SitesBLAST
Comparing Ac3H11_4644 FitnessBrowser__acidovorax_3H11:Ac3H11_4644 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 20 (the maximum) hits to proteins with known functional sites (download)
P60844 Aquaporin Z; Bacterial nodulin-like intrinsic protein; Water channel AqpZ from Escherichia coli (strain K12) (see paper)
66% identity, 90% coverage: 22:244/248 of query aligns to 2:226/231 of P60844
- C9 (≠ F29) mutation to S: No effect.
- C20 (= C40) mutation to S: Loss of oligomerization; no alteration of water permeability.
- T183 (= T201) mutation to C: No effect.
- R189 (= R207) mutation R->V,S: Loss of function.
2o9eA Crystal structure of aqpz mutant t183c complexed with mercury (see paper)
65% identity, 90% coverage: 22:244/248 of query aligns to 4:228/232 of 2o9eA
3nkaA Crystal structure of aqpz h174g,t183f (see paper)
65% identity, 90% coverage: 22:244/248 of query aligns to 4:228/230 of 3nkaA
P08995 Nodulin-26; N-26 from Glycine max (Soybean) (Glycine hispida) (see paper)
41% identity, 89% coverage: 22:242/248 of query aligns to 37:245/271 of P08995
Sites not aligning to the query:
- 262 modified: Phosphoserine; by CPK
P55088 Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4 from Mus musculus (Mouse) (see 2 papers)
35% identity, 90% coverage: 26:248/248 of query aligns to 39:255/323 of P55088
- S111 (≠ K97) modified: Phosphoserine; by PKG; mutation to A: Loss of phosphorylation by PKG (in vitro). No effect on location at cell membrane.
Sites not aligning to the query:
- 4 natural variant: G -> R
5dyeD Crystal structure of the full length s156e mutant of human aquaporin 5 (see paper)
41% identity, 87% coverage: 27:241/248 of query aligns to 15:220/253 of 5dyeD
P55064 Aquaporin-5; AQP-5 from Homo sapiens (Human) (see 2 papers)
41% identity, 87% coverage: 27:241/248 of query aligns to 16:221/265 of P55064
- A38 (≠ L52) to E: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123054
- I45 (≠ V59) to S: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123055
- N123 (≠ G140) to D: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123057
- S156 (≠ E177) mutation to A: No effect on location at the cell membrane.; mutation to E: Increased location at the cell membrane.
- I177 (= I196) to F: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs398123056
- R188 (= R207) to C: in PPKB; retains the ability to traffic to the cell membrane; dbSNP:rs368292687
P41181 Aquaporin-2; AQP-2; ADH water channel; Aquaporin-CD; AQP-CD; Collecting duct water channel protein; WCH-CD; Water channel protein for renal collecting duct from Homo sapiens (Human) (see 12 papers)
38% identity, 87% coverage: 27:242/248 of query aligns to 15:220/271 of P41181
- G64 (= G79) to R: in NDI2; loss of water channel activity; dbSNP:rs104894326
- G78 (= G93) mutation to A: Does not affect interaction with MIAC; when associated with A-79.
- C79 (≠ G94) mutation to A: Does not affect interaction with MIAC; when associated with A-78.
- S148 (≠ V170) mutation to A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; mutation to D: Retained in the endoplasmic reticulum.
- R187 (= R207) to C: in NDI2; loss of water channel activity; mutant protein does not fold properly; dbSNP:rs104894328
- A190 (≠ G210) to T: in NDI2; mutant protein does not fold properly and is not functional; dbSNP:rs104894341
- V194 (≠ F214) to I: in dbSNP:rs772051028
- S216 (≠ A238) to P: in NDI2; loss of water channel activity; dbSNP:rs104894329
- L217 (≠ A239) mutation to A: Abolishes interaction with MIAC; when associated with A-221.
Sites not aligning to the query:
- 221 Y→A: Abolishes interaction with MIAC; when associated with A-217.
- 229 S→A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; S→D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
- 231 S→A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; S→D: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
- 232 E→A: Reduces interaction with MIAC.
- 244 T→A: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.; T→E: No effect on sorting from the ER to the vesicles, redistribution to apical membrane, or endocytosis.
- 254 R → L: in NDI2; results in the loss of arginine vasopressin-mediated phosphorylation at S-256; R → Q: in NDI2; exerts a dominant-negative effect on wild-type-AQP2 in that it interferes with its trafficking to the apical membrane; is a loss of function instead of a gain of function mutation on dominant nephrogenic diabetes insipidus
- 256 modified: Phosphoserine; by PKA; S→A: Retained in vesicles.; S→D: Expressed in the apical membrane.
- 258 E → K: in NDI2; retained in the Golgi compartment; dbSNP:rs104894332
- 262 P → L: in NDI2; mutant protein folds properly and is functional but is retained in intracellular vesicles; able to assemble into tetramers with wild-type AQP2 that properly localize to the apical membrane; dbSNP:rs104894339; P→A: No effect on expression at the apical cell membrane.
4nefA X-ray structure of human aquaporin 2 (see paper)
38% identity, 87% coverage: 27:242/248 of query aligns to 14:219/239 of 4nefA
P47863 Aquaporin-4; AQP-4; Mercurial-insensitive water channel; MIWC; WCH4 from Rattus norvegicus (Rat) (see 4 papers)
33% identity, 90% coverage: 26:248/248 of query aligns to 39:255/323 of P47863
- S180 (≠ T171) modified: Phosphoserine; by PKC; mutation to A: Decreases internalization from the cell membrane in response to PKC activation.
- H201 (= H192) mutation to P: Partial loss of transport activity.
