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Conserved domains on  [gi|1336026803|gb|POB89730|]
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peptidase M23 [Vibrio vulnificus]

Protein Classification

murein hydrolase activator EnvC( domain architecture ID 11471818)

murein hydrolase activator EnvC contains a M23 family metallopeptidase domain, it activates murein hydrolases AmiA and AmiB and plays a crucial role in daughter cell separation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 20-387 9.81e-89

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 272.79  E-value: 9.81e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  20 KSGFFFLSTCVLLTFLSFPTNAASPSELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATA 99
Cdd:COG4942     2 RKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 100 KANVGQLQRKMDELEGQKKAQTERLETLIQTYYVTQRANASASLLQQG--VEEDRISQYFQHLAKARAETINELESTKKQ 177
Cdd:COG4942    82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 178 LEQSQQQLLNEQSQIESLLKQQSTKHEQLAKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAK-----AAKRN 252
Cdd:COG4942   162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARleaeaAAAAE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 253 AIPMDGLAKQAGKLPWPLKGSILHQFGTKQTGQINWKGIVIAARYGEQVKSVYPGTVVFAEYLRGYGLVVLIDHGKGDMT 332
Cdd:COG4942   242 RTPAAGFAALKGKLPWPVSGRVVRRFGERDGGGGRNKGIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLT 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1336026803 333 LYGYNQALLKKEGDKVTAGEVIALAGDTGGQDRASLYFEIRRNSEAQNPRNWLVR 387
Cdd:COG4942   322 LYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWLAK 376
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 20-387 9.81e-89

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 272.79  E-value: 9.81e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  20 KSGFFFLSTCVLLTFLSFPTNAASPSELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATA 99
Cdd:COG4942     2 RKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 100 KANVGQLQRKMDELEGQKKAQTERLETLIQTYYVTQRANASASLLQQG--VEEDRISQYFQHLAKARAETINELESTKKQ 177
Cdd:COG4942    82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 178 LEQSQQQLLNEQSQIESLLKQQSTKHEQLAKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAK-----AAKRN 252
Cdd:COG4942   162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARleaeaAAAAE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 253 AIPMDGLAKQAGKLPWPLKGSILHQFGTKQTGQINWKGIVIAARYGEQVKSVYPGTVVFAEYLRGYGLVVLIDHGKGDMT 332
Cdd:COG4942   242 RTPAAGFAALKGKLPWPVSGRVVRRFGERDGGGGRNKGIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLT 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1336026803 333 LYGYNQALLKKEGDKVTAGEVIALAGDTGGQDRASLYFEIRRNSEAQNPRNWLVR 387
Cdd:COG4942   322 LYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWLAK 376
PRK11637 PRK11637
AmiB activator; Provisional
 10-387 1.89e-80

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 253.08  E-value: 1.89e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  10 RTYVAKQKTNKSGFFFLSTCVLLTFLSFPTNAA-SPSELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENE 88
Cdd:PRK11637   11 RAVKPRRFAIRPILYASVLSAGVLLCAFSAHASdNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  89 IKQTKQALATAKANVGQLQRKMDELEGQKKAQTERLETLIQTYYvTQRANASASLLQQGVE---EDRISQYFQHLAKARA 165
Cdd:PRK11637   91 LRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLDAAF-RQGEHTGLQLILSGEEsqrGERILAYFGYLNQARQ 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 166 ETINELESTKKQLEQSQQQLLNEQSQIESLLKQQSTKHEQLAKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEI 245
Cdd:PRK11637  170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSI 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 246 AKA------------------------AKRNAI---PMD----------GLAKQAGKLPWPLKGSILHQFGTKQTGQINW 288
Cdd:PRK11637  250 ARAereakaraereareaarvrdkqkqAKRKGStykPTEserslmsrtgGLGRPRGQAFWPVRGPTLHRFGEQLQGELRW 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 289 KGIVIAARYGEQVKSVYPGTVVFAEYLRGYGLVVLIDHGKGDMTLYGYNQALLKKEGDKVTAGEVIALAGDTGGQDRASL 368
Cdd:PRK11637  330 KGMVIGASEGTEVKAIADGRVLLADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGAQVRAGQPIALVGSSGGQGRPSL 409

                         410
                  ....*....|....*....
gi 1336026803 369 YFEIRRNSEAQNPRNWLVR 387
Cdd:PRK11637  410 YFEIRRQGQAVNPQPWLGR 428
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 288-381 1.95e-36

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 128.05  E-value: 1.95e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 288 WKGIVIAARYGEQVKSVYPGTVVFAEYLRGYGLVVLIDHGKGDMTLYGYNQALLKKEGDKVTAGEVIALAGDTGGQDRAS 367
Cdd:pfam01551   3 HKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTGPH 82

                          90
                  ....*....|....
gi 1336026803 368 LYFEIRRNSEAQNP 381
Cdd:pfam01551  83 LHFEIRKNGKPVDP 96
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 289-372 4.33e-28

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 105.37  E-value: 4.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 289 KGIVIAARYGEQVKSVYPGTVVFAEYLRGYGLVVLIDHGKGDMTLYGYNQALLKKEGDKVTAGEVIALAGDTGGQDRASL 368
Cdd:cd12797     2 NGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPHL 81


                  ....
gi 1336026803 369 YFEI 372
Cdd:cd12797    82 HFEI 85
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 46-251 9.94e-09

