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Database: UniProt
Entry: A0A1E3PVM2_LIPST
LinkDB: A0A1E3PVM2_LIPST
Original site: A0A1E3PVM2_LIPST 
ID   A0A1E3PVM2_LIPST        Unreviewed;       808 AA.
AC   A0A1E3PVM2;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   RecName: Full=C2H2-type domain-containing protein {ECO:0000259|PROSITE:PS50157};
GN   ORFNames=LIPSTDRAFT_188217 {ECO:0000313|EMBL:ODQ69479.1};
OS   Lipomyces starkeyi NRRL Y-11557.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Lipomycetaceae; Lipomyces.
OX   NCBI_TaxID=675824 {ECO:0000313|EMBL:ODQ69479.1, ECO:0000313|Proteomes:UP000094385};
RN   [1] {ECO:0000313|EMBL:ODQ69479.1, ECO:0000313|Proteomes:UP000094385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-11557 {ECO:0000313|EMBL:ODQ69479.1,
RC   ECO:0000313|Proteomes:UP000094385};
RX   PubMed=27535936; DOI=10.1073/pnas.1603941113;
RA   Riley R., Haridas S., Wolfe K.H., Lopes M.R., Hittinger C.T., Goeker M.,
RA   Salamov A.A., Wisecaver J.H., Long T.M., Calvey C.H., Aerts A.L.,
RA   Barry K.W., Choi C., Clum A., Coughlan A.Y., Deshpande S., Douglass A.P.,
RA   Hanson S.J., Klenk H.-P., LaButti K.M., Lapidus A., Lindquist E.A.,
RA   Lipzen A.M., Meier-Kolthoff J.P., Ohm R.A., Otillar R.P., Pangilinan J.L.,
RA   Peng Y., Rokas A., Rosa C.A., Scheuner C., Sibirny A.A., Slot J.C.,
RA   Stielow J.B., Sun H., Kurtzman C.P., Blackwell M., Grigoriev I.V.,
RA   Jeffries T.W.;
RT   "Comparative genomics of biotechnologically important yeasts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 113:9882-9887(2016).
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DR   EMBL; KV454303; ODQ69479.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E3PVM2; -.
DR   STRING; 675824.A0A1E3PVM2; -.
DR   OrthoDB; 448292at2759; -.
DR   Proteomes; UP000094385; Unassembled WGS sequence.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR005303; MOCOS_middle.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR14237:SF19; MOLYBDENUM COFACTOR SULFURASE; 1.
DR   PANTHER; PTHR14237; MOLYBDOPTERIN COFACTOR SULFURASE MOSC; 1.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   Pfam; PF03476; MOSC_N; 1.
DR   SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
DR   PROSITE; PS50157; ZINC_FINGER_C2H2_2; 1.
PE   4: Predicted;
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094385};
KW   Zinc {ECO:0000256|PROSITE-ProRule:PRU00042};
KW   Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00042}.
FT   DOMAIN          745..769
FT                   /note="C2H2-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50157"
SQ   SEQUENCE   808 AA;  90400 MW;  5D71121EEFC92575 CRC64;
     MTQIYRHSII DIRSREYPAL NDMTYLDHAG TTLYAKSLMY QFSNDMTSGI FGNPHSASPS
     SMLSTQRVEN VRLKVLRFFK ADPEHFDVIF VANATAAIKL VLEAFRDVEV PGFWYGYHRD
     AHTSLVGLRQ LAARSRCFES DQAVEDWLKE TADGQKDAPS TAVGLFAYPA QSNMNGHRLP
     LDWPGRLRTS SHADCQKMYC LLDAAAYVTT RQLDLSNVQT APDFIALSFY KIFGFPDLGA
     LIVRKRASDI LRHRRYFGGG TVEMVTTLKG SWYAKKAHTI HEQLEDGTLP FHSIIALDSA
     FNVHEQLYGS MDNISRHTCA LASDLYNQLA SLRHANGQAV CEIYKDPNSQ YGDAKAQGPT
     IAFNIRTAQG GWIGKSEVER LAIVRNIHLR TGGVCNPGGI ATFCHLDYWE MRRNFSEGVR
     CGDGLDLLGG KPTGIVRVSL GAMSSQEDVN RFVNFVEEMF VEAGDTMEPA YILHPITSDM
     AESAVEKVQV FPILGCSGWQ VPRNISWSIK ETCLQYDREW CVVLKGSTTP LDHPSMKNIR
     PHIDIEKGIL KLTAPLKPSD ASSNSSKSEC DEEVTISLWD TPSQRIQPYL NSNHHLADSY
     DSESIVSFFT AVLGIPSTLA RFNKITESNW NDSVSPLSGD RSPRVSAVSD GEAQANIILS
     GSSKWKSQHY IRIGMHNFQL IQSPTPHTAE ESRRLRHLPN IYDRSLAAQN PTICYGDYVQ
     SFSADSASHD PALRASIASM SAGQHVCPVW NCRKDFNVAE ELAAHLHTHK RLADVTKVYD
     EAVMDVEVLL EPTPKRWRRW KLRLSRKV
//
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