ID T0M5D6_COLGC Unreviewed; 313 AA.
AC T0M5D6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=UBA/TS-N domain-containing protein {ECO:0000313|EMBL:EQB58741.1};
GN ORFNames=CGLO_00968 {ECO:0000313|EMBL:EQB58741.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB58741.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:EQB58741.1}.
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DR EMBL; AMYD01000218; EQB58741.1; -; Genomic_DNA.
DR AlphaFoldDB; T0M5D6; -.
DR STRING; 1237896.T0M5D6; -.
DR eggNOG; KOG2689; Eukaryota.
DR HOGENOM; CLU_047594_0_0_1; -.
DR OMA; AQHFPRK; -.
DR OrthoDB; 2881978at2759; -.
DR Proteomes; UP000015530; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR CDD; cd01767; UBX; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR46340; UBX DOMAIN-CONTAINING PROTEIN 1; 1.
DR PANTHER; PTHR46340:SF1; UBX DOMAIN-CONTAINING PROTEIN 1; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF54236; Ubiquitin-like; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50033; UBX; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT DOMAIN 1..39
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 79..108
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS50157"
FT DOMAIN 248..312
FT /note="UBX"
FT /evidence="ECO:0000259|PROSITE:PS50033"
FT REGION 91..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 135..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 313 AA; 34799 MW; CE29FD0AEAF1FA03 CRC64;
MTQSDLDQLL DMGFEKARAE LAVKKTGNLN GALEWLEKNQ DKPLDELTAA ADAAKADEDD
ENEVQANIDA LETGVAKSLV CNECGKRFKS QDTASYHATK TDHTDFSEST EEIAPLTDDQ
KAAKLAELRE QLKEKKAKQA LVDKEDAKRN EQIRMKATKE SQEMKEELQR KEQIKEAAKK
RQEKLDDAEA KRRIKAKIEA DKEERRRKAE EAKAAREGRA PQPGPVAAPS VPKTTVNHNE
ARLRLQTSGG NVMKTLPAET TLFEVAQMLQ TENSLEVTSF STTFPKKTFQ GATDFSKTLK
EAGLTPSAVL IVK
//