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.39  E-value: 9.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803   46 ELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQK---KAQTE 122
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIenvKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  123 RLETLIQTY------YVTQRANASASLLQQGVEE-----DRISQYFQHLAKARAETINELESTKKQLEQSQQQLLNEQSQ 191
Cdd:TIGR02169  762 ELEARIEELeedlhkLEEALNDLEARLSHSRIPEiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336026803  192 --------------IESLLKQQSTKHEQLAKTQGQRK---KTLGNIKQSISSDKNYLAELQRNETRLKAEIAKAAKR 251
Cdd:TIGR02169  842 ridlkeqiksiekeIENLNGKKEELEEELEELEAALRdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
 
Name Accession Description Interval E-value
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 20-387 9.81e-89

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 272.79  E-value: 9.81e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  20 KSGFFFLSTCVLLTFLSFPTNAASPSELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATA 99
Cdd:COG4942     2 RKLLLLALLLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 100 KANVGQLQRKMDELEGQKKAQTERLETLIQTYYVTQRANASASLLQQG--VEEDRISQYFQHLAKARAETINELESTKKQ 177
Cdd:COG4942    82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 178 LEQSQQQLLNEQSQIESLLKQQSTKHEQLAKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAK-----AAKRN 252
Cdd:COG4942   162 LAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARleaeaAAAAE 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 253 AIPMDGLAKQAGKLPWPLKGSILHQFGTKQTGQINWKGIVIAARYGEQVKSVYPGTVVFAEYLRGYGLVVLIDHGKGDMT 332
Cdd:COG4942   242 RTPAAGFAALKGKLPWPVSGRVVRRFGERDGGGGRNKGIDIAAPPGAPVRAVADGTVVYAGWLRGYGNLVIIDHGGGYLT 321

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1336026803 333 LYGYNQALLKKEGDKVTAGEVIALAGDTGGQDRASLYFEIRRNSEAQNPRNWLVR 387
Cdd:COG4942   322 LYAHLSSLLVKVGQRVKAGQPIGTVGSSGGQGGPTLYFELRKNGKPVDPLPWLAK 376
PRK11637 PRK11637
AmiB activator; Provisional
 10-387 1.89e-80

AmiB activator; Provisional


Pssm-ID: 236942 [Multi-domain]  Cd Length: 428  Bit Score: 253.08  E-value: 1.89e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  10 RTYVAKQKTNKSGFFFLSTCVLLTFLSFPTNAA-SPSELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENE 88
Cdd:PRK11637   11 RAVKPRRFAIRPILYASVLSAGVLLCAFSAHASdNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASRK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  89 IKQTKQALATAKANVGQLQRKMDELEGQKKAQTERLETLIQTYYvTQRANASASLLQQGVE---EDRISQYFQHLAKARA 165
Cdd:PRK11637   91 LRETQNTLNQLNKQIDELNASIAKLEQQQAAQERLLAAQLDAAF-RQGEHTGLQLILSGEEsqrGERILAYFGYLNQARQ 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 166 ETINELESTKKQLEQSQQQLLNEQSQIESLLKQQSTKHEQLAKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEI 245
Cdd:PRK11637  170 ETIAELKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSI 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 246 AKA------------------------AKRNAI---PMD----------GLAKQAGKLPWPLKGSILHQFGTKQTGQINW 288
Cdd:PRK11637  250 ARAereakaraereareaarvrdkqkqAKRKGStykPTEserslmsrtgGLGRPRGQAFWPVRGPTLHRFGEQLQGELRW 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 289 KGIVIAARYGEQVKSVYPGTVVFAEYLRGYGLVVLIDHGKGDMTLYGYNQALLKKEGDKVTAGEVIALAGDTGGQDRASL 368
Cdd:PRK11637  330 KGMVIGASEGTEVKAIADGRVLLADWLQGYGLVVVVEHGKGDMSLYGYNQSALVSVGAQVRAGQPIALVGSSGGQGRPSL 409

                         410
                  ....*....|....*....
gi 1336026803 369 YFEIRRNSEAQNPRNWLVR 387
Cdd:PRK11637  410 YFEIRRQGQAVNPQPWLGR 428
Peptidase_M23 pfam01551
Peptidase family M23; Members of this family are zinc metallopeptidases with a range of ...
 288-381 1.95e-36

Peptidase family M23; Members of this family are zinc metallopeptidases with a range of specificities. The peptidase family M23 is included in this family, these are Gly-Gly endopeptidases. Peptidase family M23 are also endopeptidases. This family also includes some bacterial lipoproteins such as Swiss:P33648 for which no proteolytic activity has been demonstrated. This family also includes leukocyte cell-derived chemotaxin 2 (LECT2) proteins. LECT2 is a liver-specific protein which is thought to be linked to hepatocyte growth although the exact function of this protein is unknown.


Pssm-ID: 460250 [Multi-domain]  Cd Length: 96  Bit Score: 128.05  E-value: 1.95e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 288 WKGIVIAARYGEQVKSVYPGTVVFAEYLRGYGLVVLIDHGKGDMTLYGYNQALLKKEGDKVTAGEVIALAGDTGGQDRAS 367
Cdd:pfam01551   3 HKGIDIAAPTGTPVYAAADGVVVFAGWLGGYGNLVIIDHGNGYSTLYAHLSSILVKVGQRVKAGQVIGTVGSTGRSTGPH 82

                          90
                  ....*....|....
gi 1336026803 368 LYFEIRRNSEAQNP 381
Cdd:pfam01551  83 LHFEIRKNGKPVDP 96
NlpD COG0739
Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell ...
 210-385 1.96e-36

