KGP_PLAVS
ID KGP_PLAVS Reviewed; 846 AA.
AC A5K0N4;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=cGMP-dependent protein kinase {ECO:0000305};
DE EC=2.7.11.12 {ECO:0000250|UniProtKB:Q8I719};
GN Name=PKG {ECO:0000305}; ORFNames=PVX_084705 {ECO:0000312|EMBL:EDL46881.1};
OS Plasmodium vivax (strain Salvador I).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=126793 {ECO:0000312|Proteomes:UP000008333};
RN [1] {ECO:0000312|Proteomes:UP000008333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Salvador I {ECO:0000312|Proteomes:UP000008333};
RX PubMed=18843361; DOI=10.1038/nature07327;
RA Carlton J.M., Adams J.H., Silva J.C., Bidwell S.L., Lorenzi H., Caler E.,
RA Crabtree J., Angiuoli S.V., Merino E.F., Amedeo P., Cheng Q.,
RA Coulson R.M.R., Crabb B.S., del Portillo H.A., Essien K., Feldblyum T.V.,
RA Fernandez-Becerra C., Gilson P.R., Gueye A.H., Guo X., Kang'a S.,
RA Kooij T.W.A., Korsinczky M., Meyer E.V.-S., Nene V., Paulsen I., White O.,
RA Ralph S.A., Ren Q., Sargeant T.J., Salzberg S.L., Stoeckert C.J.,
RA Sullivan S.A., Yamamoto M.M., Hoffman S.L., Wortman J.R., Gardner M.J.,
RA Galinski M.R., Barnwell J.W., Fraser-Liggett C.M.;
RT "Comparative genomics of the neglected human malaria parasite Plasmodium
RT vivax.";
RL Nature 455:757-763(2008).
RN [2] {ECO:0007744|PDB:4RZ7, ECO:0007744|PDB:5EZR, ECO:0007744|PDB:5F0A, ECO:0007744|PDB:5FET}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH INHIBITORS.
RX PubMed=28874661; DOI=10.1038/s41467-017-00572-x;
RA Baker D.A., Stewart L.B., Large J.M., Bowyer P.W., Ansell K.H.,
RA Jimenez-Diaz M.B., El Bakkouri M., Birchall K., Dechering K.J.,
RA Bouloc N.S., Coombs P.J., Whalley D., Harding D.J., Smiljanic-Hurley E.,
RA Wheldon M.C., Walker E.M., Dessens J.T., Lafuente M.J., Sanz L.M.,
RA Gamo F.J., Ferrer S.B., Hui R., Bousema T., Angulo-Barturen I.,
RA Merritt A.T., Croft S.L., Gutteridge W.E., Kettleborough C.A.,
RA Osborne S.A.;
RT "A potent series targeting the malarial cGMP-dependent protein kinase
RT clears infection and blocks transmission.";
RL Nat. Commun. 8:430-430(2017).
RN [3] {ECO:0007744|PDB:5DYL, ECO:0007744|PDB:5DZC}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEX WITH ATP ANALOG.
RX PubMed=31239348; DOI=10.1073/pnas.1905558116;
RA El Bakkouri M., Kouidmi I., Wernimont A., Amani M., Hutchinson A.,
RA Loppnau P., Kim J.J., Flueck C., Walker J.R., Seitova A., Senisterra G.,
RA Kakihara Y., Kim C., Blackman M.J., Calmettes C., Baker D.A., Hui R.;
RT "Structures of the cGMP-dependent protein kinase in malaria parasites
RT reveal a unique structural relay mechanism for activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:14164-14173(2019).
CC -!- FUNCTION: Serine/threonine protein kinase which acts as a downstream
CC effector of the second messenger cGMP. Controls the release of Ca(2+)
CC from intracellular stores by regulating phosphoinositide biosynthesis.
CC Ca(2+) signals are essential for merozoite and sporozoite invasion and
CC egress from host hepatocytes and erythrocytes, and, in the mosquito
CC vector, for gametocyte activation, and ookinete and sporozoite motility
CC (By similarity). During the host liver stage, regulates the initial
CC invasion of host hepatocytes by sporozoites by regulating sporozoite
CC motility and microneme exocytosis. Following parasite development in
CC the hepatocytes, required for the release of merosomes, a vesicle
CC containing the mature merozoites (By similarity). During the asexual
CC blood stage, required for the progression from schizont to the ring
CC stage following merozoite invasion of host erythrocytes and for
CC merozoite egress. Regulates merozoite egress by promoting the release
CC of exonemes and micronemes which contain proteins essential for egress.
