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Conserved domains on  [gi|568992122|ref|XP_006520874|]
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SUN domain-containing protein 2 isoform X2 [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 ...
545-679 7.96e-60

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: 7.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  545 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 624
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568992122  625 LLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 679
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
445-502 3.45e-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: 92.78  E-value: 3.45e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568992122  445 MHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQR 502
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
364-418 1.83e-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: 1.83e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568992122 364 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVE 418
Cdd:cd21438    1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
202-422 7.82e-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: 7.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  202 LQTLQPAVVSWWAAKESRKQPEVWES-RDASQHFQAEQRVlsrvHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAG 280
Cdd:COG4913   251 IELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELD 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  281 HGGGSSLSHE-DALSLLEGLVSRREATLKEdlRRDTVAHIQEELATLRAEHHQDSEDLfkkiVQASQESEARVQQLKTEW 359
Cdd:COG4913   327 ELEAQIRGNGgDRLEQLEREIERLERELEE--RERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEEL 400
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568992122  360 KSMTQEAFQesSVKELGRLEAQLASLRQELAALTLKQNSvadevglLPQKIQAARADVESQFP 422
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 ...
545-679 7.96e-60

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: 7.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  545 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 624
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568992122  625 LLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 679
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
445-502 3.45e-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: 92.78  E-value: 3.45e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568992122  445 MHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQR 502
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
364-418 1.83e-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: 1.83e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568992122 364 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVE 418
Cdd:cd21438    1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
202-422 7.82e-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: 7.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  202 LQTLQPAVVSWWAAKESRKQPEVWES-RDASQHFQAEQRVlsrvHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAG 280
Cdd:COG4913   251 IELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELD 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  281 HGGGSSLSHE-DALSLLEGLVSRREATLKEdlRRDTVAHIQEELATLRAEHHQDSEDLfkkiVQASQESEARVQQLKTEW 359
Cdd:COG4913   327 ELEAQIRGNGgDRLEQLEREIERLERELEE--RERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEEL 400
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568992122  360 KSMTQEAFQesSVKELGRLEAQLASLRQELAALTLKQNSvadevglLPQKIQAARADVESQFP 422
Cdd:COG4913   401 EALEEALAE--AEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDALAEALG 454
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
241-537 3.97e-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: 3.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122   241 LSRV----HSLERRLEALAAdfssnwQKE-AIRLERL--ELRQGAAGHGGGSSLSHEDALSLLEglVSRREATLKEDLRR 313
Cdd:TIGR02168  188 LDRLedilNELERQLKSLER------QAEkAERYKELkaELRELELALLVLRLEELREELEELQ--EELKEAEEELEELT 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122   314 DTVAHIQEELATLRAEHHQDSEDLfkkivqasQESEARVQQLKTEWKSMTQEAfqESSVKELGRLEAQLASLRQELAALT 393
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEI--------EELQKELYALANEISRLEQQK--QILRERLANLERQLEELEAQLEELE 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122   394 LKQNSVADEVGLLPQKIQAARADVESQfpdwirqfllgdrgarsgLLQRDEMHAQLQELENKILTKMAEMQGKSAREAAA 473
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESL------------------EAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568992122   474 SLgQILQKEGIVGVTEEQVHRIvKQALQRYSEdRIGMVDYALESGGASVISTRCSETYETKTAL 537
Cdd:TIGR02168  392 EL-QIASLNNEIERLEARLERL-EDRRERLQQ-EIEELLKKLEEAELKELQAELEELEEELEEL 452
PRK11281 PRK11281
mechanosensitive channel MscK;
315-467 2.00e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.90  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  315 TVAHIQEELATL--RAEHHQDSEDLFKKIVQASQ---ESEARVQQLKTEWKSMTQEAFQESSVKELgrlEAQLASLRQEL 389
Cdd:PRK11281   61 VQQDLEQTLALLdkIDRQKEETEQLKQQLAQAPAklrQAQAELEALKDDNDEETRETLSTLSLRQL---ESRLAQTLDQL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  390 AALtlkQNSVADEVGLL------PQKIQAARADvESQFPDWIRQFLLGDRGARSGLL--QRDEMHAQLQELENKILTKMA 461
Cdd:PRK11281  138 QNA---QNDLAEYNSQLvslqtqPERAQAALYA-NSQRLQQIRNLLKGGKVGGKALRpsQRVLLQAEQALLNAQNDLQRK 213

