SitesBLAST

SitesBLAST – Find functional sites

SitesBLAST

Comparing RR42_RS22775 FitnessBrowser__Cup4G11:RR42_RS22775 to proteins with known functional sites using BLASTp with E ≤ 0.001.

Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures

Found 10 hits to proteins with known functional sites (download)

O14289 3-isopropylmalate dehydratase; Alpha-IPM isomerase; IPMI; Isopropylmalate isomerase; EC 4.2.1.33 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
47% identity, 98% coverage: 4:207/208 of query aligns to 540:741/758 of O14289

query
sites
O14289

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Sites not aligning to the query:

486 modified: Phosphoserine
488 modified: Phosphoserine

P9WK95 3-isopropylmalate dehydratase small subunit; Alpha-IPM isomerase; IPMI; Isopropylmalate isomerase; EC 4.2.1.33 from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see paper)
37% identity, 92% coverage: 1:191/208 of query aligns to 1:186/198 of P9WK95

query
sites
P9WK95

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K154 (vs. gap) modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

Q58667 Methanogen homoaconitase small subunit; HACN; Homoaconitate hydratase; EC 4.2.1.114 from Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) (see paper)
35% identity, 61% coverage: 18:143/208 of query aligns to 13:120/170 of Q58667

query
sites
Q58667

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R26 (≠ L43) mutation R->K,V: Allows the recognition of substrates of IPMI enzymes since it becomes able to efficiently catalyze citraconate hydration and 3-isopropylmalate dehydration. Largely decreases substrate affinity for cis-homo(1-3)-aconitate.
T27 (≠ E44) mutation to A: Largely decreases substrate affinity for cis-homo(1-3)-aconitate while slightly increases activity on these substrates, and also decreases substrate affinity for maleate. Gains the ability to hydrate citraconate, an IPMI substrate.

2pkpA Crystal structure of 3-isopropylmalate dehydratase (leud)from methhanocaldococcus jannaschii dsm2661 (mj1271) (see paper)
35% identity, 61% coverage: 18:143/208 of query aligns to 13:120/167 of 2pkpA

query
sites
2pkpA

N
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binding zinc ion: D13 (≠ N18), C63 (= C79)

D9X0I3 Aconitate hydratase A; ACN; Aconitase; EC 4.2.1.3 from Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494) (see paper)
47% identity, 27% coverage: 66:122/208 of query aligns to 800:857/931 of D9X0I3

query
sites
D9X0I3

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Sites not aligning to the query:

125:129 mutation Missing: Retains 40% of aconitase activity. Improves RNA-binding ability.
538 C→A: Loss of aconitase activity. Cannot rescue the growth defect of a disruption mutant and results in only a slight increase in PTT production in the mutant. Shows weak IRE-binding activity.
763 R→E: Loss of aconitase activity and IRE-binding activity; when associated with E-767.
767 Q→E: Loss of aconitase activity and IRE-binding activity; when associated with E-763.

P21399 Cytoplasmic aconitate hydratase; Aconitase; Citrate hydro-lyase; Ferritin repressor protein; Iron regulatory protein 1; IRP1; Iron-responsive element-binding protein 1; IRE-BP 1; EC 4.2.1.3 from Homo sapiens (Human) (see 2 papers)
41% identity, 31% coverage: 67:130/208 of query aligns to 763:828/889 of P21399

query
sites
P21399

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S778 (= S81) mutation to A: No effect on iron-regulated RNA binding. Loss of aconitase activity.
R780 (= R83) mutation to Q: Nearly abolishes RNA binding.

Sites not aligning to the query:

300 C→S: No effect on aconitase activity or on RNA binding.
318 T → M: in dbSNP:rs150373174
437 C→S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
503 C→S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
506 C→S: Loss of aconitase activity. Leads to constitutive RNA binding, irrespective of iron levels.
536 R→Q: Strongly reduced RNA binding.
541 R→Q: Strongly reduced RNA binding.
699 R→K: No effect on RNA binding.

2b3xA Structure of an orthorhombic crystal form of human cytosolic aconitase (irp1) (see paper)
41% identity, 31% coverage: 67:130/208 of query aligns to 762:827/888 of 2b3xA

query
sites
2b3xA

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active site: S777 (= S81), R779 (= R83)

Sites not aligning to the query:

active site: 124, 125, 204, 535
binding iron/sulfur cluster: 175, 206, 436, 502, 505, 506, 534

3snpA Crystal structure analysis of iron regulatory protein 1 in complex with ferritin h ire RNA (see paper)
39% identity, 31% coverage: 67:130/208 of query aligns to 724:789/850 of 3snpA

query
sites
3snpA

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active site: S739 (= S81), R741 (= R83)
binding : R741 (= R83)

Sites not aligning to the query:

active site: 124, 125, 186, 505
binding : 125, 126, 188, 243, 250, 279, 283, 352, 357, 360, 419, 420, 421, 504, 505, 520, 642, 643, 644, 645, 646, 649, 665, 669, 671, 674

Q9SIB9 Aconitate hydratase 3, mitochondrial; Aconitase 3; mACO1; Citrate hydro-lyase 3; EC 4.2.1.3 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 36% coverage: 45:119/208 of query aligns to 853:913/990 of Q9SIB9

query
sites
Q9SIB9

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Sites not aligning to the query:

91 modified: Phosphoserine

A0QX20 Aconitate hydratase A; ACN; Aconitase; (2R,3S)-2-methylisocitrate dehydratase; (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase; Iron-responsive protein-like; IRP-like; Probable 2-methyl-cis-aconitate hydratase; RNA-binding protein; EC 4.2.1.3; EC 4.2.1.99 from Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis) (see paper)
41% identity, 27% coverage: 67:123/208 of query aligns to 807:864/943 of A0QX20

query
sites
A0QX20

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A

Sites not aligning to the query:

394 modified: Isoglutamyl lysine isopeptide (Lys-Gln) (interchain with Q-Cter in protein Pup)

Query Sequence

>RR42_RS22775 FitnessBrowser__Cup4G11:RR42_RS22775
MQPFTVVTGAAVPLLRANVDTDVIIRIERLTALPREQLGPYALEALRYRADGSEDPGCVF
NQPAFRGAPVLLAGANFGCGSSREGAVWALMGLGVRCVIAPSYGDIFYNNCFQNGVLPIR
LPAEAVQALAAQCASGAPVRVDLASATLSAPDGATVAFPVDRLRREALLHGLDDIGLTLK
DDALIRAWQQADRTRRPWAWTVRRQDAA

Or try a new SitesBLAST search

SitesBLAST's Database

SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.

by Morgan Price, Arkin group
Lawrence Berkeley National Laboratory