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Conserved domains on  [gi|329299035|ref|NP_001192274|]
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SUN domain-containing protein 2 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
595-729 1.60e-59

Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm.


:

Pssm-ID: 400199  Cd Length: 130  Bit Score: 196.74  E-value: 1.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  595 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 674
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 329299035  675 LLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 729
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
495-552 2.85e-23

SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, and Syne/Nesprin Homology) and SUN (Sad1 and UNC-84) proteins from the inner and outer nuclear membranes (INM and ONM, respectively). the formation of LINC complexes by KASH and SUN proteins at the nuclear envelope (NE) establishes the physical linkage between the cytoskeleton and nuclear lamina, which is instrumental for the mechanical force transmission from the cytoplasm to the nuclear interior, and is essential for cellular processes such as nuclear positioning and migration, centrosome-nucleus anchorage, and chromosome dynamics. This entry represents an HTH domain found in SUN2 that forms a three-helix bundle to lock the SUN domain in an inactive conformation acting as an inhibitory component.


:

Pssm-ID: 436594 [Multi-domain]  Cd Length: 58  Bit Score: 93.17  E-value: 2.85e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 329299035  495 MHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQR 552
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
414-468 2.10e-18

coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN domain-containing protein 2 (SUN2), also called protein unc-84 homolog B, Rab5-interacting protein (Rab5IP), or Sad1/unc-84 protein-like 2, is a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex which is involved in the connection between the nuclear lamina and the cytoskeleton. Besides the core SUN domain, SUN2 contains two coiled-coil domains (CC1 and CC2), which act as the intrinsic dynamic regulators for controlling the activity of the SUN domain. This model corresponds to CC1 that functions as an activation segment to release CC2-mediated inhibition of the SUN domain.


:

Pssm-ID: 410604 [Multi-domain]  Cd Length: 55  Bit Score: 79.28  E-value: 2.10e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 329299035 414 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVE 468
Cdd:cd21438    1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
252-472 9.53e-08

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 9.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  252 LQTLQPAVVSWWAAKESRKQPEVWES-RDASQHFQAEQRVlsrvHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAG 330
Cdd:COG4913   251 IELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELD 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  331 HGGGSSLSHE-DALSLLEGLVSRREATLKEdlRRDTVAHIQEELATLRAEHHQDSEDLfkkiVQASQESEARVQQLKTEW 409
Cdd:COG4913   327 ELEAQIRGNGgDRLEQLEREIERLERELEE--RERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEEL 400
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 329299035  410 KSMTQEAFQesSVKELGRLEAQLASLRQELAALTLKQNSvadevglLPQKIQAARADVESQFP 472
Cdd:COG4913   401 EALEEALAE--AEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDALAEALG 454
 
Name Accession Description Interval E-value
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
595-729 1.60e-59

Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm.


Pssm-ID: 400199  Cd Length: 130  Bit Score: 196.74  E-value: 1.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  595 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 674
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 329299035  675 LLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 729
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
495-552 2.85e-23

SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, and Syne/Nesprin Homology) and SUN (Sad1 and UNC-84) proteins from the inner and outer nuclear membranes (INM and ONM, respectively). the formation of LINC complexes by KASH and SUN proteins at the nuclear envelope (NE) establishes the physical linkage between the cytoskeleton and nuclear lamina, which is instrumental for the mechanical force transmission from the cytoplasm to the nuclear interior, and is essential for cellular processes such as nuclear positioning and migration, centrosome-nucleus anchorage, and chromosome dynamics. This entry represents an HTH domain found in SUN2 that forms a three-helix bundle to lock the SUN domain in an inactive conformation acting as an inhibitory component.


Pssm-ID: 436594 [Multi-domain]  Cd Length: 58  Bit Score: 93.17  E-value: 2.85e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 329299035  495 MHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQR 552
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
414-468 2.10e-18

coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN domain-containing protein 2 (SUN2), also called protein unc-84 homolog B, Rab5-interacting protein (Rab5IP), or Sad1/unc-84 protein-like 2, is a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex which is involved in the connection between the nuclear lamina and the cytoskeleton. Besides the core SUN domain, SUN2 contains two coiled-coil domains (CC1 and CC2), which act as the intrinsic dynamic regulators for controlling the activity of the SUN domain. This model corresponds to CC1 that functions as an activation segment to release CC2-mediated inhibition of the SUN domain.


