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Conserved domains on  [gi|2028477725|ref|NP_001381365|]
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SUN domain-containing protein 2 isoform 6 [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 ...
 580-714 1.33e-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: 199.44  E-value: 1.33e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 580 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 659
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477725 660 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 714
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
 481-537 2.62e-22

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: 90.47  E-value: 2.62e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477725 481 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEE-VHHIVKQALQR 537
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEqVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
 400-454 2.14e-19

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: 81.97  E-value: 2.14e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477725 400 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 454
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 278-517 4.00e-09

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: 60.07  E-value: 4.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  278 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 355
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  356 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 425
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  426 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 505
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921

                          250
                   ....*....|..
gi 2028477725  506 EAAASLSLTLQK 517
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 ...
 580-714 1.33e-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: 199.44  E-value: 1.33e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 580 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 659
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477725 660 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 714
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
 481-537 2.62e-22

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: 90.47  E-value: 2.62e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477725 481 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEE-VHHIVKQALQR 537
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEqVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
 400-454 2.14e-19

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: 81.97  E-value: 2.14e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477725 400 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 454
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 278-517 4.00e-09

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: 60.07  E-value: 4.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  278 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 355
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  356 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 425
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  426 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 505
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921

                          250
                   ....*....|..
gi 2028477725  506 EAAASLSLTLQK 517
Cdd:TIGR02168  922 EKLAQLELRLEG 933
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
262-458 3.71e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 3.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  262 EARDSSPHFQAEQRVmsrvHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHE-DTLALLEGLVSRRE 340
Cdd:COG4913    276 YLRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLE 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  341 AALKEdfRRETAARIQEELSALRAEHQQDSEDLfkkiVRASQESEARIQQLKSEWQSMTQESFQesSVKELRRLEDQLAG 420
Cdd:COG4913    352 RELEE--RERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEELEALEEALAE--AEAALRDLRRELRE 423

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2028477725  421 LQQELAALALKQSSvaeevglLPQQIQAVRDDVESQFP 458
Cdd:COG4913    424 LEAEIASLERRKSN-------IPARLLALRDALAEALG 454
PRK12704 PRK12704
phosphodiesterase; Provisional
 337-552 5.51e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 337 SRREAalkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQ-ESSVKELRRLE 415
Cdd:PRK12704   47 AKKEA---EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEElEKKEKELEQKQ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 416 DQLAGLQQELAALALKQSSVAEEV-GLLPQQI-QAVRDDVESQFpawisqflarggggrvgllqREEMQAQLRELESKil 493
Cdd:PRK12704  124 QELEKKEEELEELIEEQLQELERIsGLTAEEAkEILLEKVEEEA--------------------RHEAAVLIKEIEEE-- 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 494 thvAEMQG-KSAREaaaslsltlqkegvigvteevhhIVKQALQRYSedriglADYALES 552
Cdd:PRK12704  182 ---AKEEAdKKAKE-----------------------ILAQAIQRCA------ADHVAET 209
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 326-509 4.39e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 38.78  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 326 EDTLALLEGLVSRREAALkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQ----LKSEWQSMTQE 401
Cdd:pfam01442   3 EDSLDELSTYAEELQEQL-GPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQnveeLRQRLEPYTEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 402 sFQESSVKELRRLEDQLAGLQQELaalalkQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFlarggggrvgllqREEM 481
Cdd:pfam01442  82 -LRKRLNADAEELQEKLAPYGEEL------RERLEQNVDALRARLAPYAEELRQKLAERLEEL-------------KESL 141

                         170       180
                  ....*....|....*....|....*...
gi 2028477725 482 QAQLRELESKILTHVAEMQGKSAREAAA 509
Cdd:pfam01442 142 APYAEEVQAQLSQRLQELREKLEPQAED 169
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 360-456 5.52e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 360 SALRAEHQQDSEDLFKKIvrasQESEARIQQLKSEwqsmtqesfQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEV 439
Cdd:COG4942    19 ADAAAEAEAELEQLQQEI----AELEKELAALKKE---------EKALLKQLAALERRIAALARRIRALEQELAALEAEL 85

                          90
                  ....*....|....*..
gi 2028477725 440 GLLPQQIQAVRDDVESQ 456
Cdd:COG4942    86 AELEKEIAELRAELEAQ 102
 
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 ...
 580-714 1.33e-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: 199.44  E-value: 1.33e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 580 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 659
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477725 660 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 714
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
 481-537 2.62e-22

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: 90.47  E-value: 2.62e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477725 481 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEE-VHHIVKQALQR 537
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEqVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
 400-454 2.14e-19

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: 81.97  E-value: 2.14e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477725 400 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 454
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SUN_cc1 cd21435
coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 ...
 400-454 1.34e-11

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: 60.11  E-value: 1.34e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477725 400 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 454
Cdd:cd21435     1 QEAFQESSVKELGRLEAQLASLRQELAALTLKQEAIQKELEQTKQKTISAVGEQL 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 278-517 4.00e-09

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: 60.07  E-value: 4.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  278 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 355
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  356 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 425
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  426 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 505
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921

                          250
                   ....*....|..
gi 2028477725  506 EAAASLSLTLQK 517
Cdd:TIGR02168  922 EKLAQLELRLEG 933
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
262-458 3.71e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.77  E-value: 3.71e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  262 EARDSSPHFQAEQRVmsrvHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHE-DTLALLEGLVSRRE 340
Cdd:COG4913    276 YLRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLE 351

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  341 AALKEdfRRETAARIQEELSALRAEHQQDSEDLfkkiVRASQESEARIQQLKSEWQSMTQESFQesSVKELRRLEDQLAG 420
Cdd:COG4913    352 RELEE--RERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEELEALEEALAE--AEAALRDLRRELRE 423

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 2028477725  421 LQQELAALALKQSSvaeevglLPQQIQAVRDDVESQFP 458
Cdd:COG4913    424 LEAEIASLERRKSN-------IPARLLALRDALAEALG 454
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 271-555 4.81e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 4.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 271 QAEQRVMSRVHSLERRLEALAAEFSS-NWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREaalkedfRR 349
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-------RR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 350 ETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLK-SEWQSMTQESFQESSVKELRRLEDQLAGLQQELAAL 428
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEeAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 429 ALKQSSVAEEVGLLPQQIQAVRDDVESQfpawISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAA 508
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERL----EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAE 467

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2028477725 509 ASLSLTLQKEGVIGVTEEVHhivkQALQRYSEDRIGLADYALESGGA 555
Cdd:COG1196   468 LLEEAALLEAALAELLEELA----EAAARLLLLLEAEADYEGFLEGV 510
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
326-559 6.29e-06

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 6.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 326 EDTLALLEGLVSRREAALkEDFRR--------ETAARIQEELSALRAEHQQDSEDLfkkivrasQESEARIQQLKSEWQS 397
Cdd:COG3206   181 EEQLPELRKELEEAEAAL-EEFRQknglvdlsEEAKLLLQQLSELESQLAEARAEL--------AEAEARLAALRAQLGS 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 398 MTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQfpawISQFLARGGGgrvgllQ 477
Cdd:COG3206   252 GPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE----AQRILASLEA------E 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 478 REEMQAQLRELESKIlthvAEMQGKSAREAAASLSLT-LQKEgvIGVTEEVHhivKQALQRYSEDRIglaDYALESGGAS 556
Cdd:COG3206   322 LEALQAREASLQAQL----AQLEARLAELPELEAELRrLERE--VEVARELY---ESLLQRLEEARL---AEALTVGNVR 389


                  ...
gi 2028477725 557 VIS 559
Cdd:COG3206   390 VID 392
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 278-516 2.70e-05

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: 47.76  E-value: 2.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  278 SRVHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREAA----------LKEDF 347
Cdd:TIGR02169  709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDlhkleealndLEARL 788

