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Conserved domains on  [gi|1907072738|ref|XP_036011366|]
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centrosomal protein CEP57L1 isoform X13 [Mus musculus]

Protein Classification

Cep57_CLD and Cep57_MT_bd domain-containing protein( domain architecture ID 12163498)

Cep57_CLD and Cep57_MT_bd domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
76-225 1.14e-49

Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.


:

Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 165.88  E-value: 1.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  76 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKK----------------EKQL 139
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQelisqlaaaesrcsllEKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738 140 EYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQRRLF 219
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                  ....*.
gi 1907072738 220 QDRACE 225
Cdd:pfam14073 161 QEKAAQ 166
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
264-337 3.41e-16

Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, nucleates and bundles microtubules. The N-terminal part, family Cep57_CLD, pfam14073, is the centrosome localization domain Cep57.


:

Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 72.99  E-value: 3.41e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907072738 264 QSSGEPVSICDSLSELLMTMEEELDQMNMEHRELLRQMMQ---PGNHSVSEDIEQELEQLAKKMESKGDQISKLKKH 337
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
76-225 1.14e-49

Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.


Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 165.88  E-value: 1.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  76 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKK----------------EKQL 139
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQelisqlaaaesrcsllEKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738 140 EYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQRRLF 219
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                  ....*.
gi 1907072738 220 QDRACE 225
Cdd:pfam14073 161 QEKAAQ 166
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
264-337 3.41e-16

Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, nucleates and bundles microtubules. The N-terminal part, family Cep57_CLD, pfam14073, is the centrosome localization domain Cep57.


Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 72.99  E-value: 3.41e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907072738 264 QSSGEPVSICDSLSELLMTMEEELDQMNMEHRELLRQMMQ---PGNHSVSEDIEQELEQLAKKMESKGDQISKLKKH 337
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
75-201 4.28e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  75 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQkkEKQLEYTKRMVLNVEREKT 154
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL--EQDIARLEERRRELEERLE 319
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907072738 155 MILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDK 201
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
87-352 5.65e-04

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: 5.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738   87 KIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELikQKKEKQLEYTKRMVLNVEREKTMILEQQAQLQRE 166
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL--EELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  167 KEQDQMKLHAKLEKLHVLEKEclrltatRQTAEDKIKclEEKLKEEEHQRRLFQDRacEKTNCLKREPPQQRDHKFRTPT 246
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEE-------LAEAEAEIE--ELEAQIEQLKEELKALR--EALDELRAELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  247 FERKKPFRTTSQARANpqssgepvsicDSLSELLMTMEEELDQMNMEHRELLRQMmqpgnhsvsEDIEQELEQLAKKMES 326
Cdd:TIGR02168  825 RLESLERRIAATERRL-----------EDLEEQIEELSEDIESLAAEIEELEELI---------EELESELEALLNERAS 884
                          250       260
                   ....*....|....*....|....*.
gi 1907072738  327 KGDQISKLKKHQDSVRKLQEKIENSR 352
Cdd:TIGR02168  885 LEEALALLRSELEELSEELRELESKR 910
PTZ00121 PTZ00121
MAEBL; Provisional
82-386 1.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738   82 KTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKEKQLEYTKRmvlnVEREKTMIL---E 158
Cdd:PTZ00121  1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK----AEEDKNMALrkaE 1584
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  159 QQAQLQREKEQDQMKLHA-----KLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQRRLFQDRACEKTNCLKRE 233
Cdd:PTZ00121  1585 EAKKAEEARIEEVMKLYEeekkmKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA 1664
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  234 PPQQRDHKFRTPTFERKKPFRTTSQARANPQSSGEPVSICDSLSELL---------MTMEEELDQMNMEH--RELLRQMM 302
Cdd:PTZ00121  1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEaeekkkaeeLKKAEEENKIKAEEakKEAEEDKK 1744
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  303 QPGNHSVSEDIEQELEQLAKKMESKGDQISKLK--------KHQDSVRKLQ--EKIENSRINESSGIHGNPKG------S 366
Cdd:PTZ00121  1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavieeelDEEDEKRRMEvdKKIKDIFDNFANIIEGGKEGnlvindS 1824
                          330       340
                   ....*....|....*....|
gi 1907072738  367 KNLKTSPRKCVSETSSFQRD 386
Cdd:PTZ00121  1825 KEMEDSAIKEVADSKNMQLE 1844
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
75-191 2.49e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.48  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  75 QALVSALKTLQEKIRRLELERTQAEdnlnllsrEAAQYKKALEEETNErnlaHQELIKQKKEKQLEYTKRMVLNVEREKT 154
Cdd:cd16269   184 EAILQADQALTEKEKEIEAERAKAE--------AAEQERKLLEEQQRE----LEQKLEDQERSYEEHLRQLKEKMEEERE 251
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907072738 155 MILEQQAQLQREKEQDQMKLHAK--LEKLHVLEKECLRL 191
Cdd:cd16269   252 NLLKEQERALESKLKEQEALLEEgfKEQAELLQEEIRSL 290
 
