ID A0A163IWB6_DIDRA Unreviewed; 720 AA.
AC A0A163IWB6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=ATP binding {ECO:0000313|EMBL:KZM25985.1};
GN ORFNames=ST47_g2913 {ECO:0000313|EMBL:KZM25985.1};
OS Didymella rabiei (Chickpea ascochyta blight fungus) (Mycosphaerella
OS rabiei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Ascochyta.
OX NCBI_TaxID=5454 {ECO:0000313|EMBL:KZM25985.1, ECO:0000313|Proteomes:UP000076837};
RN [1] {ECO:0000313|EMBL:KZM25985.1, ECO:0000313|Proteomes:UP000076837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ArDII {ECO:0000313|EMBL:KZM25985.1,
RC ECO:0000313|Proteomes:UP000076837};
RX PubMed=27091329; DOI=10.1038/srep24638;
RA Verma S., Gazara R.K., Nizam S., Parween S., Chattopadhyay D., Verma P.K.;
RT "Draft genome sequencing and secretome analysis of fungal phytopathogen
RT Ascochyta rabiei provides insight into the necrotrophic effector
RT repertoire.";
RL Sci. Rep. 6:24638-24638(2016).
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:KZM25985.1}.
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DR EMBL; JYNV01000119; KZM25985.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A163IWB6; -.
DR STRING; 5454.A0A163IWB6; -.
DR Proteomes; UP000076837; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.50.261; Succinyl-CoA synthetase domains; 2.
DR InterPro; IPR003781; CoA-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR005811; SUCC_ACL_C.
DR InterPro; IPR016102; Succinyl-CoA_synth-like.
DR PANTHER; PTHR11117; SUCCINYL-COA LIGASE SUBUNIT ALPHA; 1.
DR PANTHER; PTHR11117:SF6; SYNTHETASE SUBUNIT ALPHA, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G10830)-RELATED; 1.
DR Pfam; PF02629; CoA_binding; 1.
DR Pfam; PF00549; Ligase_CoA; 2.
DR PRINTS; PR01798; SCOASYNTHASE.
DR SMART; SM00881; CoA_binding; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52210; Succinyl-CoA synthetase domains; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000076837}.
FT DOMAIN 45..140
FT /note="CoA-binding"
FT /evidence="ECO:0000259|SMART:SM00881"
FT REGION 345..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 558..580
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 720 AA; 77456 MW; E418C01FD9355191 CRC64;
MISRHTSCLS SKALSSQCLS RRVPWAAFST TSARNGYDDT IQNLKIGSHT RVMFQGFTGK
LATANAKESM EWGTNVVGGV KPGGSGEHLG LPVLPSVRKA MEELKPDATG IYVAAHQAPA
AIEEAIEAEV PLIVAVAEHI PVHDVMRIHS MLKSQSKSRL VGANAPGIIS AIGRCRIGFQ
PLPTFSPGHI GVIAKSGTLS YETVGSLTRA GLGQSLCIGM GGDVIAGTNF VDVLKVFETD
DDTQAIILVG ELGGTNEEEA ADWIKDYNKR VFNPKPIAAC IGGFQAKPGK VTGHAGAWTG
LGEGTSEVKY RALEAAGVTM VDHPAKFGGV MKDILSKSGR SVRKIEQSAA QARRGYHTSA
RRPVLDSAQS PALQQKRSLH LSADQNVKIL KKYNIDVVSN PDDQQSSHYI GISPHRVNCS
PSIIAAPTAN PDQLHQRVRR FPFDYRKGPS PQAINEAMAW LQLDAAPPKA KAQTAELISN
LWKLYTEKEA IDAHVALSLN PTKDEIQVYS PYLFFDDAAY RSNKRQADLH EQRDKLSQTE
LEAEENGIVY IPLDTPQPDS RLQASTQTPP QSSSLTPGEP RNLVGTLVNG AGLAMNTNDV
LHLRLSLPPY STANANFLDT GGKATSQTIK TSFKLILSDP RVSVVFVNIF GGLTLADMIA
EGIILAFKEV GVDKPVVVRL RGTNEDKGRK VLEAAHLPIH AFDDFEEAVK KVGELANGGT
//
