ID A0A1L0DI17_9ASCO Unreviewed; 638 AA.
AC A0A1L0DI17;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE RecName: Full=Diphthine--ammonia ligase {ECO:0000256|ARBA:ARBA00018426};
DE EC=6.3.1.14 {ECO:0000256|ARBA:ARBA00012089};
DE AltName: Full=Diphthamide synthase {ECO:0000256|ARBA:ARBA00029814};
DE AltName: Full=Diphthamide synthetase {ECO:0000256|ARBA:ARBA00031552};
GN ORFNames=SAMEA4029010_CIC11G00000002326 {ECO:0000313|EMBL:SGZ56172.1};
OS [Candida] intermedia.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC Candida/Metschnikowiaceae.
OX NCBI_TaxID=45354 {ECO:0000313|EMBL:SGZ56172.1, ECO:0000313|Proteomes:UP000182334};
RN [1] {ECO:0000313|EMBL:SGZ56172.1, ECO:0000313|Proteomes:UP000182334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 141442 {ECO:0000313|EMBL:SGZ56172.1,
RC ECO:0000313|Proteomes:UP000182334};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + diphthine-[translation elongation factor 2] + NH4(+) =
CC AMP + diphosphate + diphthamide-[translation elongation factor 2] +
CC H(+); Xref=Rhea:RHEA:19753, Rhea:RHEA-COMP:10172, Rhea:RHEA-
CC COMP:10174, ChEBI:CHEBI:15378, ChEBI:CHEBI:16692, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:82696,
CC ChEBI:CHEBI:456215; EC=6.3.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00001559};
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DR EMBL; LT635760; SGZ56172.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L0DI17; -.
DR STRING; 45354.A0A1L0DI17; -.
DR OrthoDB; 103959at2759; -.
DR Proteomes; UP000182334; Chromosome v.
DR GO; GO:0017178; F:diphthine-ammonia ligase activity; IEA:UniProtKB-EC.
DR CDD; cd01994; Alpha_ANH_like_IV; 1.
DR CDD; cd06155; eu_AANH_C_1; 1.
DR CDD; cd06156; eu_AANH_C_2; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 3.90.1490.10; putative n-type atp pyrophosphatase, domain 2; 1.
DR Gene3D; 3.30.1330.40; RutC-like; 2.
DR InterPro; IPR002761; Diphthami_syn_dom.
DR InterPro; IPR030662; DPH6/MJ0570.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR035959; RutC-like_sf.
DR InterPro; IPR006175; YjgF/YER057c/UK114.
DR NCBIfam; TIGR00290; MJ0570_dom; 1.
DR PANTHER; PTHR12196:SF2; DIPHTHINE--AMMONIA LIGASE; 1.
DR PANTHER; PTHR12196; DOMAIN OF UNKNOWN FUNCTION 71 DUF71 -CONTAINING PROTEIN; 1.
DR Pfam; PF01902; Diphthami_syn_2; 1.
DR Pfam; PF01042; Ribonuc_L-PSP; 1.
DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR SUPFAM; SSF55298; YjgF-like; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000182334}.
FT DOMAIN 1..229
FT /note="Diphthamide synthase"
FT /evidence="ECO:0000259|Pfam:PF01902"
SQ SEQUENCE 638 AA; 71088 MW; 3283E8E9FE7B65DE CRC64;
MKFVALISGG KDSFFNILQC QQNGHDLVAL ANLHPNDKNR DEIDSFMFQT VGHSVIDYYK
ECVGVPLYKR AITGGSKNVA LEYVPTTSDE IEDLYELLLK VKESHPDVEG VSCGAILSHY
QRTRVENVCD RLGLTSLAYL WQENQAELMR KMCNLGLDAR LVKVAAVGLN EKHLGKLISE
MYPILTKLNQ MYDVHVCGEG GEFETLVFDA PFFKKKLEIV SLKIVAHSSE VSYITDLEID
VLDKEDTSVE KIVTPSLLLE EFANVERQVE DSNIWNAHEN TFGPAVFALL PRVAKLNTRI
YISNVISSLE SLEDQTKDIM TQIGMYLRAE GATFADVQHM TVLVLDMSSF SRVNMIYGSF
FADIFLPPSR VCVETTLPYS HLVQISCVAL RPTYQKMGIH IRSRSYWAPQ NIGPYSQAIV
EARPTFKTAT LSGQIPLEPA NMTIDDSALA KHNAVLSLQH LYRAKKLIGV QHIADCICFI
TSKTSPSLVA KVWNSYVEEV ENGQDFCNRL LIVQTTGLPR GANVEWGALS YEKVVDMYED
EGTSDHWNPE IETVSKKFKA SVVPVGDGHV VKLVGVDILA AIDFLRSPAL SVSSVTFYST
LDNIHKLSNM GLSAEWVPVL GVWDSDGSEC AFGMIWIS
//
