SitesBLAST
Comparing CCNA_02221 FitnessBrowser__Caulo:CCNA_02221 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)
P13009 Methionine synthase; 5-methyltetrahydrofolate--homocysteine methyltransferase; Methionine synthase, vitamin-B12-dependent; MS; EC 2.1.1.13 from Escherichia coli (strain K12) (see 5 papers)
64% identity, 98% coverage: 8:889/899 of query aligns to 355:1225/1227 of P13009
- E694 (= E350) binding
- GDVHD 756:760 (= GDVHD 414:418) binding
- D757 (= D415) mutation to E: Decreases activity by about 70%.; mutation to N: Decreases activity by about 45%.
- H759 (= H417) binding axial binding residue; mutation to G: Loss of catalytic activity.
- S804 (= S462) binding
- T808 (= T466) binding
- S810 (= S468) mutation to A: Decreases activity by about 40%.
- A860 (= A519) binding
- D946 (= D605) binding
- R1134 (= R798) binding
- YY 1189:1190 (≠ YF 853:854) binding
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
- 247 binding
- 310 binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
- 311 binding ; mutation C->A,S: Loss of zinc binding. Loss of catalytic activity.
Q99707 Methionine synthase; MS; 5-methyltetrahydrofolate--homocysteine methyltransferase; Cobalamin-dependent methionine synthase; Vitamin-B12 dependent methionine synthase; EC 2.1.1.13 from Homo sapiens (Human) (see 6 papers)
56% identity, 98% coverage: 9:889/899 of query aligns to 371:1263/1265 of Q99707
- GSR 382:384 (≠ GSA 20:22) binding
- D449 (= D87) binding
- N470 (= N108) binding
- D537 (= D175) binding
- N579 (= N217) binding
- R585 (= R223) binding
- R591 (= R229) binding
- D919 (≠ Q552) to G: in dbSNP:rs1805087
- D963 (≠ P595) mutation to E: Decreases binding to MTRR; when associated with N-1071.
- K1071 (= K694) mutation to N: Decreases binding to MTRR; when associated with E-963.
Sites not aligning to the query:
- 61 natural variant: R -> K
- 255 C → Y: in dbSNP:rs1140598
3bulA E. Coli i690c/g743c meth c-terminal fragment (649-1227) (see paper)
61% identity, 65% coverage: 309:889/899 of query aligns to 3:575/577 of 3bulA
- active site: D107 (= D415), H109 (= H417), S160 (= S468)
- binding cobalamin: H109 (= H417), V116 (= V424), G152 (= G460), L153 (= L461), S154 (= S462), L156 (= L464), I157 (= I465), T158 (= T466), G183 (= G491), G184 (= G492), Q208 (≠ V517), N209 (≠ D518), A210 (= A519), T213 (≠ A522), M302 (≠ A611), D443 (= D757), A486 (= A800), P487 (= P801), G488 (= G802), Y489 (= Y803), H495 (= H809), K498 (= K812), M521 (= M835), G524 (= G838), V527 (= V841), S528 (= S842)
3ivaA Structure of the b12-dependent methionine synthase (meth) c-teminal half with adohcy bound (see paper)
61% identity, 65% coverage: 309:889/899 of query aligns to 3:575/576 of 3ivaA
- active site: D107 (= D415), H109 (= H417), S160 (= S468)
- binding cobalamin: H109 (= H417), G112 (= G420), V116 (= V424), G152 (= G460), L153 (= L461), S154 (= S462), L156 (= L464), I157 (= I465), T158 (= T466), G183 (= G491), G184 (= G492), Q208 (≠ V517), N209 (≠ D518), T303 (≠ S612), D443 (= D757), A486 (= A800), G488 (= G802), Y489 (= Y803), H495 (= H809), A520 (= A834), M521 (= M835), G524 (= G838), V527 (= V841), S528 (= S842)
- binding s-adenosyl-l-homocysteine: E447 (= E761), R484 (= R798), P485 (= P799), Y489 (= Y803), A491 (= A805), Y539 (= Y853)
3k13C Structure of the pterin-binding domain metr of 5- methyltetrahydrofolate-homocysteine methyltransferase from bacteroides thetaiotaomicron
69% identity, 32% coverage: 9:297/899 of query aligns to 4:286/287 of 3k13C
- binding n-[4-({[(6s)-2-amino-4-hydroxy-5-methyl-5,6,7,8-tetrahydropteridin-6-yl]methyl}amino)benzoyl]-l-glutamic acid: E9 (= E14), G15 (= G20), R17 (≠ A22), N103 (= N108), D170 (= D175), G209 (= G214), S211 (= S216), N212 (= N217), R218 (= R223), R224 (= R229), I244 (= I249)
4cczA Crystal structure of human 5-methyltetrahydrofolate-homocysteine methyltransferase, the homocysteine and folate binding domains
64% identity, 32% coverage: 9:293/899 of query aligns to 331:610/611 of 4cczA
