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Conserved domains on  [gi|2028477694|ref|NP_001381372|]
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SUN domain-containing protein 2 isoform 10 [Homo sapiens]

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 ...
417-551 7.93e-62

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: 199.44  E-value: 7.93e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 417 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 496
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477694 497 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 551
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
317-374 4.23e-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: 4.23e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477694 317 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQR 374
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
236-290 4.39e-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: 78.12  E-value: 4.39e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477694 236 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 290
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
114-353 2.48e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 2.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  114 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 191
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  192 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 261
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  262 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 341
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921
                          250
                   ....*....|..
gi 2028477694  342 EAAASLSLTLQK 353
Cdd:TIGR02168  922 EKLAQLELRLEG 933
 
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 ...
417-551 7.93e-62

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: 199.44  E-value: 7.93e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 417 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 496
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477694 497 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 551
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
317-374 4.23e-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: 4.23e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477694 317 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQR 374
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
236-290 4.39e-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: 78.12  E-value: 4.39e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477694 236 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 290
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
114-353 2.48e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 2.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  114 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 191
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  192 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 261
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  262 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 341
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921
                          250
                   ....*....|..
gi 2028477694  342 EAAASLSLTLQK 353
Cdd:TIGR02168  922 EKLAQLELRLEG 933
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
107-390 1.03e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 107 QAEQRVMSRVHSLERRLEALAAEFSS-NWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREaalkedfRR 185
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-------RR 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 186 ETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSewqsmtQESFQESSVKELRRLEDQLAGLQQELAALA 265
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE------AEAELAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 266 LKQSSVAEEVGLLPQQIQAVRDDVESqfpawISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAAA 345
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEA-----LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2028477694 346 SLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESG 390
Cdd:COG1196   461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
PRK12704 PRK12704
phosphodiesterase; Provisional
173-389 4.20e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 173 SRREAalkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQ-ESSVKELRRLE 251
Cdd:PRK12704   47 AKKEA---EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEElEKKEKELEQKQ 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 252 DQLAGLQQELAALALKQSSVAEEV-GLLPQQI-QAVRDDVESQFpawisqflarggggrvgllqREEMQAQLRELESKil 329
Cdd:PRK12704  124 QELEKKEEELEELIEEQLQELERIsGLTAEEAkEILLEKVEEEA--------------------RHEAAVLIKEIEEE-- 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2028477694 330 thvAEMQG-KSAREaaaslsltlqkegvigvteeqvhhIVKQALQRYSedriglADYALES 389
Cdd:PRK12704  182 ---AKEEAdKKAKE------------------------ILAQAIQRCA------ADHVAET 209
 
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 ...
417-551 7.93e-62

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: 199.44  E-value: 7.93e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 417 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 496
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477694 497 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 551
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
317-374 4.23e-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: 4.23e-23
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477694 317 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQR 374
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
236-290 4.39e-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: 78.12  E-value: 4.39e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477694 236 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 290
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SUN_cc1 cd21435
coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 ...
236-290 2.52e-10

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: 56.26  E-value: 2.52e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477694 236 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 290
Cdd:cd21435     1 QEAFQESSVKELGRLEAQLASLRQELAALTLKQEAIQKELEQTKQKTISAVGEQL 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
114-353 2.48e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.99  E-value: 2.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  114 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 191
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  192 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 261
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  262 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 341
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921
                          250
                   ....*....|..
gi 2028477694  342 EAAASLSLTLQK 353
Cdd:TIGR02168  922 EKLAQLELRLEG 933
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
107-390 1.03e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 107 QAEQRVMSRVHSLERRLEALAAEFSS-NWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREaalkedfRR 185
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-------RR 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 186 ETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSewqsmtQESFQESSVKELRRLEDQLAGLQQELAALA 265
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE------AEAELAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 266 LKQSSVAEEVGLLPQQIQAVRDDVESqfpawISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAAA 345
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEA-----LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2028477694 346 SLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESG 390
Cdd:COG1196   461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
98-350 5.50e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.06  E-value: 5.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694   98 EARDSSPHFQAEQRVMSRVHSLERRLEALaaefssnwQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREA 177
Cdd:COG4913    219 EEPDTFEAADALVEHFDDLERAHEALEDA--------REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  178 ALKE---DFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfqessvkeLRRLEDQL 254
Cdd:COG4913    291 ELLEaelEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE---------LEERERRR 361
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  255 AGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAE 334
Cdd:COG4913    362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
                          250
                   ....*....|....*..
gi 2028477694  335 MQgkSAREA-AASLSLT 350
Cdd:COG4913    442 LL--ALRDAlAEALGLD 456
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
165-323 8.37e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.68  E-value: 8.37e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  165 LALLEGLVSRREAALKE-DFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQEseARIQQLKSEWQSMtqesfqESS 243
Cdd:COG4913    612 LAALEAELAELEEELAEaEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE--REIAELEAELERL------DAS 683
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  244 VKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVR----------DDVESQFPAWISQFLARGGGGRVGLLQ 313
Cdd:COG4913    684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeeldelqdrlEAAEDLARLELRALLEERFAAALGDAV 763
                          170
                   ....*....|
gi 2028477694  314 REEMQAQLRE 323
Cdd:COG4913    764 ERELRENLEE 773
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
114-328 1.21e-04