Pssm-ID: 410604 [Multi-domain]  Cd Length: 55  Bit Score: 79.28  E-value: 2.10e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 329299035 414 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVE 468
Cdd:cd21438    1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
252-472 9.53e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 9.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  252 LQTLQPAVVSWWAAKESRKQPEVWES-RDASQHFQAEQRVlsrvHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAG 330
Cdd:COG4913   251 IELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELD 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  331 HGGGSSLSHE-DALSLLEGLVSRREATLKEdlRRDTVAHIQEELATLRAEHHQDSEDLfkkiVQASQESEARVQQLKTEW 409
Cdd:COG4913   327 ELEAQIRGNGgDRLEQLEREIERLERELEE--RERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEEL 400
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 329299035  410 KSMTQEAFQesSVKELGRLEAQLASLRQELAALTLKQNSvadevglLPQKIQAARADVESQFP 472
Cdd:COG4913   401 EALEEALAE--AEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDALAEALG 454
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
291-587 5.09e-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: 5.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035   291 LSRV----HSLERRLEALAAdfssnwQKE-AIRLERL--ELRQGAAGHGGGSSLSHEDALSLLEglVSRREATLKEDLRR 363
Cdd:TIGR02168  188 LDRLedilNELERQLKSLER------QAEkAERYKELkaELRELELALLVLRLEELREELEELQ--EELKEAEEELEELT 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035   364 DTVAHIQEELATLRAEHHQDSEDLfkkivqasQESEARVQQLKTEWKSMTQEAfqESSVKELGRLEAQLASLRQELAALT 443
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEI--------EELQKELYALANEISRLEQQK--QILRERLANLERQLEELEAQLEELE 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035   444 LKQNSVADEVGLLPQKIQAARADVESQfpdwirqfllgdrgarsgLLQRDEMHAQLQELENKILTKMAEMQGKSAREAAA 523
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESL------------------EAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 329299035   524 SLgQILQKEGIVGVTEEQVHRIvKQALQRYSEdRIGMVDYALESGGASVISTRCSETYETKTAL 587
Cdd:TIGR02168  392 EL-QIASLNNEIERLEARLERL-EDRRERLQQ-EIEELLKKLEEAELKELQAELEELEEELEEL 452
PRK11281 PRK11281
mechanosensitive channel MscK;
365-517 2.21e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.90  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  365 TVAHIQEELATL--RAEHHQDSEDLFKKIVQASQ---ESEARVQQLKTEWKSMTQEAFQESSVKELgrlEAQLASLRQEL 439
Cdd:PRK11281   61 VQQDLEQTLALLdkIDRQKEETEQLKQQLAQAPAklrQAQAELEALKDDNDEETRETLSTLSLRQL---ESRLAQTLDQL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  440 AALtlkQNSVADEVGLL------PQKIQAARADvESQFPDWIRQFLLGDRGARSGLL--QRDEMHAQLQELENKILTKMA 511
Cdd:PRK11281  138 QNA---QNDLAEYNSQLvslqtqPERAQAALYA-NSQRLQQIRNLLKGGKVGGKALRpsQRVLLQAEQALLNAQNDLQRK 213

                  ....*.
gi 329299035  512 EMQGKS 517
Cdd:PRK11281  214 SLEGNT 219
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
399-546 3.46e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 399 EARVQQLKTEWKSMTQEAfQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVgllpQKIQAARAdvesqfpdwirqf 478
Cdd:COG0542  417 ERRLEQLEIEKEALKKEQ-DEASFERLAELRDELAELEEELEALKARWEAEKELI----EEIQELKE------------- 478
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 329299035 479 llgdrgarsgllQRDEMHAQLQELENKIltkmaemqgKSAREAAASLGQILQKEgivgVTEEQVHRIV 546
Cdd:COG0542  479 ------------ELEQRYGKIPELEKEL---------AELEEELAELAPLLREE----VTEEDIAEVV 521
 
Name Accession Description Interval E-value
Sad1_UNC pfam07738
Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that ...
595-729 1.60e-59

Sad1 / UNC-like C-terminal; The C. elegans UNC-84 protein is a nuclear envelope protein that is involved in nuclear anchoring and migration during development. The S. pombe Sad1 protein localizes at the spindle pole body. UNC-84 and and Sad1 share a common C-terminal region, that is often termed the SUN (Sad1 and UNC) domain. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm.