                  ....*.
gi 568992122  462 EMQGKS 467
Cdd:PRK11281  214 SLEGNT 219
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
349-496 3.33e-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: 3.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 349 EARVQQLKTEWKSMTQEAfQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVgllpQKIQAARAdvesqfpdwirqf 428
Cdd:COG0542  417 ERRLEQLEIEKEALKKEQ-DEASFERLAELRDELAELEEELEALKARWEAEKELI----EEIQELKE------------- 478
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568992122 429 llgdrgarsgllQRDEMHAQLQELENKIltkmaemqgKSAREAAASLGQILQKEgivgVTEEQVHRIV 496
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 ...
545-679 7.96e-60

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: 7.96e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  545 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 624
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568992122  625 LLGTFAYDQDGEPIQTFYFQASKMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 679
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
445-502 3.45e-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: 92.78  E-value: 3.45e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 568992122  445 MHAQLQELENKILTKMAEMQGKSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQR 502
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
364-418 1.83e-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: 1.83e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568992122 364 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVE 418
Cdd:cd21438    1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SUN_cc1 cd21435
coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 ...
364-418 2.51e-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: 2.51e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568992122 364 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVE 418
Cdd:cd21435    1 QEAFQESSVKELGRLEAQLASLRQELAALTLKQEAIQKELEQTKQKTISAVGEQL 55
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
202-422 7.82e-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: 7.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  202 LQTLQPAVVSWWAAKESRKQPEVWES-RDASQHFQAEQRVlsrvHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAG 280
Cdd:COG4913   251 IELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELD 326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  281 HGGGSSLSHE-DALSLLEGLVSRREATLKEdlRRDTVAHIQEELATLRAEHHQDSEDLfkkiVQASQESEARVQQLKTEW 359
Cdd:COG4913   327 ELEAQIRGNGgDRLEQLEREIERLERELEE--RERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEEL 400
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568992122  360 KSMTQEAFQesSVKELGRLEAQLASLRQELAALTLKQNSvadevglLPQKIQAARADVESQFP 422
Cdd:COG4913   401 EALEEALAE--AEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDALAEALG 454
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
232-504 3.59e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 232 QHFQAEQRVL-SRVHSLERRLEALAADFSS-NWQKEAIRLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRRE----- 304
Cdd:COG1196  235 RELEAELEELeAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrel 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 305 ----ATLKEDLRRDT--VAHIQEELATLRAEH------HQDSEDLFKKIVQASQESEARVQQLKTEWKSMTQEAFQEssV 372
Cdd:COG1196  315 eerlEELEEELAELEeeLEELEEELEELEEELeeaeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA--L 392
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 373 KELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVESqfpdwirqfllgdrgARSGLLQRDEMHAQLQEL 452
Cdd:COG1196  393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE---------------EEEALEEAAEEEAELEEE 457
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 568992122 453 ENKILTKMAEmQGKSAREAAASLGQILQKEGivgvTEEQVHRIVKQALQRYS 504
Cdd:COG1196  458 EEALLELLAE-LLEEAALLEAALAELLEELA----EAAARLLLLLEAEADYE 504
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
307-505 4.13e-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: 4.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 307 LKEDLRRDTVAHIQEELATLRAEhhqdsedlfkkivqaSQESEARVQQLKTEWKSMTQEAFQESSVKELGRLEAQLASLR 386
Cdd:COG3206  168 LRREEARKALEFLEEQLPELRKE---------------LEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 387 QELAALTLKQNSVADEVGLLPQKIQAARADVESQFpdwIRQFLLGDRGARSGLLQR-DEMHAQLQELENKIltkmAEMQG 465
Cdd:COG3206  233 AELAEAEARLAALRAQLGSGPDALPELLQSPVIQQ---LRAQLAELEAELAELSARyTPNHPDVIALRAQI----AALRA 305
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568992122 466 KSAREAAASLGQILQKEGIVGVTEEQVHRIVKQALQRYSE 505
Cdd:COG3206  306 QLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAE 345
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
225-457 7.64e-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: 7.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  225 WESRDASQHFQAEQRVL-SRVHSLERRLEALAAdfssnwqkeaiRLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRR 303
Cdd:COG4913   606 FDNRAKLAALEAELAELeEELAEAEERLEALEA-----------ELDALQERREALQRLAEYSWDEIDVASAEREIAELE 674
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  304 EAtlKEDLRR--DTVAHIQEELATLRAEHhQDSEDLFKKIVQASQESEARVQQLKTEWKS---MTQEAFQESSVKELGRL 378
Cdd:COG4913   675 AE--LERLDAssDDLAALEEQLEELEAEL-EELEEELDELKGEIGRLEKELEQAEEELDElqdRLEAAEDLARLELRALL 751
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568992122  379 EAQLASLRQELAALTLKQNsVADEVGLLPQKIQAARADVESQFPDWIRQFLLGDRGARSGLLQRDEMHAQLQELENKIL 457
Cdd:COG4913   752 EERFAAALGDAVERELREN-LEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGL 829
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
241-537 3.97e-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: 3.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122   241 LSRV----HSLERRLEALAAdfssnwQKE-AIRLERL--ELRQGAAGHGGGSSLSHEDALSLLEglVSRREATLKEDLRR 313
Cdd:TIGR02168  188 LDRLedilNELERQLKSLER------QAEkAERYKELkaELRELELALLVLRLEELREELEELQ--EELKEAEEELEELT 259
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122   314 DTVAHIQEELATLRAEHHQDSEDLfkkivqasQESEARVQQLKTEWKSMTQEAfqESSVKELGRLEAQLASLRQELAALT 393
Cdd:TIGR02168  260 AELQELEEKLEELRLEVSELEEEI--------EELQKELYALANEISRLEQQK--QILRERLANLERQLEELEAQLEELE 329
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122   394 LKQNSVADEVGLLPQKIQAARADVESQfpdwirqfllgdrgarsgLLQRDEMHAQLQELENKILTKMAEMQGKSAREAAA 473
Cdd:TIGR02168  330 SKLDELAEELAELEEKLEELKEELESL------------------EAELEELEAELEELESRLEELEEQLETLRSKVAQL 391
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568992122   474 SLgQILQKEGIVGVTEEQVHRIvKQALQRYSEdRIGMVDYALESGGASVISTRCSETYETKTAL 537
Cdd:TIGR02168  392 EL-QIASLNNEIERLEARLERL-EDRRERLQQ-EIEELLKKLEEAELKELQAELEELEEELEEL 452
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
247-418 1.27e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 247 LERRLEALAADFSSNWQKEAI-RLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRREATLK-EDLRRD-TVAHIQEEL 323
Cdd:COG4717  293 LAREKASLGKEAEELQALPALeELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEElQLEELEQEI 372
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 324 ATLRAEHHQDSEDLFKKIVQASQES---EARVQQLKTEWKSMTQEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVA 400
Cdd:COG4717  373 AALLAEAGVEDEEELRAALEQAEEYqelKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR 452
                        170
                 ....*....|....*...
gi 568992122 401 DEVGLLPQKIQAARADVE 418
Cdd:COG4717  453 EELAELEAELEQLEEDGE 470
PRK11281 PRK11281
mechanosensitive channel MscK;
315-467 2.00e-04