CC Phosphorylates CDPK1 predominantly at the late schizont stage;
CC phosphorylation at 'Ser-64' regulates CDPK1 protein-protein interaction
CC and phosphorylation at 'Thr-231' may regulate CDPK1 kinase activity. In
CC the mosquito vector, required for the initiation of gametogenesis
CC induced by xanthurenic acid, specifically the gametocyte
CC differentiation from the crescent-shaped form to the spherical form (By
CC similarity). Required for the gliding motility of ookinetes to reach
CC and penetrate the midgut epithelium by promoting Ca(2+)-mediated
CC activation of CDPK1 and CDPK4. Also required for microneme secretion in
CC ookinete by promoting Ca(2+)-mediated activation of CDPK3 (By
CC similarity). {ECO:0000250|UniProtKB:A0A509AKL0,
CC ECO:0000250|UniProtKB:Q8I719}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.12;
CC Evidence={ECO:0000250|UniProtKB:Q8I719};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.12; Evidence={ECO:0000250|UniProtKB:Q8I719};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q8I719};
CC -!- ACTIVITY REGULATION: Activated by cGMP. Not activated by cAMP. cGMP
CC binding allosterically triggers a conformational change at the alpha C-
CC helix of cGMP-binding domain 4, which bridges the regulatory and
CC catalytic domains, causing the capping triad, composed of Arg-477, Gln-
CC 525 and Asp-526, to form and stabilize the active conformation. The
CC cGMP-binding domains acts cooperatively to activate PKG.
CC {ECO:0000250|UniProtKB:Q8I719}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8I719}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8I719}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8I719};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q8I719}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q8I719}. Note=Predominantly localizes to
CC the cytoplasm during schizogony. {ECO:0000250|UniProtKB:Q8I719}.
CC -!- DOMAIN: The cNMP-binding domains 1, 2 and 4 bind preferentially cGMP.
CC The cNMP-binding domain 4 binds cGMP with the highest affinity and is
CC highly selective for cGMP. The cNMP-binding domain 3 does not bind cGMP
CC but is required for cGMP-dependent catalytic activity. The cNMP-binding
CC domains 1, 2 and 4 can bind cAMP but with less affinity.
CC {ECO:0000250|UniProtKB:Q8I719}.
CC -!- DOMAIN: The autoinhibitory segment (AIS) interacts with the active site
CC and inhibits catalytic activity. {ECO:0000250|UniProtKB:Q8I719}.
CC -!- PTM: Autophosphorylated. {ECO:0000250|UniProtKB:Q8I719}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. cGMP subfamily. {ECO:0000305}.
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DR EMBL; AAKM01000002; EDL46881.1; -; Genomic_DNA.
DR RefSeq; XP_001616608.1; XM_001616558.1.
DR PDB; 4RZ7; X-ray; 2.35 A; A=1-846.
DR PDB; 5DYL; X-ray; 2.40 A; A=1-846.
DR PDB; 5DZC; X-ray; 2.30 A; A=1-846.
DR PDB; 5EZR; X-ray; 2.50 A; A=1-846.
DR PDB; 5F0A; X-ray; 2.60 A; A=1-846.
DR PDB; 5FET; X-ray; 3.07 A; A=1-846.
DR PDBsum; 4RZ7; -.
DR PDBsum; 5DYL; -.
DR PDBsum; 5DZC; -.
DR PDBsum; 5EZR; -.
DR PDBsum; 5F0A; -.
DR PDBsum; 5FET; -.
DR AlphaFoldDB; A5K0N4; -.
DR SMR; A5K0N4; -.
DR STRING; 126793.A5K0N4; -.
DR EnsemblProtists; EDL46881; EDL46881; PVX_084705.
DR GeneID; 5475916; -.
DR KEGG; pvx:PVX_084705; -.
DR InParanoid; A5K0N4; -.
DR OMA; SKNPDGH; -.
DR BRENDA; 2.7.11.12; 4894.
DR Proteomes; UP000008333; Chromosome 13.
DR Proteomes; UP000008333; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030553; F:cGMP binding; IEA:UniProtKB-KW.
DR GO; GO:0004692; F:cGMP-dependent protein kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 3.
DR CDD; cd05572; STKc_cGK; 1.
DR Gene3D; 2.60.120.10; -; 4.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR002374; cGMP_dep_kinase.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR035014; STKc_cGK.
DR Pfam; PF00027; cNMP_binding; 3.
DR Pfam; PF00069; Pkinase; 1.
DR PIRSF; PIRSF000559; cGMP-dep_kinase; 1.
DR SMART; SM00100; cNMP; 4.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF51206; SSF51206; 4.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 3.
DR PROSITE; PS00889; CNMP_BINDING_2; 3.
