ID A0A0G2EM78_9EURO Unreviewed; 803 AA.
AC A0A0G2EM78;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Putative n-carbamoylsarcosine amidase {ECO:0000313|EMBL:KKY23857.1};
GN ORFNames=UCRPC4_g02670 {ECO:0000313|EMBL:KKY23857.1};
OS Phaeomoniella chlamydospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Phaeomoniellales; Phaeomoniellaceae; Phaeomoniella.
OX NCBI_TaxID=158046 {ECO:0000313|EMBL:KKY23857.1, ECO:0000313|Proteomes:UP000053317};
RN [1] {ECO:0000313|EMBL:KKY23857.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY23857.1};
RA Lawrence D.P., Travadon R., Rolshausen P.E., Baumgartner K.;
RT "Distinctive expansion of gene families associated with plant cell wall
RT degradation and secondary metabolism in the genomes of grapevine trunk
RT pathogens.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKY23857.1, ECO:0000313|Proteomes:UP000053317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCRPC4 {ECO:0000313|EMBL:KKY23857.1};
RA Morales-Cruz A., Amrine K.C., Cantu D.;
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O(in) = H2O(out); Xref=Rhea:RHEA:29667, ChEBI:CHEBI:15377;
CC Evidence={ECO:0000256|ARBA:ARBA00034651};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:KKY23857.1}.
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DR EMBL; LCWF01000064; KKY23857.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G2EM78; -.
DR OrthoDB; 2380373at2759; -.
DR Proteomes; UP000053317; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006351; P:DNA-templated transcription; IEA:InterPro.
DR CDD; cd12148; fungal_TF_MHR; 1.
DR CDD; cd00067; GAL4; 1.
DR Gene3D; 1.20.1080.10; Glycerol uptake facilitator protein; 1.
DR InterPro; IPR023271; Aquaporin-like.
DR InterPro; IPR000425; MIP.
DR InterPro; IPR007219; Transcription_factor_dom_fun.
DR InterPro; IPR036864; Zn2-C6_fun-type_DNA-bd_sf.
DR InterPro; IPR001138; Zn2Cys6_DnaBD.
DR PANTHER; PTHR47338:SF5; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG); 1.
DR PANTHER; PTHR47338; ZN(II)2CYS6 TRANSCRIPTION FACTOR (EUROFUNG)-RELATED; 1.
DR Pfam; PF04082; Fungal_trans; 1.
DR Pfam; PF00230; MIP; 1.
DR PRINTS; PR00783; MINTRINSICP.
DR SMART; SM00906; Fungal_trans; 1.
DR SUPFAM; SSF81338; Aquaporin-like; 1.
DR SUPFAM; SSF57701; Zn2/Cys6 DNA-binding domain; 1.
DR PROSITE; PS50048; ZN2_CY6_FUNGAL_2; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053317};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 636..660
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 672..695
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 702..724
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 744..764
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 52..88
FT /note="Zn(2)-C6 fungal-type"
FT /evidence="ECO:0000259|PROSITE:PS50048"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 506..540
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..111
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..137
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 780..795
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 803 AA; 88237 MW; 379A63873FAF2787 CRC64;
MHTPQLTPQS AHVPQFPKQS APQPQHSQPR QLSQENDSSS KSAVKHRRAP VACRRCRRLR
SKCLHTNAKP PCGPCYEAGP QEAAECFFPA RGEPDKDREF RRRRIKASER SQTGDARSSS
VTLPKSTSVN GGTVASSPSA GLPEDRWDLL PPLDEVIEGC RVFFTSYFQL GFLPKAMFIE
RLQRDQRSIN PLLLLGLLGI TARFVPKLVK RYGGPVQATQ IMIEHARKLV FEEMYAPSLE
RIQGFFLLGV AEWGNGDKIQ SSIHMGIAVR MAGIMRLHQE EAYDVSKSAT ADEVVNSEVA
RRTFWVIVSQ DSLHSGATTP ACFSLNDITA LLPCDEADFA FGNIPKERAA LSGTQAAKYD
DRLAYLAIVM VLRLSNIVVR RIYLEDIMNA KTNQSDDGAP PAFWDQMSMD LFTNVLELHE
QVDAFFSLRS HDEGFPAMIV FSVYTCGSLA YYLSRWPQLC PPLMSRSSII LDRSMEVLKT
LSGAWPLAMR WQQALTRVAL RNTAIGTGDL HSEGPPAEQY GEMPVPKSEP ERQQHRPMSR
PSASANLELL INAAVQNDAQ SQMPNQLAPN PGPQQGYLNV EYSSQPYLSP SAFAADDFET
ELYVFLQGGE ASAFWNSAVV LGMCVAGSLP WIRGAFLVPA QILGGIIAAA LVSCMLPGPI
SVNTTLGPGV SIAQGVFIEM FLTAQLIFVI LMLAAEKHRA TFIAPIGIGL ALFVSMLAGV
YYTGASLNPA RSFGPSVASA SFPGYHWIYW VGPALGALLA ALYYRFVKWS NYEEVNPGQD
ATSETEKERS TSEAEAAQAR EMA
//
