ID A0A177CMB9_9PLEO Unreviewed; 553 AA.
AC A0A177CMB9;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=RING-CH-type domain-containing protein {ECO:0000259|PROSITE:PS51292};
GN ORFNames=CC84DRAFT_536843 {ECO:0000313|EMBL:OAG08092.1};
OS Paraphaeosphaeria sporulosa.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Massarineae; Didymosphaeriaceae;
OC Paraphaeosphaeria.
OX NCBI_TaxID=1460663 {ECO:0000313|EMBL:OAG08092.1, ECO:0000313|Proteomes:UP000077069};
RN [1] {ECO:0000313|EMBL:OAG08092.1, ECO:0000313|Proteomes:UP000077069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP3s5-JAC2a {ECO:0000313|EMBL:OAG08092.1,
RC ECO:0000313|Proteomes:UP000077069};
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.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KV441550; OAG08092.1; -; Genomic_DNA.
DR RefSeq; XP_018038457.1; XM_018186660.1.
DR AlphaFoldDB; A0A177CMB9; -.
DR STRING; 1460663.A0A177CMB9; -.
DR GeneID; 28770146; -.
DR InParanoid; A0A177CMB9; -.
DR OrthoDB; 2730627at2759; -.
DR Proteomes; UP000077069; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR011016; Znf_RING-CH.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR46283:SF2; AT07234P-RELATED; 1.
DR PANTHER; PTHR46283; E3 UBIQUITIN-PROTEIN LIGASE MARCH5; 1.
DR Pfam; PF12906; RINGv; 1.
DR SMART; SM00744; RINGv; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR PROSITE; PS51292; ZF_RING_CH; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000077069};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 451..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 504..527
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 75..150
FT /note="RING-CH-type"
FT /evidence="ECO:0000259|PROSITE:PS51292"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 329..356
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 392..409
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 553 AA; 61139 MW; 6C726308A2C3E3DC CRC64;
MASLPPQQHQ QRRPSPPAES ARPEQSNAAR TNSFSADSVD SQTLLLNSPP TEAVKPTEAD
ATQQHAPAQA EAQSAEDNEP RRCWICFNDE TEDDENTSEW RSPCPCVLVA HEKCLLDWIA
DMEAPDSRLR LGTTRGKILC PQCKAEIKLD RPRNVIVEYV RMTEKMTKML QLPIIFFVAG
TATYTTLRWF GKDIVYKIFG VQDAQTILRH RCVPSGLPSE SITMHLLNHI RKNWQIDLGL
PAIPVILVLS RTRMADSFLP FLPLIFLAGG GADAAQGDSL LQITWPPSAA FTVAALPYVR
SIYNSYYDRF WAPHERRWLK EVQPRAGTED EIEADAQDME DDAEAILNAI ADEDEDGEDG
EDIVEVEVDV DLLFDWNAGG AADNNNAPEN PPVPIARGPA APPLEAPPVE DGAPVAAAAN
QEEEDAAAPA PNVPQQHAQP RRPRIRRERN NISLTGSIVD TILGTFIFPG LAGTFGEVLR
IALPKSWVTP PSSGKPTGFL QNRWARSIVA GCLLVGLKDA FVLYARWKTA QNHRQRKVLD
YDGSKGKRKN KST
//
