SitesBLAST
Comparing HSERO_RS07330 FitnessBrowser__HerbieS:HSERO_RS07330 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 6 hits to proteins with known functional sites (download)
Q8NLB7 Gentisate transporter from Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) (see paper)
25% identity, 46% coverage: 26:224/432 of query aligns to 54:240/444 of Q8NLB7
- D54 (≠ E26) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- D57 (= D29) mutation to A: Loss of transport activity.; mutation to E: Retains 50% of its transport activity.
- R103 (= R81) mutation to A: Loss of transport activity.
Sites not aligning to the query:
- 309 W→V: Loss of transport activity.
- 312 D→A: Loss of transport activity.
- 313 R→A: Loss of transport activity.
- 317 mutation I->H,Y: Loss of transport activity.
- 386 R→A: Loss of transport activity.
Q9Z2I6 Synaptic vesicle glycoprotein 2C; Synaptic vesicle protein 2C from Rattus norvegicus (Rat) (see 3 papers)
32% identity, 20% coverage: 70:156/432 of query aligns to 203:281/727 of Q9Z2I6
Sites not aligning to the query:
- 1:57 Interaction with SYT1
- 529:566 (Microbial infection) C.botulinum neurotoxin type A-binding
- 559 N→A: Loss of one glycosylation site. No effect on C.botulinum neurotoxin type A (BoNT/A, botA) binding, but reduces the uptake of BoNT/A.
Q496J9 Synaptic vesicle glycoprotein 2C from Homo sapiens (Human) (see 4 papers)
32% identity, 20% coverage: 70:156/432 of query aligns to 203:281/727 of Q496J9
Sites not aligning to the query:
- 519:563 (Microbial infection) C.botulinum neurotoxin type A-binding
- 534 modified: carbohydrate, N-linked (GlcNAc...) asparagine
- 559 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→A: No change in interaction with C.botulinum neurotoxin type A heavy chain (botA, BoNT/A HC). Decreased molecular weight probably due to glycosylation loss, decreased interaction with BoNT/A HC.; N→Q: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC. Greater reduction in weight; when associated with Q-565.
- 561 S→A: Decreased molecular weight probably due to glycosylation loss, decreased binding to BoNT/A HC.
- 563 F→A: No longer interacts with BoNT/A HC.
- 565 modified: carbohydrate, N-linked (GlcNAc...) asparagine; N→Q: Decreased molecular weight probably due to glycosylation loss, no change in binding to BoNT/A heavy chain. Greater reduction in weight; when associated with Q-559.
Q02563 Synaptic vesicle glycoprotein 2A; Synaptic vesicle protein 2; Synaptic vesicle protein 2A from Rattus norvegicus (Rat) (see 2 papers)
32% identity, 20% coverage: 70:156/432 of query aligns to 217:295/742 of Q02563
Sites not aligning to the query:
- 196:200 mutation Missing: No change in uptake of C.botulinum neurotoxin type D (BoNT/D, botD) or C.botulinum neurotoxin type E (BoNT/E).
- 321:331 mutation Missing: No change in uptake of BoNT/D or BoNT/E.
- 498 N→Q: No change in uptake of BoNT/E or C.botulinum neurotoxin type A (BoNT/A, botA) by mouse SV2A/SV2B knockout neurons; SV2A apparent molecular weight decreases. No change in uptake of BoNT/E; when associated with Q-548. No change in uptake of BoNT/D.
- 548 N→Q: No change in uptake of BoNT/E or BoNT/A by mouse SV2A/SV2B knockout neurons; SV2A apparent molecular weight decreases. No change in uptake of BoNT/E; when associated with Q-498. No change in uptake of BoNT/D.
- 570:573 RLVN→TLVQ: Restores apparent molecular weight to wild-type, does not restore uptake of BoNT/E.
- 573 N→Q: BoNT/E not taken up by mouse SV2A/SV2B knockout neurons, decreased uptake of BoNT/A; SV2A apparent molecular weight decreases. No change in uptake of BoNT/D.
A0A0H2VG78 Glucose transporter GlcP; Glucose/H(+) symporter from Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200) (see paper)
26% identity, 34% coverage: 76:220/432 of query aligns to 63:199/446 of A0A0H2VG78
- R102 (= R123) mutation to A: Loss of transport activity.
- I105 (≠ Q126) mutation to S: Affects symport activity. May function as an uniporter.
- E122 (= E143) mutation to A: Loss of transport activity.
- Q137 (= Q162) mutation to A: Loss of transport activity.
Sites not aligning to the query:
- 22 D→N: Affects symport activity. May function as an uniporter.
- 250 Q→A: Loss of transport activity.
- 251 Q→A: Loss of transport activity.
- 256 N→A: Loss of transport activity.
- 357 W→A: Loss of transport activity.
O23492 Inositol transporter 4; Myo-inositol-proton symporter INT4; Protein INOSITOL TRANSPORTER 4 from Arabidopsis thaliana (Mouse-ear cress) (see paper)
26% identity, 33% coverage: 80:222/432 of query aligns to 92:219/582 of O23492
Sites not aligning to the query:
- 559:561 LLE→AAA: No effect on targeting.
- 559:582 mutation Missing: No effect on targeting.
- 564:565 FK→AA: No effect on targeting.
- 570:575 RRREKK→AAAAAA: No effect on targeting.
Query Sequence
>HSERO_RS07330 FitnessBrowser__HerbieS:HSERO_RS07330
MTTTTTNAKHSKLSTVLRVTSGNFLEMFDFFLYGFYASYISKTFFPSDNEFVSLILTFGT
FGAGFLMRPLGAIILGSYIDRVGRRQGLIVTLAIMAIGTLLIAFVPGYATIGVAAPILVL
TGRLLQGFSAGVELGGVSVYLAEMATPGNKGFYVSWQSASQQAAIMASALIGYLVSQSLS
PVQISDWGWRIPFFIGCMIVPAIFIIRRSLQETDEFLARKRHPSFGEIMSSIAQNWKIVV
AGMMMVVMTTVSFYLITVYTPTFGKNVLKLSASDSLIVTFCVGLSNFCWLPIMGALSDRV
GRRPVLVAFTLLTLLTAYPVMSWLVSDISFKNLLITELWLSFLYASYNGAAVVALTEVMP
AHVRTVGFSLAYSLATAIFGGFTPLVSTWLIETSGDKAAPGYWMSFAAVCGLLATLVLYR
GKSAAATVSPTA
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