ID F2PNF4_TRIEC Unreviewed; 816 AA.
AC F2PNF4;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE SubName: Full=IdgA domain-containing protein {ECO:0000313|EMBL:EGE03422.1};
GN ORFNames=TEQG_02458 {ECO:0000313|EMBL:EGE03422.1};
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).
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DR EMBL; DS995727; EGE03422.1; -; Genomic_DNA.
DR AlphaFoldDB; F2PNF4; -.
DR VEuPathDB; FungiDB:TEQG_02458; -.
DR eggNOG; KOG3009; Eukaryota.
DR HOGENOM; CLU_012201_3_0_1; -.
DR Proteomes; UP000009169; Unassembled WGS sequence.
DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004730; F:pseudouridylate synthase activity; IEA:InterPro.
DR CDD; cd01941; YeiC_kinase_like; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR Gene3D; 3.40.1790.10; Indigoidine synthase domain; 1.
DR HAMAP; MF_01876; PsiMP_glycosidase; 1.
DR InterPro; IPR022830; Indigdn_synthA-like.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR007342; PsuG.
DR InterPro; IPR029056; Ribokinase-like.
DR PANTHER; PTHR42909:SF1; PFKB DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR42909; ZGC:136858; 1.
DR Pfam; PF04227; Indigoidine_A; 1.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF110581; Indigoidine synthase A-like; 1.
DR SUPFAM; SSF53613; Ribokinase-like; 1.
PE 3: Inferred from homology;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Manganese {ECO:0000256|ARBA:ARBA00023211};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 428..587
FT /note="Carbohydrate kinase PfkB"
FT /evidence="ECO:0000259|Pfam:PF00294"
FT REGION 371..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 816 AA; 87665 MW; 9AD0783A41347083 CRC64;
MSTPVLRARS ALARSFLRAP AWATARQYSR PALAGLNKFL KVSEEVEDAI ATGKPVVALE
TTIYTHGFPY PDNMDLAMRL ESIVRSTGGV PATIGVIDGV ARVGMNQTEL TELASTSQRT
KVHKVSRRDL GYICGAGIRG NLMNGGTTIA GTMILAHLAG IKVFATGGLG GVHRGGETTM
DISADLTELG RTPVAVVSSG CKSFLDIQRT LEYLETEGVV VAAFADGRKG DIDFPAFFTR
DSGIKAPRVI QNAEDAAAII YAQSQLQLKS GMLFTNPVPE EHSFPKPEMD AIISRAIELA
HIEGIQGSDN TPYVLAKIEE LSGGRSVATN RALVEYNVEV GTRVAIELAK LESENGKDLD
RSVAGNIPIN QAHAEESQDG IESSVESTDT PSIQEVEQEE PELLVAGSLA VDLACDYTPL
SNGPSDGSPK LQTSNPSVIT QTLGGVGHNV ALAASYMGSS VMFCSVVADD ISGRSALDTI
QDTYNPFFQS EGIQLLPSAP DARTAQYIAV NDAKKDLMIA MADMSILELP ESKLNFRAYW
EPLVKDQVVP PSWAVVDANW GSEAATEWIQ LCRRQGIKIA LEPVSAPKAA RLFYRQNDTP
SHVPVIRATD MAPDSHVIDL AAPNRYELAA MHAAARDTGH FDSPEWWRII DALQLPSNGS
RVRLISLTNA EIVNEGIPQQ TIQLLPLIPC ILTKLGPQGV LLTQILWPGD QRLTMKDYAP
YILGRGQVDD SPVGGVYMRL FPPEETLSES DIVSVNGAGD TLLGVVMAAL GRGGRDREVR
VEDVIPIAQK ASVMTMKSKH SVSPEISQLA PLLESL
//
