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Conserved domains on  [gi|2028477699|ref|NP_001381367|]
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SUN domain-containing protein 2 isoform 7 [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 ...
551-685 8.76e-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: 8.76e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 551 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 630
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477699 631 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 685
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
451-508 2.71e-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: 2.71e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477699 451 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQR 508
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
370-424 4.07e-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: 81.20  E-value: 4.07e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477699 370 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 424
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
248-487 6.27e-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: 59.30  E-value: 6.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  248 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 325
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  326 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 395
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  396 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 475
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921
                          250
                   ....*....|..
gi 2028477699  476 EAAASLSLTLQK 487
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 ...
551-685 8.76e-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: 8.76e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 551 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 630
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477699 631 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 685
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
451-508 2.71e-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: 2.71e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477699 451 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQR 508
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
370-424 4.07e-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: 81.20  E-value: 4.07e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477699 370 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 424
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
248-487 6.27e-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: 59.30  E-value: 6.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  248 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 325
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  326 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 395
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  396 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 475
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921
                          250
                   ....*....|..
gi 2028477699  476 EAAASLSLTLQK 487
Cdd:TIGR02168  922 EKLAQLELRLEG 933
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
241-524 5.20e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 5.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 241 QAEQRVMSRVHSLERRLEALAAEFSS-NWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREaalkedfRR 319
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-------RR 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 320 ETAARIQEELSALRAEHQQDSEDLFKKIVRAsqesEARIQQLKSEWQSMTQEsfQESSVKELRRLEDQLAGLQQELAALA 399
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEEL----EEELEEAEEELEEAEAE--LAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 400 LKQSSVAEEVGLLPQQIQAVRDDVESqfpawISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAAA 479
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEA-----LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2028477699 480 SLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESG 524
Cdd:COG1196   461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
PRK12704 PRK12704
phosphodiesterase; Provisional
307-523 1.02e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 307 SRREAalkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQ-ESSVKELRRLE 385
Cdd:PRK12704   47 AKKEA---EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEElEKKEKELEQKQ 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 386 DQLAGLQQELAALALKQSSVAEEV-GLLPQQI-QAVRDDVESQFpawisqflarggggrvgllqREEMQAQLRELESKil 463
Cdd:PRK12704  124 QELEKKEEELEELIEEQLQELERIsGLTAEEAkEILLEKVEEEA--------------------RHEAAVLIKEIEEE-- 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2028477699 464 thvAEMQG-KSAREaaaslsltlqkegvigvteeqvhhIVKQALQRYSedriglADYALES 523
Cdd:PRK12704  182 ---AKEEAdKKAKE------------------------ILAQAIQRCA------ADHVAET 209
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
330-426 6.46e-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: 6.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 330 SALRAEHQQDSEDLFKKIvrasQESEARIQQLKSEwqsmtqesfQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEV 409
Cdd:COG4942    19 ADAAAEAEAELEQLQQEI----AELEKELAALKKE---------EKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
                          90
                  ....*....|....*..
gi 2028477699 410 GLLPQQIQAVRDDVESQ 426
Cdd:COG4942    86 AELEKEIAELRAELEAQ 102
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
296-479 6.49e-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: 38.01  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 296 EDTLALLEGLVSRREAALkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQ----LKSEWQSMTQE 371
Cdd:pfam01442   3 EDSLDELSTYAEELQEQL-GPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQnveeLRQRLEPYTEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 372 sFQESSVKELRRLEDQLAGLQQELaalalkQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFlarggggrvgllqREEM 451
Cdd:pfam01442  82 -LRKRLNADAEELQEKLAPYGEEL------RERLEQNVDALRARLAPYAEELRQKLAERLEEL-------------KESL 141
                         170       180
                  ....*....|....*....|....*...
gi 2028477699 452 QAQLRELESKILTHVAEMQGKSAREAAA 479
Cdd:pfam01442 142 APYAEEVQAQLSQRLQELREKLEPQAED 169
 
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 ...
