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Conserved domains on  [gi|2028477692|ref|NP_001381368|]
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SUN domain-containing protein 2 isoform 8 [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 ...
 535-669 6.85e-61

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: 6.85e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 535 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 614
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477692 615 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 669
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
 435-492 2.22e-24

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: 96.25  E-value: 2.22e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477692 435 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQR 492
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
 354-408 3.08e-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: 81.59  E-value: 3.08e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477692 354 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 408
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 232-471 4.04e-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: 4.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  232 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 309
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  310 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 379
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  380 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 459
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921

                          250
                   ....*....|..
gi 2028477692  460 EAAASLSLTLQK 471
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 ...
 535-669 6.85e-61

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: 6.85e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 535 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 614
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477692 615 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 669
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
 435-492 2.22e-24

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: 96.25  E-value: 2.22e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477692 435 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQR 492
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
 354-408 3.08e-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: 81.59  E-value: 3.08e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477692 354 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 408
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 232-471 4.04e-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: 4.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  232 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 309
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  310 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 379
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  380 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 459
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921

                          250
                   ....*....|..
gi 2028477692  460 EAAASLSLTLQK 471
Cdd:TIGR02168  922 EKLAQLELRLEG 933
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 225-508 3.86e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 225 QAEQRVMSRVHSLERRLEALAAEFSS-NWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREaalkedfRR 303
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-------RR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 304 ETAARIQEELSALRAEHQQDSEDLFKKIVRAsqesEARIQQLKSEWQSMTQEsfQESSVKELRRLEDQLAGLQQELAALA 383
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEEL----EEELEEAEEELEEAEAE--LAEAEEALLEAEAELAEAEEELEELA 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 384 LKQSSVAEEVGLLPQQIQAVRDDVESqfpawISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAAA 463
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEA-----LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2028477692 464 SLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESG 508
Cdd:COG1196   461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
PRK12704 PRK12704
phosphodiesterase; Provisional
 291-507 7.73e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 7.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 291 SRREAalkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQ-ESSVKELRRLE 369
Cdd:PRK12704   47 AKKEA---EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEElEKKEKELEQKQ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 370 DQLAGLQQELAALALKQSSVAEEV-GLLPQQI-QAVRDDVESQFpawisqflarggggrvgllqREEMQAQLRELESKil 447
Cdd:PRK12704  124 QELEKKEEELEELIEEQLQELERIsGLTAEEAkEILLEKVEEEA--------------------RHEAAVLIKEIEEE-- 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2028477692 448 thvAEMQG-KSAREaaaslsltlqkegvigvteeqvhhIVKQALQRYSedriglADYALES 507
Cdd:PRK12704  182 ---AKEEAdKKAKE------------------------ILAQAIQRCA------ADHVAET 209
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 280-463 5.29e-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: 38.40  E-value: 5.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 280 EDTLALLEGLVSRREAALkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQ----LKSEWQSMTQE 355
Cdd:pfam01442   3 EDSLDELSTYAEELQEQL-GPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQnveeLRQRLEPYTEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 356 sFQESSVKELRRLEDQLAGLQQELaalalkQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFlarggggrvgllqREEM 435
Cdd:pfam01442  82 -LRKRLNADAEELQEKLAPYGEEL------RERLEQNVDALRARLAPYAEELRQKLAERLEEL-------------KESL 141

                         170       180
                  ....*....|....*....|....*...
gi 2028477692 436 QAQLRELESKILTHVAEMQGKSAREAAA 463
Cdd:pfam01442 142 APYAEEVQAQLSQRLQELREKLEPQAED 169
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 314-410 6.67e-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: 39.36  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 314 SALRAEHQQDSEDLFKKIvrasQESEARIQQLKSEwqsmtqesfQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEV 393
Cdd:COG4942    19 ADAAAEAEAELEQLQQEI----AELEKELAALKKE---------EKALLKQLAALERRIAALARRIRALEQELAALEAEL 85

                          90
                  ....*....|....*..
gi 2028477692 394 GLLPQQIQAVRDDVESQ 410
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 ...
 535-669 6.85e-61

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: 6.85e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 535 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 614
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477692 615 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 669
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
 435-492 2.22e-24

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: 96.25  E-value: 2.22e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477692 435 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQR 492
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
 354-408 3.08e-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: 81.59  E-value: 3.08e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477692 354 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 408
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SUN_cc1 cd21435
coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 ...
 354-408 1.98e-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: 59.34  E-value: 1.98e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477692 354 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 408
Cdd:cd21435     1 QEAFQESSVKELGRLEAQLASLRQELAALTLKQEAIQKELEQTKQKTISAVGEQL 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 232-471 4.04e-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: 4.04e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  232 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 309
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  310 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 379
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  380 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 459
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921

                          250
                   ....*....|..
gi 2028477692  460 EAAASLSLTLQK 471
Cdd:TIGR02168  922 EKLAQLELRLEG 933
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 225-508 3.86e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 50.32  E-value: 3.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 225 QAEQRVMSRVHSLERRLEALAAEFSS-NWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREaalkedfRR 303
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-------RR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 304 ETAARIQEELSALRAEHQQDSEDLFKKIVRAsqesEARIQQLKSEWQSMTQEsfQESSVKELRRLEDQLAGLQQELAALA 383
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEEL----EEELEEAEEELEEAEAE--LAEAEEALLEAEAELAEAEEELEELA 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 384 LKQSSVAEEVGLLPQQIQAVRDDVESqfpawISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAAA 463
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEA-----LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2028477692 464 SLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESG 508
Cdd:COG1196   461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 232-470 2.27e-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: 2.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  232 SRVHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREAA----------LKEDF 301
Cdd:TIGR02169  709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDlhkleealndLEARL 788

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  302 RRETAARIQEELSALRAEHQqdsedlfkKIVRASQESEARIQQLKSEWQSMTQESfqESSVKELRRLEDQLAGLQQELAA 381
Cdd:TIGR02169  789 SHSRIPEIQAELSKLEEEVS--------RIEARLREIEQKLNRLTLEKEYLEKEI--QELQEQRIDLKEQIKSIEKEIEN 858

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  382 LALKQSSVAEEVgllpQQIQAVRDDVESQfpawisqflargggGRVGLLQREEMQAQLRELESKILThvAEMQGKSAREA 461
Cdd:TIGR02169  859 LNGKKEELEEEL----EELEAALRDLESR--------------LGDLKKERDELEAQLRELERKIEE--LEAQIEKKRKR 918


                   ....*....
gi 2028477692  462 AASLSLTLQ 470
Cdd:TIGR02169  919 LSELKAKLE 927
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 228-462 3.23e-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: 3.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  228 QRVMSRVHSLERRLEALAAEFssnwQKEAMRLERLELRQGApgqggggglsHEDTLALLEGLVSRREAALKEDFRR---- 303
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQI----------LRERLANLERQLEELEAQLEELESKldel 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  304 -ETAARIQEELSALRAEHQQDSEDLfKKIVRASQESEARIQQLKSEWQSMTQESFQ------------ESSVKELRRLED 370
Cdd:TIGR02168  336 aEELAELEEKLEELKEELESLEAEL-EELEAELEELESRLEELEEQLETLRSKVAQlelqiaslnneiERLEARLERLED 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  371 QLAGLQQELAALALKQSSVA-EEVGLLPQQIQAVRDDVESQFPAWIsqflarggggrvglLQREEMQAQLRELESKILTH 449
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLE--------------EALEELREELEEAEQALDAA 480

                          250
                   ....*....|...
gi 2028477692  450 VAEMQGKSAREAA 462
Cdd:TIGR02168  481 ERELAQLQARLDS 493
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
280-514 3.40e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 3.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 280 EDTLALLEGLVSRREAALkEDFRR--------ETAARIQEELSALRAEHQQDSEDLfkkivrasQESEARIQQLKSEWQS 351
Cdd:COG3206   181 EEQLPELRKELEEAEAAL-EEFRQknglvdlsEEAKLLLQQLSELESQLAEARAEL--------AEAEARLAALRAQLGS 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 352 MTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQfpawISQFLARGGGgrvgllQ 431
Cdd:COG3206   252 GPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE----AQRILASLEA------E 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 432 REEMQAQLRELESKIlthvAEMQGKSAREAAASLSLT-LQKEgvIGVTEEqvhhIVKQALQRYSEDRIglaDYALESGGA 510
Cdd:COG3206   322 LEALQAREASLQAQL----AQLEARLAELPELEAELRrLERE--VEVARE----LYESLLQRLEEARL---AEALTVGNV 388