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: 45.06  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  114 SRVHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREA----------ALKEDF 183
Cdd:TIGR02169  709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEdlhkleealnDLEARL 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  184 RRETAARIQEELSALRAEHQqdsedlfkKIVRASQESEARIQQLKSEWQSMTQESfqESSVKELRRLEDQLAGLQQELAA 263
Cdd:TIGR02169  789 SHSRIPEIQAELSKLEEEVS--------RIEARLREIEQKLNRLTLEKEYLEKEI--QELQEQRIDLKEQIKSIEKEIEN 858
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2028477694  264 LALKQSSVAEEVgllpQQIQAVRDDVESQFpawisqflarggggRVGLLQREEMQAQLRELESKI 328
Cdd:TIGR02169  859 LNGKKEELEEEL----EELEAALRDLESRL--------------GDLKKERDELEAQLRELERKI 905
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
162-396 1.85e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 44.24  E-value: 1.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 162 EDTLALLEGLVSRREAALkEDFRR--------ETAARIQEELSALRAEHQQDSEDLfkkivrasQESEARIQQLKSEWQS 233
Cdd:COG3206   181 EEQLPELRKELEEAEAAL-EEFRQknglvdlsEEAKLLLQQLSELESQLAEARAEL--------AEAEARLAALRAQLGS 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 234 MTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQfpawisqflaRGGGGRVGLLQ 313
Cdd:COG3206   252 GPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE----------AQRILASLEAE 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 314 REEMQAQLRELESKIlthvAEMQGKSAREAAASLSLT-LQKEgvIGVTEEqvhhIVKQALQRYSEDRIglaDYALESGGA 392
Cdd:COG3206   322 LEALQAREASLQAQL----AQLEARLAELPELEAELRrLERE--VEVARE----LYESLLQRLEEARL---AEALTVGNV 388

                  ....
gi 2028477694 393 SVIS 396
Cdd:COG3206   389 RVID 392
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
110-344 2.36e-04

