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Conserved domains on  [gi|1720384008|ref|XP_030104362|]
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SUN domain-containing protein 2 isoform X1 [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 ...
561-695 1.01e-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: 1.01e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 561 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 640
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720384008 641 LLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 695
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
461-518 5.42e-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: 92.39  E-value: 5.42e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720384008 461 MHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQR 518
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
380-434 3.84e-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: 78.50  E-value: 3.84e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720384008 380 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVE 434
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
218-438 1.05e-07

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: 55.31  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  218 LQTLQPAVVSWWAAKESRKQPEVWES-RDASQHFQAEQRVlsrvHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAG 296
Cdd:COG4913    251 IELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELD 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  297 HGGGSSLSHE-DALSLLEGLVSRREATLKEdlRRDTVAHIQEELATLRAEHHQDSEDLfkkiVQASQESEARVQQLKTEW 375
Cdd:COG4913    327 ELEAQIRGNGgDRLEQLEREIERLERELEE--RERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEEL 400
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720384008  376 KSMTQEAFQesSVKELGRLEAQLASLRQELAALTLKQNSvadevglLPQKIQAARADVESQFP 438
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 ...
561-695 1.01e-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: 1.01e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 561 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 640
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720384008 641 LLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 695
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
461-518 5.42e-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: 92.39  E-value: 5.42e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720384008 461 MHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQR 518
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
380-434 3.84e-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: 78.50  E-value: 3.84e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720384008 380 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVE 434
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
218-438 1.05e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  218 LQTLQPAVVSWWAAKESRKQPEVWES-RDASQHFQAEQRVlsrvHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAG 296
Cdd:COG4913    251 IELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELD 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  297 HGGGSSLSHE-DALSLLEGLVSRREATLKEdlRRDTVAHIQEELATLRAEHHQDSEDLfkkiVQASQESEARVQQLKTEW 375
Cdd:COG4913    327 ELEAQIRGNGgDRLEQLEREIERLERELEE--RERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEEL 400
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720384008  376 KSMTQEAFQesSVKELGRLEAQLASLRQELAALTLKQNSvadevglLPQKIQAARADVESQFP 438
Cdd:COG4913    401 EALEEALAE--AEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDALAEALG 454
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
257-555 9.60e-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: 45.82  E-value: 9.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  257 LSRV----HSLERRLEALAAdfssnwQKE-AIRLERL--ELRQGAAGHGGGSSLSHEDALSLLEglVSRREATLKEDLRR 329
Cdd:TIGR02168  188 LDRLedilNELERQLKSLER------QAEkAERYKELkaELRELELALLVLRLEELREELEELQ--EELKEAEEELEELT 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  330 DTVAHIQEELATLRAEHHQDSEDLfkkivqasQESEARVQQLKTEWKSMTQEAfqESSVKELGRLEAQLASLRQELAALT 409
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEI--------EELQKELYALANEISRLEQQK--QILRERLANLERQLEELEAQLEELE 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  410 LKQNSVADEVGLLPQKIQAARADVESQfpdwirqfllgdrgarsgLLQRDEMHAQLQELENKILTKMAEMQGKSAREAAA 489
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESL------------------EAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720384008  490 SLgQILQKEGIVGVTEEQVHRIvKQALQRYSEdRIGMVDYALESGGASVISTRCSETYETKTALLS 555
Cdd:TIGR02168  392 EL-QIASLNNEIERLEARLERL-EDRRERLQQ-EIEELLKKLEEAELKELQAELEELEEELEELQE 454
PRK11281 PRK11281
mechanosensitive channel MscK;
331-483 2.46e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.52  E-value: 2.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  331 TVAHIQEELATL--RAEHHQDSEDLFKKIVQASQ---ESEARVQQLKTEWKSMTQEAFQESSVKELgrlEAQLASLRQEL 405
Cdd:PRK11281    61 VQQDLEQTLALLdkIDRQKEETEQLKQQLAQAPAklrQAQAELEALKDDNDEETRETLSTLSLRQL---ESRLAQTLDQL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  406 AALtlkQNSVADEVGLL------PQKIQAARADvESQFPDWIRQFLLGDRGARSGLL--QRDEMHAQLQELENKILTKMA 477
Cdd:PRK11281   138 QNA---QNDLAEYNSQLvslqtqPERAQAALYA-NSQRLQQIRNLLKGGKVGGKALRpsQRVLLQAEQALLNAQNDLQRK 213

                   ....*.
gi 1720384008  478 EMQGKS 483
Cdd:PRK11281   214 SLEGNT 219
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
365-512 3.90e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.45  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 365 EARVQQLKTEWKSMTQEAfQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVgllpQKIQAARAdvesqfpdwirqf 444
Cdd:COG0542   417 ERRLEQLEIEKEALKKEQ-DEASFERLAELRDELAELEEELEALKARWEAEKELI----EEIQELKE------------- 478
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720384008 445 llgdrgarsgllQRDEMHAQLQELENKIltkmaemqgKSAREAAASLGQILQKEgivgVTEEQVHRIV 512
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 ...