551-685 8.76e-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: 8.76e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 551 LWYHSQSPRVILQPDVHPGNCWAFQGPQGFAVVRLSARIRPTAVTLEHVPKALspnstISSAPKDFAIFGFDEDLQQEGT 630
Cdd:pfam07738   1 LNYEAKPPKVILQPDYMPGPCWSFKGSRGFVVIELSEFIIVEAITLEHVEKSV-----FSSAPKDFEVSGSDRYPTTKWV 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477699 631 LLGKFTYDQDGEPIQTFHFQAPTMATYQVVELRILTNWGHPEYTCIYRFRVHGEP 685
Cdd:pfam07738  76 LLGEFSYDLDGKTIQTFQLENPPDIWVKYVKLRILSNYGNEHYTCLYRFRVHGTV 130
HTH_SUN2 pfam18580
SUN2 helix-turn-helix domain; LINC complexes are formed by coupling of KASH (Klarsicht, ANC-1, ...
451-508 2.71e-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: 2.71e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477699 451 MQAQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQR 508
Cdd:pfam18580   1 LQAQLQDLEQRILAKLAEEQGKSARDAAASVGVALQQEGVTGVTEEQVHRIVNQALKR 58
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
370-424 4.07e-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: 81.20  E-value: 4.07e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477699 370 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 424
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
SUN_cc1 cd21435
coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 ...
370-424 2.07e-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: 2.07e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2028477699 370 QESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVE 424
Cdd:cd21435     1 QEAFQESSVKELGRLEAQLASLRQELAALTLKQEAIQKELEQTKQKTISAVGEQL 55
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
248-487 6.27e-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: 59.30  E-value: 6.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  248 SRVHSLERRLEALAAEFSsNWQKEAMRLERLELRQGAPGQGGGGGLS-HEDTLALLEGLVSRREAALKE-DFRRETAARI 325
Cdd:TIGR02168  691 EKIAELEKALAELRKELE-ELEEELEQLRKELEELSRQISALRKDLArLEAEVEQLEERIAQLSKELTElEAEIEELEER 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  326 QEELSALRAEHQQDSEDL----------FKKIVRASQESEARIQQLKSEWQsmTQESFQESSVKELRRLEDQLAGLQQEL 395
Cdd:TIGR02168  770 LEEAEEELAEAEAEIEELeaqieqlkeeLKALREALDELRAELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQI 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  396 AALALKQSSVAEEVGllpqQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQgkSAR 475
Cdd:TIGR02168  848 EELSEDIESLAAEIE----ELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE--ELR 921
                          250
                   ....*....|..
gi 2028477699  476 EAAASLSLTLQK 487
Cdd:TIGR02168  922 EKLAQLELRLEG 933
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
241-524 5.20e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.94  E-value: 5.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 241 QAEQRVMSRVHSLERRLEALAAEFSS-NWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREaalkedfRR 319
Cdd:COG1196   239 AELEELEAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE-------RR 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 320 ETAARIQEELSALRAEHQQDSEDLFKKIVRAsqesEARIQQLKSEWQSMTQEsfQESSVKELRRLEDQLAGLQQELAALA 399
Cdd:COG1196   312 RELEERLEELEEELAELEEELEELEEELEEL----EEELEEAEEELEEAEAE--LAEAEEALLEAEAELAEAEEELEELA 385
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 400 LKQSSVAEEVGLLPQQIQAVRDDVESqfpawISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAEMQGKSAREAAA 479
Cdd:COG1196   386 EELLEALRAAAELAAQLEELEEAEEA-----LLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA 460
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2028477699 480 SLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRIGLADYALESG 524
Cdd:COG1196   461 LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
296-530 3.39e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 47.32  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 296 EDTLALLEGLVSRREAALkEDFRR--------ETAARIQEELSALRAEHQQDSEDLfkkivrasQESEARIQQLKSEWQS 367
Cdd:COG3206   181 EEQLPELRKELEEAEAAL-EEFRQknglvdlsEEAKLLLQQLSELESQLAEARAEL--------AEAEARLAALRAQLGS 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 368 MTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQfpawISQFLARGGGgrvgllQ 447
Cdd:COG3206   252 GPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE----AQRILASLEA------E 321
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 448 REEMQAQLRELESKIlthvAEMQGKSAREAAASLSLT-LQKEgvIGVTEEqvhhIVKQALQRYSEDRIglaDYALESGGA 526
Cdd:COG3206   322 LEALQAREASLQAQL----AQLEARLAELPELEAELRrLERE--VEVARE----LYESLLQRLEEARL---AEALTVGNV 388

                  ....
