Comparing GFF3781 FitnessBrowser__Marino:GFF3781 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P23533 Phosphoenolpyruvate-protein phosphotransferase; Phosphotransferase system, enzyme I; EC 2.7.3.9 from Staphylococcus carnosus (strain TM300) (see paper)
38% identity, 57% coverage: 425:978/978 of query aligns to 3:569/573 of P23533
2wqdA Crystal structure of enzyme i of the phosphoenolpyruvate:sugar phosphotransferase system in the dephosphorylated state (see paper)
38% identity, 56% coverage: 427:978/978 of query aligns to 4:569/570 of 2wqdA
2hwgA Structure of phosphorylated enzyme i of the phosphoenolpyruvate:sugar phosphotransferase system (see paper)
39% identity, 56% coverage: 427:971/978 of query aligns to 1:560/572 of 2hwgA
P08839 Phosphoenolpyruvate-protein phosphotransferase; Phosphotransferase system, enzyme I; EC 2.7.3.9 from Escherichia coli (strain K12) (see 2 papers)
39% identity, 56% coverage: 427:971/978 of query aligns to 2:561/575 of P08839
2xz7A Crystal structure of the phosphoenolpyruvate-binding domain of enzyme i in complex with phosphoenolpyruvate from the thermoanaerobacter tengcongensis pep-sugar phosphotransferase system (pts) (see paper)
43% identity, 31% coverage: 673:976/978 of query aligns to 9:318/324 of 2xz7A
2xz9A Crystal structure from the phosphoenolpyruvate-binding domain of enzyme i in complex with pyruvate from the thermoanaerobacter tengcongensis pep-sugar phosphotransferase system (pts) (see paper)
43% identity, 31% coverage: 673:976/978 of query aligns to 2:311/317 of 2xz9A
5lu4A C4-type pyruvate phosphate dikinase: conformational intermediate of central domain in the swiveling mechanism (see paper)
31% identity, 38% coverage: 573:944/978 of query aligns to 426:844/850 of 5lu4A
Sites not aligning to the query:
5jvjB C4-type pyruvate phosphate dikinase: different conformational states of the nucleotide binding domain in the dimer (see paper)
29% identity, 38% coverage: 573:944/978 of query aligns to 353:789/797 of 5jvjB
Sites not aligning to the query:
5jvlA C4-type pyruvate phospate dikinase: nucleotide binding domain with bound atp analogue (see paper)
30% identity, 38% coverage: 573:944/978 of query aligns to 426:866/874 of 5jvlA
Sites not aligning to the query:
Q39735 Pyruvate, phosphate dikinase, chloroplastic; Cold-sensitive pyruvate, orthophosphate dikinase; Pyruvate, orthophosphate dikinase; EC 2.7.9.1 from Flaveria bidentis (Coastal plain yellowtops) (Ethulia bidentis) (see 2 papers)
30% identity, 38% coverage: 573:944/978 of query aligns to 505:945/953 of Q39735
Sites not aligning to the query:
P22983 Pyruvate, phosphate dikinase; Pyruvate, orthophosphate dikinase; EC 2.7.9.1 from Clostridium symbiosum (Bacteroides symbiosus) (see 4 papers)
27% identity, 38% coverage: 573:942/978 of query aligns to 425:861/874 of P22983
Sites not aligning to the query:
1kc7A Pyruvate phosphate dikinase with bound mg-phosphonopyruvate (see paper)
27% identity, 38% coverage: 573:942/978 of query aligns to 424:860/872 of 1kc7A