Name Accession Description Interval E-value
Cep57_CLD pfam14073
Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is ...
76-225 1.14e-49

Centrosome localization domain of Cep57; The CLD or centrosome localization domain of Cep57 is found at the N-terminus, and lies approximately between residues 58 and 239. This region lies within the first alpha-helical coiled-coil segment of Cep57, and localizes to the centrosome internally to gamma-tubulin, suggesting that it is either on both centrioles or on a centromatrix component. This N-terminal region can also multimerize with the N-terminus of other Cep57 molecules. The C-terminal part, Family Cep57_MT_bd, pfam06657, is the microtubule-binding region of Cep57.


Pssm-ID: 464080 [Multi-domain]  Cd Length: 178  Bit Score: 165.88  E-value: 1.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  76 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKK----------------EKQL 139
Cdd:pfam14073   1 AVLSALKNLQEKIRRLELERKQAEDNLKQLSRETSHYKEVLQKENDARDPSRGEVSKQNQelisqlaaaesrcsllEKQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738 140 EYTKRMVLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQRRLF 219
Cdd:pfam14073  81 EYMRKMVENAEKERTAVLEKQASLERERSQDSSELQAQLEKLEKLEQEYLRLTRTQSLAETKIKELEEKLQEEEHQRKLV 160

                  ....*.
gi 1907072738 220 QDRACE 225
Cdd:pfam14073 161 QEKAAQ 166
Cep57_MT_bd pfam06657
Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, ...
264-337 3.41e-16

Centrosome microtubule-binding domain of Cep57; This C-terminal region of Cep57 binds, nucleates and bundles microtubules. The N-terminal part, family Cep57_CLD, pfam14073, is the centrosome localization domain Cep57.


Pssm-ID: 461976 [Multi-domain]  Cd Length: 77  Bit Score: 72.99  E-value: 3.41e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907072738 264 QSSGEPVSICDSLSELLMTMEEELDQMNMEHRELLRQMMQ---PGNHSVSEDIEQELEQLAKKMESKGDQISKLKKH 337
Cdd:pfam06657   1 ATMRPSQSPGEALAEVLKELEDEFEHLKLEYQELAAQYNAldpSLGKRKRKDLAEELEELLKRLEAKADQIYALYDV 77
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
75-201 4.28e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  75 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQkkEKQLEYTKRMVLNVEREKT 154
Cdd:COG1196   242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARL--EQDIARLEERRRELEERLE 319
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1907072738 155 MILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDK 201
Cdd:COG1196   320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
75-203 4.73e-05

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: 4.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  75 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELikQKKEKQLEYTKRMVLNVEREKT 154
Cdd:COG1196   298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEEL--EEAEAELAEAEEALLEAEAELA 375
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907072738 155 MILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIK 203
Cdd:COG1196   376 EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELE 424
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
75-203 1.95e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 1.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  75 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAhQELIKQKKEKQLEYTKRMvlnvEREKT 154
Cdd:COG1196   256 EELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL-EERRRELEERLEELEEEL----AELEE 330
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907072738 155 MILEQQAQLQR---EKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIK 203
Cdd:COG1196   331 ELEELEEELEEleeELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELE 382
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
87-352 5.65e-04

