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Conserved domains on  [gi|2028477690|ref|NP_001381357|]
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SUN domain-containing protein 2 isoform 1 [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 ...
 602-736 1.79e-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: 1.79e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 602 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 681
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477690 682 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 736
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
 502-559 1.04e-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: 97.40  E-value: 1.04e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477690 502 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQR 559
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
 421-475 2.71e-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: 2.71e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477690 421 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 475
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 299-538 4.48e-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: 4.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  299 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 376
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  377 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 446
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  447 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 526
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921

                          250
                   ....*....|..
gi 2028477690  527 EAAASLSLTLQK 538
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 ...
 602-736 1.79e-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: 1.79e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 602 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 681
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477690 682 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 736
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
 502-559 1.04e-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: 97.40  E-value: 1.04e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477690 502 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQR 559
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
 421-475 2.71e-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: 2.71e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477690 421 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 475
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 299-538 4.48e-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: 4.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  299 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 376
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  377 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 446
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  447 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 526
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921

                          250
                   ....*....|..
gi 2028477690  527 EAAASLSLTLQK 538
Cdd:TIGR02168  922 EKLAQLELRLEG 933
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 292-575 3.95e-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: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 292 QAEQRVMSRVHSLERRLEALAAEFSS-NWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREaalkedfRR 370
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-------RR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 371 ETAARIQEELSALRAEHQQDSEDLFKKIVRAsqesEARIQQLKSEWQSMTQEsfQESSVKELRRLEDQLAGLQQELAALA 450
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEEL----EEELEEAEEELEEAEAE--LAEAEEALLEAEAELAEAEEELEELA 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 451 LKQSSVAEEVGLLPQQIQAVRDDVESqfpawISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAAA 530
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEA-----LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2028477690 531 SLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESG 575
Cdd:COG1196   461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
PRK12704 PRK12704
phosphodiesterase; Provisional
 358-574 7.81e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 7.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 358 SRREAalkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQ-ESSVKELRRLE 436
Cdd:PRK12704   47 AKKEA---EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEElEKKEKELEQKQ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 437 DQLAGLQQELAALALKQSSVAEEV-GLLPQQI-QAVRDDVESQFpawisqflarggggrvgllqREEMQAQLRELESKil 514
Cdd:PRK12704  124 QELEKKEEELEELIEEQLQELERIsGLTAEEAkEILLEKVEEEA--------------------RHEAAVLIKEIEEE-- 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2028477690 515 thvAEMQG-KSAREaaaslsltlqkegvigvteeqvhhIVKQALQRYSedriglADYALES 574
Cdd:PRK12704  182 ---AKEEAdKKAKE------------------------ILAQAIQRCA------ADHVAET 209
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 347-530 4.63e-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: 4.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 347 EDTLALLEGLVSRREAALkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQ----LKSEWQSMTQE 422
Cdd:pfam01442   3 EDSLDELSTYAEELQEQL-GPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQnveeLRQRLEPYTEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 423 sFQESSVKELRRLEDQLAGLQQELaalalkQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFlarggggrvgllqREEM 502
Cdd:pfam01442  82 -LRKRLNADAEELQEKLAPYGEEL------RERLEQNVDALRARLAPYAEELRQKLAERLEEL-------------KESL 141

                         170       180
                  ....*....|....*....|....*...
gi 2028477690 503 QAQLRELESKILTHVAEMQGKSAREAAA 530
Cdd:pfam01442 142 APYAEEVQAQLSQRLQELREKLEPQAED 169
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 381-477 5.44e-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: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 381 SALRAEHQQDSEDLFKKIvrasQESEARIQQLKSEwqsmtqesfQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEV 460
Cdd:COG4942    19 ADAAAEAEAELEQLQQEI----AELEKELAALKKE---------EKALLKQLAALERRIAALARRIRALEQELAALEAEL 85

                          90
                  ....*....|....*..
gi 2028477690 461 GLLPQQIQAVRDDVESQ 477
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 ...
 602-736 1.79e-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: 1.79e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 602 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 681
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477690 682 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 736
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
 502-559 1.04e-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: 97.40  E-value: 1.04e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477690 502 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQR 559
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
 421-475 2.71e-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: 2.71e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477690 421 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 475
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SUN_cc1 cd21435
coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 ...
 421-475 1.66e-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: 59.73  E-value: 1.66e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477690 421 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 475
Cdd:cd21435     1 QEAFQESSVKELGRLEAQLASLRQELAALTLKQEAIQKELEQTKQKTISAVGEQL 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 299-538 4.48e-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: 4.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  299 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 376
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  377 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 446
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  447 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 526
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921

