ID A0A178EZP0_TRIRU Unreviewed; 1713 AA.
AC A0A178EZP0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=D-lactate dehydrogenase (cytochrome) {ECO:0000256|ARBA:ARBA00038897};
DE EC=1.1.2.4 {ECO:0000256|ARBA:ARBA00038897};
GN ORFNames=A7C99_2707 {ECO:0000313|EMBL:OAL65610.1};
OS Trichophyton rubrum (Athlete's foot fungus) (Epidermophyton rubrum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=5551 {ECO:0000313|EMBL:OAL65610.1, ECO:0000313|Proteomes:UP000243015};
RN [1] {ECO:0000313|EMBL:OAL65610.1, ECO:0000313|Proteomes:UP000243015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCC(F)T1i {ECO:0000313|Proteomes:UP000243015};
RA Zhan P., Tao Y., Liu W.;
RT "Genome sequencing of Trichophyton rubrum CMCC(F)T1i isolated from hair.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the eukaryotic ribosomal protein eS4 family.
CC {ECO:0000256|ARBA:ARBA00007500}.
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:OAL65610.1}.
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DR EMBL; LHPM01000013; OAL65610.1; -; Genomic_DNA.
DR VEuPathDB; FungiDB:TERG_02402; -.
DR VEuPathDB; FungiDB:TERG_02403; -.
DR VEuPathDB; FungiDB:TERG_02404; -.
DR Proteomes; UP000243015; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008271; F:secondary active sulfate transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd06087; KOW_RPS4; 1.
DR CDD; cd00165; S4; 1.
DR CDD; cd07042; STAS_SulP_like_sulfate_transporter; 1.
DR Gene3D; 2.30.30.30; -; 1.
DR Gene3D; 2.40.50.740; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR Gene3D; 3.30.70.2740; -; 1.
DR Gene3D; 3.10.290.10; RNA-binding S4 domain; 1.
DR Gene3D; 3.30.750.24; STAS domain; 1.
DR HAMAP; MF_00485; Ribosomal_S4e; 1.
DR InterPro; IPR004113; FAD-bd_oxidored_4_C.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR016164; FAD-linked_Oxase-like_C.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR014722; Rib_uL2_dom2.
DR InterPro; IPR000876; Ribosomal_eS4.
DR InterPro; IPR032277; Ribosomal_eS4_C.
DR InterPro; IPR013845; Ribosomal_eS4_central_region.
DR InterPro; IPR038237; Ribosomal_eS4_central_sf.
DR InterPro; IPR041982; Ribosomal_eS4_KOW.
DR InterPro; IPR013843; Ribosomal_eS4_N.
DR InterPro; IPR018199; Ribosomal_eS4_N_CS.
DR InterPro; IPR018045; S04_transporter_CS.
DR InterPro; IPR036986; S4_RNA-bd_sf.
DR InterPro; IPR011547; SLC26A/SulP_dom.
DR InterPro; IPR001902; SLC26A/SulP_fam.
DR InterPro; IPR002645; STAS_dom.
DR InterPro; IPR036513; STAS_dom_sf.
DR InterPro; IPR016171; Vanillyl_alc_oxidase_C-sub2.
DR NCBIfam; TIGR00815; sulP; 1.
DR PANTHER; PTHR11748; D-LACTATE DEHYDROGENASE; 1.
DR PANTHER; PTHR11748:SF111; D-LACTATE DEHYDROGENASE, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF16121; 40S_S4_C; 1.
DR Pfam; PF02913; FAD-oxidase_C; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR Pfam; PF00900; Ribosomal_S4e; 1.
DR Pfam; PF08071; RS4NT; 1.
DR Pfam; PF00916; Sulfate_transp; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR SUPFAM; SSF55103; FAD-linked oxidases, C-terminal domain; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00528; RIBOSOMAL_S4E; 1.
DR PROSITE; PS50889; S4; 1.
DR PROSITE; PS01130; SLC26A; 1.
DR PROSITE; PS50801; STAS; 1.
