GenomeNet

Database: UniProt
Entry: A0A094EJJ2_9PEZI
LinkDB: A0A094EJJ2_9PEZI
Original site: A0A094EJJ2_9PEZI 
ID   A0A094EJJ2_9PEZI        Unreviewed;      1335 AA.
AC   A0A094EJJ2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   28-JUN-2023, entry version 40.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KFY47312.1};
GN   ORFNames=V494_00067 {ECO:0000313|EMBL:KFY47312.1};
OS   Pseudogymnoascus sp. VKM F-4513 (FW-928).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420907 {ECO:0000313|EMBL:KFY47312.1, ECO:0000313|Proteomes:UP000029288};
RN   [1] {ECO:0000313|EMBL:KFY47312.1, ECO:0000313|Proteomes:UP000029288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4513 (FW-928) {ECO:0000313|Proteomes:UP000029288};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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:KFY47312.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JPJW01000010; KFY47312.1; -; Genomic_DNA.
DR   STRING; 1420907.A0A094EJJ2; -.
DR   HOGENOM; CLU_005089_0_0_1; -.
DR   OrthoDB; 1459320at2759; -.
DR   Proteomes; UP000029288; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR041175; VLRF1/Vms1.
DR   InterPro; IPR013087; Znf_C2H2_type.
DR   PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF18826; bVLRF1; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR   SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
DR   PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000029288}.
FT   DOMAIN          664..1112
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
FT   DOMAIN          780..978
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          1256..1332
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   REGION          30..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          149..175
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          214..235
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          287..310
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..436
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          554..641
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        38..56
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        290..307
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..436
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        562..601
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        624..641
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1335 AA;  147394 MW;  105A45DB38CA0391 CRC64;
     MEQQREQRRD QMVRRPLYVY NLPSDILTTL QQKDGVVPDT PEEQDNEAKA EHDGTKSDGA
     TSTTACSLCD QLFSTVEEQR SHIRSDIHSY NLKLKLRGLE PVSEVEFETL VKGYLDESLS
     GSDESESDDD QGPAGRNETT LVALLNKRAA KSTQEGEDGA HLGSQKDNSS KQPLVWFTSP
     SVPPNSYLGV YRAIFTTEEQ NNNGNFVETI KKKQLQPKMP IKHSSDNGEV SKPTSESIGP
     HMFMCMIGGG HFAAMVVSMV PKQSGSSATG PLAKEATVIA HKTFHRYTTR RKQGGSQSAN
     DSSKGAAHSA GASIRRYNEV ALNDEVRLLL TEWKSLIDTS ELLFVRATGN TNRRTLFGPY
     EGQVLQSNDP RIRSIPFNTR RATQKELMRS FIELTRVKVR EFDEQPPATQ PSDSLPKTDT
     SQSSTKASST ATKPAFSDEE ETFILHTTQI QALIRRSKLP ALLSYLKNNS LGDDFRFYPP
     SAPQNFHTPT PLHFAASLNN PVVVTGLLVK AHANPEALNS DGKPPFDLAG DRSTRDAFRL
     ARSRLATASP PVTWDWEKTH IPSPLTDADV ETRRAEESLG QRREEEDRRK AETERLKNEG
     PKVTESGPLG KSASMGRALA MEAARKTAQE KREEESRGLT PEMRLKLDRE RRARAAEERF
     KAMQANKVLI ANRGEIALRV GRTAAESGIR CTTLYTDPDA HSQHALSSPF AVNLGQASAY
     LDGERIIAVA KEQGCQALHP GYGFLSENSA FAKRCVEEGL VFIGPPWKAI EAMGNKSRSK
     DIMIKAGVPC IPGYHGANQD PENLLEESRK IGFPVLVKAV RGGGGKGMRI AMNEAEFLDK
     LESAKSEGRN SFGDDEMLVE KYITTPRHIE VQVFADKHGN AVALGERDCS LQRRHQKILE
     EAPAPNLPEE IRQDLWEKAR AAALAVGYEG AGTVEFIFDN DSNQFFFMEM NTRLQVEHPV
     TEVVTGEDLV SWQFKVAAGE PLPLTQEAIA KRISERGWAI EARIYAENPD QDFMPDSGKL
     THLRTPQITD NVRIDAGFVE GDTISSNYDG MIAKLIVSGE TRDIAIQRMY SALQDYEVVG
     LSTNIEFLKK ICLSPGFAAG DVETGYIKKN HDELFEKEAV ENTSFAQAAL ALFTKDATAS
     KSLAKAGPHG NEADLSTILG ERQFRFSLLS GSEPIDVTVT IKQSSRNIFD VSVDGPGIRE
     SYSNVTCESI ESSVTSYFPH TRVKSTVVRD GDNITMFQKG KMIKLRLAQP LWYEKALGIK
     DVANSVLAPM PCKILKNEVN EGDIVEKDAA LVVIESMKME TIIRSPQRGT VAKLVHKPGD
     ICKAGTVLVL FEEAE
//
DBGET integrated database retrieval system