Murein DD-endopeptidase MepM and murein hydrolase activator NlpD, contains LysM domain [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440502 [Multi-domain]  Cd Length: 196  Bit Score: 131.25  E-value: 1.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 210 QGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAKAAKRNAIPMDGLAKQAGKLPWPLKGSILHQFGTKQTGQINW- 288
Cdd:COG0739    15 ALLASAAGAAAAVAAAAAAAAAAAALAAAALAAAVSAAASAAAAAAAAAAAIALGSGAWPVKGRITSGFGYRRHPVTGRr 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 289 ---KGIVIAARYGEQVKSVYPGTVVFAEYLRGYGLVVLIDHGKGDMTLYGYNQALLKKEGDKVTAGEVIALAGDTGGQDR 365
Cdd:COG0739    95 rfhKGIDIAAPTGTPVYAAADGTVVFAGWNGGYGNLVIIDHGNGYTTLYAHLSSILVKVGQRVKAGQVIGYVGNTGRSTG 174

                         170       180
                  ....*....|....*....|
gi 1336026803 366 ASLYFEIRRNSEAQNPRNWL 385
Cdd:COG0739   175 PHLHFEVRVNGKPVDPLPFL 194
M23_peptidase cd12797
M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; ...
 289-372 4.33e-28

M23 family metallopeptidase, also known as beta-lytic metallopeptidase, and similar proteins; This model describes the metallopeptidase M23 family, which includes beta-lytic metallopeptidase and lysostaphin. Members of this family are zinc endopeptidases that lyse bacterial cell wall peptidoglycans; they cleave either the N-acylmuramoyl-Ala bond between the cell wall peptidoglycan and the cross-linking peptide (e.g. beta-lytic endopeptidase) or a bond within the cross-linking peptide (e.g. stapholysin, and lysostaphin). Beta-lytic metallopeptidase, formerly known as beta-lytic protease, has a preference for cleavage of Gly-X bonds and favors hydrophobic or apolar residues on either side. It inhibits growth of sensitive organisms and may potentially serve as an antimicrobial agent. Lysostaphin, produced by Staphylococcus genus, cleaves pentaglycine cross-bridges of cell wall peptidoglycan, acting as autolysins to maintain cell wall metabolism or as toxins and weapons against competing strains. Staphylolysin (also known as LasA) is implicated in a range of processes related to Pseudomonas virulence, including stimulating shedding of the ectodomain of cell surface heparan sulphate proteoglycan syndecan-1, and elastin degradation in connective tissue. Its active site is less constricted and contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules, possibly contributing to its activity against a wider range of substrates than those used by related lytic enzymes, consistent with its multiple roles in Pseudomonas virulence. The family includes members that do not appear to have the conserved zinc-binding site and might be lipoproteins lacking proteolytic activity.


Pssm-ID: 410984 [Multi-domain]  Cd Length: 85  Bit Score: 105.37  E-value: 4.33e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 289 KGIVIAARYGEQVKSVYPGTVVFAEYLRGYGLVVLIDHGKGDMTLYGYNQALLKKEGDKVTAGEVIALAGDTGGQDRASL 368
Cdd:cd12797     2 NGIDIAAPEGTPVYAAADGTVVFAGWDGGYGNYVIIDHGNGYYTLYAHLSSILVKVGQRVKKGQVIGTVGNTGRSTGPHL 81


                  ....
gi 1336026803 369 YFEI 372
Cdd:cd12797    82 HFEI 85
SpoIIQ2 COG5821
Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell ...
 260-385 2.78e-24

Stage II sporulation protein SpoIIQ, clostridial version, metallopeptidase M23 family [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444523 [Multi-domain]  Cd Length: 200  Bit Score: 98.95  E-value: 2.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 260 AKQAGKLPWPLKGSILHQFGT-----KQTGQINW-KGIVIAARYGEQVKSVYPGTVVFAEYLRGYGLVVLIDHGKGDMTL 333
Cdd:COG5821    63 ASTSNKFLKPVSGKITREFGEdlvysKTLNEWRThTGIDIAAKEGTPVKAAADGVVVEVGKDPKYGITVVIDHGNGIKTV 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1336026803 334 YGYNQALLK-KEGDKVTAGEVIALAGDTGGQDRA---SLYFEIRRNSEAQNPRNWL 385
Cdd:COG5821   143 YANLDSKIKvKVGQKVKKGQVIGKVGSTALFESSegpHLHFEVLKNGKPVDPMKYL 198
nlpD PRK10871
murein hydrolase activator NlpD;
268-385 7.99e-15

murein hydrolase activator NlpD;


Pssm-ID: 236782 [Multi-domain]  Cd Length: 319  Bit Score: 74.49  E-value: 7.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 268 WPLKGSILHQFGTKQTGQinwKGIVIAARYGEQVKSVYPGTVVFA-EYLRGYGLVVLIDHGKGDMTLYGYNQALLKKEGD 346
Cdd:PRK10871  202 WPTDGKVIENFSASEGGN---KGIDIAGSKGQAIIATADGRVVYAgNALRGYGNLIIIKHNDDYLSAYAHNDTMLVREQQ 278

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1336026803 347 KVTAGEVIALAGDTgGQDRASLYFEIRRNSEAQNPRNWL 385
Cdd:PRK10871  279 EVKAGQKIATMGST-GTSSTRLHFEIRYKGKSVNPLRYL 316
SpoIVFA COG5833
Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, ...
 282-381 3.95e-13

Stage IV sporulation protein SpoIVFA, regulates SpoIVFB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444535 [Multi-domain]  Cd Length: 219  Bit Score: 68.09  E-value: 3.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 282 QTGQINWKGIVIAARYGEQVKSVYPGTVVFAEYLRGYGLVVLIDHGKGDMTLYGYNQALLKKEGDKVTAGEVIALAGDTG 361
Cdd:COG5833   114 ESFQENGKGVDIETPGGANVKAVKEGYVIFAGKDEETGKTVIIQHADGSESWYGNLSSIDVKLYDFVEAGQKIGTVPATE 193