Sites not aligning to the query:
O23404 Pyruvate, phosphate dikinase 1, chloroplastic; Pyruvate, orthophosphate dikinase 1; EC 2.7.9.1 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
28% identity, 38% coverage: 573:944/978 of query aligns to 515:954/963 of O23404
P11155 Pyruvate, phosphate dikinase 1, chloroplastic; Pyruvate, orthophosphate dikinase 1; EC 2.7.9.1 from Zea mays (Maize) (see 7 papers)
29% identity, 38% coverage: 573:944/978 of query aligns to 499:939/947 of P11155
Sites not aligning to the query:
1vbgA Pyruvate phosphate dikinase from maize (see paper)
29% identity, 38% coverage: 573:944/978 of query aligns to 426:866/874 of 1vbgA
Sites not aligning to the query:
5jvlB C4-type pyruvate phospate dikinase: nucleotide binding domain with bound atp analogue (see paper)
30% identity, 27% coverage: 685:944/978 of query aligns to 181:512/520 of 5jvlB
Sites not aligning to the query:
Q02KR1 Phosphoenolpyruvate synthase; PEP synthase; Pyruvate, water dikinase; EC 2.7.9.2 from Pseudomonas aeruginosa (strain UCBPP-PA14) (see paper)
28% identity, 35% coverage: 577:918/978 of query aligns to 381:754/791 of Q02KR1
P37349 PEP-dependent dihydroxyacetone kinase, phosphoryl donor subunit DhaM; Dihydroxyacetone kinase subunit M; EC 2.7.1.121 from Escherichia coli (strain K12) (see paper)
30% identity, 34% coverage: 308:637/978 of query aligns to 154:462/472 of P37349
Sites not aligning to the query:
1vbhA Pyruvate phosphate dikinase with bound mg-pep from maize (see paper)
28% identity, 38% coverage: 573:944/978 of query aligns to 417:854/862 of 1vbhA
Sites not aligning to the query:
1j6tA Complex of enzyme iiamtl and the histidine-containing phosphocarrier protein hpr from escherichia coli nmr, restrained regularized mean structure (see paper)
38% identity, 14% coverage: 36:175/978 of query aligns to 1:142/144 of 1j6tA
>GFF3781 FitnessBrowser__Marino:GFF3781
MISDHICFTIDFKHADTIQQTKTDTQYQNKKRGNLMLTLTANDVRLGATASDWQDALQQA
ARDLERAGRTSPEYLAGMNAREQQSSTVLGNGIAIPHGTPESRDAVLETGVRILQFPEGV
SWHDGARVHVLVAIAAQSDEHLDILRHLTRVLDKPGLAEKLGHATDATELVALLSKAPAV
AKCDSETLCLGIDASTPNELALIAAARLQSLRCVDTDFLASIVGQPPVDLGQGFWLTHHT
VGARRPTLSLATPKRATAELRGVFCLAGPGDECHDLLERIDTFLAGDEPIQGLSAEALLA
RLSGEAADAVTAKVTLLNTHGLHARPAKQLVQEARRHNASIRLRLLEGEGAAVSATSLTR
VIGLGARRGQTLLLSATGDDASQAIQSLTSAIEGGLGEKVSPLRSADPQTKVPEAEQAPA
LTDDQPVKAVAASPGLALAPAFVMRQPTLEYPQFAEDSEQQIQRLNQAVDSADGQLRTLI
RQAEGGEAAPILSVHVEMLQDEDLYQATLEAINEGASAEAGWWKAIDTAARGQEALADRL
LAERAADLRDVGRRVLSNLCGVAMPTPPDTPYILVADDLGPSDVARLDTTRVRGLVTARG
GATSHSAILARALGLPAVVGTGERILTILNGSDLVVDGERGCLVPNPGAERCEKIRRRLQ
QLDALQAEAHENRNQPATTVDGHTIEVCANLGNTAHTPDAVERGADGVGLLRTEFIFMAH
PEAPDLATQVTEYQHAFDALNGLPLVARTLDVGGDKPLDYWPLPQEDNPFLGMRGIRLSL
TRPDILETQVRALLTAAGDRPLRIMFPMVKDLEEFRAARAIVTKVQSEVSASNVQVGVMI
EVPSCALLASTLAPEVDFFSIGTNDLTQYTLAIDRGHGQLSAESDGLHPSVLRLIRMTVE
AAHAHNRWVGVCGELASDPQAIPVLVGLDVDELSVTSRRVPLVKACIRGLNLENARQQAE
KALSLATASEVRDALEAW
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SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory