ID A0A1V6U857_9EURO Unreviewed; 376 AA.
AC A0A1V6U857;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=DOMON domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PENCOP_c016G00436 {ECO:0000313|EMBL:OQE34668.1};
OS Penicillium coprophilum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=36646 {ECO:0000313|EMBL:OQE34668.1, ECO:0000313|Proteomes:UP000191500};
RN [1] {ECO:0000313|Proteomes:UP000191500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 31321 {ECO:0000313|Proteomes:UP000191500};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
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:OQE34668.1}.
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DR EMBL; MDDG01000016; OQE34668.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6U857; -.
DR STRING; 36646.A0A1V6U857; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000191500; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd09630; CDH_like_cytochrome; 1.
DR CDD; cd08760; Cyt_b561_FRRS1_like; 1.
DR Gene3D; 1.20.120.1770; -; 1.
DR Gene3D; 2.60.40.1210; Cellobiose dehydrogenase, cytochrome domain; 1.
DR InterPro; IPR015920; Cellobiose_DH_cyt.
DR InterPro; IPR006593; Cyt_b561/ferric_Rdtase_TM.
DR InterPro; IPR005018; DOMON_domain.
DR PANTHER; PTHR47797:SF1; CYTOCHROME B561 DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR47797; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_8G05805)-RELATED; 1.
DR Pfam; PF16010; CDH-cyt; 1.
DR Pfam; PF03188; Cytochrom_B561; 1.
DR SMART; SM00665; B561; 1.
DR SMART; SM00664; DoH; 1.
DR SUPFAM; SSF49344; CBD9-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000191500};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..376
FT /note="DOMON domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012822401"
FT TRANSMEM 219..240
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..271
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 59..148
FT /note="DOMON"
FT /evidence="ECO:0000259|SMART:SM00664"
FT DOMAIN 217..339
FT /note="Cytochrome b561"
FT /evidence="ECO:0000259|SMART:SM00665"
SQ SEQUENCE 376 AA; 41621 MW; FB22FB018ED9D4B5 CRC64;
MVRHIFSWLW ASSALAQVQS FHPQEHDEIT YSFNVPNNTA KSNSGPIYFQ MNSTRQVQWF
AIGQGRQMAG ANMFVVYTSG NNVTVSPRSG VGEIQPLYNK DAQVTVLNGS GVHDGVITAN
IRCDTCLKWN GGTENVNSSS SPWIWAIKYG ESLNSRNLSE DIKHHDDHGV MIIDLQRATG
GSSSNPFAQL DRVSISPSEE DPQYAAFRNT IRKKKTAHAV LMILAFVVMF PFFALGLHIF
PSRWTVKIHG TFQHLTLAVA IAGLGVGVSM ARQIELIDTY HTILGIIIVA SLALFQPAMG
MLQHIFFRKT GRKGPFAFMH RWFGRFIMIL GIINVGLGFK LAQGPRGAVI TTCVVASIIA
MVYIVIVSWI KRPRGN
//
