ID A0A0D2ING9_9EURO Unreviewed; 602 AA.
AC A0A0D2ING9;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Rhinocladiella mackenziei CBS 650.93 unplaced genomic scaffold supercont1.4, whole genome shotgun sequence {ECO:0000313|EMBL:KIX04681.1};
GN ORFNames=Z518_05551 {ECO:0000313|EMBL:KIX04681.1};
OS Rhinocladiella mackenziei CBS 650.93.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Rhinocladiella.
OX NCBI_TaxID=1442369 {ECO:0000313|EMBL:KIX04681.1, ECO:0000313|Proteomes:UP000053617};
RN [1] {ECO:0000313|EMBL:KIX04681.1, ECO:0000313|Proteomes:UP000053617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 650.93 {ECO:0000313|EMBL:KIX04681.1,
RC ECO:0000313|Proteomes:UP000053617};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Rhinocladiella mackenzie CBS 650.93.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; KN847478; KIX04681.1; -; Genomic_DNA.
DR RefSeq; XP_013271817.1; XM_013416363.1.
DR AlphaFoldDB; A0A0D2ING9; -.
DR STRING; 1442369.A0A0D2ING9; -.
DR GeneID; 25293622; -.
DR VEuPathDB; FungiDB:Z518_05551; -.
DR HOGENOM; CLU_006504_7_3_1; -.
DR OrthoDB; 449862at2759; -.
DR Proteomes; UP000053617; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:InterPro.
DR CDD; cd13851; CuRO_1_Fet3p; 1.
DR CDD; cd13877; CuRO_2_Fet3p_like; 1.
DR CDD; cd13899; CuRO_3_Fet3p; 1.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 3.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR001117; Cu-oxidase_2nd.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR044130; CuRO_2_Fet3-like.
DR PANTHER; PTHR11709:SF361; IRON TRANSPORT MULTICOPPER OXIDASE FET3; 1.
DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 1.
DR SUPFAM; SSF49503; Cupredoxins; 3.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 3: Inferred from homology;
KW Copper {ECO:0000256|ARBA:ARBA00023008}; Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053617};
KW Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..602
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002255511"
FT TRANSMEM 559..581
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 33..149
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07732"
FT DOMAIN 159..303
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF00394"
FT DOMAIN 364..498
FT /note="Plastocyanin-like"
FT /evidence="ECO:0000259|Pfam:PF07731"
SQ SEQUENCE 602 AA; 67207 MW; E749A412D0BB6AAE CRC64;
MSISTAQMWL FLLIFTSILQ STLSSNVTYD FNITWVAVNP DGAFTRPTIG VNGQWPPPQI
HANLGDTITV NVLNLLGNQS TSLHFHGLFM NGSTHMDGPA QVSQCAIAPG SSFTYRFRAE
QVGTYWYHSH TQSQYPDGLR APLIIHDPDN PYAEQFDQEL VLTVSDWYHQ QMADLIPQYM
KSGHMMSHEP VPDASLLNDT HDLQVGVVPG KTYLVRMVNM AAFAGQYFWI EGHTMTIVEI
DGVYTRATEA EMIYLASGQR CSFLLTTKSQ SSHNYPFVAS MDQSLFMMAG HVNSDVTGWL
VYDSAHPLPR PKKIDQFNPT DDMTIVPYDE MQLLPKADKS ISLNLEMRHS QGATYYMFND
ISYRSPEIPS LYTALTSGNS ATDPAVYGIS TNPFVLERND VVELVLYNRH MLRHPFHLHG
HHFQAIYRSE EYGGRYEDSG VTEANLPQKP IRRDTLVLPP GGSMVIRFRA DNPGVWLFHC
HMEWHVHTGL VATMIEAPIE LQQQRRSQPL PADHIGACVA TGTPATENDP GQVDDLLDVQ
NENDPTQGKP EGVSISDAVV SLAAGSVLVM TGLVFLVWFG VKNWGARKAQ YAPLAMNVEE
DL
//
