Comparing WP_017752629.1 NCBI__GCF_000816635.1:WP_017752629.1 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)
I1CR68 Aquaporin-1 from Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880) (Mucormycosis agent) (Rhizopus arrhizus var. delemar) (see paper)
35% identity, 97% coverage: 3:229/234 of query aligns to 60:295/306 of I1CR68
Q8II36 Aquaglyceroporin; PfAQP; Aquaporin-1 from Plasmodium falciparum (isolate 3D7) (see 2 papers)
31% identity, 100% coverage: 1:233/234 of query aligns to 10:241/258 of Q8II36
3c02A X-ray structure of the aquaglyceroporin from plasmodium falciparum (see paper)
31% identity, 100% coverage: 1:233/234 of query aligns to 3:234/242 of 3c02A
P08995 Nodulin-26; N-26 from Glycine max (Soybean) (Glycine hispida) (see paper)
30% identity, 100% coverage: 1:233/234 of query aligns to 37:247/271 of P08995
Sites not aligning to the query:
P0AER0 Glycerol uptake facilitator protein; Aquaglyceroporin; Glycerol facilitator from Escherichia coli (strain K12) (see 3 papers)
33% identity, 98% coverage: 3:231/234 of query aligns to 10:252/281 of P0AER0
1fx8A Crystal structure of the e. Coli glycerol facilitator (glpf) with substrate glycerol (see paper)
33% identity, 98% coverage: 3:231/234 of query aligns to 5:247/254 of 1fx8A
6n1gA Crystal structure of aquaglyceroporin aqp7 (see paper)
32% identity, 99% coverage: 1:232/234 of query aligns to 3:243/249 of 6n1gA
Q96PS8 Aquaporin-10; AQP-10; Aquaglyceroporin-10; Small intestine aquaporin from Homo sapiens (Human) (see 2 papers)
29% identity, 99% coverage: 2:233/234 of query aligns to 22:263/301 of Q96PS8
6f7hC Crystal structure of human aqp10 (see paper)
29% identity, 99% coverage: 2:233/234 of query aligns to 7:248/253 of 6f7hC
8c9hA Aqp7_inhibitor (see paper)
32% identity, 99% coverage: 1:232/234 of query aligns to 9:249/253 of 8c9hA
2evuA Crystal structure of aquaporin aqpm at 2.3a resolution (see paper)
33% identity, 98% coverage: 2:231/234 of query aligns to 6:241/245 of 2evuA
O14520 Aquaporin-7; AQP-7; Aquaglyceroporin-7; Aquaporin adipose; AQPap; Aquaporin-7-like from Homo sapiens (Human) (see 5 papers)
32% identity, 99% coverage: 1:232/234 of query aligns to 34:274/342 of O14520
Sites not aligning to the query:
B1VB61 Propanediol uptake facilitator PduF from Citrobacter freundii (see paper)
29% identity, 99% coverage: 2:233/234 of query aligns to 7:252/269 of B1VB61
P37451 Propanediol uptake facilitator PduF from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
29% identity, 97% coverage: 6:231/234 of query aligns to 11:250/264 of P37451
8ofxA Molecular mechanism of trypanosomal aqp2
30% identity, 98% coverage: 2:231/234 of query aligns to 4:239/244 of 8ofxA
8jy8A Structure of tbaqp2 in complex with anti-trypanosomatid drug pentamidine (see paper)
30% identity, 98% coverage: 2:231/234 of query aligns to 2:237/242 of 8jy8A
8jy6A Structure of tbaqp2 in complex with anti-trypanosomatid drug melarsoprol (see paper)
30% identity, 98% coverage: 2:231/234 of query aligns to 2:237/242 of 8jy6A
3nkaA Crystal structure of aqpz h174g,t183f (see paper)
35% identity, 83% coverage: 1:194/234 of query aligns to 4:197/230 of 3nkaA
8uy6A Aquaporin z with alfa tag and bound to nanobody (see paper)
34% identity, 83% coverage: 1:194/234 of query aligns to 2:195/244 of 8uy6A
Sites not aligning to the query:
P60844 Aquaporin Z; Bacterial nodulin-like intrinsic protein; Water channel AqpZ from Escherichia coli (strain K12) (see paper)
34% identity, 83% coverage: 1:194/234 of query aligns to 2:195/231 of P60844
>WP_017752629.1 NCBI__GCF_000816635.1:WP_017752629.1
MSKLIAEFVGTMILVYLGDGVCANCTLTKSKGQNGGWMVITAGWAFAVGIPALMFGSVSG
AHFNPALTIGLAAAGKFPAAEVPGYIIAQMLGGIVGGALVWITYLPHWEKTEDKAAKLGI
FCTAPAIRNLPSNFLTEFLGTALLVFAILGMGAQHTALGIGTLFVVFLIWSIGLSLGGPT
GYAINPARDLAPRIAHAILPIAGKGGSDWSYSWIPVFGPIAGGICGALLFNVIF
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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