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Conserved domains on  [gi|1907112017|ref|XP_036015248|]
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SUN domain-containing protein 2 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SUN_cc1 cd21435
coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 ...
412-465 2.52e-17

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: 75.91  E-value: 2.52e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907112017 412 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADV 465
Cdd:cd21435     1 QEAFQESSVKELGRLEAQLASLRQELAALTLKQEAIQKELEQTKQKTISAVGEQ 54
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
250-464 3.91e-07

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 3.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017  250 LQTLQPAVVSWWAAKESRKQPEVWES-RDASQHFQAEQRVlsrvHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAG 328
Cdd:COG4913    251 IELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELD 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017  329 HGGGSSLSHE-DALSLLEGLVSRREATLKEdlRRDTVAHIQEELATLRAEHHQDSEDLfkkiVQASQESEARVQQLKTEW 407
Cdd:COG4913    327 ELEAQIRGNGgDRLEQLEREIERLERELEE--RERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEEL 400
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907112017  408 KSMTQEAFQesSVKELGRLEAQLASLRQELAALTLKQNSvadevglLPQKIQAARAD 464
Cdd:COG4913    401 EALEEALAE--AEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDA 448
 
Name Accession Description Interval E-value
SUN_cc1 cd21435
coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 ...
412-465 2.52e-17

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: 75.91  E-value: 2.52e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907112017 412 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADV 465
Cdd:cd21435     1 QEAFQESSVKELGRLEAQLASLRQELAALTLKQEAIQKELEQTKQKTISAVGEQ 54
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
250-464 3.91e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 3.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017  250 LQTLQPAVVSWWAAKESRKQPEVWES-RDASQHFQAEQRVlsrvHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAG 328
Cdd:COG4913    251 IELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELD 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017  329 HGGGSSLSHE-DALSLLEGLVSRREATLKEdlRRDTVAHIQEELATLRAEHHQDSEDLfkkiVQASQESEARVQQLKTEW 407
Cdd:COG4913    327 ELEAQIRGNGgDRLEQLEREIERLERELEE--RERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEEL 400
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907112017  408 KSMTQEAFQesSVKELGRLEAQLASLRQELAALTLKQNSvadevglLPQKIQAARAD 464
Cdd:COG4913    401 EALEEALAE--AEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDA 448
PRK11281 PRK11281
mechanosensitive channel MscK;
363-438 2.49e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.67  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017  363 TVAHIQEELATL--RAEHHQDSEDLFKKIVQASQ---ESEARVQQLKTEWKSMTQEAFQESSVKELgrlEAQLASLRQEL 437
Cdd:PRK11281    61 VQQDLEQTLALLdkIDRQKEETEQLKQQLAQAPAklrQAQAELEALKDDNDEETRETLSTLSLRQL---ESRLAQTLDQL 137

                   .
gi 1907112017  438 A 438
Cdd:PRK11281   138 Q 138
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
286-464 8.30e-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: 38.88  E-value: 8.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017  286 QRVLSRVHSLERRLEALAAdfssnwQKE-AIRLERL--ELRQGAAGHGGGSSLSHEDALSLLEglVSRREATLKEDLRRD 362
Cdd:TIGR02168  189 DRLEDILNELERQLKSLER------QAEkAERYKELkaELRELELALLVLRLEELREELEELQ--EELKEAEEELEELTA 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017  363 TVAHIQEELATLRAEHHQDSEDL------FKKIVQASQESEARVQQLKTEWKSMTQEafQESSVKELGRLEAQLASLRQE 436
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELEEEIeelqkeLYALANEISRLEQQKQILRERLANLERQ--LEELEAQLEELESKLDELAEE 338
                          170       180
                   ....*....|....*....|....*...
gi 1907112017  437 LAALTLKQNSVADEVGLLPQKIQAARAD 464
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAE 366
 
Name Accession Description Interval E-value
SUN_cc1 cd21435
coiled-coil domain 1 of SUN domain-containing proteins; SUN (Sad1 and UNC-84) proteins (SUN1 ...
412-465 2.52e-17