                          250
                   ....*....|..
gi 2028477690  527 EAAASLSLTLQK 538
Cdd:TIGR02168  922 EKLAQLELRLEG 933
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 292-575 3.95e-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: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 292 QAEQRVMSRVHSLERRLEALAAEFSS-NWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREaalkedfRR 370
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-------RR 311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 371 ETAARIQEELSALRAEHQQDSEDLFKKIVRAsqesEARIQQLKSEWQSMTQEsfQESSVKELRRLEDQLAGLQQELAALA 450
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEEL----EEELEEAEEELEEAEAE--LAEAEEALLEAEAELAEAEEELEELA 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 451 LKQSSVAEEVGLLPQQIQAVRDDVESqfpawISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAAA 530
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEA-----LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2028477690 531 SLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESG 575
Cdd:COG1196   461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
347-581 2.17e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.09  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 347 EDTLALLEGLVSRREAALkEDFRR--------ETAARIQEELSALRAEHQQDSEDLfkkivrasQESEARIQQLKSEWQS 418
Cdd:COG3206   181 EEQLPELRKELEEAEAAL-EEFRQknglvdlsEEAKLLLQQLSELESQLAEARAEL--------AEAEARLAALRAQLGS 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 419 MTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQfpawISQFLARGGGgrvgllQ 498
Cdd:COG3206   252 GPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE----AQRILASLEA------E 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 499 REEMQAQLRELESKIlthvAEMQGKSAREAAASLSLT-LQKEgvIGVTEEqvhhIVKQALQRYSEDRIglaDYALESGGA 577
Cdd:COG3206   322 LEALQAREASLQAQL----AQLEARLAELPELEAELRrLERE--VEVARE----LYESLLQRLEEARL---AEALTVGNV 388


                  ....
gi 2028477690 578 SVIS 581
Cdd:COG3206   389 RVID 392
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
283-535 2.96e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 2.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  283 EARDSSPHFQAEQRVMSRVHSLERRLEALaaefssnwQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREA 362
Cdd:COG4913    219 EEPDTFEAADALVEHFDDLERAHEALEDA--------REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL 290

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  363 ALKE---DFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfqessvkeLRRLEDQL 439
Cdd:COG4913    291 ELLEaelEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE---------LEERERRR 361

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  440 AGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAE 519
Cdd:COG4913    362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441

                          250
                   ....*....|....*..
gi 2028477690  520 MQgkSAREA-AASLSLT 535
Cdd:COG4913    442 LL--ALRDAlAEALGLD 456
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
350-508 3.33e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 3.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  350 LALLEGLVSRREAALKE-DFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQEseARIQQLKSEWQSMtqesfqESS 428
Cdd:COG4913    612 LAALEAELAELEEELAEaEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE--REIAELEAELERL------DAS 683

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  429 VKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVR----------DDVESQFPAWISQFLARGGGGRVGLLQ 498
Cdd:COG4913    684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeeldelqdrlEAAEDLARLELRALLEERFAAALGDAV 763

                          170
                   ....*....|
gi 2028477690  499 REEMQAQLRE 508
Cdd:COG4913    764 ERELRENLEE 773
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 299-513 3.42e-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: 47.37  E-value: 3.42e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  299 SRVHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREA----------ALKEDF 368
Cdd:TIGR02169  709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEdlhkleealnDLEARL 788

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  369 RRETAARIQEELSALRAEHQqdsedlfkKIVRASQESEARIQQLKSEWQSMTQESfqESSVKELRRLEDQLAGLQQELAA 448
Cdd:TIGR02169  789 SHSRIPEIQAELSKLEEEVS--------RIEARLREIEQKLNRLTLEKEYLEKEI--QELQEQRIDLKEQIKSIEKEIEN 858

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2028477690  449 LALKQSSVAEEVgllpQQIQAVRDDVESQFpawisqflarggggRVGLLQREEMQAQLRELESKI 513
Cdd:TIGR02169  859 LNGKKEELEEEL----EELEAALRDLESRL--------------GDLKKERDELEAQLRELERKI 905
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 295-529 3.49e-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: 3.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  295 QRVMSRVHSLERRLEALAAEFssnwQKEAMRLERLELRQGApgqggggglsHEDTLALLEGLVSRREAALKEDFRR---- 370
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQI----------LRERLANLERQLEELEAQLEELESKldel 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  371 -ETAARIQEELSALRAEHQQDSEDLfKKIVRASQESEARIQQLKSEWQSMTQESFQ------------ESSVKELRRLED 437
Cdd:TIGR02168  336 aEELAELEEKLEELKEELESLEAEL-EELEAELEELESRLEELEEQLETLRSKVAQlelqiaslnneiERLEARLERLED 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  438 QLAGLQQELAALALKQSSVA-EEVGLLPQQIQAVRDDVESQFPAWIsqflarggggrvglLQREEMQAQLRELESKILTH 516
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLE--------------EALEELREELEEAEQALDAA 480