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  348 RRETAARIQEELSALRAEHQqdsedlfkKIVRASQESEARIQQLKSEWQSMTQESfqESSVKELRRLEDQLAGLQQELAA 427
Cdd:TIGR02169  789 SHSRIPEIQAELSKLEEEVS--------RIEARLREIEQKLNRLTLEKEYLEKEI--QELQEQRIDLKEQIKSIEKEIEN 858

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  428 LALKQSSVAEEVgllpQQIQAVRDDVESQFpawisqflarggggRVGLLQREEMQAQLRELESKILThvAEMQGKSAREA 507
Cdd:TIGR02169  859 LNGKKEELEEEL----EELEAALRDLESRL--------------GDLKKERDELEAQLRELERKIEE--LEAQIEKKRKR 918


                   ....*....
gi 2028477725  508 AASLSLTLQ 516
Cdd:TIGR02169  919 LSELKAKLE 927
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 274-508 3.15e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 3.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  274 QRVMSRVHSLERRLEALAAEFssnwQKEAMRLERLELRQGApgqggggglsHEDTLALLEGLVSRREAALKEDFRR---- 349
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQI----------LRERLANLERQLEELEAQLEELESKldel 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  350 -ETAARIQEELSALRAEHQQDSEDLfKKIVRASQESEARIQQLKSEWQSMTQESFQ------------ESSVKELRRLED 416
Cdd:TIGR02168  336 aEELAELEEKLEELKEELESLEAEL-EELEAELEELESRLEELEEQLETLRSKVAQlelqiaslnneiERLEARLERLED 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  417 QLAGLQQELAALALKQSSVA-EEVGLLPQQIQAVRDDVESQFPAWIsqflarggggrvglLQREEMQAQLRELESKILTH 495
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLE--------------EALEELREELEEAEQALDAA 480

                          250
                   ....*....|...
gi 2028477725  496 VAEMQGKSAREAA 508
Cdd:TIGR02168  481 ERELAQLQARLDS 493
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
329-487 3.67e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 3.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  329 LALLEGLVSRREAALKE-DFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQEseARIQQLKSEWQSMtqesfqESS 407
Cdd:COG4913    612 LAALEAELAELEEELAEaEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE--REIAELEAELERL------DAS 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  408 VKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVR----------DDVESQFPAWISQFLARGGGGRVGLLQ 477
Cdd:COG4913    684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeeldelqdrlEAAEDLARLELRALLEERFAAALGDAV 763

                          170
                   ....*....|
gi 2028477725  478 REEMQAQLRE 487
Cdd:COG4913    764 ERELRENLEE 773
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
283-489 4.76e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 46.68  E-value: 4.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 283 LERRLEALAAEFSSNWQKEAM-RLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREA--ALKEDFRRETAARIQEEL 359
Cdd:COG4717   293 LAREKASLGKEAEELQALPALeELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELlrEAEELEEELQLEELEQEI 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 360 SALRAEHQQDSEDLFKKIVRASQES---EARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVA 436
Cdd:COG4717   373 AALLAEAGVEDEEELRAALEQAEEYqelKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR 452

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2028477725 437 EEVGLLPQQIQAVRDDVEsqfpawISQFLArggggrvgllQREEMQAQLRELE 489
Cdd:COG4717   453 EELAELEAELEQLEEDGE------LAELLQ----------ELEELKAELRELA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 339-551 9.03e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 9.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 339 REAALKEDFRRETAARIQEELSALRAEHQQDSEDLfkkivrasQESEARIQQLKSEWQSMTQESfqESSVKELRRLEDQL 418
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAEL--------AELEAELEELRLELEELELEL--EEAQAEEYELLAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 419 AGLQQELAALALKQSSVAEEVGLLPQQIQ---AVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTH 495
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAeleEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2028477725 496 VAEMQGKsAREAAASLSLTLQKEGVIGVTEEVHHIVKQALQRYSEDRIGLADYALE 551
Cdd:COG1196   378 EEELEEL-AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAE 432
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
262-492 9.28e-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: 9.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  262 EARDSSPHFQAEQRVMSRVHSLERRLEALaaefssnwQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREA 341
Cdd:COG4913    219 EEPDTFEAADALVEHFDDLERAHEALEDA--------REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  342 ALKE---DFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfqessvkeLRRLEDQL 418
Cdd:COG4913    291 ELLEaelEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE---------LEERERRR 361