gi 2028477699 527 SVIS 530
Cdd:COG3206   389 RVID 392
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
248-462 3.62e-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: 3.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  248 SRVHSLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREA----------ALKEDF 317
Cdd:TIGR02169  709 QELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEdlhkleealnDLEARL 788
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  318 RRETAARIQEELSALRAEHQqdsedlfkKIVRASQESEARIQQLKSEWQSMTQESfqESSVKELRRLEDQLAGLQQELAA 397
Cdd:TIGR02169  789 SHSRIPEIQAELSKLEEEVS--------RIEARLREIEQKLNRLTLEKEYLEKEI--QELQEQRIDLKEQIKSIEKEIEN 858
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2028477699  398 LALKQSSVAEEVgllpQQIQAVRDDVESQFpawisqflarggggRVGLLQREEMQAQLRELESKI 462
Cdd:TIGR02169  859 LNGKKEELEEEL----EELEAALRDLESRL--------------GDLKKERDELEAQLRELERKI 905
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
232-484 4.04e-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: 4.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  232 EARDSSPHFQAEQRVMSRVHSLERRLEALaaefssnwQKEAMRLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREA 311
Cdd:COG4913    219 EEPDTFEAADALVEHFDDLERAHEALEDA--------REQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRL 290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  312 ALKE---DFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfqessvkeLRRLEDQL 388
Cdd:COG4913    291 ELLEaelEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERE---------LEERERRR 361
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  389 AGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTHVAE 468
Cdd:COG4913    362 ARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPAR 441
                          250
                   ....*....|....*..
gi 2028477699  469 MQgkSAREA-AASLSLT 484
Cdd:COG4913    442 LL--ALRDAlAEALGLD 456
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
299-457 4.60e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 4.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  299 LALLEGLVSRREAALKE-DFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQEseARIQQLKSEWQSMtqesfqESS 377
Cdd:COG4913    612 LAALEAELAELEEELAEaEERLEALEAELDALQERREALQRLAEYSWDEIDVASAE--REIAELEAELERL------DAS 683
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  378 VKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVR----------DDVESQFPAWISQFLARGGGGRVGLLQ 447
Cdd:COG4913    684 SDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEeeldelqdrlEAAEDLARLELRALLEERFAAALGDAV 763
                          170
                   ....*....|
gi 2028477699  448 REEMQAQLRE 457
Cdd:COG4913    764 ERELRENLEE 773
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
244-478 5.10e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 5.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  244 QRVMSRVHSLERRLEALAAEFssnwQKEAMRLERLELRQGApgqggggglsHEDTLALLEGLVSRREAALKEDFRR---- 319
Cdd:TIGR02168  270 EELRLEVSELEEEIEELQKEL----YALANEISRLEQQKQI----------LRERLANLERQLEELEAQLEELESKldel 335
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  320 -ETAARIQEELSALRAEHQQDSEDLfKKIVRASQESEARIQQLKSEWQSMTQESFQ------------ESSVKELRRLED 386
Cdd:TIGR02168  336 aEELAELEEKLEELKEELESLEAEL-EELEAELEELESRLEELEEQLETLRSKVAQlelqiaslnneiERLEARLERLED 414
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  387 QLAGLQQELAALALKQSSVA-EEVGLLPQQIQAVRDDVESQFPAWIsqflarggggrvglLQREEMQAQLRELESKILTH 465
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLE--------------EALEELREELEEAEQALDAA 480
                          250
                   ....*....|...