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 44.90  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  315 TVAHIQEELATL--RAEHHQDSEDLFKKIVQASQ---ESEARVQQLKTEWKSMTQEAFQESSVKELgrlEAQLASLRQEL 389
Cdd:PRK11281   61 VQQDLEQTLALLdkIDRQKEETEQLKQQLAQAPAklrQAQAELEALKDDNDEETRETLSTLSLRQL---ESRLAQTLDQL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  390 AALtlkQNSVADEVGLL------PQKIQAARADvESQFPDWIRQFLLGDRGARSGLL--QRDEMHAQLQELENKILTKMA 461
Cdd:PRK11281  138 QNA---QNDLAEYNSQLvslqtqPERAQAALYA-NSQRLQQIRNLLKGGKVGGKALRpsQRVLLQAEQALLNAQNDLQRK 213

                  ....*.
gi 568992122  462 EMQGKS 467
Cdd:PRK11281  214 SLEGNT 219
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
290-420 4.09e-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: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 290 EDALSLLEGLVSRREA---TLKEDLRRDTVAHIQEELAtlRAEhhqdsedlfkkivQASQESEARVQQLKTEWKSMTQEA 366
Cdd:COG3524  150 EDAQAIAEALLAESEElvnQLSERAREDAVRFAEEEVE--RAE-------------ERLRDAREALLAFRNRNGILDPEA 214
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 568992122 367 FQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVESQ 420
Cdd:COG3524  215 TAEALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAE 268
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
302-462 8.52e-04

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: 8.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  302 RREATLKEDLR--RDTVAHIQEELATLRAEHHQDSE--DLFKKIVQAS------QESEARVQQLKTEWKSMtqeafqESS 371
Cdd:COG4913   610 AKLAALEAELAelEEELAEAEERLEALEAELDALQErrEALQRLAEYSwdeidvASAEREIAELEAELERL------DAS 683
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  372 VKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAAR----------ADVESQFPDWIRQFLLGDRGARSGLLQ 441
Cdd:COG4913   684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeeldelqdrlEAAEDLARLELRALLEERFAAALGDAV 763
                         170       180       190
                  ....*....|....*....|....*....|..
gi 568992122  442 RDEMHAQLQE-----------LENKILTKMAE 462
Cdd:COG4913   764 ERELRENLEEridalrarlnrAEEELERAMRA 795
PRK12704 PRK12704
phosphodiesterase; Provisional
332-506 3.15e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 3.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 332 QDSEDLFKKIVQASQ-ESEA----RVQQLKTEWKSMTQEAFQESSVK--ELGRLEAQLA----SLRQELAALTLKQNSVA 400
Cdd:PRK12704  34 KEAEEEAKRILEEAKkEAEAikkeALLEAKEEIHKLRNEFEKELRERrnELQKLEKRLLqkeeNLDRKLELLEKREEELE 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 401 DEVGLLPQKIQaaradvesqfpdwirqfllgdrgarsgllQRDEMHAQLQELENKILTKMAEMQGKSAREAAASLGQILQ 480
Cdd:PRK12704 114 KKEKELEQKQQ-----------------------------ELEKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVE 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 568992122 481 KEG------IVGVTEEQVH--------RIVKQALQRYSED 506
Cdd:PRK12704 165 EEArheaavLIKEIEEEAKeeadkkakEILAQAIQRCAAD 204
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
349-496 3.33e-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: 3.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 349 EARVQQLKTEWKSMTQEAfQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVgllpQKIQAARAdvesqfpdwirqf 428
Cdd:COG0542  417 ERRLEQLEIEKEALKKEQ-DEASFERLAELRDELAELEEELEALKARWEAEKELI----EEIQELKE------------- 478
