ID A0A093XM51_9PEZI Unreviewed; 2410 AA.
AC A0A093XM51;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=CTP synthase (glutamine hydrolyzing) {ECO:0008006|Google:ProtNLM};
GN ORFNames=V490_08009 {ECO:0000313|EMBL:KFX87809.1};
OS Pseudogymnoascus sp. VKM F-3557.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1437433 {ECO:0000313|EMBL:KFX87809.1, ECO:0000313|Proteomes:UP000029320};
RN [1] {ECO:0000313|EMBL:KFX87809.1, ECO:0000313|Proteomes:UP000029320}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-3557 {ECO:0000313|EMBL:KFX87809.1,
RC ECO:0000313|Proteomes:UP000029320};
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 -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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:KFX87809.1}.
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DR EMBL; JPJS01002421; KFX87809.1; -; Genomic_DNA.
DR STRING; 1437433.A0A093XM51; -.
DR HOGENOM; CLU_000192_5_1_1; -.
DR Proteomes; UP000029320; Unassembled WGS sequence.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0051015; F:actin filament binding; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006996; P:organelle organization; IEA:UniProt.
DR CDD; cd01377; MYSc_class_II; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.340; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.30.70.1590; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 2.30.30.360; Myosin S1 fragment, N-terminal; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 4.10.270.10; Myosin, subunit A; 1.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR45615:SF40; MYOSIN HEAVY CHAIN, MUSCLE-RELATED; 1.
DR PANTHER; PTHR45615; MYOSIN HEAVY CHAIN, NON-MUSCLE; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF90257; Myosin rod fragments; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57997; Tropomyosin; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Reference proteome {ECO:0000313|Proteomes:UP000029320}.
FT DOMAIN 110..160
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000259|PROSITE:PS51844"
FT DOMAIN 164..856
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..757
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 1507..1548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1657..1697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2251..2270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2368..2410
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 934..968
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 997..1115
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1155..1350
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1374..1429
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1710..1737
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 1941..2053
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 2103..2137
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1531..1546