                  ....
gi 2028477692 511 SVIS 514
Cdd:COG3206   389 RVID 392
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
216-468 3.42e-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: 3.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  216 EARDSSPHFQAEQRVMSRVHSLERRLEALaaefssnwQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREA 295
Cdd:COG4913    219 EEPDTFEAADALVEHFDDLERAHEALEDA--------REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  296 ALKE---DFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfqessvkeLRRLEDQL 372
Cdd:COG4913    291 ELLEaelEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE---------LEERERRR 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  373 AGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAE 452
Cdd:COG4913    362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441

                          250
                   ....*....|....*..
gi 2028477692  453 MQgkSAREA-AASLSLT 468
Cdd:COG4913    442 LL--ALRDAlAEALGLD 456
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
283-441 3.75e-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: 3.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  283 LALLEGLVSRREAALKE-DFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQEseARIQQLKSEWQSMtqesfqESS 361
Cdd:COG4913    612 LAALEAELAELEEELAEaEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE--REIAELEAELERL------DAS 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  362 VKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVR----------DDVESQFPAWISQFLARGGGGRVGLLQ 431
Cdd:COG4913    684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeeldelqdrlEAAEDLARLELRALLEERFAAALGDAV 763

                          170
                   ....*....|
gi 2028477692  432 REEMQAQLRE 441
Cdd:COG4913    764 ERELRENLEE 773
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
237-443 7.62e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 7.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 237 LERRLEALAAEFSSNWQKEAM-RLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREA--ALKEDFRRETAARIQEEL 313
Cdd:COG4717   293 LAREKASLGKEAEELQALPALeELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELlrEAEELEEELQLEELEQEI 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 314 SALRAEHQQDSEDLFKKIVRASQES---EARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVA 390
Cdd:COG4717   373 AALLAEAGVEDEEELRAALEQAEEYqelKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR 452

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2028477692 391 EEVGLLPQQIQAVRDDVESQfpawisqflarggggrVGLLQREEMQAQLRELE 443
Cdd:COG4717   453 EELAELEAELEQLEEDGELA----------------ELLQELEELKAELRELA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 293-506 1.14e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 293 REAALKEDFRRETAARIQEELSALRAEHQQDSEDLfkkivrasQESEARIQQLKSEWQSMTQESfqESSVKELRRLEDQL 372
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAEL--------AELEAELEELRLELEELELEL--EEAQAEEYELLAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 373 AGLQQELAALALKQSSVAEEVGLLPQQIQ---AVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTH 449
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAeleEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2028477692 450 VAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHivKQALQRYSEDRIGLADYALE 506
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEAL--LERLERLEEELEELEEALAE 432
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
296-492 1.27e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 296 ALKEDFRRETAARIQEELSALRAEhqqdsedlfkkivraSQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGL 375
Cdd:COG3206   167 ELRREEARKALEFLEEQLPELRKE---------------LEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEA 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 376 QQELAALALKQSSVAEEVGLLPQQIQAVRDD------------VESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELE 443
Cdd:COG3206   232 RAELAEAEARLAALRAQLGSGPDALPELLQSpviqqlraqlaeLEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA 311

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2028477692 444 SKILTHV-AEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHivkQALQR 492
Cdd:COG3206   312 QRILASLeAELEALQAREASLQAQLAQLEARLAELPELEAEL---RRLER 358
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 236-446 2.55e-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: 2.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 236 SLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTL-ALLEGLVSRREAALKEDFRRETAARIQEELS 314
Cdd:COG1196   580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLvAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 315 ALRAEHQQdsedlfkkivRASQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEvg 394
Cdd:COG1196   660 GSLTGGSR----------RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE-- 727