                          90       100
                  ....*....|....*....|
gi 1336026803 362 GQdRASLYFEIRRNSEAQNP 381
Cdd:COG5833   194 GE-EGTFYFAIKKGGKFIDP 212
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 46-250 9.79e-13

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.97  E-value: 9.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  46 ELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQTERLE 125
Cdd:COG1196   261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 126 TLIQtyyvtQRANASASLLQQGVEEDRISQYFQHLAKARAETINELESTKKQLEQSQQQLLNEQSQIESLLKQQSTKHEQ 205
Cdd:COG1196   341 ELEE-----ELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLER 415

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1336026803 206 LAKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAKAAK 250
Cdd:COG1196   416 LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 53-339 3.31e-11

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 64.08  E-value: 3.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  53 EISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQTERLETLIQTYY 132
Cdd:COG3883    17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 133 VTQRANASASLL--QQGVEE--DRISqYFQHLAKARAETINELESTKKQLEQSQQQLLNEQSQIESLLKQQSTKHEQLAK 208
Cdd:COG3883    97 RSGGSVSYLDVLlgSESFSDflDRLS-ALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 209 TQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAKAAKRNAIPMDGLAKQAGKLPWPLKGSILHQFGTKQTGQINW 288
Cdd:COG3883   176 QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAA 255

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1336026803 289 KGIVIAARYGEQVKSVYPGTVVFAEYLRGYGLVVLIDHGKGDMTLYGYNQA 339
Cdd:COG3883   256 GAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGSGGG 306
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 46-253 1.10e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 63.42  E-value: 1.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  46 ELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQTERLE 125
Cdd:COG1196   233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRR 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 126 TLIQtyyvtQRANASASLLQQGVEEDRISQYFQHLAKARAETINELESTKKQLEQSQQQLLNEQSQIESLLKQQSTKHEQ 205
Cdd:COG1196   313 ELEE-----RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEE 387

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1336026803 206 LAKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAKAAKRNA 253
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
PRK11649 PRK11649
putative peptidase; Provisional
 283-381 6.28e-10

putative peptidase; Provisional


Pssm-ID: 236946 [Multi-domain]  Cd Length: 439  Bit Score: 60.45  E-value: 6.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 283 TGQIN-WKGIVIAARYGEQVKSVYPGTVVFAEYLRGYGLVVLIDHGKGDMTLYGYNQALLKKEGDKVTAGEVIALAGDTG 361
Cdd:PRK11649  307 TGRVApHRGVDFAMPVGTPVLAVGDGEVVVAKRSGAAGNYVAIRHGRQYTTRYMHLRKLLVKPGQKVKRGDRIALSGNTG 386

                          90       100
                  ....*....|....*....|
gi 1336026803 362 GQDRASLYFEIRRNSEAQNP 381
Cdd:PRK11649  387 RSTGPHLHYEVWINQQAVNP 406
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 45-274 7.30e-09

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 7.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  45 SELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQ----KKAQ 120
Cdd:COG1196   295 AELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAlleaEAEL 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 121 TERLETLIQTYYVTQRANASASLLQQGVEEDRISQyfQHLAKARAETINELESTKKQLEQSQQQLLNEQSQIESLLKQQS 200
Cdd:COG1196   375 AEAEEELEELAEELLEALRAAAELAAQLEELEEAE--EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336026803 201 TKHEQLAKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAKAAKRNAIPMDGLAKQAGKLPWPLKGSI 274
Cdd:COG1196   453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAV 526
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 46-251 9.94e-09

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.39  E-value: 9.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803   46 ELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQK---KAQTE 122
Cdd:TIGR02169  682 RLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIenvKSELK 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  123 RLETLIQTY------YVTQRANASASLLQQGVEE-----DRISQYFQHLAKARAETINELESTKKQLEQSQQQLLNEQSQ 191
Cdd:TIGR02169  762 ELEARIEELeedlhkLEEALNDLEARLSHSRIPEiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQ 841

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336026803  192 --------------IESLLKQQSTKHEQLAKTQGQRK---KTLGNIKQSISSDKNYLAELQRNETRLKAEIAKAAKR 251
Cdd:TIGR02169  842 ridlkeqiksiekeIENLNGKKEELEEELEELEAALRdleSRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 51-251 2.66e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.83  E-value: 2.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803   51 KNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQTERLETLIQT 130
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQ 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  131 YyvtQRANASASLLQQGVEEDrisqyfQHLAKARAETINELESTKKQLEQSQQQLLNEQSQIESLLKQQSTKHEQLAKTQ 210
Cdd:TIGR02168  318 L---EELEAQLEELESKLDEL------AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKV 388

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1336026803  211 GQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAKAAKR 251
Cdd:TIGR02168  389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 45-248 7.33e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 7.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803   45 SELQGVKNEISRqqkalsnQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQTERL 124
Cdd:TIGR02168  288 KELYALANEISR-------LEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  125 ETLIQTYyvtQRANASASLLQQGVEEDRiSQYFQHLAKARAETiNELESTKKQLEQSQQQLLNEQSQIESLLKQQSTKhe 204
Cdd:TIGR02168  361 EELEAEL---EELESRLEELEEQLETLR-SKVAQLELQIASLN-NEIERLEARLERLEDRRERLQQEIEELLKKLEEA-- 433

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1336026803  205 QLAKTQGQrkktLGNIKQSISSDKNYLAELQRNETRLKAEIAKA 248
Cdd:TIGR02168  434 ELKELQAE----LEELEEELEELQEELERLEEALEELREELEEA 473
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 45-253 5.86e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 5.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803   45 SELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQTERL 124
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  125 ETLiqTYYVTQRANASASLLQQGVEEDRISQYFQHLAKARAETINELESTKKQLEQSQQQLLNEQSQIESLLKQQSTKHE 204
Cdd:TIGR02168  340 AEL--EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRE 417