                          250
                   ....*....|...
gi 2028477690  517 VAEMQGKSAREAA 529
Cdd:TIGR02168  481 ERELAQLQARLDS 493
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
304-510 4.17e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 4.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 304 LERRLEALAAEFSSNWQKEAM-RLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREA--ALKEDFRRETAARIQEEL 380
Cdd:COG4717   293 LAREKASLGKEAEELQALPALeELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELlrEAEELEEELQLEELEQEI 372

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 381 SALRAEHQQDSEDLFKKIVRASQES---EARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVA 457
Cdd:COG4717   373 AALLAEAGVEDEEELRAALEQAEEYqelKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR 452

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2028477690 458 EEVGLLPQQIQAVRDDVEsqfpawISQFLArggggrvgllQREEMQAQLRELE 510
Cdd:COG4717   453 EELAELEAELEQLEEDGE------LAELLQ----------ELEELKAELRELA 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 360-573 1.11e-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: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 360 REAALKEDFRRETAARIQEELSALRAEHQQDSEDLfkkivrasQESEARIQQLKSEWQSMTQESfqESSVKELRRLEDQL 439
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAEL--------AELEAELEELRLELEELELEL--EEAQAEEYELLAEL 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 440 AGLQQELAALALKQSSVAEEVGLLPQQIQ---AVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTH 516
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAeleEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2028477690 517 VAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHivKQALQRYSEDRIGLADYALE 573
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEAL--LERLERLEEELEELEEALAE 432
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
283-565 1.28e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.53  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 283 EARDSSPHFQAEQRvmsRVHSLERRLEALAAEFSsNWQKEAMRLERLE--LRQGAPGQGGGGGLSHEDTL--ALLEGLVS 358
Cdd:COG4717    82 EAEEKEEEYAELQE---ELEELEEELEELEAELE-ELREELEKLEKLLqlLPLYQELEALEAELAELPERleELEERLEE 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 359 RREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfQESSVKELRRLEDQ 438
Cdd:COG4717   158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE--LEELEEELEQLENE 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 439 LAGLQQE---------------LAALALKQSSVAEEVGLLPQQIQAVrddveSQFPAWISQFLARGGGGRVGLLQREEMQ 503
Cdd:COG4717   236 LEAAALEerlkearlllliaaaLLALLGLGGSLLSLILTIAGVLFLV-----LGLLALLFLLLAREKASLGKEAEELQAL 310

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2028477690 504 AQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRI 565
Cdd:COG4717   311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 303-513 2.32e-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: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 303 SLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTL-ALLEGLVSRREAALKEDFRRETAARIQEELS 381
Cdd:COG1196   580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLvAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 382 ALRAEHQQdsedlfkkivRASQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEvg 461
Cdd:COG1196   660 GSLTGGSR----------RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE-- 727

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2028477690 462 llpQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKI 513
Cdd:COG1196   728 ---EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
PRK12704 PRK12704
phosphodiesterase; Provisional
 358-574 7.81e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 7.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 358 SRREAalkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQ-ESSVKELRRLE 436
Cdd:PRK12704   47 AKKEA---EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEElEKKEKELEQKQ 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 437 DQLAGLQQELAALALKQSSVAEEV-GLLPQQI-QAVRDDVESQFpawisqflarggggrvgllqREEMQAQLRELESKil 514
Cdd:PRK12704  124 QELEKKEEELEELIEEQLQELERIsGLTAEEAkEILLEKVEEEA--------------------RHEAAVLIKEIEEE-- 181

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2028477690 515 thvAEMQG-KSAREaaaslsltlqkegvigvteeqvhhIVKQALQRYSedriglADYALES 574
Cdd:PRK12704  182 ---AKEEAdKKAKE------------------------ILAQAIQRCA------ADHVAET 209
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 304-461 7.90e-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: 7.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  304 LERRLEALAAEFSSNWQKEAMRLERLElrqgapgQGGGGGLSHEDTLALLEGLVSRREAALKEdfRRETAARIQEELSAL 383
Cdd:TIGR02169  369 LRAELEEVDKEFAETRDELKDYREKLE-------KLKREINELKRELDRLQEELQRLSEELAD--LNAAIAGIEAKINEL 439