gi 2028477699  466 VAEMQGKSAREAA 478
Cdd:TIGR02168  481 ERELAQLQARLDS 493
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
253-459 8.72e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.91  E-value: 8.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 253 LERRLEALAAEFSSNWQKEAM-RLERLELRQGAPGQGGGGGLSHEDTLALLEGLVSRREA--ALKEDFRRETAARIQEEL 329
Cdd:COG4717   293 LAREKASLGKEAEELQALPALeELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELlrEAEELEEELQLEELEQEI 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 330 SALRAEHQQDSEDLFKKIVRASQES---EARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVA 406
Cdd:COG4717   373 AALLAEAGVEDEEELRAALEQAEEYqelKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR 452
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2028477699 407 EEVGLLPQQIQAVRDDVESQfpawisqflarggggrVGLLQREEMQAQLRELE 459
Cdd:COG4717   453 EELAELEAELEQLEEDGELA----------------ELLQELEELKAELRELA 489
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
312-508 1.36e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.01  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 312 ALKEDFRRETAARIQEELSALRAEhqqdsedlfkkivraSQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGL 391
Cdd:COG3206   167 ELRREEARKALEFLEEQLPELRKE---------------LEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEA 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 392 QQELAALALKQSSVAEEVGLLPQQIQAVRDD------------VESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELE 459
Cdd:COG3206   232 RAELAEAEARLAALRAQLGSGPDALPELLQSpviqqlraqlaeLEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEA 311
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2028477699 460 SKILTHV-AEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHivkQALQR 508
Cdd:COG3206   312 QRILASLeAELEALQAREASLQAQLAQLEARLAELPELEAEL---RRLER 358
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
309-522 1.49e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 309 REAALKEDFRRETAARIQEELSALRAEHQQDSEDLfkkivrasQESEARIQQLKSEWQSMTQESfqESSVKELRRLEDQL 388
Cdd:COG1196   228 ELLLLKLRELEAELEELEAELEELEAELEELEAEL--------AELEAELEELRLELEELELEL--EEAQAEEYELLAEL 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 389 AGLQQELAALALKQSSVAEEVGLLPQQIQ---AVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKILTH 465
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAeleEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2028477699 466 VAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHivKQALQRYSEDRIGLADYALE 522
Cdd:COG1196   378 EEELEELAEELLEALRAAAELAAQLEELEEAEEAL--LERLERLEEELEELEEALAE 432
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
252-462 2.97e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 252 SLERRLEALAAEFSSNWQKEAMRLERLELRQGAPGQGGGGGLSHEDTL-ALLEGLVSRREAALKEDFRRETAARIQEELS 330
Cdd:COG1196   580 DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLvAARLEAALRRAVTLAGRLREVTLEGEGGSAG 659
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 331 ALRAEHQQdsedlfkkivRASQESEARIQQLKSEWQSMTQESFQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEvg 410
Cdd:COG1196   660 GSLTGGSR----------RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE-- 727
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2028477699 411 llpQQIQAVRDDVESQFPAWISQFLARGGGGRVGLLQREEMQAQLRELESKI 462
Cdd:COG1196   728 ---EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREI 776
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
232-514 3.47e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 3.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 232 EARDSSPHFQAEQRvmsRVHSLERRLEALAAEFSsNWQKEAMRLERLE--LRQGAPGQGGGGGLSHEDTL--ALLEGLVS 307
Cdd:COG4717    82 EAEEKEEEYAELQE---ELEELEEELEELEAELE-ELREELEKLEKLLqlLPLYQELEALEAELAELPERleELEERLEE 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 308 RREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfQESSVKELRRLEDQ 387
Cdd:COG4717   158 LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE--LEELEEELEQLENE 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 388 LAGLQQE---------------LAALALKQSSVAEEVGLLPQQIQAVrddveSQFPAWISQFLARGGGGRVGLLQREEMQ 452
Cdd:COG4717   236 LEAAALEerlkearlllliaaaLLALLGLGGSLLSLILTIAGVLFLV-----LGLLALLFLLLAREKASLGKEAEELQAL 310