Sites not aligning to the query:
- 13 modified: S-palmitoyl cysteine; C→A: Reduced palmitoylation. Loss of palmitoylation; when associated with A-17.
- 17 modified: S-palmitoyl cysteine; C→A: Reduced palmitoylation. Loss of palmitoylation; when associated with A-13.
- 285 modified: Phosphoserine
P56402 Aquaporin-2; AQP-2; ADH water channel; Aquaporin-CD; AQP-CD; Collecting duct water channel protein; WCH-CD; Water channel protein for renal collecting duct from Mus musculus (Mouse) (see 2 papers)
36% identity, 88% coverage: 27:245/248 of query aligns to 15:223/271 of P56402
- T126 (≠ P144) mutation to M: Does not cause loss of water channel activity, but impairs trafficking from cytoplasmic vesicles to the cell membrane.
Sites not aligning to the query:
- 256 modified: Phosphoserine; S → L: in cph; loss of a phosphorylation site and loss of trafficking to the apical cell membrane; causes aberrant location at the basolateral cell membrane
8ct2D Local refinement of aqp1 tetramer (c1; refinement mask included d1 of protein 4.2 and ankyrin-1 ar1-5) in class 2 of erythrocyte ankyrin-1 complex (see paper)
36% identity, 87% coverage: 27:241/248 of query aligns to 14:225/247 of 8ct2D
8sjxA Structure of lens aquaporin-0 array in sphingomyelin/cholesterol bilayer (2sm:1chol)
36% identity, 88% coverage: 27:244/248 of query aligns to 10:217/220 of 8sjxA
- binding cholesterol: I82 (≠ P102), F193 (≠ Y218), W200 (= W227)
- binding [(E,2S,3R)-2-(hexadecanoylamino)-3-oxidanyl-octadec-4-enyl] 2-(trimethylazaniumyl)ethyl phosphate: F12 (= F29), V86 (= V106), V86 (= V106), L89 (≠ V109), L90 (= L110), L90 (= L110), L90 (= L110), Y100 (= Y120), Y100 (= Y120), S101 (≠ L121), I188 (≠ L213), L189 (≠ F214), R191 (≠ P216), F193 (≠ Y218)
Sites not aligning to the query:
Q06611 Aquaporin PIP1-2; AtPIP1;2; Plasma membrane intrinsic protein 1b; PIP1b; Transmembrane protein A; AthH2; TMP-A from Arabidopsis thaliana (Mouse-ear cress) (see paper)
34% identity, 95% coverage: 7:242/248 of query aligns to 32:273/286 of Q06611
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
P06624 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Bos taurus (Bovine) (see 4 papers)
35% identity, 87% coverage: 27:241/248 of query aligns to 15:219/263 of P06624
- Y149 (≠ T171) mutation to G: Increases constitutive water permeability. Abolishes regulation by cytoplasmic calcium levels.; mutation to L: Strongly decreases water permeability. Abolishes regulation by cytoplasmic calcium levels.; mutation to S: Slightly decreases water permeability, but has a minor effect on the regulation by cytoplasmic calcium levels.
Sites not aligning to the query:
- 227 L→A: Strongly reduced CALM binding.
- 227:237 Interaction with CALM
- 230 V→A: Strongly reduced CALM binding.
- 235 modified: Phosphoserine
- 243 modified: Phosphoserine; by PKA
- 245 modified: Phosphoserine
- 246 Interaction with BFSP1; modified: Deamidated asparagine
- 250 interaction with BFSP1
P09011 Lens fiber major intrinsic protein; Aquaporin-0; MIP26; MP26 from Rattus norvegicus (Rat) (see 2 papers)
35% identity, 87% coverage: 27:241/248 of query aligns to 13:217/261 of P09011
Sites not aligning to the query:
- 233 modified: Phosphoserine
- 244 N→D: No effects.
Q08733 Aquaporin PIP1-3; AtPIP1;3; Plasma membrane intrinsic protein 1c; PIP1c; Transmembrane protein B; TMP-B from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 90% coverage: 21:244/248 of query aligns to 44:275/286 of Q08733
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
P61837 Aquaporin PIP1-1; AtPIP1;1; Plasma membrane aquaporin-1; Plasma membrane intrinsic protein 1a; PIP1a from Arabidopsis thaliana (Mouse-ear cress) (see paper)
33% identity, 90% coverage: 21:242/248 of query aligns to 44:273/286 of P61837
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
Q39196 Probable aquaporin PIP1-4; Plasma membrane intrinsic protein 1-4; AtPIP1;4; Transmembrane protein C; TMP-C from Arabidopsis thaliana (Mouse-ear cress) (see paper)
32% identity, 96% coverage: 7:244/248 of query aligns to 33:276/287 of Q39196
Sites not aligning to the query:
- 1 modified: N-acetylmethionine
2evuA Crystal structure of aquaporin aqpm at 2.3a resolution (see paper)
34% identity, 92% coverage: 18:244/248 of query aligns to 1:243/245 of 2evuA
Query Sequence
>Ac3H11_4644 FitnessBrowser__acidovorax_3H11:Ac3H11_4644
LAAGLRQQLPPAFLDKPMPTSLQKWSAEFLGTFWLTFGGCGSAVLAAAFPQLGIGFLGVS
LAFGLTVLTGAYALGPISGGHFNPAVSVGLALGGRFKVSELPGYVVAQVLGAIVAAGVLY
LIATGKPGADIGGFATNGYGEHSPGGYGLLAAVVAEVVLTAVFLIVILGVTSRRAAEGVG
GMAIGLCLTLIHLISIPVTNTSVNPARSTGPALFGPSYALSELWVFWAAPIAGALLGAAI
YRGLFGED
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