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477690  384 RAEhqqdSEDLFKKIvrasQESEARIQQLKSEWQSMTQESFQESSvkELRRLEDQLAGLQQELAALALKQSSVAEEVG 461
Cdd:TIGR02169  440 EEE----KEDKALEI----KKQEWKLEQLAADLSKYEQELYDLKE--EYDRVEKELSKLQRELAEAEAQARASEERVR 507
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
294-449 1.09e-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: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 294 EQRVMSRVHSLERRLEALAAEFSsnwQKEAmRLERLELRQGAPGQGGGGGLSHEDTLALLEGL--VSRREAALKEDFRRE 371
Cdd:COG3206   214 AKLLLQQLSELESQLAEARAELA---EAEA-RLAALRAQLGSGPDALPELLQSPVIQQLRAQLaeLEAELAELSARYTPN 289

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 372 --TAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfqessVKELRRLEDQLAGLQQELAAL 449
Cdd:COG3206   290 hpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR------LAELPELEAELRRLEREVEVA 363
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 353-513 1.34e-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: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  353 LEGLVSRREAALKE-DFRRETAARIQEELSALRAEH---QQDSEDLFKKIVRASQESEARIQQLKSewqsmtQESFQESS 428
Cdd:TIGR02168  826 LESLERRIAATERRlEDLEEQIEELSEDIESLAAEIeelEELIEELESELEALLNERASLEEALAL------LRSELEEL 899

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  429 VKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQfpaWISQFLARGGGGRVGLLQREEMQAQLRE 508
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE---YSLTLEEAEALENKIEDDEEEARRRLKR 976


                   ....*
gi 2028477690  509 LESKI 513
Cdd:TIGR02168  977 LENKI 981
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 370-569 2.87e-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: 41.10  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 370 RETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWqSMTQESFQE---------SSVKELRRLEDqla 440
Cdd:COG5185   299 AEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEI-EQGQESLTEnleaikeeiENIVGEVELSK--- 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 441 gLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISqflarggggrVGLLQREEMQAQLRELESKIlthvaEM 520
Cdd:COG5185   375 -SSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLK----------AADRQIEELQRQIEQATSSN-----EE 438

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2028477690 521 QGKSAREAAASLSLTLQKEGVIG---VTEEQVHHI--VKQALQRYSEDRIGLAD 569
Cdd:COG5185   439 VSKLLNELISELNKVMREADEESqsrLEEAYDEINrsVRSKKEDLNEELTQIES 492
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
358-582 3.87e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.27  E-value: 3.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 358 SRREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFK---KIVRASQESEARIQQLKS--EWQSMTQESFQESSvKEL 432
Cdd:COG4372    32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarsELEQLEEELEELNEQLQAaqAELAQAQEELESLQ-EEA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 433 RRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAvrddvesqfpawisqflarggggrvGLLQREEMQAQLRELESK 512
Cdd:COG4372   111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE-------------------------REEELKELEEQLESLQEE 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2028477690 513 ILTHVAEMQGKSAREA----AASLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESGGASVIST 582
Cdd:COG4372   166 LAALEQELQALSEAEAeqalDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALL 239
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
 347-530 4.63e-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: 4.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 347 EDTLALLEGLVSRREAALkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQ----LKSEWQSMTQE 422
Cdd:pfam01442   3 EDSLDELSTYAEELQEQL-GPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQnveeLRQRLEPYTEE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 423 sFQESSVKELRRLEDQLAGLQQELaalalkQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFlarggggrvgllqREEM 502
Cdd:pfam01442  82 -LRKRLNADAEELQEKLAPYGEEL------RERLEQNVDALRARLAPYAEELRQKLAERLEEL-------------KESL 141

                         170       180
                  ....*....|....*....|....*...
gi 2028477690 503 QAQLRELESKILTHVAEMQGKSAREAAA 530
Cdd:pfam01442 142 APYAEEVQAQLSQRLQELREKLEPQAED 169
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 381-477 5.44e-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: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 381 SALRAEHQQDSEDLFKKIvrasQESEARIQQLKSEwqsmtqesfQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEV 460
Cdd:COG4942    19 ADAAAEAEAELEQLQQEI----AELEKELAALKKE---------EKALLKQLAALERRIAALARRIRALEQELAALEAEL 85

