Table 2.

Starting and ending positions of conserved motifs in CA-II, associated E-values and motif contribution to function. Residues from Table S1 are underlined and highlighted in bold. SNV positions (K18E, K18Q, H107Y and N252D) are underlined, italicized and presented in bold red.

Motif	Residue Range	Residues	E-Value	Residue Count	Contribution to Functions
1	190–209	YWTYPGSLTTPPLLECVTWI	2.2 × 10${}^{-164}$	20	Catalytic mechanism and Primary CO${}_2$ binding pocket formation
2	104–123	GSEHTVDKKKYAAELHLVHW	4.4 × 10${}^{-140}$	20	Active site and/or Zn${}^{2+}$ stability
3	240–259	MVDNWRPAQPLKNRQIKASF	1.2 × 10${}^{-108}$	20	Tertiary CO${}_2$ binding pocket formation and enzyme stability
4	79–98	LKGGPLDGTYRLIQFHFHWG	3.0 × 10${}^{-89}$	20	Enzyme stability and/or Zn${}^{2+}$ coordination
5	25–44	GERQSPVDIDTHTAKYDPSL	6.5 × 10${}^{-86}$	20	Enzyme stability
6	127–146	YGDFGKAVQQPDGLAVLGIF	3.8 × 10${}^{-73}$	20	Primary CO${}_2$ binding pocket formation
7	166–185	IKTKGKSADFTNFDPRGLLP	6.0 × 10${}^{-54}$	20	Participated in secondary aromatic cluster
8	210–229	VLKEPISVSSEQVLKFRKLN	6.4 × 10${}^{-40}$	20	Enzyme stability and secondary CO${}_2$ binding pocket formation
9	53–72	QATSLRILNNGHAFNVEFDD	1.9 × 10${}^{-41}$	20	Enzyme stability and/or catalytic mechanism
10	5–20	WGYGKHNGPEHWHKDF	7.7 × 10${}^{-25}$	16	Enzyme stability
11	148–163	KVGSAKPGLQKVVDVL	2.3 × 10${}^{-6}$	16	Enzyme stability