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
//