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568992122 429 llgdrgarsgllQRDEMHAQLQELENKIltkmaemqgKSAREAAASLGQILQKEgivgVTEEQVHRIV 496
Cdd:COG0542  479 ------------ELEQRYGKIPELEKEL---------AELEEELAELAPLLREE----VTEEDIAEVV 521
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
215-392 4.69e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 4.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 215 AKESRKQPEVWESRDASQHFQAEqRVLSRVHSLERRLEALaadfssnwqKEAI-RLERLELRQGAAghgggsslshEDAL 293
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAE-EAREEVAELNSKLAEL---------KERIeSLERIRTLLAAI----------ADAE 605
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 294 SLLEGLVSRREA-TLKEDLRRDTVAHIQEELATLRAEHhqdSEDLFKKIVQASQESEARVQQLKTEWKSMTQEafQESSV 372
Cdd:PRK02224 606 DEIERLREKREAlAELNDERRERLAEKRERKRELEAEF---DEARIEEAREDKERAEEYLEQVEEKLDELREE--RDDLQ 680
                        170       180
                 ....*....|....*....|...
gi 568992122 373 KELGRLE---AQLASLRQELAAL 392
Cdd:PRK02224 681 AEIGAVEnelEELEELRERREAL 703
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
244-401 4.71e-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: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  244 VHSLERRLEALAAdfssnwQKEAIRLERLELRQGAAGHGGGSSlSHEDALSLLEGL---VSRREA--TLKEDLRR----- 313
Cdd:COG3096   436 PENAEDYLAAFRA------KEQQATEEVLELEQKLSVADAARR-QFEKAYELVCKIageVERSQAwqTARELLRRyrsqq 508
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122  314 ---DTVAHIQEELATL--RAEHHQDSEDLFKKIVQASQESEARVQQLKTEwkSMTQEAFQESSVKELGRLEAQLASLRQE 388
Cdd:COG3096   509 alaQRLQQLRAQLAELeqRLRQQQNAERLLEEFCQRIGQQLDAAEELEEL--LAELEAQLEELEEQAAEAVEQRSELRQQ 586
                         170
                  ....*....|...
gi 568992122  389 LAALTLKQNSVAD 401
Cdd:COG3096   587 LEQLRARIKELAA 599
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
303-501 4.89e-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: 39.94  E-value: 4.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 303 REATLKEDLRRDT-----VAHIQEELATL-RAEHHQDSE--DLFKKIVQASQESEARVQQLKTEWKSMTQEAFQESSVKE 374
Cdd:COG5185  299 AEYTKSIDIKKATesleeQLAAAEAEQELeESKRETETGiqNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEE 378
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 375 LGRLEAQLASLRQELaaLTLKQN----------SVADEVGLLPQKIQAARADVE---SQFPDWIRQFL-LGDRGARSGLL 440
Cdd:COG5185  379 LDSFKDTIESTKESL--DEIPQNqrgyaqeilaTLEDTLKAADRQIEELQRQIEqatSSNEEVSKLLNeLISELNKVMRE 456
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568992122 441 QRDEMHAQLQELENKILTKMAEMQGKSARE---AAASLGQILQK-EGIVGVTEEQVHRIVKQALQ 501
Cdd:COG5185  457 ADEESQSRLEEAYDEINRSVRSKKEDLNEEltqIESRVSTLKATlEKLRAKLERQLEGVRSKLDQ 521
PRK09039 PRK09039
peptidoglycan -binding protein;
291-392 6.70e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.18  E-value: 6.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 291 DALSLleglvsrrEATLKEDLRrDTVAHIQEELATLRAEHHQdSEDLFKKIVQASQESEARVQQLKTEWKSmtQEAFQES 370
Cdd:PRK09039  67 DLLSL--------ERQGNQDLQ-DSVANLRASLSAAEAERSR-LQALLAELAGAGAAAEGRAGELAQELDS--EKQVSAR 134
                         90       100
                 ....*....|....*....|..
gi 568992122 371 SVKELGRLEAQLASLRQELAAL 392
Cdd:PRK09039 135 ALAQVELLNQQIAALRRQLAAL 156
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
215-404 9.62e-03