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: 75.91  E-value: 2.52e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907112017 412 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADV 465
Cdd:cd21435     1 QEAFQESSVKELGRLEAQLASLRQELAALTLKQEAIQKELEQTKQKTISAVGEQ 54
SUN2_cc1 cd21438
coiled-coil domain 1 of SUN domain-containing protein 2 and similar proteins; SUN ...
412-466 3.04e-17

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: 75.42  E-value: 3.04e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1907112017 412 QEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARADVS 466
Cdd:cd21438     1 QEDLQENFQKELGRLEAQLAGLRQELAALRSDQKALSQQVESFPGQIKAVRDDVE 55
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
250-464 3.91e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.61  E-value: 3.91e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017  250 LQTLQPAVVSWWAAKESRKQPEVWES-RDASQHFQAEQRVlsrvHSLERRLEALAADFSSNWQKEAIRLERLELRQGAAG 328
Cdd:COG4913    251 IELLEPIRELAERYAAARERLAELEYlRAALRLWFAQRRL----ELLEAELEELRAELARLEAELERLEARLDALREELD 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017  329 HGGGSSLSHE-DALSLLEGLVSRREATLKEdlRRDTVAHIQEELATLRAEHHQDSEDLfkkiVQASQESEARVQQLKTEW 407
Cdd:COG4913    327 ELEAQIRGNGgDRLEQLEREIERLERELEE--RERRRARLEALLAALGLPLPASAEEF----AALRAEAAALLEALEEEL 400
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907112017  408 KSMTQEAFQesSVKELGRLEAQLASLRQELAALTLKQNSvadevglLPQKIQAARAD 464
Cdd:COG4913    401 EALEEALAE--AEAALRDLRRELRELEAEIASLERRKSN-------IPARLLALRDA 448
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
295-464 2.73e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.60  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017 295 LERRLEALAADFSSNWQKEAI-RLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRREATLK-EDLRRD-TVAHIQEEL 371
Cdd:COG4717   293 LAREKASLGKEAEELQALPALeELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEElQLEELEQEI 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017 372 ATLRAEHHQDSEDLFKKIVQASQES---EARVQQLKTEWKSMTQEAFQESSVKELGRLEAQLASLRQELAALTLKQNSVA 448
Cdd:COG4717   373 AALLAEAGVEDEEELRAALEQAEEYqelKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELR 452
                         170
                  ....*....|....*.
gi 1907112017 449 DEVGLLPQKIQAARAD 464
Cdd:COG4717   453 EELAELEAELEQLEED 468
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
338-463 1.08e-03

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 40.99  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017 338 EDALSLLEGLVSRREA---TLKEDLRRDTVAHIQEELAtlRAEhhqdsedlfkkivQASQESEARVQQLKTEWKSMTQEA 414
Cdd:COG3524   150 EDAQAIAEALLAESEElvnQLSERAREDAVRFAEEEVE--RAE-------------ERLRDAREALLAFRNRNGILDPEA 214
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907112017 415 FQESSVKELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARA 463
Cdd:COG3524   215 TAEALLQLIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEK 263
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
280-463 1.45e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017 280 QHFQAEQRVL-SRVHSLERRLEALAADFSS-NWQKEAIRLERLELRQGAAGHGGGSSLSHEDALSLLEGLVSRRE----- 352
Cdd:COG1196   235 RELEAELEELeAELEELEAELEELEAELAElEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrel 314
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017 353 ----ATLKEDLRRDT--VAHIQEELATLRAEH------HQDSEDLFKKIVQASQESEARVQQLKTEWKSMTQEAFQEssV 420
Cdd:COG1196   315 eerlEELEEELAELEeeLEELEEELEELEEELeeaeeeLEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA--L 392
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1907112017 421 KELGRLEAQLASLRQELAALTLKQNSVADEVGLLPQKIQAARA 463
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
285-470 1.77e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017 285 EQRVLSRVHSLERRLEALAADFSsnwQKEAiRLERLElRQGAAGHGGGSSLSHEDALSLLEGLVSRREATLKEDLRRDTV 364
Cdd:COG3206   214 AKLLLQQLSELESQLAEARAELA---EAEA-RLAALR-AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTP 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017 365 AH-----IQEELATLRAEHHQDSEDLFKKIVQASQESEARVQQLKTEWKSMTQEafqessVKELGRLEAQLASLRQELAA 439
Cdd:COG3206   289 NHpdviaLRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR------LAELPELEAELRRLEREVEV 362
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1907112017 440 LTLKQNSVAdevgllpQKIQAARADVSGKYP 470
Cdd:COG3206   363 ARELYESLL-------QRLEEARLAEALTVG 386
PRK11281 PRK11281
mechanosensitive channel MscK;
363-438 2.49e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.67  E-value: 2.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017  363 TVAHIQEELATL--RAEHHQDSEDLFKKIVQASQ---ESEARVQQLKTEWKSMTQEAFQESSVKELgrlEAQLASLRQEL 437
Cdd:PRK11281    61 VQQDLEQTLALLdkIDRQKEETEQLKQQLAQAPAklrQAQAELEALKDDNDEETRETLSTLSLRQL---ESRLAQTLDQL 137