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1336026803  205 QLAKTQGQRKKTLgnikqsissDKNYLAELQRNETRLKAEIAKAAKRNA 253
Cdd:TIGR02168  418 RLQQEIEELLKKL---------EEAELKELQAELEELEEELEELQEELE 457
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
58-173 3.14e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.53  E-value: 3.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803   58 QKALSNQEKQLDELQKS---LRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQTERLETLIQTYYVT 134
Cdd:COG4913    667 EREIAELEAELERLDASsddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1336026803  135 QRANASASLLQQGVE--EDRISQYFQHLAKARAETINELES 173
Cdd:COG4913    747 LRALLEERFAAALGDavERELRENLEERIDALRARLNRAEE 787
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 46-248 6.09e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 48.53  E-value: 6.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803   46 ELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQL--------ENEIKQTKQALATAKANVGQLQRKMDELEGQK 117
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnkkikdlgEEEQLRVKEKIGELEAEIASLERSIAEKEREL 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  118 KAQTERLETLIQTYYVTQR--ANASASLLQQGVEEDRISQYFQHLAKARAETINELESTKKQLEQSQQQLLNEQSQIESL 195
Cdd:TIGR02169  318 EDAEERLAKLEAEIDKLLAeiEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1336026803  196 ---LKQQSTKHEQLAKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAKA 248
Cdd:TIGR02169  398 kreINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 52-251 6.18e-06

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 6.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  52 NEISRQQKALSNQ----------EKQLDELQKSLRSQEtsIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQT 121
Cdd:COG1196   196 GELERQLEPLERQaekaeryrelKEELKELEAELLLLK--LRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 122 ERLETLIQTYYVTQRANASASLLQQGVEEDRISQyfQHLAKARAETINELESTKKQLEQSQQQLLNEQSQIESLLKQQST 201
Cdd:COG1196   274 LELEELELELEEAQAEEYELLAELARLEQDIARL--EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1336026803 202 KHEQLAKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAKAAKR 251
Cdd:COG1196   352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 45-252 1.25e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 1.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803   45 SELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQTERL 124
Cdd:TIGR02168  705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEI 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  125 ETLIQTYYVTQRANASASLLQQGVEED--RISQYFQHLAKARAETINELESTKKQLEQSQQQLLNEQSQIESLLKQQSTK 202
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAEltLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1336026803  203 HEQLAKTQGQRKKtLGNIKQSISSdknYLAELQRNETRLKAEIAKAAKRN 252
Cdd:TIGR02168  865 EELIEELESELEA-LLNERASLEE---ALALLRSELEELSEELRELESKR 910
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-246 1.87e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.97  E-value: 1.87e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803   46 ELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQTERLE 125
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  126 TLIQTYYVT--QRANASASLLQQGVEEDRISQYFQHLAKARA-----------------ETINELESTKKQLEQSQQQLL 186
Cdd:TIGR02168  842 DLEEQIEELseDIESLAAEIEELEELIEELESELEALLNERAsleealallrseleelsEELRELESKRSELRRELEELR 921

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1336026803  187 NEQSQIEslLKQQSTK---HEQLAKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIA 246
Cdd:TIGR02168  922 EKLAQLE--LRLEGLEvriDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIK 982
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 44-172 2.26e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.30  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  44 PSELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVgQLQRKMDELEGQKKAQTER 123
Cdd:COG1579    30 PAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNK-EYEALQKEIESLKRRISDL 108

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1336026803 124 LETLIQTYYvtQRANASASLLQQGVEEDRISQYFQHLAKARAETINELE 172
Cdd:COG1579   109 EDEILELME--RIEELEEELAELEAELAELEAELEEKKAELDEELAELE 155
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
46-250 2.46e-05

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.45  E-value: 2.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803   46 ELQGVKNEISRQQKALS-----NQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQ 120
Cdd:COG4913    263 RYAAARERLAELEYLRAalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQ 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  121 TERletliqtyyvtQRANASASLLQQGVEEDRISQYFQHLAKARAETINELESTKKQLEQSQQQLLNEQSQIESLLKQQS 200
Cdd:COG4913    343 LER-----------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE 411

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1336026803  201 TKHEQLAKTQGQRKKTLGNIKQSISsdkNYLAELQrnetRLKAEIAKAAK 250
Cdd:COG4913    412 AALRDLRRELRELEAEIASLERRKS---NIPARLL----ALRDALAEALG 454
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 61-261 3.18e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 44.92  E-value: 3.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  61 LSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQTERLETLIQtyyvtqranas 140
Cdd:COG1579    12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEE----------- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 141 aslLQQGVEEDRISQYFQHlakaraetinELESTKKQLEQSqqqllnEQSQIEsLLKQQSTKHEQLAKTQGQRKKTLGNI 220
Cdd:COG1579    81 ---QLGNVRNNKEYEALQK----------EIESLKRRISDL------EDEILE-LMERIEELEEELAELEAELAELEAEL 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1336026803 221 KQSISSDKNYLAELQRNETRLKAEIAKAAKRnaIPMDGLAK 261
Cdd:COG1579   141 EEKKAELDEELAELEAELEELEAEREELAAK--IPPELLAL 179
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 40-247 5.05e-05

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 45.40  E-value: 5.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  40 NAASPSELQGVKNEISRQQKalsnQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKA 119
Cdd:pfam05667 313 PAATSSPPTKVETEEELQQQ----REEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQYKV 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 120 QTERLETLIQtyyvtqrANASASLLQQGVEEDriSQYFQHLA----KARAETINELESTKKQLEQSQQQLLNEQSQIESl 195
Cdd:pfam05667 389 KKKTLDLLPD-------AEENIAKLQALVDAS--AQRLVELAgqweKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKE- 458

