ID   A0A177DWD6_ALTAL        Unreviewed;       961 AA.
AC   A0A177DWD6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=ZZ-type domain-containing protein {ECO:0000259|PROSITE:PS50135};
GN   ORFNames=CC77DRAFT_694348 {ECO:0000313|EMBL:OAG23109.1};
OS   Alternaria alternata (Alternaria rot fungus) (Torula alternata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Alternaria;
OC   Alternaria sect. Alternaria; Alternaria alternata complex.
OX   NCBI_TaxID=5599 {ECO:0000313|EMBL:OAG23109.1, ECO:0000313|Proteomes:UP000077248};
RN   [1] {ECO:0000313|EMBL:OAG23109.1, ECO:0000313|Proteomes:UP000077248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SRC1lrK2f {ECO:0000313|EMBL:OAG23109.1,
RC   ECO:0000313|Proteomes:UP000077248};
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.
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DR   EMBL; KV441473; OAG23109.1; -; Genomic_DNA.
DR   RefSeq; XP_018388530.1; XM_018532783.1.
DR   AlphaFoldDB; A0A177DWD6; -.
DR   STRING; 5599.A0A177DWD6; -.
DR   GeneID; 29118377; -.
DR   KEGG; aalt:CC77DRAFT_694348; -.
DR   VEuPathDB; FungiDB:CC77DRAFT_694348; -.
DR   OMA; NKHGHHP; -.
DR   OrthoDB; 145583at2759; -.
DR   Proteomes; UP000077248; Unassembled WGS sequence.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd14947; NBR1_like; 1.
DR   CDD; cd02249; ZZ; 1.
DR   CDD; cd02340; ZZ_NBR1_like; 2.
DR   Gene3D; 3.30.60.90; -; 4.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR032350; N_BRCA1_central.
DR   InterPro; IPR000433; Znf_ZZ.
DR   InterPro; IPR043145; Znf_ZZ_sf.
DR   PANTHER; PTHR20930; OVARIAN CARCINOMA ANTIGEN CA125-RELATED; 1.
DR   PANTHER; PTHR20930:SF0; PROTEIN ILRUN; 1.
DR   Pfam; PF16158; N_BRCA1_IG; 1.
DR   Pfam; PF00569; ZZ; 2.
DR   SMART; SM00291; ZnF_ZZ; 4.
DR   SUPFAM; SSF57850; RING/U-box; 4.
DR   PROSITE; PS50135; ZF_ZZ_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077248};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833};
KW   Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW   ProRule:PRU00228}.
FT   DOMAIN          373..425
FT                   /note="ZZ-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50135"
FT   REGION          149..170
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          513..536
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          775..814
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          826..920
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        781..808
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        826..844
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        856..874
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        891..920
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   961 AA;  106436 MW;  3017BF07F87A5C16 CRC64;
     MAATNNVPVT LDTPIVVKVL FRGQTKKFKL PLKDLGAHVL PDKLRSILQL EAGEQVVFER
     YSDSAASYVI LDADKPQVYK TLFRAAKAKL KLRLRATVPG EEPVPAPAPA PMPPHTLPGY
     APSVHRMSSD TLTPQGNAPV SPVIARSPDM EKKEAISPVS PPKTADADGE APVPQAFTAR
     QNFFNNLATA NYNSGLAFRP KPSNVCTSWV VYCNNCNEPM EDEHFHCSVC DGGDYDLCPA
     CVDNGVHCPG SGHWMVKRFV KNGSVVNSTT QRIAPKVKAE EPQQQDIPGA FTDEKQSVTY
     EQEPTRTCNC CVTVLPEKEF VTCIPCDDYD LCLTCHVSNK HGHHPGHTFK PATSETVLPT
     LADFLCNSGR NVRHNAVCDG CDKFIYGVRH KCLNCPDWDY CSDCLKNAKF IHPRHRFVPI
     YEPLAEPMNT ANRHYGIYCD GPLCKDKENL SYIDGIRYKC AVCHDTDFCQ NCEAHPSNKH
     NHTHPLIKFQ TPVRSVSVTT LNDDKQHKSV ARLGDRIADR RSTSTETTPV APSTNAATQV
     QTIVDMKPSA EPQVKKEKIA IRDLLVDSVE PVQEKPVQPI QPTVPIKSEA ISIARSDTAT
     EGLDAHFIRD TIIDGSKICA GHQFVQVWTL RNPGPNAWPR GCSVRHVGGD NMLNIDNTRP
     LSHTDLAEAS ESNILGHTVE AGEEAQFRVL MKAPQREGTA ISYWRLKTPE GMPFGHRLWC
     DIAVVGVPSP VVAQPAIPPA PVQSVPTPTP GSATTFEVAP RSNPLYERLL QARAERMKHV
     QHSQQQQMNL QKMKDAHHSL QQQLDQQKME RVQRVRKAAM ERLLEGRRKV HEETNRRKEH
     EAALATINQE PIVPSKAEIK PEEPVAELPV EEKQRSSEPL ASGMIFPQLD KESPESSTYE
     SSTTAQPMSP SSEKSTVART VTVASDDEFF EDAESVALMS DDGFMTDEEY DILDASDEEM
     P
//