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2028477725  419 AGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFpAWISQFLARGGGgrvgllQREEMQAQLRELESKI 492
Cdd:COG4913    362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEEL-EALEEALAEAEA------ALRDLRRELRELEAEI 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 282-492 2.43e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 282 SLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTL-ALLEGLVSRREAALKEDFRRETAARIQEELS 360
Cdd:COG1196   580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLvAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 361 ALRAEHQQdsedlfkkivRASQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEvg 440
Cdd:COG1196   660 GSLTGGSR----------RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE-- 727

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2028477725 441 llpQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKI 492
Cdd:COG1196   728 ---EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
262-543 2.58e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 262 EARDSSPHFQAEQRvmsRVHSLERRLEALAAEFSsNWQKEAMRLERLE--LRQGAPGQGGGGGLSHEDTL--ALLEGLVS 337
Cdd:COG4717    82 EAEEKEEEYAELQE---ELEELEEELEELEAELE-ELREELEKLEKLLqlLPLYQELEALEAELAELPERleELEERLEE 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 338 RREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfQESSVKELRRLEDQ 417
Cdd:COG4717   158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE--LEELEEELEQLENE 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 418 LAGLQQE---------------LAALALKQSSVAEEVGLLPQQIQAVrddveSQFPAWISQFLARGGGGRVGLLQREEMQ 482
Cdd:COG4717   236 LEAAALEerlkearlllliaaaLLALLGLGGSLLSLILTIAGVLFLV-----LGLLALLFLLLAREKASLGKEAEELQAL 310

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2028477725 483 AQLRELESKILTHVAEMQGKSAREAAASLSLTLQK-EGVIGVTEEVHHIVKQALQRYSEDRI 543
Cdd:COG4717   311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRiEELQELLREAEELEEELQLEELEQEI 372
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
342-518 3.37e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 342 ALKEDFRRETAARIQEELSALRAEhqqdsedlfkkivraSQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGL 421
Cdd:COG3206   167 ELRREEARKALEFLEEQLPELRKE---------------LEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEA 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 422 QQELAALALKQSSVAEEVGLLPQQIQAVRDD------------VESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELE 489
Cdd:COG3206   232 RAELAEAEARLAALRAQLGSGPDALPELLQSpviqqlraqlaeLEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA 311

                         170       180       190
                  ....*....|....*....|....*....|
gi 2028477725 490 SKILTHV-AEMQGKSAREAAASLSLTLQKE 518
Cdd:COG3206   312 QRILASLeAELEALQAREASLQAQLAQLEA 341
PRK12704 PRK12704
phosphodiesterase; Provisional
 337-552 5.51e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 43.23  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 337 SRREAalkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQ-ESSVKELRRLE 415
Cdd:PRK12704   47 AKKEA---EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEElEKKEKELEQKQ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 416 DQLAGLQQELAALALKQSSVAEEV-GLLPQQI-QAVRDDVESQFpawisqflarggggrvgllqREEMQAQLRELESKil 493
Cdd:PRK12704  124 QELEKKEEELEELIEEQLQELERIsGLTAEEAkEILLEKVEEEA--------------------RHEAAVLIKEIEEE-- 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 494 thvAEMQG-KSAREaaaslsltlqkegvigvteevhhIVKQALQRYSedriglADYALES 552
Cdd:PRK12704  182 ---AKEEAdKKAKE-----------------------ILAQAIQRCA------ADHVAET 209
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 283-440 6.98e-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: 43.13  E-value: 6.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  283 LERRLEALAAEFSSNWQKEAMRLERLElrqgapgQGGGGGLSHEDTLALLEGLVSRREAALKEdfRRETAARIQEELSAL 362
Cdd:TIGR02169  369 LRAELEEVDKEFAETRDELKDYREKLE-------KLKREINELKRELDRLQEELQRLSEELAD--LNAAIAGIEAKINEL 439