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: 44.28  E-value: 2.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  110 QRVMSRVHSLERRLEALAAEFssnwQKEAMRLERLELRQGApgqggggglsHEDTLALLEGLVSRREAALKEDFRR---- 185
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQI----------LRERLANLERQLEELEAQLEELESKldel 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  186 -ETAARIQEELSALRAEHQQDSEDLfKKIVRASQESEARIQQLKSEWQSMTQESFQ------------ESSVKELRRLED 252
Cdd:TIGR02168  336 aEELAELEEKLEELKEELESLEAEL-EELEAELEELESRLEELEEQLETLRSKVAQlelqiaslnneiERLEARLERLED 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  253 QLAGLQQELAALALKQSSVA-EEVGLLPQQIQAVRDDVESQFPAWIsqflarggggrvglLQREEMQAQLRELESKILTH 331
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLE--------------EALEELREELEEAEQALDAA 480
                          250
                   ....*....|...
gi 2028477694  332 VAEMQGKSAREAA 344
Cdd:TIGR02168  481 ERELAQLQARLDS 493
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
178-374 3.24e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 178 ALKEDFRRETAARIQEELSALRAEhqqdsedlfkkivraSQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGL 257
Cdd:COG3206   167 ELRREEARKALEFLEEQLPELRKE---------------LEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEA 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 258 QQELAALALKQSSVAEEVGLLPQQIQAVRDD------------VESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELE 325
Cdd:COG3206   232 RAELAEAEARLAALRAQLGSGPDALPELLQSpviqqlraqlaeLEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA 311
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2028477694 326 SKILTHV-AEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHivkQALQR 374
Cdd:COG3206   312 QRILASLeAELEALQAREASLQAQLAQLEARLAELPELEAEL---RRLER 358
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
175-388 3.44e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 175 REAALKEDFRRETAARIQEELSALRAEHQQDSEDLfkkivrasQESEARIQQLKSEWQSMTQESfqESSVKELRRLEDQL 254
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAEL--------AELEAELEELRLELEELELEL--EEAQAEEYELLAEL 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 255 AGLQQELAALALKQSSVAEEVGLLPQQIQ---AVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTH 331
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAeleEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2028477694 332 VAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHivKQALQRYSEDRIGLADYALE 388
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEAL--LERLERLEEELEELEEALAE 432
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
140-325 4.60e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.22  E-value: 4.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 140 RLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREA--ALKEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRAS 217
Cdd:COG4717   315 ELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELlrEAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQA 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 218 QES---EARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQfp 294
Cdd:COG4717   395 EEYqelKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELA-- 472
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2028477694 295 awisqflarggggrVGLLQREEMQAQLRELE 325
Cdd:COG4717   473 --------------ELLQELEELKAELRELA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
118-328 6.65e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 6.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 118 SLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTL-ALLEGLVSRREAALKEDFRRETAARIQEELS 196
Cdd:COG1196   580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLvAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 197 ALRAEHQQdsedlfkkivRASQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEvg 276
Cdd:COG1196   660 GSLTGGSR----------RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE-- 727
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2028477694 277 llpQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKI 328
Cdd:COG1196   728 ---EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
115-380 2.17e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 115 RVHSLERRLEALAAEFSsNWQKEAMRLERLE--LRQGAPGQGGGGGLSHEDTL--ALLEGLVSRREAALKEDFRRETAAR 190
Cdd:COG4717    96 ELEELEEELEELEAELE-ELREELEKLEKLLqlLPLYQELEALEAELAELPERleELEERLEELRELEEELEELEAELAE 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 191 IQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfQESSVKELRRLEDQLAGLQQE---------- 260
Cdd:COG4717   175 LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE--LEELEEELEQLENELEAAALEerlkearlll 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 261 -----LAALALKQSSVAEEVGLLPQQIQAVrddveSQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEM 335
Cdd:COG4717   253 liaaaLLALLGLGGSLLSLILTIAGVLFLV-----LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAA 327
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2028477694 336 QGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRI 380
Cdd:COG4717   328 LGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
119-276 2.52e-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: 40.82  E-value: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  119 LERRLEALAAEFSSNWQKEAMRLERLElrqgapgQGGGGGLSHEDTLALLEGLVSRREAALKEdfRRETAARIQEELSAL 198
Cdd:TIGR02169  369 LRAELEEVDKEFAETRDELKDYREKLE-------KLKREINELKRELDRLQEELQRLSEELAD--LNAAIAGIEAKINEL 439
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477694  199 RAEhqqdSEDLFKKIvrasQESEARIQQLKSEWQSMTQESFQESSvkELRRLEDQLAGLQQELAALALKQSSVAEEVG 276
Cdd:TIGR02169  440 EEE----KEDKALEI----KKQEWKLEQLAADLSKYEQELYDLKE--EYDRVEKELSKLQRELAEAEAQARASEERVR 507
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
109-264 3.79e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 3.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 109 EQRVMSRVHSLERRLEALAAEFSsnwQKEAmRLERLELRQGAPGQGGGGGLSHEDTLALLEGL--VSRREAALKEDFRRE 186
Cdd:COG3206   214 AKLLLQQLSELESQLAEARAELA---EAEA-RLAALRAQLGSGPDALPELLQSPVIQQLRAQLaeLEAELAELSARYTPN 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 187 --TAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfqessVKELRRLEDQLAGLQQELAAL 264
Cdd:COG3206   290 hpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR------LAELPELEAELRRLEREVEVA 363
PRK12704 PRK12704
phosphodiesterase; Provisional
173-389 4.20e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 173 SRREAalkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQ-ESSVKELRRLE 251
Cdd:PRK12704   47 AKKEA---EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEElEKKEKELEQKQ 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694 252 DQLAGLQQELAALALKQSSVAEEV-GLLPQQI-QAVRDDVESQFpawisqflarggggrvgllqREEMQAQLRELESKil 329
Cdd:PRK12704  124 QELEKKEEELEELIEEQLQELERIsGLTAEEAkEILLEKVEEEA--------------------RHEAAVLIKEIEEE-- 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2028477694 330 thvAEMQG-KSAREaaaslsltlqkegvigvteeqvhhIVKQALQRYSedriglADYALES 389
Cdd:PRK12704  182 ---AKEEAdKKAKE------------------------ILAQAIQRCA------ADHVAET 209
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
168-328 4.58e-03

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: 40.04  E-value: 4.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  168 LEGLVSRREAALKE-DFRRETAARIQEELSALRAEH---QQDSEDLFKKIVRASQESEARIQQLKSewqsmtQESFQESS 243
Cdd:TIGR02168  826 LESLERRIAATERRlEDLEEQIEELSEDIESLAAEIeelEELIEELESELEALLNERASLEEALAL------LRSELEEL 899
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477694  244 VKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQfpaWISQFLARGGGGRVGLLQREEMQAQLRE 323
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE---YSLTLEEAEALENKIEDDEEEARRRLKR 976

                   ....*
gi 2028477694  324 LESKI 328
Cdd:TIGR02168  977 LENKI 981
PRK11281 PRK11281
mechanosensitive channel MscK;
194-262 7.20e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.51  E-value: 7.20e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2028477694  194 ELSALRAEHQQDSEDLFKKIVRASQ---ESEARIQQLKSEWQSMTQESFQESSvkeLRRLEDQLAGLQQELA 262
Cdd:PRK11281    70 ALLDKIDRQKEETEQLKQQLAQAPAklrQAQAELEALKDDNDEETRETLSTLS---LRQLESRLAQTLDQLQ 138
 
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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