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1336026803 196 LKQQSTKHEQLAKTQGQRKKTLGNIKQSISSDKNYLAELQR------NETRLKAEIAK 247
Cdd:pfam05667 459 LREKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRSAYTRRileivkNIKKQKEEITK 516
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 47-250 5.93e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.43  E-value: 5.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803   47 LQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALAtakanvgQLQRKMDELEGQKKAQTERLET 126
Cdd:TIGR02168  672 ILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE-------ELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  127 LIQTYYVTQRANASAsllqqgveEDRISQYFQHLAKARAETInELESTKKQLEQSQQQLLNEQSQIESLLKQQSTKHEQL 206
Cdd:TIGR02168  745 LEERIAQLSKELTEL--------EAEIEELEERLEEAEEELA-EAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1336026803  207 AKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAKAAK 250
Cdd:TIGR02168  816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
PRK09039 PRK09039
peptidoglycan -binding protein;
53-152 1.13e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 43.80  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  53 EISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQTERLETLIQTY- 131
Cdd:PRK09039   47 EISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELd 126

                          90       100
                  ....*....|....*....|....
gi 1336026803 132 ---YVTQRANASASLLQQGVEEDR 152
Cdd:PRK09039  127 sekQVSARALAQVELLNQQIAALR 150
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
45-254 2.27e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 2.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803   45 SELQGVKNEISRQQKALSNQEKQLDELQKSLRS---------QETSIAQLENEIKQTKQALATAKAN---VGQLQRKMDE 112
Cdd:COG4913    617 AELAELEEELAEAEERLEALEAELDALQERREAlqrlaeyswDEIDVASAEREIAELEAELERLDASsddLAALEEQLEE 696

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  113 LEGQKKAQTERLETLIQTYYVTQRANASASLLQQ-------GVEEDRISQYFQHLAKARAETINElestkkqlEQSQQQL 185
Cdd:COG4913    697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDelqdrleAAEDLARLELRALLEERFAAALGD--------AVERELR 768

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1336026803  186 LNEQSQIESLLKQQSTKHEQLAKTQGQRKKTLGNIKQSISSDK----NYLAELQRNET----RLKAEIAKAAKRNAI 254
Cdd:COG4913    769 ENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLeslpEYLALLDRLEEdglpEYEERFKELLNENSI 845
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
50-251 4.54e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 4.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  50 VKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLeneikQTKQALATAKANVGQLQRKMDELEGQK-KAQTERLETLI 128
Cdd:COG3206   166 LELRREEARKALEFLEEQLPELRKELEEAEAALEEF-----RQKNGLVDLSEEAKLLLQQLSELESQLaEARAELAEAEA 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 129 QTYYVTQRANASASLLQQGVEEDRISQYFQHLAKARAEtINELESTkkqleqsqqqLLNEQSQIESLLKQQSTKHEQLAK 208
Cdd:COG3206   241 RLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAE-LAELSAR----------YTPNHPDVIALRAQIAALRAQLQQ 309

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1336026803 209 tqgQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAKAAKR 251
Cdd:COG3206   310 ---EAQRILASLEAELEALQAREASLQAQLAQLEARLAELPEL 349
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
45-254 5.00e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  45 SELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQTERL 124
Cdd:COG4372    59 EELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQI 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 125 ETLIQTYYVTQR----ANASASLLQQGVEEDRISQYFQHLAKARAETINELESTKKQLEQSQQQLLNEQSQIESLLKQQS 200
Cdd:COG4372   139 AELQSEIAEREEelkeLEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAE 218

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1336026803 201 TKHEQLAKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAKAAKRNAI 254
Cdd:COG4372   219 ELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
70-251 6.00e-04

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 6.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  70 ELQKSLRSQETS--IAQLENEIKQTKQALATAKANVGQLQRKMD--ELEGQKKAQTERLETLiqtyyVTQRANASASLLQ 145
Cdd:COG3206   163 EQNLELRREEARkaLEFLEEQLPELRKELEEAEAALEEFRQKNGlvDLSEEAKLLLQQLSEL-----ESQLAEARAELAE 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 146 QgveEDRISQYFQHLAKARAETINELESTkkQLEQSQQQLLNEQSQIESLLKQQSTKHEQLAKTQGQRKKTLGNIKQSI- 224
Cdd:COG3206   238 A---EARLAALRAQLGSGPDALPELLQSP--VIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAq 312

                         170       180       190
                  ....*....|....*....|....*....|
gi 1336026803 225 ---SSDKNYLAELQRNETRLKAEIAKAAKR 251
Cdd:COG3206   313 rilASLEAELEALQAREASLQAQLAQLEAR 342
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 40-130 6.64e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 6.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  40 NAASPSELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKAnvgQLQRKMDELEGQKKA 119
Cdd:COG1579    84 NVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA---ELDEELAELEAELEE 160

                          90
                  ....*....|.
gi 1336026803 120 QTERLETLIQT 130
Cdd:COG1579   161 LEAEREELAAK 171
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
53-208 6.94e-04

