Molecular Chaperones of Leishmania: Central Players in Many Stress-Related and -Unrelated Physiological Processes

Table 3

Classification of L. major HSP40s according to their structural features.

Name^1	GeneDB ID	Size^2	J domain	G/F-rich	Zn-finger	Type	Remarks
J1	LmjF32.3030	329	14–76	—	—	III
J2	LmjF27.2400	396	6–70	78–94	120–205	I
J3	LmjF21.0490	448	6–71	82–99	125–210	I
J4	LmjF15.1220	478	6–71	87–115	144–227	I
J5	LmjF36.1330	316	39–111	123–135	—	II
J6	LmjF36.6270	345	4–70	93–125	—	II	GMPG repeats
J7	LmjF32.1940	323	3–71	78–105	—	II
J8	LmjF24.0520	795	43–111	—	—	III
J10	LmjF17.0460	216	36–103	139–166	—	II
J11	LmjF04.0780	573	9–72	—	—	III
J13	LmjF18.1490	184	14–93	—	—	III
J14	LmjF08.0990	326	22–95/164–233	—	—	III	Two J domains
J15	LmjF19.0080	432	5–67	—	—	III
J16	LmjF20.1130	653	137–202	210–242	—	II	SANT, DNA-binding domain (513–567) SMART accession number: SM00717
J17	LmjF12.1110	733	88–143	148–209	—	II
J18	LmjF27.0410	321	16–80	—	—	III
J19	LmjF34.4080	257	29–115	131–147	—	II
J20	LmjF36.0610	261	172–239	—	—	III	J domain at C-terminus
J21	LmjF26.1410	536	405–474	—	—	III	J domain at C-terminus
J22	LmjF36.2110	286	19–83	111–124	—	II
J23	LmjF18.0330	244	49–112	—	—	III
J24	LmjF30.1790	456	27–89	134–167	—	II
J25	LmjF26.1270	852	391–468	479–500	—	II	J domain in the middle
J26	LmjF17.0040	262	84–146	—	—	III
J27	LmjF04.0940	487	86–150	156–210	247–325	I
J28	LmjF26.1200	646	282–346	365–389	—	II	J domain in the middle
J29	LmjF24.1080	436	376–436	—	—	III	J domain at C-terminus
J30	LmjF07.0780	299	—	—	—	—	Truncated in L. major
J31	LmjF26.0940	843	36–106	—	—	IV
J32	LmjF25.2190	377	8–74	80–119	322–351	I
J33	LmjF36.4470	275	7–69	—	—	III
J34	LmjF35.4630	491	134–203	202–240	—	II
J35	LmjF14.0110	523	444–514	—	—	III	J domain at C-terminus
J36	LmjF25.1690	278	60–154	—	—	III
J37	LmjF18.1430	1119	5–70	—	—	III
J38	LmjF30.2450	336	15–69	—	—	III
J40	LmjF10.1050	276	40–108	—	—	III
J41	LmjF31.0510	596	283–348	360–391	—	II	J domain in the middle
J42	LmjF18.1650	580	518–580	—	—	III	J domain at C-end; Tetratricopeptide repeat domain (TPR, 136–463)
J43	LmjF35.4040	388	4–109	—	—	III
J44	LmjF31.3100	217	18–89	—	—	II
J45	LmjF32.3300	400	54–121	139–159	176–259	I
J46	LmjF25.1100	395	54–123	142–149	174–257	I
J47	LmjF20.0550	545	350–483	—	257–335	IV	J domain at C-terminus
J49	LmjF30.1030	416	52–119	—	—	III
J50	LmjF35.2980	478	48–109	119–164	185–270	I
J51	LmjF34.2430	808	700–770	775–807	—	II	J domain at C-end; two TPR domains (345–451 and 572–677)
J52	LmjF36.0500	510	377–448	455–510	—	II	J domain at C-end, 2 Tetratricopeptide repeat (TPR) domains: 17–118 and 254–359
J53	LmjF14.1330	564	431–503	513–560	—	II	J domain at C-terminus; two TPR domains (49–118 and 221–288)
J54	LmjF33.0900	580	3–66	85–140	—	II
J55	LmjF28.1270	472	9–80	—	—	III
J56	LmjF33.2690	267	45–136	—	—	III
J57	LmjF29.1890	395	14–86	144–177	—	II
J58	LmjF24.1300	807	15–87	—	—	III
J59	LmjF30.2210	2458	1384–1463	—	—	III	putative endosomal trafficking protein RME-8
J60	LmjF09.1440	413	42–110	—	—	III
J61	LmjF08.0650	286	3–78	—	—	III
J62	LmjF34.0040	679	95–163	—	—	III
J63	LmjF32.0590	316	40–107	—	—	III
J64	LmjF07.0770	402	153–221	—	—	III	J domain in the middle
J65	LmjF34.3870	781	707–777	—	—	III	J domain at C-terminus; TPR domain (481–630)
J66	LmjF22.0080	331	156–279	—	52–139	IV	J domain at C-terminus
J67	LmjF36.0760	855	779–852	—	—	III	J domain at C-terminus; two TPR domains (237–338 and 574–645)
J68	LmjF24.1910	121	51–119	—	—	IV
J69	LmjF36.4970	345	18–89	—	—	III
J71	LmjF24.0070	439	49–109	—	—	III
J72	LmjF35.3090	427	20–74	—	—	III
J73	LmjF26.2520	489	29–86	—	—	III
J74	LmjF28.1900	655	143–199	—	—	III

Nomenclature according to Folgueira and Requena [15].
²Number of amino acids deduced from the annotated gene sequences in the GeneDB database.