561-695 1.01e-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: 1.01e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 561 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 640
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720384008 641 LLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 695
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
461-518 5.42e-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: 92.39  E-value: 5.42e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720384008 461 MHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQR 518
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
380-434 3.84e-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: 78.50  E-value: 3.84e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720384008 380 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVE 434
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SUN_cc1 cd21435
coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 ...
380-434 5.49e-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: 78.22  E-value: 5.49e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720384008 380 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVE 434
Cdd:cd21435     1 QEAFQESSVKELGRLEAQLASLRQELAALTLKQEAIQKELEQTKQKTISAVGEQL 55
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
218-438 1.05e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  218 LQTLQPAVVSWWAAKESRKQPEVWES-RDASQHFQAEQRVlsrvHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAG 296
Cdd:COG4913    251 IELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELD 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  297 HGGGSSLSHE-DALSLLEGLVSRREATLKEdlRRDTVAHIQEELATLRAEHHQDSEDLfkkiVQASQESEARVQQLKTEW 375
Cdd:COG4913    327 ELEAQIRGNGgDRLEQLEREIERLERELEE--RERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEEL 400
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720384008  376 KSMTQEAFQesSVKELGRLEAQLASLRQELAALTLKQNSvadevglLPQKIQAARADVESQFP 438
Cdd:COG4913    401 EALEEALAE--AEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDALAEALG 454
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
248-520 5.18e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 5.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 248 QHFQAEQRVL-SRVHSLERRLEALAADFSS-NWQKEAIRLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRRE----- 320
Cdd:COG1196   235 RELEAELEELeAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrel 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 321 ----ATLKEDLRRDT--VAHIQEELATLRAEH------HQDSEDLFKKIVQASQESEARVQQLKTEWKSMTQEAFQEssV 388
Cdd:COG1196   315 eerlEELEEELAELEeeLEELEEELEELEEELeeaeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA--L 392
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 389 KELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVESqfpdwirqfllgdrgARSGLLQRDEMHAQLQEL 468
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE---------------EEEALEEAAEEEAELEEE 457
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720384008 469 ENKILTKMAEmQGKSAREAAASLGQILQKEGivgvTEEQVHRIVKQALQRYS 520
Cdd:COG1196   458 EEALLELLAE-LLEEAALLEAALAELLEELA----EAAARLLLLLEAEADYE 504
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
323-521 5.91e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 5.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 323 LKEDLRRDTVAHIQEELATLRAEhhqdsedlfkkivqaSQESEARVQQLKTEWKSMTQEAFQESSVKELGRLEAQLASLR 402
Cdd:COG3206   168 LRREEARKALEFLEEQLPELRKE---------------LEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 403 QELAALTLKQNSVADEVGLLPQKIQAARADVESQFpdwIRQFLLGDRGARSGLLQR-DEMHAQLQELENKIltkmAEMQG 481
Cdd:COG3206   233 AELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSARyTPNHPDVIALRAQI----AALRA 305
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720384008 482 KSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQRYSE 521
Cdd:COG3206   306 QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
241-473 1.09e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.76  E-value: 1.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  241 WESRDASQHFQAEQRVL-SRVHSLERRLEALAAdfssnwqkeaiRLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRR 319
Cdd:COG4913    606 FDNRAKLAALEAELAELeEELAEAEERLEALEA-----------ELDALQERREALQRLAEYSWDEIDVASAEREIAELE 674