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 6.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  53 EISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKA--NVGQLQRKMDELEGQKKAQTERLETLIQT 130
Cdd:COG4717    75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLEELEER 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336026803 131 YyvTQRANASASLLQQgveEDRISQYFQHLAKARAETINELESTKKQLEQSQQQLLNEQSQIESLLKQQSTKHEQLAK 208
Cdd:COG4717   155 L--EELRELEEELEEL---EAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 61-243 8.48e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.42  E-value: 8.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  61 LSNQ-EKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQTERLETLIQTYYVTQRANA 139
Cdd:pfam07888  32 LQNRlEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 140 SAS------LLQQGVEEDRI---SQYFQHLAKARAETINELESTKKQLEQSQQQLLNEQSQIESL----------LKQQS 200
Cdd:pfam07888 112 ELSeekdalLAQRAAHEARIrelEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLqaklqqteeeLRSLS 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1336026803 201 TKHEQLAKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKA 243
Cdd:pfam07888 192 KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEA 234
PRK10920 PRK10920
putative uroporphyrinogen III C-methyltransferase; Provisional
 51-114 1.39e-03

putative uroporphyrinogen III C-methyltransferase; Provisional


Pssm-ID: 236795  Cd Length: 390  Bit Score: 40.46  E-value: 1.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1336026803  51 KNEISRQQKALSNQEKQLDELQKSlrsQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELE 114
Cdd:PRK10920   59 KQQAQNQTATNDALANQLTALQKA---QESQKQELEGILKQQAKALDQANRQQAALAKQLDELQ 119
Surf_Exclu_PgrA TIGR04320
SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface ...
 41-126 1.77e-03

SEC10/PgrA surface exclusion domain; This model describes a conserved domain found in surface proteins of a number of Firmutes. Many members have LPXTG C-terminal anchoring motifs and a substantial number have the KxYKxGKxW putative sorting signal at the N-terminus. The tetracycline resistance plasmid pCF10 in Enterococcus faecalis promotes conjugal plasmid transfer in response to sex pheromones, but PgrA/Sec10 encoded by that plasmid, a member of this family, specifically inhibits the ability of cells to receive homologous plasmids. The phenomenon is called surface exclusion.


Pssm-ID: 275124 [Multi-domain]  Cd Length: 356  Bit Score: 40.10  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  41 AASPSELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQL-QRKMDELEGQKKA 119
Cdd:TIGR04320 250 PNPPNSLAALQAKLATAQADLAAAQTALNTAQAALTSAQTAYAAAQAALATAQKELANAQAQALQTaQNNLATAQAALAN 329


                  ....*..
gi 1336026803 120 QTERLET 126
Cdd:TIGR04320 330 AEARLAK 336
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 46-251 2.00e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.48  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  46 ELQGVKNEISrqqKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQTERLE 125
Cdd:pfam05483 433 ELKGKEQELI---FLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEAS 509

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 126 TLiqtyyVTQRANASASLLQQGVEEDRISQYFQHLAKARAETINELESTKKQLEQSQQQLLNEQSQIESLLKQQSTKHEQ 205
Cdd:pfam05483 510 DM-----TLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLK 584

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1336026803 206 LAKTQGQRKKTLGNIKQSISSDKNYLAELQRNETRLKAEIAKAAKR 251
Cdd:pfam05483 585 KEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQ 630
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
42-166 2.25e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803   42 ASPSELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAkanvgqlqrkmdeLEGQKKAQT 121
Cdd:COG4913    682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAA-------------EDLARLELR 748

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1336026803  122 ERLETLIQTYYVTQRANASASLLQQGVE--EDRISQYFQHLAKARAE 166
Cdd:COG4913    749 ALLEERFAAALGDAVERELRENLEERIDalRARLNRAEEELERAMRA 795
RNase_Y_N pfam12072
RNase Y N-terminal region;
45-125 2.67e-03

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 38.71  E-value: 2.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  45 SELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQalatakanvgQLQRKMDELEGQKKAQTERL 124
Cdd:pfam12072  71 RELKERRNELQRQERRLLQKEETLDRKDESLEKKEESLEKKEKELEAQQQ----------QLEEKEEELEELIEEQRQEL 140


                  .
gi 1336026803 125 E 125
Cdd:pfam12072 141 E 141
PRK06148 PRK06148
hypothetical protein; Provisional
 298-362 3.35e-03

hypothetical protein; Provisional


Pssm-ID: 180426 [Multi-domain]  Cd Length: 1013  Bit Score: 39.62  E-value: 3.35e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1336026803  298 GEQVKSVYPGTVVFAEYLR---GYGLVVLIDH--GKGD--MTLYGY--NQALLK-KEGDKVTAGEVIALAGDT---GG 362
Cdd:PRK06148   451 GTPVYAPLAGTVRSVEIEAvplGYGGLVALEHetPGGDpfYTLYGHlaHEAVSRlKPGDRLAAGELFGAMGDAhenGG 528
46 PHA02562
endonuclease subunit; Provisional
 44-129 3.43e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 39.61  E-value: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  44 PSELQGVKNEISRQQKALSNQEKQLDELQK---SLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDELEGQKKAQ 120
Cdd:PHA02562  298 PDRITKIKDKLKELQHSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDN 377


                  ....*....
gi 1336026803 121 TERLETLIQ 129
Cdd:PHA02562  378 AEELAKLQD 386
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
45-127 4.35e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  45 SELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQ--------TKQALATAKANVGQLQRKMDELEGQ 116
Cdd:COG4717   135 EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEElleqlslaTEEELQDLAEELEELQQRLAELEEE 214

                          90
                  ....*....|.
gi 1336026803 117 KKAQTERLETL 127
Cdd:COG4717   215 LEEAQEELEEL 225
PRK01156 PRK01156
chromosome segregation protein; Provisional
 42-262 5.07e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 39.11  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  42 ASPSELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATAKANVGQLQRKMDEL----EGQK 117
Cdd:PRK01156  180 AEISNIDYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKnryeSEIK 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803 118 KAQTERLETLIQTYYVTQRANASASLLQQGV--EEDRISQYFQHLAK--ARAETINELESTKKQLEQSQQQLLNEQSQIE 193
Cdd:PRK01156  260 TAESDLSMELEKNNYYKELEERHMKIINDPVykNRNYINDYFKYKNDieNKKQILSNIDAEINKYHAIIKKLSVLQKDYN 339