                          90
                  ....*....|....*..
gi 2028477690 461 GLLPQQIQAVRDDVESQ 477
Cdd:COG4942    86 AELEKEIAELRAELEAQ 102
PRK11281 PRK11281
mechanosensitive channel MscK;
379-447 5.92e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.28  E-value: 5.92e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2028477690  379 ELSALRAEHQQDSEDLFKKIVRASQ---ESEARIQQLKSEWQSMTQESFQESSvkeLRRLEDQLAGLQQELA 447
Cdd:PRK11281    70 ALLDKIDRQKEETEQLKQQLAQAPAklrQAQAELEALKDDNDEETRETLSTLS---LRQLESRLAQTLDQLQ 138
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
281-514 6.80e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 6.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  281 GWEARDSSPHFQAE-QRVMSRVHSLERRLEALAAEfSSNWQKEAMRLERLElrqgAPGQGGGGGLSHEDTLALLEglvSR 359
Cdd:COG4913    605 GFDNRAKLAALEAElAELEEELAEAEERLEALEAE-LDALQERREALQRLA----EYSWDEIDVASAEREIAELE---AE 676

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  360 REAALKEDfrrETAARIQEELSALRAEHQQDSEDLFKKIVRASQEsEARIQQLKSEWQS--MTQESFQESSVKELR-RLE 436
Cdd:COG4913    677 LERLDASS---DDLAALEEQLEELEAELEELEEELDELKGEIGRL-EKELEQAEEELDElqDRLEAAEDLARLELRaLLE 752

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477690  437 DQLAGLQQElAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKIL 514
Cdd:COG4913    753 ERFAAALGD-AVERELRENLEERIDALRARLNRAEEELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGL 829
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 287-487 8.09e-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: 8.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  287 SSPHFQAEQRVM-SRVHSLERRLEALAAEfssnwQKEAMRLERLELRQGAPGQGGggglSHEDTLALLEGLVSRREAALK 365
Cdd:TIGR00618  716 YDREFNEIENASsSLGSDLAAREDALNQS-----LKELMHQARTVLKARTEAHFN----NNEEVTAALQTGAELSHLAAE 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  366 EDFRRETAARIQEELSALRAEHQQDSEDlFKKIVRASQESEA-RIQQLKSEWQSMTQesfqesSVKELRRLEDQLAGLQQ 444
Cdd:TIGR00618  787 IQFFNRLREEDTHLLKTLEAEIGQEIPS-DEDILNLQCETLVqEEEQFLSRLEEKSA------TLGEITHQLLKYEECSK 859

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2028477690  445 ELAALALKQSSVAEEVGLLpqqiqAVRDDVESQFPAWISQFLA 487
Cdd:TIGR00618  860 QLAQLTQEQAKIIQLSDKL-----NGINQIKIQFDGDALIKFL 897
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 366-470 8.95e-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: 8.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690 366 EDFRREtAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQESSVKE-LRRLEDQLAGLQQ 444
Cdd:COG0542   414 DELERR-LEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEeLEQRYGKIPELEK 492

                          90       100       110
                  ....*....|....*....|....*....|
gi 2028477690 445 ELAA----LALKQSSVAEEVGllPQQIQAV 470
Cdd:COG0542   493 ELAEleeeLAELAPLLREEVT--EEDIAEV 520
mukB PRK04863
chromosome partition protein MukB;
347-565 9.18e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.56  E-value: 9.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  347 EDTLALLEGLVSRREAALKEDFRRETAARIQEELSALRAEHQQDSEDL-------------FKKIVRASQ---------E 404
Cdd:PRK04863   286 EEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAsdhlnlvqtalrqQEKIERYQAdleeleerlE 365

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  405 SEARIQQLKSEWQSMTQESFQ--ESSVKELRRledQLAGLQQELAALALKQSSVAEEVGLL--PQQIQAVRDDVESQFPA 480
Cdd:PRK04863   366 EQNEVVEEADEQQEENEARAEaaEEEVDELKS---QLADYQQALDVQQTRAIQYQQAVQALerAKQLCGLPDLTADNAED 442

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477690  481 WISQFLArggggrvgllQREEMQAQLRELESKIltHVAEMqGKSAREAAASLSLTLqkegVIGVTEEQVHHIVKQALQRY 560
Cdd:PRK04863   443 WLEEFQA----------KEQEATEELLSLEQKL--SVAQA-AHSQFEQAYQLVRKI----AGEVSRSEAWDVARELLRRL 505


                   ....*
gi 2028477690  561 SEDRI 565
Cdd:PRK04863   506 REQRH 510
 
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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