Genomic_DNA.
DR RefSeq; XP_018391849.1; XM_018523263.1.
DR GeneID; 29108857; -.
DR KEGG; aalt:CC77DRAFT_1004379; -.
DR VEuPathDB; FungiDB:CC77DRAFT_1004379; -.
DR OMA; DAHWLEQ; -.
DR OrthoDB; 54187at2759; -.
DR Proteomes; UP000077248; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR InterPro; IPR003864; CSC1/OSCA1-like_7TM.
DR InterPro; IPR027815; CSC1/OSCA1-like_cyt.
DR InterPro; IPR032880; Csc1/OSCA1-like_N.
DR InterPro; IPR038769; MTC4.
DR InterPro; IPR022257; PHM7_ext.
DR PANTHER; PTHR38426; MAINTENANCE OF TELOMERE CAPPING PROTEIN 4; 1.
DR PANTHER; PTHR38426:SF1; MAINTENANCE OF TELOMERE CAPPING PROTEIN 4; 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 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 1167..1193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1205..1222
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1242..1268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1332..1355
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1375..1394
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1613..1634
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1654..1675
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1704..1731
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1813..1840
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1861..1883
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1889..1907
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1247..1396
FT /note="CSC1/OSCA1-like N-terminal transmembrane"
FT /evidence="ECO:0000259|Pfam:PF13967"
FT DOMAIN 1419..1599
FT /note="CSC1/OSCA1-like cytosolic"
FT /evidence="ECO:0000259|Pfam:PF14703"
FT DOMAIN 1613..1883
FT /note="CSC1/OSCA1-like 7TM region"
FT /evidence="ECO:0000259|Pfam:PF02714"
FT DOMAIN 1975..2065
FT /note="10TM putative phosphate transporter extracellular
FT tail"
FT /evidence="ECO:0000259|Pfam:PF12621"
FT REGION 1..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..280
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..764
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 782..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..877
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 897..1000
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1525..1552
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 158..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 218..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..280
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..584
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..763
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 833..858
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 863..877
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 897..924
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..955
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2081 AA; 233145 MW; 60C66547E143D869 CRC64;
MSVPSSHGRP SGDSDRWTTS SHTYIASNSG AYTDNGEGSS SPRRSQDSRP GTGATNGLGG
SAASANLLAR DSVHEEDFAR RKQRVRRSGG FLLDSNFSSG PRQRHANHEA RGEDKGGKRS
SRHYGAHEKE AGSSPLSREV QRDGLSPAAP GAASRIDFAD SQDRHDERMR IGKTRRSAYD
MPSTAHDRDP SPNTAPPRQA IDPNQLVHMA LNLSESRRRH TNTGQLLSSQ PRVASGSQRE
GSFSNYGAGG SLKHYLNEQR RTSRNISPMG KSSPTRHMST SMQRSGSIAF PTSQNINPSA
ATLARVEKAR AYIELRIEYL RLLEFLPPLK PDANAPGNFV FTSTNSPGSP QAQLTRVPSH
AGKQYELGRP YNPLQYIRNR RSRARERVTL HHSSEEFEDV EQVREWVDRV EQQAKRAGYR
RDDAVQLPKI HHDHEVGPAP QKPARPHKGW IFSPQELLAD AHWLEQDDNK MLVENRYGRR
VYPPKEVQQK DFLSPRASKE YSGDRRKSWV DGFPSIAVDH TTGDESDKGS ERGRKRRLLP
ALRTDSPRGG KHSRRGSRLR SHDDSDSSES ESDTRRRKAR IVTDPDHNIG PLALLLEQQA
RQSLSEARPP PDFTPDTPNK WGRNGDVTSE SKPSRDSLEV PRPTNGFAFI KDRGNFKMPP
KPRKNPNLSI DDPEPRSSFD DQDSTAPNTP HAKRFPHIGS DLSPPPSRSE SQTRKAKRGK
FNTIFHSHEH NEDHKHELRP DSAGTDRKGR SRQTSEETPD DKHIGTAILA APGAVMNLLG
HRKNDSVSSL PSPDKLRRRD TQEPHSAVTR FFKGVKNEGT KVGDIIFRRD RADDSDADTM
SDRNSVDFDD DGPVKTKHTK RPPISRTVTA GTDGSITNKE RSHLELPSFR PVHTIADENS
DYEHHISRQA REQKNSRSPR VDRLLPPRMD LGTISGNSST GSLTLTRSHS QERINQVLAR
PGGDMAGLPP TGLRDANRQR SSSRPGLNGR HWSIADGDDN AVDRNKNDAN TVTQADIARV
RALFLCSGVK AREITRRANS TREPPPDFLS RAAATSKMKI YPVPRKEEHV LAARILVKDL
ESSTKALQTS LESFRDKAIQ QLTNQISALQ STVDSDLMPR ILESGDKAVR ITSEVSGQGP
LQVKQITDEI DRMIRTRKRR MRWVRGFGWM LVEWALVALM WCLWLIVVLV GSVKRVFVSE
KTRMFLVLLV FEVAVSRYQR WISRQCSSPK TVAPAMSSHG PSSLAALAAA FIPTAIIATL
YMVAFVLIRH RFPKIYSPRT YIGTVPEKDR TPCPKSPGYF DWIHTMRTVP DKFVLYHQSL
DSYLFLRFMR TLIFICIIGA LITWPVLLPA NWTGGGSSKE LNRFGIGNVK NKDHLYAHAV
VAWVFFSFVM FTVARERLWL IGLRQAWNLS KPNAKRLSSR TVLYLSAPTA ALDEGNMQRF
FGEDAVRIWP ITKGEKLVSL VSERNSKVEE LESAEMSLIL NVNKEVGKSH NRNIKYEQLP
KQMKKSLRPT HKSKTPVVGK EVDSISYYRD QIREKEDDIE KARESNETAE SLGGAAAVFV
EFRTQPAAQR AYQQIASADV LSLTPRFVGT TPNEVVWANL NLAPARRISQ SGVALTLVIA
TIAFWSIPVG IVGALSNVQY LAENFKWLAF LNKIPSGIMS LLSGLLPPLV LSALARYVPN
IFRYIFTTFG EPTKTVIEIK VLKWYFVFQV LQVFLVTTLA SGAAAVASQI VQDPSSVPQL
LAERLPRASN TYLAYFVVQA LTNAPSNILN YTDVLSFWFF DKLFDKTPRQ KYNSYITMRG
MAWGKLFPKY GNFVIIAIVY ACIAPLVLGF AAIGLVIFYW SYRYQLLYTA QPKIDTKGHA
YTLSLQQILV GIYLAEICLI GLFSLRDATG PLIMLVVLLL ATIMFNYTTN RYLAPLEQFL
PADLALESED DEQAPLLSSA EEGESDALEH AESRINRISE RTRVPSNVVS PLARFLQPHV
FGSHTALKAW LRDGDFDEDE EPQYSEEDLK KAYLNPAFTS KTPIVWLAKD SIGASKHEIS
ENEKTGLKAT DQGAWVTGDG KLKWSVDNFE ELPVFKKAIK W
//