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2028477692 395 llpQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKI 446
Cdd:COG1196   728 ---EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
216-498 2.86e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 2.86e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 216 EARDSSPHFQAEQRvmsRVHSLERRLEALAAEFSsNWQKEAMRLERLE--LRQGAPGQGGGGGLSHEDTL--ALLEGLVS 291
Cdd:COG4717    82 EAEEKEEEYAELQE---ELEELEEELEELEAELE-ELREELEKLEKLLqlLPLYQELEALEAELAELPERleELEERLEE 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 292 RREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfQESSVKELRRLEDQ 371
Cdd:COG4717   158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE--LEELEEELEQLENE 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 372 LAGLQQE---------------LAALALKQSSVAEEVGLLPQQIQAVrddveSQFPAWISQFLARGGGGRVGLLQREEMQ 436
Cdd:COG4717   236 LEAAALEerlkearlllliaaaLLALLGLGGSLLSLILTIAGVLFLV-----LGLLALLFLLLAREKASLGKEAEELQAL 310

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2028477692 437 AQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRI 498
Cdd:COG4717   311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 237-394 5.99e-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: 5.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  237 LERRLEALAAEFSSNWQKEAMRLERLElrqgapgQGGGGGLSHEDTLALLEGLVSRREAALKEdfRRETAARIQEELSAL 316
Cdd:TIGR02169  369 LRAELEEVDKEFAETRDELKDYREKLE-------KLKREINELKRELDRLQEELQRLSEELAD--LNAAIAGIEAKINEL 439

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477692  317 RAEhqqdSEDLFKKIvrasQESEARIQQLKSEWQSMTQESFQESSvkELRRLEDQLAGLQQELAALALKQSSVAEEVG 394
Cdd:TIGR02169  440 EEE----KEDKALEI----KKQEWKLEQLAADLSKYEQELYDLKE--EYDRVEKELSKLQRELAEAEAQARASEERVR 507
PRK12704 PRK12704
phosphodiesterase; Provisional
 291-507 7.73e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 7.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 291 SRREAalkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQ-ESSVKELRRLE 369
Cdd:PRK12704   47 AKKEA---EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEElEKKEKELEQKQ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 370 DQLAGLQQELAALALKQSSVAEEV-GLLPQQI-QAVRDDVESQFpawisqflarggggrvgllqREEMQAQLRELESKil 447
Cdd:PRK12704  124 QELEKKEEELEELIEEQLQELERIsGLTAEEAkEILLEKVEEEA--------------------RHEAAVLIKEIEEE-- 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2028477692 448 thvAEMQG-KSAREaaaslsltlqkegvigvteeqvhhIVKQALQRYSedriglADYALES 507
Cdd:PRK12704  182 ---AKEEAdKKAKE------------------------ILAQAIQRCA------ADHVAET 209
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 286-446 1.32e-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: 41.97  E-value: 1.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  286 LEGLVSRREAALKE-DFRRETAARIQEELSALRAEH---QQDSEDLFKKIVRASQESEARIQQLKSewqsmtQESFQESS 361
Cdd:TIGR02168  826 LESLERRIAATERRlEDLEEQIEELSEDIESLAAEIeelEELIEELESELEALLNERASLEEALAL------LRSELEEL 899

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  362 VKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQfpaWISQFLARGGGGRVGLLQREEMQAQLRE 441
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE---YSLTLEEAEALENKIEDDEEEARRRLKR 976


                   ....*
gi 2028477692  442 LESKI 446
Cdd:TIGR02168  977 LENKI 981
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
227-382 1.62e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.54  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 227 EQRVMSRVHSLERRLEALAAEFSsnwQKEAmRLERLELRQGAPGQGGGGGLSHEDTLALLEGL--VSRREAALKEDFRRE 304
Cdd:COG3206   214 AKLLLQQLSELESQLAEARAELA---EAEA-RLAALRAQLGSGPDALPELLQSPVIQQLRAQLaeLEAELAELSARYTPN 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 305 --TAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfqessVKELRRLEDQLAGLQQELAAL 382
Cdd:COG3206   290 hpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR------LAELPELEAELRRLEREVEVA 363
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 303-502 1.85e-03