Pssm-ID: 400199  Cd Length: 130  Bit Score: 196.74  E-value: 1.60e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  595 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 674
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 329299035  675 LLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 729
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
495-552 2.85e-23

SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, and Syne/Nesprin Homology) and SUN (Sad1 and UNC-84) proteins from the inner and outer nuclear membranes (INM and ONM, respectively). the formation of LINC complexes by KASH and SUN proteins at the nuclear envelope (NE) establishes the physical linkage between the cytoskeleton and nuclear lamina, which is instrumental for the mechanical force transmission from the cytoplasm to the nuclear interior, and is essential for cellular processes such as nuclear positioning and migration, centrosome-nucleus anchorage, and chromosome dynamics. This entry represents an HTH domain found in SUN2 that forms a three-helix bundle to lock the SUN domain in an inactive conformation acting as an inhibitory component.


Pssm-ID: 436594 [Multi-domain]  Cd Length: 58  Bit Score: 93.17  E-value: 2.85e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 329299035  495 MHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQR 552
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
414-468 2.10e-18

coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN domain-containing protein 2 (SUN2), also called protein unc-84 homolog B, Rab5-interacting protein (Rab5IP), or Sad1/unc-84 protein-like 2, is a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex which is involved in the connection between the nuclear lamina and the cytoskeleton. Besides the core SUN domain, SUN2 contains two coiled-coil domains (CC1 and CC2), which act as the intrinsic dynamic regulators for controlling the activity of the SUN domain. This model corresponds to CC1 that functions as an activation segment to release CC2-mediated inhibition of the SUN domain.


Pssm-ID: 410604 [Multi-domain]  Cd Length: 55  Bit Score: 79.28  E-value: 2.10e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 329299035 414 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVE 468
Cdd:cd21438    1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SUN_cc1 cd21435
coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 ...
414-468 2.47e-18

coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 and SUN2) are components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex which is involved in the connection between the nuclear lamina and the cytoskeleton. Besides the core SUN domain, SUN proteins contain two coiled-coil domains (CC1 and CC2), which act as intrinsic dynamic regulators controlling the activity of the SUN domain. The model corresponds to CC1 that functions as an activation segment to release CC2-mediated inhibition of the SUN domain.


Pssm-ID: 410603 [Multi-domain]  Cd Length: 55  Bit Score: 78.99  E-value: 2.47e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 329299035 414 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVE 468
Cdd:cd21435    1 QEAFQESSVKELGRLEAQLASLRQELAALTLKQEAIQKELEQTKQKTISAVGEQL 55
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
252-472 9.53e-08