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2028477699 453 AQLRELESKILTHVAEMQGKSAREAAASLSLTLQKEGVIGVTEEQVHHIVKQALQRYSEDRI 514
Cdd:COG4717   311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEI 372
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
253-410 8.68e-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: 42.75  E-value: 8.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  253 LERRLEALAAEFSSNWQKEAMRLERLElrqgapgQGGGGGLSHEDTLALLEGLVSRREAALKEdfRRETAARIQEELSAL 332
Cdd:TIGR02169  369 LRAELEEVDKEFAETRDELKDYREKLE-------KLKREINELKRELDRLQEELQRLSEELAD--LNAAIAGIEAKINEL 439
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2028477699  333 RAEhqqdSEDLFKKIvrasQESEARIQQLKSEWQSMTQESFQESSvkELRRLEDQLAGLQQELAALALKQSSVAEEVG 410
Cdd:TIGR02169  440 EEE----KEDKALEI----KKQEWKLEQLAADLSKYEQELYDLKE--EYDRVEKELSKLQRELAEAEAQARASEERVR 507
PRK12704 PRK12704
phosphodiesterase; Provisional
307-523 1.02e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 307 SRREAalkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQ-ESSVKELRRLE 385
Cdd:PRK12704   47 AKKEA---EAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEElEKKEKELEQKQ 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 386 DQLAGLQQELAALALKQSSVAEEV-GLLPQQI-QAVRDDVESQFpawisqflarggggrvgllqREEMQAQLRELESKil 463
Cdd:PRK12704  124 QELEKKEEELEELIEEQLQELERIsGLTAEEAkEILLEKVEEEA--------------------RHEAAVLIKEIEEE-- 181
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2028477699 464 thvAEMQG-KSAREaaaslsltlqkegvigvteeqvhhIVKQALQRYSedriglADYALES 523
Cdd:PRK12704  182 ---AKEEAdKKAKE------------------------ILAQAIQRCA------ADHVAET 209
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
243-398 1.57e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 243 EQRVMSRVHSLERRLEALAAEFSsnwQKEAmRLERLELRQGAPGQGGGGGLSHEDTLALLEGL--VSRREAALKEDFRRE 320
Cdd:COG3206   214 AKLLLQQLSELESQLAEARAELA---EAEA-RLAALRAQLGSGPDALPELLQSPVIQQLRAQLaeLEAELAELSARYTPN 289
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 321 --TAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQEsfqessVKELRRLEDQLAGLQQELAAL 398
Cdd:COG3206   290 hpDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR------LAELPELEAELRRLEREVEVA 363
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
302-462 1.75e-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: 41.58  E-value: 1.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  302 LEGLVSRREAALKE-DFRRETAARIQEELSALRAEH---QQDSEDLFKKIVRASQESEARIQQLKSewqsmtQESFQESS 377
Cdd:TIGR02168  826 LESLERRIAATERRlEDLEEQIEELSEDIESLAAEIeelEELIEELESELEALLNERASLEEALAL------LRSELEEL 899
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699  378 VKELRRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQfpaWISQFLARGGGGRVGLLQREEMQAQLRE 457
Cdd:TIGR02168  900 SEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE---YSLTLEEAEALENKIEDDEEEARRRLKR 976

                   ....*
gi 2028477699  458 LESKI 462
Cdd:TIGR02168  977 LENKI 981
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
319-518 2.69e-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: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 319 RETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWqSMTQESFQE---------SSVKELRRLEDqla 389
Cdd:COG5185   299 AEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEI-EQGQESLTEnleaikeeiENIVGEVELSK--- 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 390 gLQQELAALALKQSSVAEEVGLLPQQIQAVRDDVESQFPAWISqflarggggrVGLLQREEMQAQLRELESKIlthvaEM 469
Cdd:COG5185   375 -SSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLK----------AADRQIEELQRQIEQATSSN-----EE 438
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2028477699 470 QGKSAREAAASLSLTLQKEGVIG---VTEEQVHHI--VKQALQRYSEDRIGLAD 518
Cdd:COG5185   439 VSKLLNELISELNKVMREADEESqsrLEEAYDEINrsVRSKKEDLNEELTQIES 492
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
330-426 6.46e-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: 6.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 330 SALRAEHQQDSEDLFKKIvrasQESEARIQQLKSEwqsmtqesfQESSVKELRRLEDQLAGLQQELAALALKQSSVAEEV 409
Cdd:COG4942    19 ADAAAEAEAELEQLQQEI----AELEKELAALKKE---------EKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
                          90
                  ....*....|....*..
