ID A0A0V0R0Y8_PSEPJ Unreviewed; 463 AA.
AC A0A0V0R0Y8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Ubiquitin-like modifier-activating enzyme 5 {ECO:0000256|ARBA:ARBA00016279};
GN ORFNames=PPERSA_01708 {ECO:0000313|EMBL:KRX08163.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX08163.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX08163.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX08163.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
CC -!- SIMILARITY: Belongs to the ubiquitin-activating E1 family. UBA5
CC subfamily. {ECO:0000256|ARBA:ARBA00005339}.
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:KRX08163.1}.
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DR EMBL; LDAU01000073; KRX08163.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0R0Y8; -.
DR EnsemblProtists; KRX08163; KRX08163; PPERSA_01708.
DR InParanoid; A0A0V0R0Y8; -.
DR OMA; ITINAYE; -.
DR OrthoDB; 180391at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008641; F:ubiquitin-like modifier activating enzyme activity; IEA:InterPro.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR045886; ThiF/MoeB/HesA.
DR InterPro; IPR000594; ThiF_NAD_FAD-bd.
DR InterPro; IPR035985; Ubiquitin-activating_enz.
DR PANTHER; PTHR10953; UBIQUITIN-ACTIVATING ENZYME E1; 1.
DR PANTHER; PTHR10953:SF9; UBIQUITIN-LIKE MODIFIER-ACTIVATING ENZYME 5; 1.
DR Pfam; PF00899; ThiF; 1.
DR SUPFAM; SSF69572; Activating enzymes of the ubiquitin-like proteins; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..231
FT /note="THIF-type NAD/FAD binding fold"
FT /evidence="ECO:0000259|Pfam:PF00899"
FT COILED 359..411
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 463 AA; 54669 MW; 00CED015D18DB534 CRC64;
MEEEKELNQK IFDRQIRIKD WDQEKLENQK VLILGMGGLG TVVLIQLLRL GVKEIHFLDF
DTIDLSNLPR QFLFGKEDVG KKKVDVALKN AQIHNISNSQ LYGYHMDAIK EFQKVIELAK
KCDFVFNLID HGDYWDLAVC SLCLSLKIPH ISGGNFASSM MLDFYMRTGE PCYLCLTPDL
KEKEIVEKFH PDLIQNYRDI SFIPANDNPI SQSSATLCTS CGVFLANMFK CAIMTPEKDQ
KSRRVMIYLD NIETLDFGVV AEPKCKYCNK NPIAIKFTDS GIIQKESEQV WEDIKGMNFK
NFDEIFFQQI EKQEVEKQEG EKIKKETIYQ IKLLDNTIHE LEIKQLNDKE QIIEFDWKIL
LKQQNLDQNN ELNENLEDNE KIIEINKLEK KEELQDKMEE LSENNKLQEY KKNEIILIKN
KIQIKNISLQ KWTFMEWEWE FPDEQEIKYI EKFRKIIKQV FQI
//