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.69  E-value: 9.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  252 LQTLQPAVVSWWAAKESRKQPEVWES-RDASQHFQAEQRVlsrvHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAG 330
Cdd:COG4913   251 IELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELD 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  331 HGGGSSLSHE-DALSLLEGLVSRREATLKEdlRRDTVAHIQEELATLRAEHHQDSEDLfkkiVQASQESEARVQQLKTEW 409
Cdd:COG4913   327 ELEAQIRGNGgDRLEQLEREIERLERELEE--RERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEEL 400
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 329299035  410 KSMTQEAFQesSVKELGRLEAQLASLRQELAALTLKQNSvadevglLPQKIQAARADVESQFP 472
Cdd:COG4913   401 EALEEALAE--AEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDALAEALG 454
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
282-554 3.17e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.71  E-value: 3.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 282 QHFQAEQRVL-SRVHSLERRLEALAADFSS-NWQKEAIRLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRRE----- 354
Cdd:COG1196  235 RELEAELEELeAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrel 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 355 ----ATLKEDLRRDT--VAHIQEELATLRAEH------HQDSEDLFKKIVQASQESEARVQQLKTEWKSMTQEAFQEssV 422
Cdd:COG1196  315 eerlEELEEELAELEeeLEELEEELEELEEELeeaeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA--L 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 423 KELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVESqfpdwirqfllgdrgARSGLLQRDEMHAQLQEL 502
Cdd:COG1196  393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE---------------EEEALEEAAEEEAELEEE 457
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 329299035 503 ENKILTKMAEmQGKSAREAAASLGQILQKEGivgvTEEQVHRIVKQALQRYS 554
Cdd:COG1196  458 EEALLELLAE-LLEEAALLEAALAELLEELA----EAAARLLLLLEAEADYE 504
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
357-555 4.83e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 50.02  E-value: 4.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 357 LKEDLRRDTVAHIQEELATLRAEhhqdsedlfkkivqaSQESEARVQQLKTEWKSMTQEAFQESSVKELGRLEAQLASLR 436
Cdd:COG3206  168 LRREEARKALEFLEEQLPELRKE---------------LEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 437 QELAALTLKQNSVADEVGLLPQKIQAARADVESQFpdwIRQFLLGDRGARSGLLQR-DEMHAQLQELENKIltkmAEMQG 515
Cdd:COG3206  233 AELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSARyTPNHPDVIALRAQI----AALRA 305
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 329299035 516 KSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQRYSE 555
Cdd:COG3206  306 QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
275-507 9.33e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 9.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  275 WESRDASQHFQAEQRVL-SRVHSLERRLEALAAdfssnwqkeaiRLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRR 353
Cdd:COG4913   606 FDNRAKLAALEAELAELeEELAEAEERLEALEA-----------ELDALQERREALQRLAEYSWDEIDVASAEREIAELE 674
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  354 EAtlKEDLRR--DTVAHIQEELATLRAEHhQDSEDLFKKIVQASQESEARVQQLKTEWKS---MTQEAFQESSVKELGRL 428
Cdd:COG4913   675 AE--LERLDAssDDLAALEEQLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDElqdRLEAAEDLARLELRALL 751
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 329299035  429 EAQLASLRQELAALTLKQNsVADEVGLLPQKIQAARADVESQFPDWIRQFLLGDRGARSGLLQRDEMHAQLQELENKIL 507
Cdd:COG4913   752 EERFAAALGDAVERELREN-LEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGL 829
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
291-587 5.09e-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: 5.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035   291 LSRV----HSLERRLEALAAdfssnwQKE-AIRLERL--ELRQGAAGHGGGSSLSHEDALSLLEglVSRREATLKEDLRR 363
Cdd:TIGR02168  188 LDRLedilNELERQLKSLER------QAEkAERYKELkaELRELELALLVLRLEELREELEELQ--EELKEAEEELEELT 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035   364 DTVAHIQEELATLRAEHHQDSEDLfkkivqasQESEARVQQLKTEWKSMTQEAfqESSVKELGRLEAQLASLRQELAALT 443
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEI--------EELQKELYALANEISRLEQQK--QILRERLANLERQLEELEAQLEELE 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035   444 LKQNSVADEVGLLPQKIQAARADVESQfpdwirqfllgdrgarsgLLQRDEMHAQLQELENKILTKMAEMQGKSAREAAA 523
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESL------------------EAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 329299035   524 SLgQILQKEGIVGVTEEQVHRIvKQALQRYSEdRIGMVDYALESGGASVISTRCSETYETKTAL 587
Cdd:TIGR02168  392 EL-QIASLNNEIERLEARLERL-EDRRERLQQ-EIEELLKKLEEAELKELQAELEELEEELEEL 452
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
297-468 1.22e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 297 LERRLEALAADFSSNWQKEAI-RLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRREATLK-EDLRRD-TVAHIQEEL 373
Cdd:COG4717  293 LAREKASLGKEAEELQALPALeELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEElQLEELEQEI 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 374 ATLRAEHHQDSEDLFKKIVQASQES---EARVQQLKTEWKSMTQEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVA 450
Cdd:COG4717  373 AALLAEAGVEDEEELRAALEQAEEYqelKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR 452
                        170
                 ....*....|....*...
gi 329299035 451 DEVGLLPQKIQAARADVE 468
Cdd:COG4717  453 EELAELEAELEQLEEDGE 470
PRK11281 PRK11281
mechanosensitive channel MscK;
365-517 2.21e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.90  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  365 TVAHIQEELATL--RAEHHQDSEDLFKKIVQASQ---ESEARVQQLKTEWKSMTQEAFQESSVKELgrlEAQLASLRQEL 439
Cdd:PRK11281   61 VQQDLEQTLALLdkIDRQKEETEQLKQQLAQAPAklrQAQAELEALKDDNDEETRETLSTLSLRQL---ESRLAQTLDQL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  440 AALtlkQNSVADEVGLL------PQKIQAARADvESQFPDWIRQFLLGDRGARSGLL--QRDEMHAQLQELENKILTKMA 511
Cdd:PRK11281  138 QNA---QNDLAEYNSQLvslqtqPERAQAALYA-NSQRLQQIRNLLKGGKVGGKALRpsQRVLLQAEQALLNAQNDLQRK 213