gi 2028477699 410 GLLPQQIQAVRDDVESQ 426
Cdd:COG4942    86 AELEKEIAELRAELEAQ 102
Apolipoprotein pfam01442
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ...
296-479 6.49e-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: 38.01  E-value: 6.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 296 EDTLALLEGLVSRREAALkEDFRRETAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQ----LKSEWQSMTQE 371
Cdd:pfam01442   3 EDSLDELSTYAEELQEQL-GPVAQELVDRLEKETEALRERLQKDLEEVRAKLEPYLEELQAKLGQnveeLRQRLEPYTEE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 372 sFQESSVKELRRLEDQLAGLQQELaalalkQSSVAEEVGLLPQQIQAVRDDVESQFPAWISQFlarggggrvgllqREEM 451
Cdd:pfam01442  82 -LRKRLNADAEELQEKLAPYGEEL------RERLEQNVDALRARLAPYAEELRQKLAERLEEL-------------KESL 141
                         170       180
                  ....*....|....*....|....*...
gi 2028477699 452 QAQLRELESKILTHVAEMQGKSAREAAA 479
Cdd:pfam01442 142 APYAEEVQAQLSQRLQELREKLEPQAED 169
PRK11281 PRK11281
mechanosensitive channel MscK;
328-396 7.22e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.89  E-value: 7.22e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2028477699  328 ELSALRAEHQQDSEDLFKKIVRASQ---ESEARIQQLKSEWQSMTQESFQESSvkeLRRLEDQLAGLQQELA 396
Cdd:PRK11281    70 ALLDKIDRQKEETEQLKQQLAQAPAklrQAQAELEALKDDNDEETRETLSTLS---LRQLESRLAQTLDQLQ 138
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
307-418 7.42e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 307 SRREAALKEDFRRETAARIQEELSALRAEHQQDSEDLFK---KIVRASQESEARIQQLKS--EWQSMTQESFQESSvKEL 381
Cdd:COG4372    32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQarsELEQLEEELEELNEQLQAaqAELAQAQEELESLQ-EEA 110
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2028477699 382 RRLEDQLAGLQQELAALALKQSSVAEEVGLLPQQIQA 418
Cdd:COG4372   111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAE 147
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
315-419 9.37e-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: 9.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2028477699 315 EDFRREtAARIQEELSALRAEHQQDSEDLFKKIVRASQESEARIQQLKSEWQSMTQESFQESSVKE-LRRLEDQLAGLQQ 393
Cdd:COG0542   414 DELERR-LEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEeLEQRYGKIPELEK 492
                          90       100       110
                  ....*....|....*....|....*....|
gi 2028477699 394 ELAA----LALKQSSVAEEVGllPQQIQAV 419
Cdd:COG0542   493 ELAEleeeLAELAPLLREEVT--EEDIAEV 520
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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