PE 3: Inferred from homology;
KW Kinase {ECO:0000313|EMBL:OAL65610.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Reference proteome {ECO:0000313|Proteomes:UP000243015};
KW Ribonucleoprotein {ECO:0000256|ARBA:ARBA00023274};
KW Ribosomal protein {ECO:0000256|ARBA:ARBA00022980};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|PROSITE-
KW ProRule:PRU00182};
KW rRNA-binding {ECO:0000256|ARBA:ARBA00022730, ECO:0000256|PROSITE-
KW ProRule:PRU00182}; Transferase {ECO:0000313|EMBL:OAL65610.1};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 83..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..269
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 412..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 457..480
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 487..504
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 555..688
FT /note="STAS"
FT /evidence="ECO:0000259|PROSITE:PS50801"
FT DOMAIN 991..1168
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
FT REGION 719..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 743..757
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1713 AA; 188987 MW; 53A7B001A88A5BFF CRC64;
MSASKLGRTL AKAVGIDVDY RKEPRESMRT AAESIRSLEH FDEDEPSAKE WLRNHSPTVK
GTVDYFNSLF PFWNWIFHYN TQWLIGDIIA GVTVGFVVVP QGMAYALLAR LPPEYGLYTS
FVGFILYWAF ATSKDITIGT VAVMSTIVGN IVTKVQAKEP DISAPTIARA LSLIAGGFLL
FIGLTRLGWI VEFIPLVAIT SFMTGAAISI GVGQIPAMMG LKEVNNREST YKVFINVLKN
LGHTRLDAAM GLSALVVLYV IRFFCNYMSQ RQPNRRKMWF FISTLRMTFV ILLYTMISWL
VNRHVKDYKK AKFKILGPVP KGFQHAGVPE IEARLVKAFA PDLPATIIVL IIEHIAISKS
FGRINNYVIN PSQELVAIGF TNLFGPFLGA YPATGSFSRT AIKSKAGVRT PLAGIFTAVI
VLLALYALTS VFFYIPLASL SGLIIHAVGD LITPPNVVYQ FWEVSPLEVF IFFGGVLLTI
FTEIENGIYL TIAASAALLI YRIAKAKGTF LGQVKVYRVT KDDSLRKSDK FGEDAKLNSR
EAFLPVEHQD GSNPLIEAQS PHPGVFIYRF NEGFTYPNEG RYLHHLTEYI FKVTRRTQLD
TFAKLGDRPW NDPGPRRSEA VNVHDARPIL RAIILDFSSV NHVDVSSIQG LIDVRNQLDR
YAAPEIVEWH FACISNRWTK RALASAGFGY PSPKSPELLG NWRPIFSVAA VGAEEVVNDK
PGTSHRANAS SNPAAPSDDL EIGHAPSSDE GEYEDEKTNT QIITNQVNSS SHALPRRVGN
VHSINRPFFH IDIQAAVEST LLNIETRTAS AKNSSAPSVT KGFAGEISTG KAIKTQSALH
ASGRYQTGLQ TDIKSIMNFA PRLSARAIPR GLRAIRQPHQ HHGQNIARRW ISTAAGRGAE
VSLGLPWKTG QVVGALAVAI GAGYALGVYN SGSASLGLLG HKHEVSPVYG SIKDFERAIV
ELREVLGEDA ISTDDEDLRL HGYSEWSTVN CDQLPVAVAY PKSTADVSKI AQVCYKFKVP
MVPFSGGSSL EGNFSAPFGG MSIDFAHMDK IIKLHPDDLD VVVQPSIQWM ELNEQIKQSG
LFFPIDPGPS AKIGGMIGTN CSGTNAVRYG TMKDWVINLT VVLADGRVIK TRNRPRKSSA
GYNLAGIFVG SEGTLGLVTE ATLKLAVIPE ESRVGIATFP SIRDAANVAM AVIRSGVQVQ
CVEILDDVHM DIINRAGGTN RTWKPATTLF FKFSGTRNGV ADSISRTKSI AREHNSTSFE
FARTDQEGHE LWSARKQTLW SMLALRKEGS DDIWSTDVAV PLSRLPDIIE LSKKDLDELD
LFAGIVGHIG DGNFHEGIVY NRNNPEEVSR IEKCVHDMVD RALEMDGSCT GEHGIGLGKK
KYLVKELGMD TLNVMRSIKR SLDPLWLLNP GKIFDAVPAC IVKAGCLEAK SLATRRHRRL
LDKPNSNVDK YIKMARGPKK HQKRLSAPSH WLLDKLSGAY APRPSPGPHK LRDCLPLIVF
LRNRSLKYAL NGRETNSILM QRLVKVDGKV RTDSTYPAGF MDVITIEKTG ENFRLIYDTK
GRFTVHRIQA EEAEYKLGKV KRVQLGKGGI PFLVTHDART IRYPDPSIRV NDTVKIDIAT
GKITDFIKFD TGVIAMATGG RNMGRVGVIT HRERHDGGFG IVHIKDAIDN TFATRESNVF
VIGQEKPWVS LPKGKGVKLT IAEERDRRRA MTN
//