                  ....*.
gi 329299035  512 EMQGKS 517
Cdd:PRK11281  214 SLEGNT 219
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
340-470 4.63e-04

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 43.30  E-value: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 340 EDALSLLEGLVSRREA---TLKEDLRRDTVAHIQEELAtlRAEhhqdsedlfkkivQASQESEARVQQLKTEWKSMTQEA 416
Cdd:COG3524  150 EDAQAIAEALLAESEElvnQLSERAREDAVRFAEEEVE--RAE-------------ERLRDAREALLAFRNRNGILDPEA 214
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 329299035 417 FQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVESQ 470
Cdd:COG3524  215 TAEALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAE 268
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
352-512 1.03e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  352 RREATLKEDLR--RDTVAHIQEELATLRAEHHQDSE--DLFKKIVQAS------QESEARVQQLKTEWKSMtqeafqESS 421
Cdd:COG4913   610 AKLAALEAELAelEEELAEAEERLEALEAELDALQErrEALQRLAEYSwdeidvASAEREIAELEAELERL------DAS 683
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  422 VKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAAR----------ADVESQFPDWIRQFLLGDRGARSGLLQ 491
Cdd:COG4913   684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeeldelqdrlEAAEDLARLELRALLEERFAAALGDAV 763
                         170       180       190
                  ....*....|....*....|....*....|..
gi 329299035  492 RDEMHAQLQE-----------LENKILTKMAE 512
Cdd:COG4913   764 ERELRENLEEridalrarlnrAEEELERAMRA 795
PRK12704 PRK12704
phosphodiesterase; Provisional
382-556 2.78e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 2.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 382 QDSEDLFKKIVQASQ-ESEA----RVQQLKTEWKSMTQEAFQESSVK--ELGRLEAQLA----SLRQELAALTLKQNSVA 450
Cdd:PRK12704  34 KEAEEEAKRILEEAKkEAEAikkeALLEAKEEIHKLRNEFEKELRERrnELQKLEKRLLqkeeNLDRKLELLEKREEELE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 451 DEVGLLPQKIQaaradvesqfpdwirqfllgdrgarsgllQRDEMHAQLQELENKILTKMAEMQGKSAREAAASLGQILQ 530
Cdd:PRK12704 114 KKEKELEQKQQ-----------------------------ELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVE 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 329299035 531 KEG------IVGVTEEQVH--------RIVKQALQRYSED 556
Cdd:PRK12704 165 EEArheaavLIKEIEEEAKeeadkkakEILAQAIQRCAAD 204
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
399-546 3.46e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.84  E-value: 3.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 399 EARVQQLKTEWKSMTQEAfQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVgllpQKIQAARAdvesqfpdwirqf 478
Cdd:COG0542  417 ERRLEQLEIEKEALKKEQ-DEASFERLAELRDELAELEEELEALKARWEAEKELI----EEIQELKE------------- 478
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 329299035 479 llgdrgarsgllQRDEMHAQLQELENKIltkmaemqgKSAREAAASLGQILQKEgivgVTEEQVHRIV 546
Cdd:COG0542  479 ------------ELEQRYGKIPELEKEL---------AELEEELAELAPLLREE----VTEEDIAEVV 521
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
