ID M9LT71_PSEA3 Unreviewed; 1276 AA.
AC M9LT71;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Molybdopterin synthase sulfurylase {ECO:0000313|EMBL:GAC71724.1};
GN ORFNames=PANT_5c00042 {ECO:0000313|EMBL:GAC71724.1};
OS Pseudozyma antarctica (strain T-34) (Yeast) (Candida antarctica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Moesziomyces.
OX NCBI_TaxID=1151754 {ECO:0000313|EMBL:GAC71724.1, ECO:0000313|Proteomes:UP000011976};
RN [1] {ECO:0000313|Proteomes:UP000011976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T-34 {ECO:0000313|Proteomes:UP000011976};
RX PubMed=23558529; DOI=10.1128/genomea.00064-13;
RA Morita T., Koike H., Koyama Y., Hagiwara H., Ito E., Fukuoka T., Imura T.,
RA Machida M., Kitamoto D.;
RT "Genome sequence of the basidiomycetous yeast Pseudozyma antarctica T-34, a
RT producer of the glycolipid biosurfactants mannosylerythritol lipids.";
RL Genome Announc. 1:E0006413-E0006413(2013).
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DR EMBL; DF196771; GAC71724.1; -; Genomic_DNA.
DR AlphaFoldDB; M9LT71; -.
DR STRING; 1151754.M9LT71; -.
DR OrthoDB; 53913at2759; -.
DR Proteomes; UP000011976; Unassembled WGS sequence.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR CDD; cd00757; ThiF_MoeB_HesA_family; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 1.10.8.270; putative rabgap domain of human tbc1 domain family member 14 like domains; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 1.
DR Gene3D; 1.10.472.80; Ypt/Rab-GAP domain of gyp1p, domain 3; 1.
DR InterPro; IPR000195; Rab-GAP-TBC_dom.
DR InterPro; IPR035969; Rab-GAP_TBC_sf.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953:SF102; ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3; 1.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR Pfam; PF00566; RabGAP-TBC; 2.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00899; ThiF; 1.
DR SMART; SM00450; RHOD; 1.
DR SMART; SM00164; TBC; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
DR SUPFAM; SSF47923; Ypt/Rab-GAP domain of gyp1p; 2.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS50086; TBC_RABGAP; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000011976};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 70..391
FT /note="Rab-GAP TBC"
FT /evidence="ECO:0000259|PROSITE:PS50086"
FT DOMAIN 1140..1271
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 300..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 470..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 648..693
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1221..1250
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1276 AA; 136630 MW; 97B221688072453A CRC64;
MTDPLAASSS PLRPRPSPSP SPSQSVFTAA QSTSTNDPIS SRWASLLGRG VTPAIESLRQ
RGIEGKIASQ DDASLRWIQW KLFLTEHISS IPSSWHAVLQ RDRDAYNELR SRLLRAPDGN
YPPEVGFDGR HTTLESALTG SNSSQKRHTP AVTHDLSVNN PLSLDDSNPW KTYYSTLETR
RVILQDVERT FPDLPLFRQV RVQQSLTNIL FLWALQNEDV GYRQGMHELA AVLWKVRSDG
AVDSRRAAAT QASRLSTQAT DDAPFDHALA DVFVEHDVYA LFGALMQSAE SWYAWRESSG
SSPPTSPSAN PLAPANARQS PETARRPLPI VVKCEYILDL LRRLDPALAQ HLESLGIEPQ
IFCLRWIRMI FTREFGLDDA IAIWDGLFAS GRSLALIDYV CIAMLLRIRN QLLAGDHTSA
LQSLLRYPPE AQAQPSLLIQ QAIFMQKSSD RPGTGVAVVM QNRDLLGIPV QSMPAPDEAV
PSNSSPARAQ RLGGPKFATV GRAASGPANR VSPWSRLEQD QSPRGGTPAH HASPDARRWQ
PPAAAGDPLG ALPQSSSSVD ANGARAFGIN PAAYVPEGIS DFAKGWYERA ELPQSLNSAL
VNVSRSVAAA AAAGVAGAYR GNKPETSGFP SGFDQAFSSQ AALRTTGSAA TVGHAASEKK
SRPGLSVMEA AEQAESVPAS TVRASPSVSM RSKDVAEEAS DPLAKLTTAN KAIGSALSVC
IQVLEQSWLD RSAAPQPDEL EQNDINTLMS FTALKHIRDV LGGTAAEFDP ATLPVATASK
RPVSQPQSAD QAAPRPVPAA DVPAPAPMDA QPPAASHDVT IPPTVPPPKT ALPMALGEYA
RYGRQMILPD FGLDGQLRLR RAKVLVVGAG GLGCPAIQYL AAAGVGRISI LDHDVVEPSN
LARQILHSEH TVGMAKAVSA AQAAQRINPH ITALPLQYAL TAANARELMR GQDLVLDCTD
NPLTRYLVSD AAVLEGVQVV SGAAQGYDGQ LVVLHKRIKA EFAGPKATAG TDARGPCYRC
LFPKAPRPDE VTNCEDGGVL GGVTGLVGTM QALEATKILA GIGEDTPPML TLVAPMTGTP
FRSVKIRPRR IATCRACGDP AQVAETMITD LEQEDYASFC GLNAVPTQGD ELPRIAVSGM
HPRALVVDVR PKVEFGITRL DGSLNVPIQQ LLRDPQSAWD TITHERDRTK AEEVLVVCKK
GNDSQLAVRS LLQLQRELRA EKDTPAETSP SHPLDLSAPS GAQAEAKREP HAELKVSDLI
GGLRAYAAAN PGFPVY
//