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477725  363 RAEhqqdSEDLFKKIvrasQESEARIQQLKSEWQSMTQESFQESSvkELRRLEDQLAGLQQELAALALKQSSVAEEVG 440
Cdd:TIGR02169  440 EEE----KEDKALEI----KKQEWKLEQLAADLSKYEQELYDLKE--EYDRVEKELSKLQRELAEAEAQARASEERVR 507
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
273-428 1.24e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 273 EQRVMSRVHSLERRLEALAAEFSsnwQKEAmRLERLELRQGAPGQGGGGGLSHEDTLALLEGL--VSRREAALKEDFRRE 350
Cdd:COG3206   214 AKLLLQQLSELESQLAEARAELA---EAEA-RLAALRAQLGSGPDALPELLQSPVIQQLRAQLaeLEAELAELSARYTPN 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 351 --TAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfqessVKELRRLEDQLAGLQQELAAL 428
Cdd:COG3206   290 hpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR------LAELPELEAELRRLEREVEVA 363
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 270-492 1.26e-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: 42.35  E-value: 1.26e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  270 FQAEQRVMSRVHSLERRLEALAAEFSSNwqKEAMRLERLELRQGAPGQGgggglsheDTLALLEGLVSRREAALKE-DFR 348
Cdd:TIGR02168  774 EEELAEAEAEIEELEAQIEQLKEELKAL--REALDELRAELTLLNEEAA--------NLRERLESLERRIAATERRlEDL 843

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  349 RETAARIQEELSALRAEH---QQDSEDLFKKIVRASQESEARIQQLKSewqsmtQESFQESSVKELRRLEDQLAGLQQEL 425
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIeelEELIEELESELEALLNERASLEEALAL------LRSELEELSEELRELESKRSELRREL 917

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2028477725  426 AALALKQSSVAEEVGLLPQQIQAVRDDVESQfpaWISQFLARGGGGRVGLLQREEMQAQLRELESKI 492
Cdd:TIGR02168  918 EELREKLAQLELRLEGLEVRIDNLQERLSEE---YSLTLEEAEALENKIEDDEEEARRRLKRLENKI 981
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
337-448 3.90e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 3.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 337 SRREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFK---KIVRASQESEARIQQLKS--EWQSMTQESFQESSvKEL 411
Cdd:COG4372    32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarsELEQLEEELEELNEQLQAaqAELAQAQEELESLQ-EEA 110

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2028477725 412 RRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQA 448
Cdd:COG4372   111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 326-509 4.39e-03

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.


Pssm-ID: 460211 [Multi-domain]  Cd Length: 175  Bit Score: 38.78  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 326 EDTLALLEGLVSRREAALkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQ----LKSEWQSMTQE 401
Cdd:pfam01442   3 EDSLDELSTYAEELQEQL-GPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQnveeLRQRLEPYTEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 402 sFQESSVKELRRLEDQLAGLQQELaalalkQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFlarggggrvgllqREEM 481
Cdd:pfam01442  82 -LRKRLNADAEELQEKLAPYGEEL------RERLEQNVDALRARLAPYAEELRQKLAERLEEL-------------KESL 141

                         170       180
                  ....*....|....*....|....*...
gi 2028477725 482 QAQLRELESKILTHVAEMQGKSAREAAA 509
Cdd:pfam01442 142 APYAEEVQAQLSQRLQELREKLEPQAED 169
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 360-456 5.52e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.75  E-value: 5.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 360 SALRAEHQQDSEDLFKKIvrasQESEARIQQLKSEwqsmtqesfQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEV 439
Cdd:COG4942    19 ADAAAEAEAELEQLQQEI----AELEKELAALKKE---------EKALLKQLAALERRIAALARRIRALEQELAALEAEL 85