                   .
gi 1907112017  438 A 438
Cdd:PRK11281   138 Q 138
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
355-464 3.65e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.00  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017 355 LKEDLRRDTVAHIQEELATLRAEhhqdsedlfkkivqaSQESEARVQQLKTEWKSMTQEAFQESSVKELGRLEAQLASLR 434
Cdd:COG3206   168 LRREEARKALEFLEEQLPELRKE---------------LEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR 232
                          90       100       110
                  ....*....|....*....|....*....|
gi 1907112017 435 QELAALTLKQNSVADEVGLLPQKIQAARAD 464
Cdd:COG3206   233 AELAEAEARLAALRAQLGSGPDALPELLQS 262
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
292-449 6.90e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 39.17  E-value: 6.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017  292 VHSLERRLEALAAdfssnwQKEAIRLERLELRQGAAGHGGGSSlSHEDALSLLEGL---VSRREA--TLKEDLRR----- 361
Cdd:COG3096    436 PENAEDYLAAFRA------KEQQATEEVLELEQKLSVADAARR-QFEKAYELVCKIageVERSQAwqTARELLRRyrsqq 508
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017  362 ---DTVAHIQEELATL--RAEHHQDSEDLFKKIVQASQESEARVQQLKTEwkSMTQEAFQESSVKELGRLEAQLASLRQE 436
Cdd:COG3096    509 alaQRLQQLRAQLAELeqRLRQQQNAERLLEEFCQRIGQQLDAAEELEEL--LAELEAQLEELEEQAAEAVEQRSELRQQ 586
                          170
                   ....*....|...
gi 1907112017  437 LAALTLKQNSVAD 449
Cdd:COG3096    587 LEQLRARIKELAA 599
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
286-464 8.30e-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: 38.88  E-value: 8.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017  286 QRVLSRVHSLERRLEALAAdfssnwQKE-AIRLERL--ELRQGAAGHGGGSSLSHEDALSLLEglVSRREATLKEDLRRD 362
Cdd:TIGR02168  189 DRLEDILNELERQLKSLER------QAEkAERYKELkaELRELELALLVLRLEELREELEELQ--EELKEAEEELEELTA 260
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017  363 TVAHIQEELATLRAEHHQDSEDL------FKKIVQASQESEARVQQLKTEWKSMTQEafQESSVKELGRLEAQLASLRQE 436
Cdd:TIGR02168  261 ELQELEEKLEELRLEVSELEEEIeelqkeLYALANEISRLEQQKQILRERLANLERQ--LEELEAQLEELESKLDELAEE 338
                          170       180
                   ....*....|....*....|....*...
gi 1907112017  437 LAALTLKQNSVADEVGLLPQKIQAARAD 464
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEELEAE 366
PRK09039 PRK09039
peptidoglycan -binding protein;
339-440 9.58e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 38.02  E-value: 9.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907112017 339 DALSLleglvsrrEATLKEDLRrDTVAHIQEELATLRAEHHQdSEDLFKKIVQASQESEARVQQLKTEWKSmtQEAFQES 418
Cdd:PRK09039   67 DLLSL--------ERQGNQDLQ-DSVANLRASLSAAEAERSR-LQALLAELAGAGAAAEGRAGELAQELDS--EKQVSAR 134
                          90       100
                  ....*....|....*....|..
gi 1907112017 419 SVKELGRLEAQLASLRQELAAL 440
Cdd:PRK09039  135 ALAQVELLNQQIAALRRQLAAL 156
 
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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