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: 39.28  E-value: 9.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122   215 AKESRKQPEVWESRDASQHFQAE-QRVLSRVHSLERRLEALAADFSSnWQKEAIRL--ERLELRQGAAGHGGGSSLSHED 291
Cdd:TIGR02169  308 RSIAEKERELEDAEERLAKLEAEiDKLLAEIEELEREIEEERKRRDK-LTEEYAELkeELEDLRAELEEVDKEFAETRDE 386
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122   292 ALSL---LEGLVSRRE------ATLKEDLRRDT--VAHIQEELATLRAEHHQ---DSEDLFKKIVQASQESEARVQQLKT 357
Cdd:TIGR02169  387 LKDYrekLEKLKREINelkrelDRLQEELQRLSeeLADLNAAIAGIEAKINEleeEKEDKALEIKKQEWKLEQLAADLSK 466
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 568992122   358 EwksmTQEAFQESSvkELGRLEAQLASLRQELAALTLKQNSVADEVG 404
Cdd:TIGR02169  467 Y----EQELYDLKE--EYDRVEKELSKLQRELAEAEAQARASEERVR 507
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
301-480 9.87e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 9.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 301 SRREATLKEDLRRDTVAHIQEELATLRAEHHQDSEDLFK---KIVQASQESEARVQQLKTEWKSM--TQEAFQESSvKEL 375
Cdd:COG4372   32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarsELEQLEEELEELNEQLQAAQAELaqAQEELESLQ-EEA 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568992122 376 GRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARAdvesqfpdwirqfllgdrgarsgllQRDEMHAQLQELENK 455
Cdd:COG4372  111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREE-------------------------ELKELEEQLESLQEE 165
                        170       180
                 ....*....|....*....|....*
gi 568992122 456 ILTKMAEMQGKSAREAAASLGQILQ 480
Cdd:COG4372  166 LAALEQELQALSEAEAEQALDELLK 190
 
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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