                          90
                  ....*....|....*..
gi 2028477725 440 GLLPQQIQAVRDDVESQ 456
Cdd:COG4942    86 AELEKEIAELRAELEAQ 102
PRK11281 PRK11281
mechanosensitive channel MscK;
358-426 6.42e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.89  E-value: 6.42e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2028477725  358 ELSALRAEHQQDSEDLFKKIVRASQ---ESEARIQQLKSEWQSMTQESFQESSvkeLRRLEDQLAGLQQELA 426
Cdd:PRK11281    70 ALLDKIDRQKEETEQLKQQLAQAPAklrQAQAELEALKDDNDEETRETLSTLS---LRQLESRLAQTLDQLQ 138
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 266-466 7.93e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.57  E-value: 7.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  266 SSPHFQAEQRVM-SRVHSLERRLEALAAEfssnwQKEAMRLERLELRQGAPGQGGggglSHEDTLALLEGLVSRREAALK 344
Cdd:TIGR00618  716 YDREFNEIENASsSLGSDLAAREDALNQS-----LKELMHQARTVLKARTEAHFN----NNEEVTAALQTGAELSHLAAE 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  345 EDFRRETAARIQEELSALRAEHQQDSEDlFKKIVRASQESEA-RIQQLKSEWQSMTQesfqesSVKELRRLEDQLAGLQQ 423
Cdd:TIGR00618  787 IQFFNRLREEDTHLLKTLEAEIGQEIPS-DEDILNLQCETLVqEEEQFLSRLEEKSA------TLGEITHQLLKYEECSK 859

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2028477725  424 ELAALALKQSSVAEEVGLLpqqiqAVRDDVESQFPAWISQFLA 466
Cdd:TIGR00618  860 QLAQLTQEQAKIIQLSDKL-----NGINQIKIQFDGDALIKFL 897
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
260-493 8.24e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 8.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  260 GWEARDSSPHFQAE-QRVMSRVHSLERRLEALAAEfSSNWQKEAMRLERLElrqgAPGQGGGGGLSHEDTLALLEglvSR 338
Cdd:COG4913    605 GFDNRAKLAALEAElAELEEELAEAEERLEALEAE-LDALQERREALQRLA----EYSWDEIDVASAEREIAELE---AE 676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725  339 REAALKEDfrrETAARIQEELSALRAEHQQDSEDLFKKIVRASQEsEARIQQLKSEWQS--MTQESFQESSVKELR-RLE 415
Cdd:COG4913    677 LERLDASS---DDLAALEEQLEELEAELEELEEELDELKGEIGRL-EKELEQAEEELDElqDRLEAAEDLARLELRaLLE 752

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477725  416 DQLAGLQQElAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKIL 493
Cdd:COG4913    753 ERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGL 829
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 274-439 8.59e-03

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


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 38.37  E-value: 8.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 274 QRVMSRVHSLERRLEALAAEFSsnwQKEAmRLERLELRQGAPGQGGGgglSHEDTLALLEGLVSRREAALKEDFRRETAA 353
Cdd:COG1579    13 QELDSELDRLEHRLKELPAELA---ELED-ELAALEARLEAAKTELE---DLEKEIKRLELEIEEVEARIKKYEEQLGNV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 354 RIQEELSALRAE------HQQDSEDLFKKIVRASQESEARIQQLKSEWqsmtqESFQESSVKELRRLEDQLAGLQQELAA 427
Cdd:COG1579    86 RNNKEYEALQKEieslkrRISDLEDEILELMERIEELEEELAELEAEL-----AELEAELEEKKAELDEELAELEAELEE 160

                         170
                  ....*....|..
gi 2028477725 428 LALKQSSVAEEV 439
Cdd:COG1579   161 LEAEREELAAKI 172
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 345-449 8.76e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 39.29  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477725 345 EDFRREtAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQESSVKE-LRRLEDQLAGLQQ 423
Cdd:COG0542   414 DELERR-LEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEeLEQRYGKIPELEK 492

                          90       100       110
                  ....*....|....*....|....*....|
gi 2028477725 424 ELAA----LALKQSSVAEEVGllPQQIQAV 449
Cdd:COG0542   493 ELAEleeeLAELAPLLREEVT--EEDIAEV 520
 
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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