- binding (6s)-5,6,7,8-tetrahydrofolate: E336 (= E14), G342 (= G20), R344 (≠ A22), N430 (= N108), M458 (= M136), D497 (= D175), G536 (= G214), S538 (= S216), N539 (= N217), F542 (= F220), R545 (= R223), R551 (= R229)
1bmtA How a protein binds b12: a 3.O angstrom x-ray structure of the b12- binding domains of methionine synthase (see paper)
74% identity, 27% coverage: 309:555/899 of query aligns to 3:246/246 of 1bmtA
- active site: D107 (= D415), H109 (= H417), S160 (= S468)
- binding co-methylcobalamin: E44 (= E350), M48 (= M354), M51 (= M357), G55 (= G361), L65 (= L371), V68 (= V374), D107 (= D415), V108 (= V416), H109 (= H417), D110 (= D418), I111 (= I419), I115 (= I423), G152 (= G460), L153 (= L461), S154 (= S462), L156 (= L464), I157 (= I465), T158 (= T466), G183 (= G491), G184 (= G492), A185 (= A493), V207 (= V516), N209 (≠ D518), A210 (= A519)
6bdyA Crystal structure of the meth reactivation domain bound to sinefungin (see paper)
53% identity, 36% coverage: 564:889/899 of query aligns to 5:325/326 of 6bdyA
1mskA Methionine synthase (activation domain) (see paper)
53% identity, 36% coverage: 564:889/899 of query aligns to 5:325/327 of 1mskA
8g3hA Structure of cobalamin-dependent methionine synthase (meth) in a resting state (see paper)
38% identity, 54% coverage: 12:500/899 of query aligns to 335:806/841 of 8g3hA
- binding cobalamin: F675 (= F364), V685 (= V374), K693 (= K382), G720 (= G414), V722 (= V416), H723 (= H417), D724 (= D418), I725 (= I419), G726 (= G420), V730 (= V424), M767 (≠ L461), S768 (= S462), L770 (= L464), V772 (≠ T466), I795 (≠ L489), L796 (≠ I490), G797 (= G491), G798 (= G492), A799 (= A493)
Sites not aligning to the query:
8sseA Methionine synthase, c-terminal fragment, cobalamin and reactivation domains from thermus thermophilus hb8
31% identity, 60% coverage: 317:856/899 of query aligns to 4:506/507 of 8sseA
- binding cobalamin: H97 (= H417), G100 (= G420), V104 (= V424), S142 (= S462), L145 (≠ I465), V146 (≠ T466), I169 (≠ L489), G171 (= G491), G172 (= G492), A173 (= A493), H405 (≠ S753), V409 (≠ D757), S451 (≠ A800), F452 (≠ P801), G453 (= G802), Y454 (= Y803), Q463 (≠ K812), L485 (≠ M835), E488 (≠ G838), A490 (= A840), S492 (= S842)
5vooA Methionine synthase folate-binding domain with methyltetrahydrofolate from thermus thermophilus hb8 (see paper)
35% identity, 30% coverage: 12:283/899 of query aligns to 5:273/282 of 5vooA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: E7 (= E14), R8 (= R15), G13 (= G20), S14 (= S21), K15 (≠ A22), D77 (= D87), N98 (= N108), D165 (= D175), G204 (= G214), N207 (= N217), F210 (= F220), R217 (= R229), I237 (= I249)
7xcnP Crystal structure of the mttb-mttc complex at 2.7 a resolution (see paper)
32% identity, 19% coverage: 329:497/899 of query aligns to 20:188/215 of 7xcnP
- binding 5-hydroxybenzimidazolylcobamide: D104 (= D415), I105 (≠ V416), H106 (= H417), I108 (= I419), G109 (= G420), V113 (= V424), S150 (≠ L461), S151 (= S462), L153 (= L464), M154 (≠ I465), T155 (= T466), M180 (≠ L489), G182 (= G491), G183 (= G492)
Sites not aligning to the query:
2i2xB Crystal structure of methanol:cobalamin methyltransferase complex mtabc from methanosarcina barkeri (see paper)
35% identity, 20% coverage: 317:497/899 of query aligns to 37:216/258 of 2i2xB
- active site: D134 (= D415), H136 (= H417), T187 (≠ S468)
- binding 5-hydroxybenzimidazolylcob(iii)amide: G133 (= G414), D134 (= D415), V135 (= V416), H136 (= H417), D137 (= D418), I138 (= I419), G139 (= G420), V143 (= V424), T179 (≠ G460), T181 (≠ S462), L183 (= L464), M184 (≠ I465), T185 (= T466), A208 (≠ L489), G210 (= G491), G211 (= G492), G212 (≠ A493)
Sites not aligning to the query:
Q46EH4 Methanol--corrinoid protein; Methanol:corrinoid methyltransferase 1 subunit of 27 kDa; MT1 subunit 27 kDa from Methanosarcina barkeri (strain Fusaro / DSM 804) (see paper)
35% identity, 20% coverage: 317:497/899 of query aligns to 37:216/258 of Q46EH4
- H129 (≠ A410) mutation to K: Does not affect cobalamin-binding.
