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Database: UniProt
Entry: F2PL56_TRIEC
LinkDB: F2PL56_TRIEC
Original site: F2PL56_TRIEC 
ID   F2PL56_TRIEC            Unreviewed;       477 AA.
AC   F2PL56;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   SubName: Full=CobW domain-containing protein {ECO:0000313|EMBL:EGE02654.1};
GN   ORFNames=TEQG_01689 {ECO:0000313|EMBL:EGE02654.1};
OS   Trichophyton equinum (strain ATCC MYA-4606 / CBS 127.97) (Horse ringworm
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=559882 {ECO:0000313|Proteomes:UP000009169};
RN   [1] {ECO:0000313|Proteomes:UP000009169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4606 / CBS 127.97 {ECO:0000313|Proteomes:UP000009169};
RX   PubMed=22951933; DOI=10.1128/mbio.00259-12;
RA   Martinez D.A., Oliver B.G., Graeser Y., Goldberg J.M., Li W.,
RA   Martinez-Rossi N.M., Monod M., Shelest E., Barton R.C., Birch E.,
RA   Brakhage A.A., Chen Z., Gurr S.J., Heiman D., Heitman J., Kosti I.,
RA   Rossi A., Saif S., Samalova M., Saunders C.W., Shea T., Summerbell R.C.,
RA   Xu J., Young S., Zeng Q., Birren B.W., Cuomo C.A., White T.C.;
RT   "Comparative genome analysis of Trichophyton rubrum and related
RT   dermatophytes reveals candidate genes involved in infection.";
RL   MBio 3:E259-E259(2012).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC         Evidence={ECO:0000256|ARBA:ARBA00001702};
CC   -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. ZNG1
CC       subfamily. {ECO:0000256|ARBA:ARBA00034320}.
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DR   EMBL; DS995723; EGE02654.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2PL56; -.
DR   VEuPathDB; FungiDB:TEQG_01689; -.
DR   eggNOG; KOG2743; Eukaryota.
DR   HOGENOM; CLU_017452_2_1_1; -.
DR   Proteomes; UP000009169; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.1220.10; CobW-like, C-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR036627; CobW-likC_sf.
DR   InterPro; IPR011629; CobW-like_C.
DR   InterPro; IPR003495; CobW/HypB/UreG_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43603; COBW DOMAIN-CONTAINING PROTEIN DDB_G0274527; 1.
DR   PANTHER; PTHR43603:SF1; COBW DOMAIN-CONTAINING PROTEIN DDB_G0274527; 1.
DR   Pfam; PF02492; cobW; 1.
DR   Pfam; PF07683; CobW_C; 1.
DR   SMART; SM00833; CobW_C; 1.
DR   SUPFAM; SSF90002; Hypothetical protein YjiA, C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          207..382
FT                   /note="CobW C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00833"
FT   REGION          239..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..477
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        243..266
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..435
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        436..453
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..470
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   477 AA;  54053 MW;  64AFF3E0A9CFD36D CRC64;
     MANEVEYVVI ESTGISEPMQ VAETFTAEFS AAMLEAEDQI VDADEDSKNI LAEIAELGGL
     HTLASLDTTV TVIDAFNLLS NFDTTEFLSD RYGAKEIVPE DERTISDLMV DQIEFADVVI
     INKIETVNED TRRRIKQLVN LLNPEAKVLE ASYSKVDVRE IIDTKRFNFL KAASGSGWLR
     SLHEMTIMNT ANGQRMAPKP ETLEYGINNF VYSARRPFHP RHLFALLHDK FILLQHSEGG
     DEDEANEGND DDKMDLDEDD GDDEDTEKQG VSGFEQPDPA VILANKRSHV FGPVLRSKGF
     FWLATRPLQF GEWSQAGGML TVSCGGPWFA EVPSDAWPED EDVRKSIEND FKGPWGDRRQ
     ELVFIGEGID TEKITALLDN CLLDDKEMAR WERVMGNKEL SRDEKAELLG TMWEDGWEDW
     PPFEIEGEDD DDEDMEETRP KHYISDYLGP AKKDGHKHHH HHHPHKNGER KKSAKAA
//
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