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: 5.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738   87 KIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELikQKKEKQLEYTKRMVLNVEREKTMILEQQAQLQRE 166
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEL--EELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  167 KEQDQMKLHAKLEKLHVLEKEclrltatRQTAEDKIKclEEKLKEEEHQRRLFQDRacEKTNCLKREPPQQRDHKFRTPT 246
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEE-------LAEAEAEIE--ELEAQIEQLKEELKALR--EALDELRAELTLLNEEAANLRE 824
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  247 FERKKPFRTTSQARANpqssgepvsicDSLSELLMTMEEELDQMNMEHRELLRQMmqpgnhsvsEDIEQELEQLAKKMES 326
Cdd:TIGR02168  825 RLESLERRIAATERRL-----------EDLEEQIEELSEDIESLAAEIEELEELI---------EELESELEALLNERAS 884
                          250       260
                   ....*....|....*....|....*.
gi 1907072738  327 KGDQISKLKKHQDSVRKLQEKIENSR 352
Cdd:TIGR02168  885 LEEALALLRSELEELSEELRELESKR 910
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
75-203 1.00e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  75 QALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKEKQLeytkrmvlnVEREKT 154
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEE---------AEAELA 361
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907072738 155 MILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIK 203
Cdd:COG1196   362 EAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
PTZ00121 PTZ00121
MAEBL; Provisional
82-386 1.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738   82 KTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKEKQLEYTKRmvlnVEREKTMIL---E 158
Cdd:PTZ00121  1509 KKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK----AEEDKNMALrkaE 1584
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  159 QQAQLQREKEQDQMKLHA-----KLEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQRRLFQDRACEKTNCLKRE 233
Cdd:PTZ00121  1585 EAKKAEEARIEEVMKLYEeekkmKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAA 1664
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  234 PPQQRDHKFRTPTFERKKPFRTTSQARANPQSSGEPVSICDSLSELL---------MTMEEELDQMNMEH--RELLRQMM 302
Cdd:PTZ00121  1665 EEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEaeekkkaeeLKKAEEENKIKAEEakKEAEEDKK 1744
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  303 QPGNHSVSEDIEQELEQLAKKMESKGDQISKLK--------KHQDSVRKLQ--EKIENSRINESSGIHGNPKG------S 366
Cdd:PTZ00121  1745 KAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeavieeelDEEDEKRRMEvdKKIKDIFDNFANIIEGGKEGnlvindS 1824
                          330       340
                   ....*....|....*....|
gi 1907072738  367 KNLKTSPRKCVSETSSFQRD 386
Cdd:PTZ00121  1825 KEMEDSAIKEVADSKNMQLE 1844
PTZ00121 PTZ00121
MAEBL; Provisional
86-409 1.19e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 1.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738   86 EKIRRLELERTQAEDNLNLLSR--EAAQYKKALEEETNERNLAHQELIKQKKE---KQLEYTKRMVLNVEREKTMILEQQ 160
Cdd:PTZ00121  1584 EEAKKAEEARIEEVMKLYEEEKkmKAEEAKKAEEAKIKAEELKKAEEEKKKVEqlkKKEAEEKKKAEELKKAEEENKIKA 1663
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  161 AQLQREKEQDQMKLHaklEKLHVLEKECLRLTATRQTAEDKIKCLEEKLKEEEHQRRLFQDRACEKTNCLKREPPQQRDH 240
Cdd:PTZ00121  1664 AEEAKKAEEDKKKAE---EAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAE 1740
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  241 KFRTPTFERKKpfRTTSQARANPQSSGEPVSICDSLSELLMTMEEELDQMNMEHRELLRQMMQpgnhsvseDIEQELEQL 320
Cdd:PTZ00121  1741 EDKKKAEEAKK--DEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK--------DIFDNFANI 1810
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  321 AKKMESKGDQISKLKKHQDSVRKLQEKIENSRINESSGI--HGNPKGSKNLKTSPRKCVSETSSFQRDRGFQPVQVHSLQ 398
Cdd:PTZ00121  1811 IEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFekHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEI 1890
                          330
                   ....*....|.
gi 1907072738  399 SKLRRDDIKWE 409
Cdd:PTZ00121  1891 EKIDKDDIERE 1901
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
79-187 1.77e-03

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


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 40.45  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  79 SALKTLQEKIRRLELERTQAEDNLNLLSRE-AAQYKKALEEETNERNLAHQeliKQKKEKQLeytkrmvLNVEREKTMIL 157
Cdd:COG0542   411 EELDELERRLEQLEIEKEALKKEQDEASFErLAELRDELAELEEELEALKA---RWEAEKEL-------IEEIQELKEEL 480
                          90       100       110
                  ....*....|....*....|....*....|
gi 1907072738 158 EQQAQLQREKEQDQMKLHAKLEKLHVLEKE 187
Cdd:COG0542   481 EQRYGKIPELEKELAELEEELAELAPLLRE 510
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
75-191 2.49e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 39.48  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  75 QALVSALKTLQEKIRRLELERTQAEdnlnllsrEAAQYKKALEEETNErnlaHQELIKQKKEKQLEYTKRMVLNVEREKT 154
Cdd:cd16269   184 EAILQADQALTEKEKEIEAERAKAE--------AAEQERKLLEEQQRE----LEQKLEDQERSYEEHLRQLKEKMEEERE 251
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1907072738 155 MILEQQAQLQREKEQDQMKLHAK--LEKLHVLEKECLRL 191
Cdd:cd16269   252 NLLKEQERALESKLKEQEALLEEgfKEQAELLQEEIRSL 290
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
75-203 2.78e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  75 QALVSALKTLQEKIRRLELERTQAE-----DNLNLLSREAAQYKK---ALEEETNERNLAHQELIKQKKEKQLEYTKRM- 145
Cdd:COG1196   216 RELKEELKELEAELLLLKLRELEAEleeleAELEELEAELEELEAelaELEAELEELRLELEELELELEEAQAEEYELLa 295
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907072738 146 -VLNVEREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIK 203
Cdd:COG1196   296 eLARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
76-349 6.89e-03