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


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.48  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 303 RETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWqSMTQESFQE---------SSVKELRRLEDqla 373
Cdd:COG5185   299 AEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEI-EQGQESLTEnleaikeeiENIVGEVELSK--- 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 374 gLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISqflarggggrVGLLQREEMQAQLRELESKIlthvaEM 453
Cdd:COG5185   375 -SSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLK----------AADRQIEELQRQIEQATSSN-----EE 438

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2028477692 454 QGKSAREAAASLSLTLQKEGVIG---VTEEQVHHI--VKQALQRYSEDRIGLAD 502
Cdd:COG5185   439 VSKLLNELISELNKVMREADEESqsrLEEAYDEINrsVRSKKEDLNEELTQIES 492
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 280-463 5.29e-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: 38.40  E-value: 5.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 280 EDTLALLEGLVSRREAALkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQ----LKSEWQSMTQE 355
Cdd:pfam01442   3 EDSLDELSTYAEELQEQL-GPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQnveeLRQRLEPYTEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 356 sFQESSVKELRRLEDQLAGLQQELaalalkQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFlarggggrvgllqREEM 435
Cdd:pfam01442  82 -LRKRLNADAEELQEKLAPYGEEL------RERLEQNVDALRARLAPYAEELRQKLAERLEEL-------------KESL 141

                         170       180
                  ....*....|....*....|....*...
gi 2028477692 436 QAQLRELESKILTHVAEMQGKSAREAAA 463
Cdd:pfam01442 142 APYAEEVQAQLSQRLQELREKLEPQAED 169
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
291-402 5.65e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.50  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 291 SRREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFK---KIVRASQESEARIQQLKS--EWQSMTQESFQESSvKEL 365
Cdd:COG4372    32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarsELEQLEEELEELNEQLQAaqAELAQAQEELESLQ-EEA 110

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2028477692 366 RRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQA 402
Cdd:COG4372   111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 314-410 6.67e-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: 39.36  E-value: 6.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 314 SALRAEHQQDSEDLFKKIvrasQESEARIQQLKSEwqsmtqesfQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEV 393
Cdd:COG4942    19 ADAAAEAEAELEQLQQEI----AELEKELAALKKE---------EKALLKQLAALERRIAALARRIRALEQELAALEAEL 85

                          90
                  ....*....|....*..
gi 2028477692 394 GLLPQQIQAVRDDVESQ 410
Cdd:COG4942    86 AELEKEIAELRAELEAQ 102
PRK11281 PRK11281
mechanosensitive channel MscK;
312-380 7.57e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.51  E-value: 7.57e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2028477692  312 ELSALRAEHQQDSEDLFKKIVRASQ---ESEARIQQLKSEWQSMTQESFQESSvkeLRRLEDQLAGLQQELA 380
Cdd:PRK11281    70 ALLDKIDRQKEETEQLKQQLAQAPAklrQAQAELEALKDDNDEETRETLSTLS---LRQLESRLAQTLDQLQ 138
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 299-403 8.42e-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: 8.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692 299 EDFRREtAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQESSVKE-LRRLEDQLAGLQQ 377
Cdd:COG0542   414 DELERR-LEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEeLEQRYGKIPELEK 492

                          90       100       110
                  ....*....|....*....|....*....|
gi 2028477692 378 ELAA----LALKQSSVAEEVGllPQQIQAV 403
Cdd:COG0542   493 ELAEleeeLAELAPLLREEVT--EEDIAEV 520
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
214-447 9.96e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 9.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  214 GWEARDSSPHFQAE-QRVMSRVHSLERRLEALAAEfSSNWQKEAMRLERLElrqgAPGQGGGGGLSHEDTLALLEglvSR 292
Cdd:COG4913    605 GFDNRAKLAALEAElAELEEELAEAEERLEALEAE-LDALQERREALQRLA----EYSWDEIDVASAEREIAELE---AE 676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477692  293 REAALKEDfrrETAARIQEELSALRAEHQQDSEDLFKKIVRASQEsEARIQQLKSEWQS--MTQESFQESSVKELR-RLE 369
Cdd:COG4913    677 LERLDASS---DDLAALEEQLEELEAELEELEEELDELKGEIGRL-EKELEQAEEELDElqDRLEAAEDLARLELRaLLE 752

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477692  370 DQLAGLQQElAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKIL 447
Cdd:COG4913    753 ERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGL 829
 
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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