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1657..1692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2396..2410
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 257..264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 2410 AA; 274918 MW; C6D26B890CEC8795 CRC64;
MAQNGSQLRA SPFARARATT SPYNQSNSNQ IQSSGIESPP PTHSVSHTRN QSYSPVTTST
LGKGPVHTRQ RSESKISAIK SNTFAPSFIK TDESQERTKV DGIEGENDFS GKRYVWLKDP
GSAFVRGWIV EELEGGQILV QCDDGSQREV HGENVDKVNP AKFDKADDMA ELTHLNEASV
VHNLHMRYQA DLIYTYSGLF LVTINPYCSL PIYTNEYINM YRGRSREDTK PHIYAMADEA
FRNLVDEGQN QSILVTGESG AGKTENTKKV IQYLAAVAHS DSPVKNKIQQ SNLSAQILRA
NPILEAFGNA QTVRNNNSSR FGKFIRIEFT RTGTIAGAFI DWYLLEKSRV VRLNSQERNY
HVFYQLLKGA DRQMKQKYLL ENLDVQDFTY TRDGNDTISG ISDRDEWNSL IEAFDVMGFS
EKDQDSIFRT VAAVLHLGNI SVMNESRGAD QARLAPNARG EAEKFCRLLG ISVEPFLSGL
LHPRVKAGRE WVEKVQTPEQ VRLAIDALAK GIYERGFGDL VSKINQQLDR TGMGLDDSHF
IGVLDIAGFE IFEENSFEQL CINYTNEKLQ QFFNHHMFVL EQEEYAREQI EWKFIDFGRD
LQPTIDLIEL SNPIGIFSCL DEDSVMPKAT DKSFTEKLNS LWDRKNPKYR SSRLKQGFLL
THYAAEVEYS TEGWLEKNKD PLNDNITRLL AASADKHVSN LFVDCADPDD ESGGTRSRVK
KGLFRTVAQR HKEHLSNLMT QLHSTHPHFV RCIIPNHKKK PKQLSAPLVL DQLRCNGVLE
GIRIARTGFP NRLPFSEFRQ RYEVLCRNMP KGYLEGQAAA TIMLEKLTLD KSMFRVGLTK
VFFRAGVLAE LEEQRDALIR EIMSRFQSVA RGFSQRRIAH KRLYRAEATR IIQRNFQVYL
NLCDNPWWQL LAKMKPLLGA TRTSGEVKKR DEMIQRLGEK IKQEATDRQR IEDERRNAYA
EMQRIQTTLE SERSLALDKE EIFKRLQMRE VELSDKLAGA IDDQEKLEDH LDELLEAKKK
AEEQSEDLRA QLSHAGTIIY NLEAEKQNLI QKLADMDSKF EELSQAQSQR SSAEAQLSQE
VQMLQSQLSL KDRKAQELEK KLLQIDQDLD VKLARTTKDL QASHSREQAL ADETRKAQQQ
LAELASTSTG YEDLVRRKES ELAILRSDNK KYEANQASFE DEKKSLLDSK NIIAARVREV
QAEMVAMKTQ KSQLEREAAD AKKLLEARLT EDAEAGQSRK LLETQIKDLK DQLFAVQTDL
SRERQSRDDV QLLGEHKFQK LKEEYQVLNE AKITIEKELY VQQDTLRRAT EGRAAAEKER
NEARNEIRKL REAKSAMEEL KIQAELAGER NASRVARERE AGLMRDLEAE QGRLKWFEAE
CTKLSQQVDE LNKMILESGN FGLQVDQQKE RLESELNTVK SRLMASENDN RALLNKIQQK
GLELARAGSQ ASESQRGKVI ALQREKAKNE EQNMKLSKQL EEAQILAASV QKKNEKLQLT
VEDLNHEVSR EHKASRNAEM NSSTATTQLA EAKRKIEKEE QLRTQSQELV KKLQSSLDGR
DRELEELRAQ RLQLLKVVDP EVSAQVPQGD GAAATSILEK YDLVRKVQDL QHDLRIQMAG
RSNAESQLSD LRKKYETDIE SVERPRTKLE EIHPNQVPFQ SPTHARTKAN GRVHSNVSTP
TRRVATNDAD PTLDSGRSDR TADLLSFNNR MDLKTELEEV QNQLQLTQMQ NRHLQSQIER
STPTRELWPD DSPSLRRVHK LEKANTRLHD MLDDSAKKVS QLERSVQSGA LSLRDVQTRS
HEELYELISN QEEARRSLVH LNDDAAAELS DIKDHFDGLK HARATLEVEL RDAKSDLEEM
ARARDQDVTS RNQLLQEFAD LQIQFDAESS KVAEVSSSLA LYKGRADEYF NKLEQAEIAV
LKASRAEQFA RSQAREAEET CATIMSERKQ MEGSIEDLQR QNQSYEERLE DLSADLEGAI
QARKRLQHEL EDYRSQRAMD IEDKETSMEQ TRKKYQAEFA TLTNELDIAR EERLFKQSEN
TRLREELDDL RSKWDDEVLN SSTWSKEKAR LEVTLADLVS SRDEASNAHN DAQGKIVSLL
SQVRSLRTSV DDVAAERDAL QREKRGLEAR LEEAKNGFEG LVRGDSPSLR NAAGLDKELL
ELKSSLAQNE DIAAAAVEKM RRAEALTSEM QKDIVAERET TVQLHKEKAA LEKSLKDVQV
RLVDLETKGY SSASQDVRFL HGRVQELESQ LEAQESERSK SQRDVRNVDR TVKDLQQQIE
RREKANSQLQ DDINRSREKA EKLLKTIDEL QASDSSNQLS ARRAERELRE EKEKALRLER
ELGAWKALRM EKGATISGGA VRRSGQWARG GMSSEWGDEN ASILGGDDGI VIPKRKGSQS
RQTSMSKGFL
//