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  320 EAtlKEDLRR--DTVAHIQEELATLRAEHhQDSEDLFKKIVQASQESEARVQQLKTEWKS---MTQEAFQESSVKELGRL 394
Cdd:COG4913    675 AE--LERLDAssDDLAALEEQLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDElqdRLEAAEDLARLELRALL 751
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720384008  395 EAQLASLRQELAALTLKQNsVADEVGLLPQKIQAARADVESQFPDWIRQFLLGDRGARSGLLQRDEMHAQLQELENKIL 473
Cdd:COG4913    752 EERFAAALGDAVERELREN-LEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGL 829
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
257-555 9.60e-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: 45.82  E-value: 9.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  257 LSRV----HSLERRLEALAAdfssnwQKE-AIRLERL--ELRQGAAGHGGGSSLSHEDALSLLEglVSRREATLKEDLRR 329
Cdd:TIGR02168  188 LDRLedilNELERQLKSLER------QAEkAERYKELkaELRELELALLVLRLEELREELEELQ--EELKEAEEELEELT 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  330 DTVAHIQEELATLRAEHHQDSEDLfkkivqasQESEARVQQLKTEWKSMTQEAfqESSVKELGRLEAQLASLRQELAALT 409
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEI--------EELQKELYALANEISRLEQQK--QILRERLANLERQLEELEAQLEELE 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  410 LKQNSVADEVGLLPQKIQAARADVESQfpdwirqfllgdrgarsgLLQRDEMHAQLQELENKILTKMAEMQGKSAREAAA 489
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESL------------------EAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720384008  490 SLgQILQKEGIVGVTEEQVHRIvKQALQRYSEdRIGMVDYALESGGASVISTRCSETYETKTALLS 555
Cdd:TIGR02168  392 EL-QIASLNNEIERLEARLERL-EDRRERLQQ-EIEELLKKLEEAELKELQAELEELEEELEELQE 454
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
263-434 2.17e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 263 LERRLEALAADFSSNWQKEAI-RLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRREATLK-EDLRRD-TVAHIQEEL 339
Cdd:COG4717   293 LAREKASLGKEAEELQALPALeELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEElQLEELEQEI 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 340 ATLRAEHHQDSEDLFKKIVQASQES---EARVQQLKTEWKSMTQEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVA 416
Cdd:COG4717   373 AALLAEAGVEDEEELRAALEQAEEYqelKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR 452
                         170
                  ....*....|....*...
gi 1720384008 417 DEVGLLPQKIQAARADVE 434
Cdd:COG4717   453 EELAELEAELEQLEEDGE 470
PRK11281 PRK11281
mechanosensitive channel MscK;
331-483 2.46e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.52  E-value: 2.46e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  331 TVAHIQEELATL--RAEHHQDSEDLFKKIVQASQ---ESEARVQQLKTEWKSMTQEAFQESSVKELgrlEAQLASLRQEL 405
Cdd:PRK11281    61 VQQDLEQTLALLdkIDRQKEETEQLKQQLAQAPAklrQAQAELEALKDDNDEETRETLSTLSLRQL---ESRLAQTLDQL 137
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  406 AALtlkQNSVADEVGLL------PQKIQAARADvESQFPDWIRQFLLGDRGARSGLL--QRDEMHAQLQELENKILTKMA 477
Cdd:PRK11281   138 QNA---QNDLAEYNSQLvslqtqPERAQAALYA-NSQRLQQIRNLLKGGKVGGKALRpsQRVLLQAEQALLNAQNDLQRK 213

                   ....*.
gi 1720384008  478 EMQGKS 483
Cdd:PRK11281   214 SLEGNT 219
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
306-436 4.36e-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: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 306 EDALSLLEGLVSRREA---TLKEDLRRDTVAHIQEELAtlRAEhhqdsedlfkkivQASQESEARVQQLKTEWKSMTQEA 382
Cdd:COG3524   150 EDAQAIAEALLAESEElvnQLSERAREDAVRFAEEEVE--RAE-------------ERLRDAREALLAFRNRNGILDPEA 214
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720384008 383 FQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVESQ 436
Cdd:COG3524   215 TAEALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAE 268
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
318-478 1.21e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 1.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  318 RREATLKEDLR--RDTVAHIQEELATLRAEHHQDSE--DLFKKIVQASqESEARVQQLKTEWKSMTQEAFQ-ESSVKELG 392
Cdd:COG4913    610 AKLAALEAELAelEEELAEAEERLEALEAELDALQErrEALQRLAEYS-WDEIDVASAEREIAELEAELERlDASSDDLA 688
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  393 RLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAAR----------ADVESQFPDWIRQFLLGDRGARSGLLQRDEMH 462
Cdd:COG4913    689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeeldelqdrlEAAEDLARLELRALLEERFAAALGDAVERELR 768
                          170       180
                   ....*....|....*....|....*..