DR PROSITE; PS50042; CNMP_BINDING_3; 4.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; cGMP; cGMP-binding; Cytoplasm;
KW Endoplasmic reticulum; Kinase; Magnesium; Membrane; Metal-binding;
KW Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..846
FT /note="cGMP-dependent protein kinase"
FT /id="PRO_0000451909"
FT DOMAIN 534..791
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 792..846
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 1..22
FT /note="Autoinhibitory segment"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT REGION 51..166
FT /note="cNMP-binding domain 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT REGION 169..268
FT /note="cNMP-binding domain 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT REGION 288..391
FT /note="cNMP-binding domain 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT REGION 411..510
FT /note="cNMP-binding domain 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT REGION 824..846
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 657
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 106
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 115
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 116
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 118
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 125
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 126
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="1"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 466
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 475
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 476
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 478
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 485
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 486
FT /ligand="3',5'-cyclic GMP"
FT /ligand_id="ChEBI:CHEBI:57746"
FT /ligand_label="2"
FT /ligand_note="allosteric activator"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT BINDING 540..548
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 563
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:31239348, ECO:0007744|PDB:5DZC"
FT SITE 477
FT /note="Part of a catalytic triad required for cGMP binding
FT and cGMP-dependent kinase activity"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT SITE 525
FT /note="Part of a catalytic triad required for cGMP binding
FT and cGMP-dependent kinase activity"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT SITE 526
FT /note="Part of a catalytic triad required for cGMP binding
FT and cGMP-dependent kinase activity"
FT /evidence="ECO:0000250|UniProtKB:Q8I719"
FT HELIX 21..28
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 52..54
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 57..66
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 142..165
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 168..170
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 175..182
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 186..190
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 234..238
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 246..259
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 260..266
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 294..303
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 305..309
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 324..332
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 341..346
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 354..358
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 366..380
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 381..388
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 393..406
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 410..413
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 417..425
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 428..432
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 437..439
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 447..454
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 456..460
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 476..479
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 486..491
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 496..502
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 503..507
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 512..526
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 531..533
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 534..541
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 544..553
FT /evidence="ECO:0007829|PDB:5DZC"
FT TURN 554..556
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 559..566
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 567..572
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 576..588
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 597..601
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 604..612
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 619..626
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 631..650
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 660..662
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 663..665
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 671..673
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 693..695
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 698..701
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 710..723
FT /evidence="ECO:0007829|PDB:5DZC"
FT STRAND 728..732
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 736..745
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 757..766
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 771..773
FT /evidence="ECO:0007829|PDB:5DZC"
FT TURN 779..782
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 783..786
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 789..791
FT /evidence="ECO:0007829|PDB:5DZC"
FT HELIX 796..800
FT /evidence="ECO:0007829|PDB:5DZC"
SQ SEQUENCE 846 AA; 96548 MW; F4816715FBBB8211 CRC64;
MRCNERNKKK AIFSNDDFSG EDTLMEDHLQ LREKLSEDIE MIKASLKNNL VCSTLNDNEI
LTLSNYMQFF VFKGGDLVIK QGEKGSYFFI INSGKFDVYV NDKKVKSMGK GSSFGEAALI
HNTQRSATIM AETDGTLWGV QRSTFRATLK QLSNRNFNEN RSFIDSVSVF DMLTEAQKNM
ITNACVIQMF KPGETIVKQG DYGDVLFILK EGKATVFIND KEIRVLNKGS YFGERALLYD
EPRSATIIAK EPTACASICR KLLNIVLGNL QVVLFRNIMT EALQQSEIFR QFSAEQLNDL
ADTAIVRDYP ANYHILHKDK VKSVKYLIVL EGKVELFLDD ESIGILTRGK SFGDQYVLNQ
KQKFRHTVKS LDVCKIALIT ESCLADCLGD NNIDASIDHN NKKSIIKKMY IFRYLSEQQC
NLLIEAFRTT RYEEGDYIIQ EGEVGSRFYI IKNGEVEVTK NGKRLRTLGK NDYFGERALL
YDEPRTASII SKATSVECWF VDKSVFLQII QGPMLTHLEE RIKMQDTKVE MHELETERII
GRGTFGTVKL VHHKPTQIRY ALKCVSKRSI ISLNQQNNIK LEREITAEND HPFIIRLVRT
FKDSNCFYFL TELVTGGELY DAIRKLGLLS KPQAQFYLGS IILAIEYLHE RNIVYRDLKP
ENILLDKQGY VKLIDFGCAK KIQGRAYTLV GTPHYMAPEV ILGKGYGCTV DIWALGVCLY
EFICGPLPFG NDQEDQLEIF RDILTGQLTF PDYVSDQDSI NLMKRLLCRL PQGRIGCSIN
GFKDIKEHAF FGNFNWDKLA GRLLEPPLVS KGETYAEDID IKQIEEEDAL NEGEPLDGDD
SWDVDF