- H136 (= H417) mutation H->G,K: Abolishes cobalamin-binding.
Sites not aligning to the query:
- 256:258 HKH→KKK: Does not affect cobalamin-binding.
3ezxA Structure of methanosarcina barkeri monomethylamine corrinoid protein
35% identity, 17% coverage: 317:469/899 of query aligns to 7:156/212 of 3ezxA
- active site: D100 (= D415), H102 (= H417), S155 (= S468)
- binding 5-hydroxybenzimidazolylcobamide: M47 (= M357), F54 (= F364), D100 (= D415), I101 (≠ V416), H102 (= H417), D103 (= D418), I104 (= I419), V109 (= V424), V147 (≠ S462), S149 (vs. gap), L151 (= L464), M152 (≠ I465), T153 (= T466)
Sites not aligning to the query:
4jgiB 1.5 angstrom crystal structure of a novel cobalamin-binding protein from desulfitobacterium hafniense dcb-2 (see paper)
34% identity, 15% coverage: 356:492/899 of query aligns to 45:174/206 of 4jgiB
- active site: D95 (= D415), H97 (= H417), A148 (≠ S468)
- binding co-methylcobalamin: L63 (≠ V374), D95 (= D415), L96 (≠ V416), H97 (= H417), D98 (= D418), I99 (= I419), G100 (= G420), F104 (≠ V424), G140 (= G460), S142 (= S462), L145 (≠ I465), G173 (= G491), G174 (= G492)
Sites not aligning to the query:
2yckX Methyltransferase bound with tetrahydrofolate (see paper)
30% identity, 27% coverage: 8:250/899 of query aligns to 10:238/272 of 2yckX
- binding (6s)-5,6,7,8-tetrahydrofolate: M21 (≠ S21), F22 (≠ A22), D85 (= D87), N106 (= N108), D170 (= D175), G206 (= G214), N209 (= N217), Q212 (≠ F220), K213 (≠ S221), R217 (= R229), I237 (= I249)
2ycjA Methyltransferase bound with methyltetrahydrofolate (see paper)
30% identity, 27% coverage: 8:250/899 of query aligns to 9:237/271 of 2ycjA
- binding 5-methyl-5,6,7,8-tetrahydrofolic acid: M20 (≠ S21), F21 (≠ A22), D84 (= D87), N105 (= N108), D169 (= D175), G205 (= G214), N208 (= N217), Q211 (≠ F220), R216 (= R229), I236 (= I249)
2yciX Methyltransferase native (see paper)
30% identity, 27% coverage: 8:250/899 of query aligns to 9:237/271 of 2yciX
Query Sequence
>CCNA_02221 FitnessBrowser__Caulo:CCNA_02221
MDPEMRPVFVNIGERTNVTGSAKFKKLIVEGNYPEALSVARQQVEAGAQVIDVNMDEGLL
DSQQAMVTFLNLMAAEPDIARVPVMIDSSKWEVIEAGLKCVQGKAIVNSISLKEGEEKFL
EQATLCLRYGAAVVVMAFDEVGQADTEKRKVEICTRAYNTLVDKVGFPPEDIIFDPNIFA
VATGIEEHDNYAVDFIEATRRIKQMLPYARVSGGVSNVSFSFRGNEPVRRAIHSVFLYHA
INAGMDMGIVNAGDLPVYDDIDPALREAVEDVILNRPQRDPVMTNTERLVEMAPRYKGEK
GQQQVANLEWRKGTVNERLTHALVHGITEFIEQDTEEARLAAERPLHVIEGPLMDGMNVV
GDLFGAGKMFLPQVVKSARVMKQAVAWLMPFMEAEKEGQERKAAGKVLMATVKGDVHDIG
KNIVGVVLQCNNYEVVDLGVMVPADRILDEAKKHKVDMIGLSGLITPSLDEMVFVAAEME
RQGFDIPLLIGGATTSRTHTAVKIEPAYRRGPTTYVVDASRAVGVVSGLLSEGERDRIIA
ETRAEYVKVREQYARGQTTKARASIQEARKRAFAIDWKGYAPPKPAFIGTRVFEPSLAEL
VPFIDWSPFFASWELIGRFPQILEDDVVGQAATDLYRDARAMLDKVVEEKWFGAKGVIGF
WPAQAQGDDIVLYTDETRVAEFSRLHTLRQQMDKGADKSGEAKANVALSDFVAPIGQGAD
YVGGFAVTAGHGEDEIVAKFKAAGDDYNAIMASALADRLAEAFAEWLHYKARVELWGYAA
DEDADVERLIAEKYQGIRPAPGYPAQPDHTEKGTLFKLLDAEAATGLQLTESYAMTPGAA
VSGLFFSHRQAHYFGVGKIDADQVEDYARRKGWDMETAERWLSPILNYDPLARARGAAA
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