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: 38.90  E-value: 6.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738   76 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKEKQLEYTKRM------VLNV 149
Cdd:TIGR02169  227 ELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIgeleaeIASL 306
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  150 EREKTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIKcleeklkeeehqrrlfqdrACEKTNC 229
Cdd:TIGR02169  307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYA-------------------ELKEELE 367
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  230 LKREPPQQRDHKFRTpTFERKKPFRTTSQARANPQssGEPVSICDSLSELLMTMEEELDQMNMEHRELLRQmmQPGNHSV 309
Cdd:TIGR02169  368 DLRAELEEVDKEFAE-TRDELKDYREKLEKLKREI--NELKRELDRLQEELQRLSEELADLNAAIAGIEAK--INELEEE 442
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1907072738  310 SEDI-------EQELEQLAKKMESKGDQISKLKKHQDSVRKLQEKIE 349
Cdd:TIGR02169  443 KEDKaleikkqEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQ 489
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
80-203 7.49e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 7.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  80 ALKTL---QEKIRRLELERTQAEDNLNLLSREAAQYKK--ALEEETNERNLAHQELIKQKKEKQLEYTKRMVLNVEREKT 154
Cdd:COG1196   177 AERKLeatEENLERLEDILGELERQLEPLERQAEKAERyrELKEELKELEAELLLLKLRELEAELEELEAELEELEAELE 256
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1907072738 155 MILEQQAQLQREKEQDQMKLHAKLEKLHVLEKECLRLTATRQTAEDKIK 203
Cdd:COG1196   257 ELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
82-180 7.56e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 38.65  E-value: 7.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  82 KTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALEEETNERNLAHQELIKQKKEKQLEYTKRMVLNVEREKTMILEQQA 161
Cdd:PRK00409  530 RELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGGYASVKAHEL 609
                          90       100
                  ....*....|....*....|
gi 1907072738 162 Q-LQREKEQDQMKLHAKLEK 180
Cdd:PRK00409  610 IeARKRLNKANEKKEKKKKK 629
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
76-351 8.61e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 38.67  E-value: 8.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738   76 ALVSALKTLQEKIRRLELERTQAEDNLNLLSREAAQYKKALE--EETNERNLAHQELIKQKKEKQLEYTKRM----VLNV 149
Cdd:pfam12128  608 KAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKnaRLDLRRLFDEKQSEKDKKNKALAERKDSanerLNSL 687
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  150 ERE-KTMILEQQAQLQREKEQDQMKLHAKLEKLHVLEkeclrltATRQTAEDKIKcLEEKLKEEEHQRRLFQDRACEKTN 228
Cdd:pfam12128  688 EAQlKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVE-------GALDAQLALLK-AAIAARRSGAKAELKALETWYKRD 759
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907072738  229 CLKREPPQQRDHKFRTptfERKKPFRTTSQARANPQSSgepvsicdslsellmtmeEELDQMnMEHRELLRqmmQPGNHS 308
Cdd:pfam12128  760 LASLGVDPDVIAKLKR---EIRTLERKIERIAVRRQEV------------------LRYFDW-YQETWLQR---RPRLAT 814
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1907072738  309 VSEDIEQELE----QLAKKMESKGDQISKLKKHQDSVRKLQEKIENS 351
Cdd:pfam12128  815 QLSNIERAISelqqQLARLIADTKLRRAKLEMERKASEKQQVRLSEN 861
PRK12704 PRK12704
phosphodiesterase; Provisional
108-182 8.78e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.22  E-value: 8.78e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907072738 108 EAAQYKKALEEETNERN--LAHQELIKQKKEKQLEytKRMVLNVEREKtmILEQQAQLQREKEQDQMKLHAKLEKLH 182
Cdd:PRK12704   65 EIHKLRNEFEKELRERRneLQKLEKRLLQKEENLD--RKLELLEKREE--ELEKKEKELEQKQQELEKKEEELEELI 137
 
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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