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}.
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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
//