294-451 5.06e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 40.32  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  294 VHSLERRLEALAAdfssnwQKEAIRLERLELRQGAAGHGGGSSlSHEDALSLLEGL---VSRREA--TLKEDLRR----- 363
Cdd:COG3096   436 PENAEDYLAAFRA------KEQQATEEVLELEQKLSVADAARR-QFEKAYELVCKIageVERSQAwqTARELLRRyrsqq 508
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035  364 ---DTVAHIQEELATL--RAEHHQDSEDLFKKIVQASQESEARVQQLKTEwkSMTQEAFQESSVKELGRLEAQLASLRQE 438
Cdd:COG3096   509 alaQRLQQLRAQLAELeqRLRQQQNAERLLEEFCQRIGQQLDAAEELEEL--LAELEAQLEELEEQAAEAVEQRSELRQQ 586
                         170
                  ....*....|...
gi 329299035  439 LAALTLKQNSVAD 451
Cdd:COG3096   587 LEQLRARIKELAA 599
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
265-442 5.54e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 5.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 265 AKESRKQPEVWESRDASQHFQAEqRVLSRVHSLERRLEALaadfssnwqKEAI-RLERLELRQGAAghgggsslshEDAL 343
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAE-EAREEVAELNSKLAEL---------KERIeSLERIRTLLAAI----------ADAE 605
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 344 SLLEGLVSRREA-TLKEDLRRDTVAHIQEELATLRAEHhqdSEDLFKKIVQASQESEARVQQLKTEWKSMTQEafQESSV 422
Cdd:PRK02224 606 DEIERLREKREAlAELNDERRERLAEKRERKRELEAEF---DEARIEEAREDKERAEEYLEQVEEKLDELREE--RDDLQ 680
                        170       180
                 ....*....|....*....|...
gi 329299035 423 KELGRLE---AQLASLRQELAAL 442
Cdd:PRK02224 681 AEIGAVEnelEELEELRERREAL 703
PRK09039 PRK09039
peptidoglycan -binding protein;
341-442 7.44e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.18  E-value: 7.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 341 DALSLleglvsrrEATLKEDLRrDTVAHIQEELATLRAEHHQdSEDLFKKIVQASQESEARVQQLKTEWKSmtQEAFQES 420
Cdd:PRK09039  67 DLLSL--------ERQGNQDLQ-DSVANLRASLSAAEAERSR-LQALLAELAGAGAAAEGRAGELAQELDS--EKQVSAR 134
                         90       100
                 ....*....|....*....|..
gi 329299035 421 SVKELGRLEAQLASLRQELAAL 442
Cdd:PRK09039 135 ALAQVELLNQQIAALRRQLAAL 156
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
353-551 7.93e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 39.56  E-value: 7.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 353 REATLKEDLRRDT-----VAHIQEELATL-RAEHHQDSE--DLFKKIVQASQESEARVQQLKTEWKSMTQEAFQESSVKE 424
Cdd:COG5185  299 AEYTKSIDIKKATesleeQLAAAEAEQELeESKRETETGiqNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEE 378
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 329299035 425 LGRLEAQLASLRQELaaLTLKQN----------SVADEVGLLPQKIQAARADVE---SQFPDWIRQFL-LGDRGARSGLL 490
Cdd:COG5185  379 LDSFKDTIESTKESL--DEIPQNqrgyaqeilaTLEDTLKAADRQIEELQRQIEqatSSNEEVSKLLNeLISELNKVMRE 456
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 329299035 491 QRDEMHAQLQELENKILTKMAEMQGKSARE---AAASLGQILQK-EGIVGVTEEQVHRIVKQALQ 551
Cdd:COG5185  457 ADEESQSRLEEAYDEINRSVRSKKEDLNEEltqIESRVSTLKATlEKLRAKLERQLEGVRSKLDQ 521
 
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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