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Database: UniProt
Entry: A0A1Y2HVM2_9FUNG
LinkDB: A0A1Y2HVM2_9FUNG
Original site: A0A1Y2HVM2_9FUNG 
ID   A0A1Y2HVM2_9FUNG        Unreviewed;      1065 AA.
AC   A0A1Y2HVM2;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=PAS domain-containing protein {ECO:0000259|PROSITE:PS50112};
GN   ORFNames=BCR44DRAFT_1429871 {ECO:0000313|EMBL:ORZ37743.1};
OS   Catenaria anguillulae PL171.
OC   Eukaryota; Fungi; Fungi incertae sedis; Blastocladiomycota;
OC   Blastocladiomycetes; Blastocladiales; Catenariaceae; Catenaria.
OX   NCBI_TaxID=765915 {ECO:0000313|EMBL:ORZ37743.1, ECO:0000313|Proteomes:UP000193411};
RN   [1] {ECO:0000313|EMBL:ORZ37743.1, ECO:0000313|Proteomes:UP000193411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PL171 {ECO:0000313|EMBL:ORZ37743.1,
RC   ECO:0000313|Proteomes:UP000193411};
RG   DOE Joint Genome Institute;
RA   Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA   Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA   Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA   Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA   Visel A., Grigoriev I.V.;
RT   "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ERT1/acuK family.
CC       {ECO:0000256|ARBA:ARBA00010855}.
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:ORZ37743.1}.
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DR   EMBL; MCFL01000011; ORZ37743.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2HVM2; -.
DR   OrthoDB; 2869796at2759; -.
DR   Proteomes; UP000193411; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProt.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.30.450.350; CHASE domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR006189; CHASE_dom.
DR   InterPro; IPR042240; CHASE_sf.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   Pfam; PF03924; CHASE; 1.
DR   Pfam; PF00989; PAS; 1.
DR   SMART; SM00091; PAS; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50112; PAS; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193411};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        86..106
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        380..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          426..468
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          485..648
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          678..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          855..884
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..19
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        36..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..514
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..566
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        581..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        616..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        701..723
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1065 AA;  116701 MW;  B3CD2348B733DAA9 CRC64;
     MHSHILPTDP SSPATATYQP AANADVEPDP HPRPILSSRL STSAGRHQGF TPVITTSTGD
     SQDQLRRNRW AKSTLAKWFV RWGPNLAMLF VIMIGIASAT GLYLWFHSVE EQNFSRDFES
     LSRISVRSLE AVMSVRCFQH LRNLAAFGYA VPELTRDTLV TFAKHSSFDA KVVYNLAFFV
     IVPRVQQPDF ERHYNVSVWN SPGSDQLVKN DSFMVMPVLI HPYEERATNR FFGYNALSDP
     SRRTPILTVI ESNSWGISQP IRFKDTGEPG FITWHTVSER EPTALTPFTK YLASVSIAFT
     DLFSTTLNQR LKSPQASDVA VYISFESGER VYEYVPPQNT SATRLNTRRT LHLTFDGFSA
     KWRVDFVPTR RYVKRFQTPV PWVVLGSALA VFVLLSYAAR RGMARFIVSQ QVMKKLRVQD
     TLLESLQEYS KAIIQAIPDG VVMLDEQGWI IGINDAALKM TGYELSDFAQ PKKIDVLLAG
     SGSGAERRQR EMWDKGEDDS EGGSDADENE DDETDPLLSP RHVSDSSSPS RSGNQAPANS
     ISSSPVHARF GTAATTTTTK NRLEPGNQQT RMRRKDGSVF IAQVTISNVD NPPSDGEQAP
     DTATAAEAAA PDSESEPVDS SFSPTIDRRP SELTQAIPPQ LRDAHTSNNG IMHRLEVALP
     MPLLRRLSST NRVGVVSRNS LPQLASDMQA ETQRDQDDYC PAPPAPTPCR SPSPAPAEPE
     PEPEPATRSS SRQLAQVYMF YDCTEKVETL RAVAEMERQA SEAAKAKHQL LEFLVHCMLD
     PLRHMKEDIK AIHAQVVEAR ASDSIGNGND EVEAVNEEEM NEARMAAEHI VRVLEDIAGF
     ADITLASDQV PAGVVTEDAP SPSNTAASNV RAGRPGAGPP PGPGTLGHFV TSCILAQDMM
     DSLASRHIQF TANANPPHAN ILVPGILIDT ITRTKVAQIV RRLLALGETC AQPDGLMTMA
     VELQHLRQVA ATGAYQIVAM MTVSHFDPAL PQSTSLDMAQ LGVSANGGEG EGDLMTRGTK
     FANIGLTWAA VLKMVERMGG KVEQTRVSMQ AGLVVVVTLP LPVAL
//
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