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1336026803 194 SLLKQQSTKHE---QLAKTQGQRKKTLGNIKqSISSDKNYLAELQRNETRLKAEIAKAAKRNAIPMDGLAKQ 262
Cdd:PRK01156  340 DYIKKKSRYDDlnnQILELEGYEMDYNSYLK-SIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKE 410
SARS-CoV-like_Spike_SD1-2_S1-S2_S2 cd22378
SD-1 and SD-2 subdomains, the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) ...
 51-155 5.78e-03

SD-1 and SD-2 subdomains, the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) glycoprotein from SARS-CoV-2 (COVID-19) and related betacoronaviruses in the B lineage; This group contains the SD-1 and SD-2 subdomains of the S1 subunit C-terminal domain (C-domain), the S1/S2 cleavage region, and the S2 fusion subunit of the spike (S) glycoprotein from betacoronaviruses in the sarbecovirus subgenus (B lineage), including highly pathogenic human CoVs such as Severe acute respiratory syndrome (SARS) coronavirus (SARS-CoV), and SARS-CoV-2 (also known as a 2019 novel coronavirus or 2019-nCoV). The CoV S protein is an envelope glycoprotein that plays a very important role in viral attachment, fusion, and entry into host cells, and serves as a major target for the development of neutralizing antibodies, inhibitors of viral entry, and vaccines. It is synthesized as a precursor protein that is cleaved into an N-terminal S1 subunit (~700 amino acids) and a C-terminal S2 subunit (~600 amino acids) that mediates attachment and membrane fusion, respectively. Three S1/S2 heterodimers assemble to form a trimer spike protruding from the viral envelope. The S1 subunit contains a receptor-binding domain (RBD), while the S2 subunit contains the coronavirus fusion machinery and is primarily alpha-helical. S1 contains two structurally independent domains, the N-terminal domain (NTD) and the C-domain. The S1 C-domain also contains two subdomains (SD-1 and SD-2), which connect the S1 and S2 subunits. Depending on the virus, either the NTD or the C-domain can serve as the receptor-binding domain (RBD). While the RBD of mouse hepatitis virus (MHV) is located at the NTD, most CoVs, including SARS-CoV-2, SARS-CoV and MERS-CoV use the C-domain to bind their receptors. The S2 subunit comprises the fusion peptide (FP), a second proteolytic site (S2'), followed by an internal fusion peptide (IFP) and two heptad-repeat domains (HR1 and HR2) preceding the transmembrane domain (TM). After binding of the S1 subunit RBD on the virion to its receptor on the target cell, the HR1 and HR2 domains interact with each other to form a six-helix bundle (6-HB) fusion core, bringing viral and cellular membranes into close proximity for fusion and infection. In order to catalyze the membrane fusion reaction, CoV S needs to be primed through cleavage at the S1/S2 and S2' sites. Notably, SARS-CoV-2 has a functional polybasic (furin) cleavage site through the insertion of PRRAR*SV (* indicates the cleavage site) at the S1/S2 interface, which is absent in SARS-CoV and other SARS-related coronaviruses. The region modeled in this cd (SD-1 and SD-2, the S1/S2 cleavage region, and the S2 fusion subunit) plays an essential role in viral entry by initiating fusion of the viral and cellular membranes.


Pssm-ID: 411965 [Multi-domain]  Cd Length: 662  Bit Score: 38.82  E-value: 5.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  51 KNEISRQQKALSNQ-EKQLDELQKSLRSQETSIAQLENEIKQTKQALAT----AKANVGQLQ-------RKMDELEGQKK 118
Cdd:cd22378   367 QNVLYENQKQIANQfNKAISQIQESLTTTSTALGKLQDVVNQNAQALNTlvkqLSSNFGAISsvlndilSRLDKVEAEVQ 446

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1336026803 119 AQ---TERLETLiQTyYVTQ---RA---NASASLLQQGVEEDRISQ 155
Cdd:cd22378   447 IDrliTGRLQSL-QT-YVTQqliRAaeiRASANLAATKMSECVLGQ 490
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
38-127 6.19e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 38.69  E-value: 6.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  38 PTNAASPSELQGVKNEISRQQKALSNQEKQLDELQKSLRSQETSIAQLENEIKQTKQALATA----------KANVGQLQ 107
Cdd:COG2433   399 REKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREirkdreisrlDREIERLE 478

                          90       100
                  ....*....|....*....|
gi 1336026803 108 RKMDELEGQKKAQTERLETL 127
Cdd:COG2433   479 RELEEERERIEELKRKLERL 498
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
82-251 6.88e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 6.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803   82 IAQLENEIKQTKQALATAKANVGQLQRKMDELEgQKKAQTERLETLIQTYYVTQRANASASLLQQGVEE-----DRISQY 156
Cdd:COG4913    612 LAALEAELAELEEELAEAEERLEALEAELDALQ-ERREALQRLAEYSWDEIDVASAEREIAELEAELERldassDDLAAL 690

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1336026803  157 FQHLAKARAEtINELESTKKQLEQSQQQLLNEQSQIESLLKQQSTKHEQLAKTQGQRKKTLGNIKQSISSDKNYLAELQR 236
Cdd:COG4913    691 EEQLEELEAE-LEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769

                          170
                   ....*....|....*
gi 1336026803  237 NetrLKAEIAKAAKR 251
Cdd:COG4913    770 N---LEERIDALRAR 781
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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