gi 1720384008  463 AQLQE-----------LENKILTKMAE 478
Cdd:COG4913    769 ENLEEridalrarlnrAEEELERAMRA 795
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
365-512 3.90e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.45  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 365 EARVQQLKTEWKSMTQEAfQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVgllpQKIQAARAdvesqfpdwirqf 444
Cdd:COG0542   417 ERRLEQLEIEKEALKKEQ-DEASFERLAELRDELAELEEELEALKARWEAEKELI----EEIQELKE------------- 478
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720384008 445 llgdrgarsgllQRDEMHAQLQELENKIltkmaemqgKSAREAAASLGQILQKEgivgVTEEQVHRIV 512
Cdd:COG0542   479 ------------ELEQRYGKIPELEKEL---------AELEEELAELAPLLREE----VTEEDIAEVV 521
PRK12704 PRK12704
phosphodiesterase; Provisional
348-522 4.10e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 4.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 348 QDSEDLFKKIVQASQ-ESEA----RVQQLKTEWKSMTQEAFQESSVK--ELGRLEAQLA----SLRQELAALTLKQNSVA 416
Cdd:PRK12704   34 KEAEEEAKRILEEAKkEAEAikkeALLEAKEEIHKLRNEFEKELRERrnELQKLEKRLLqkeeNLDRKLELLEKREEELE 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 417 DEVGLLPQKIQaaradvesqfpdwirqfllgdrgarsgllQRDEMHAQLQELENKILTKMAEMQGKSAREAAASLGQILQ 496
Cdd:PRK12704  114 KKEKELEQKQQ-----------------------------ELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVE 164
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720384008 497 KEG------IVGVTEEQVH--------RIVKQALQRYSED 522
Cdd:PRK12704  165 EEArheaavLIKEIEEEAKeeadkkakEILAQAIQRCAAD 204
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
260-417 6.42e-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: 39.94  E-value: 6.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  260 VHSLERRLEALAAdfssnwQKEAIRLERLELRQGAAGHGGGSSlSHEDALSLLEGL---VSRREA--TLKEDLRR----- 329
Cdd:COG3096    436 PENAEDYLAAFRA------KEQQATEEVLELEQKLSVADAARR-QFEKAYELVCKIageVERSQAwqTARELLRRyrsqq 508
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008  330 ---DTVAHIQEELATL--RAEHHQDSEDLFKKIVQASQESEARVQQLKTEwkSMTQEAFQESSVKELGRLEAQLASLRQE 404
Cdd:COG3096    509 alaQRLQQLRAQLAELeqRLRQQQNAERLLEEFCQRIGQQLDAAEELEEL--LAELEAQLEELEEQAAEAVEQRSELRQQ 586
                          170
                   ....*....|...
gi 1720384008  405 LAALTLKQNSVAD 417
Cdd:COG3096    587 LEQLRARIKELAA 599
PRK09039 PRK09039
peptidoglycan -binding protein;
307-408 7.33e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.18  E-value: 7.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 307 DALSLleglvsrrEATLKEDLRrDTVAHIQEELATLRAEHHQdSEDLFKKIVQASQESEARVQQLKTEWKSmtQEAFQES 386
Cdd:PRK09039   67 DLLSL--------ERQGNQDLQ-DSVANLRASLSAAEAERSR-LQALLAELAGAGAAAEGRAGELAQELDS--EKQVSAR 134
                          90       100
                  ....*....|....*....|..
gi 1720384008 387 SVKELGRLEAQLASLRQELAAL 408
Cdd:PRK09039  135 ALAQVELLNQQIAALRRQLAAL 156
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
231-408 8.07e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 8.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 231 AKESRKQPEVWESRDASQHFQAEqRVLSRVHSLERRLEALaadfssnwqKEAI-RLERLELRQGAAghgggsslshEDAL 309
Cdd:PRK02224  546 AAELEAEAEEKREAAAEAEEEAE-EAREEVAELNSKLAEL---------KERIeSLERIRTLLAAI----------ADAE 605
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720384008 310 SLLEGLVSRREA-TLKEDLRRDTVAHIQEELATLRAEHhqdSEDLFKKIVQASQESEARVQQLKTEWKSMTQEafQESSV 388
Cdd:PRK02224  606 DEIERLREKREAlAELNDERRERLAEKRERKRELEAEF---DEARIEEAREDKERAEEYLEQVEEKLDELREE--RDDLQ 680
                         170       180
                  ....*....|....*....|...
gi 1720384008 389 KELGRLE---AQLASLRQELAAL 408
Cdd:PRK02224  681 AEIGAVEnelEELEELRERREAL 703
 
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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