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Conserved domains on  [gi|58037369|ref|NP_083199|]
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mRNA export factor GLE1 [Mus musculus]

Protein Classification

Smc and GLE1 domain-containing protein( domain architecture ID 10544838)

Smc and GLE1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GLE1 pfam07817
GLE1-like protein; The members of this family are sequences that are similar to the human ...
411-650 9.51e-107

GLE1-like protein; The members of this family are sequences that are similar to the human protein GLE1. This protein is localized at the nuclear pore complexes and functions in poly(A)+ RNA export to the cytoplasm.


:

Pssm-ID: 462280  Cd Length: 234  Bit Score: 323.77  E-value: 9.51e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   411 SKDSQTKKIKMDLQKAATIPVSQISTIAgSKLKEIFDKIHSLL-SGKPVQSGgrsvsvtLNPQGLDFVQYKLAEKFVKQG 489
Cdd:pfam07817   1 KQDPELKKYRFQLKRAINPKVGQLSNSS-EQLTDITNELNELLdSGKPVPVG-------HPQLAYIWILNFLAKAIVSQA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   490 EEEVASHHEAAFPIAVVASGIWMLHPKVGDLILAHLHKKCPYSVPFYPAFKEGMALEDYQRMLGYQVT-DSKVEQQDNFL 568
Cdd:pfam07817  73 ETEVSVKPEAAFPLARVAVGLWSRHPELGDLLLARFVKKCPYLVPFYPPKTCGQDTEEYRKRLGYKRSdDGKWETEDKYL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   569 KRMSGMIRLYAAIIQLQWPYGNRQEAHPHGLNHGWRWLAQVLNMEPLSDVTATLLFDFLEVCGNALMKQYQVQFWKMILL 648
Cdd:pfam07817 153 ERMSGIIRLYAAITQTPLPKSSKQNPHPHGLPIGWRWLARILNTEPLSNTTATLLGAFLEVAGNRLLQAYGKQFIKLLQL 232

                  ..
gi 58037369   649 IK 650
Cdd:pfam07817 233 IQ 234
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
149-351 4.66e-08

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: 56.60  E-value: 4.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    149 LRQWQEEQERKVRALSEMASEQLKRFDELKElKLHKEFQDLQEVMEKS--TREALGHQEKLKEEHRHRAKILNLKLREAE 226
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEE-ELEQLRKELEELSRQIsaLRKDLARLEAEVEQLEERIAQLSKELTELE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    227 QQRVKQAEQEQLRKEEGQVRLRSLYSLQEEVLQLNQQLDA-----SSQHKEL--LSVDLAAFQTRGNQLCGLISSIIRTT 299
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealDELRAELtlLNEEAANLRERLESLERRIAATERRL 840
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 58037369    300 LESGYPTAENQAEAERALQEMRDL---LSDLEQEITRASQVKKKHEEEAKVKRQE 351
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSE 895
 
Name Accession Description Interval E-value
GLE1 pfam07817
GLE1-like protein; The members of this family are sequences that are similar to the human ...
411-650 9.51e-107

GLE1-like protein; The members of this family are sequences that are similar to the human protein GLE1. This protein is localized at the nuclear pore complexes and functions in poly(A)+ RNA export to the cytoplasm.


Pssm-ID: 462280  Cd Length: 234  Bit Score: 323.77  E-value: 9.51e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   411 SKDSQTKKIKMDLQKAATIPVSQISTIAgSKLKEIFDKIHSLL-SGKPVQSGgrsvsvtLNPQGLDFVQYKLAEKFVKQG 489
Cdd:pfam07817   1 KQDPELKKYRFQLKRAINPKVGQLSNSS-EQLTDITNELNELLdSGKPVPVG-------HPQLAYIWILNFLAKAIVSQA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   490 EEEVASHHEAAFPIAVVASGIWMLHPKVGDLILAHLHKKCPYSVPFYPAFKEGMALEDYQRMLGYQVT-DSKVEQQDNFL 568
Cdd:pfam07817  73 ETEVSVKPEAAFPLARVAVGLWSRHPELGDLLLARFVKKCPYLVPFYPPKTCGQDTEEYRKRLGYKRSdDGKWETEDKYL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   569 KRMSGMIRLYAAIIQLQWPYGNRQEAHPHGLNHGWRWLAQVLNMEPLSDVTATLLFDFLEVCGNALMKQYQVQFWKMILL 648
Cdd:pfam07817 153 ERMSGIIRLYAAITQTPLPKSSKQNPHPHGLPIGWRWLARILNTEPLSNTTATLLGAFLEVAGNRLLQAYGKQFIKLLQL 232

                  ..
gi 58037369   649 IK 650
Cdd:pfam07817 233 IQ 234
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
149-351 4.66e-08

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: 56.60  E-value: 4.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    149 LRQWQEEQERKVRALSEMASEQLKRFDELKElKLHKEFQDLQEVMEKS--TREALGHQEKLKEEHRHRAKILNLKLREAE 226
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEE-ELEQLRKELEELSRQIsaLRKDLARLEAEVEQLEERIAQLSKELTELE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    227 QQRVKQAEQEQLRKEEGQVRLRSLYSLQEEVLQLNQQLDA-----SSQHKEL--LSVDLAAFQTRGNQLCGLISSIIRTT 299
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealDELRAELtlLNEEAANLRERLESLERRIAATERRL 840
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 58037369    300 LESGYPTAENQAEAERALQEMRDL---LSDLEQEITRASQVKKKHEEEAKVKRQE 351
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSE 895
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
154-351 2.78e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369  154 EEQERKVRALSEMAsEQLKRFDELKElklhkEFQDLQEVMEKSTREALGHQEKLKEEHRHRakiLNLKLREAEQQRV-KQ 232
Cdd:COG4913  245 EDAREQIELLEPIR-ELAERYAAARE-----RLAELEYLRAALRLWFAQRRLELLEAELEE---LRAELARLEAELErLE 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369  233 AEQEQLRKEEGQVRLRSLYSLQEEVLQLNQQLDASSQHKELLSVDLAAFQTRGNQLcGLISSIIRTTLesgyptAENQAE 312
Cdd:COG4913  316 ARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL-GLPLPASAEEF------AALRAE 388
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 58037369  313 AERALQEMRDLLSDLEQEITRASQVKKKHEEEAKVKRQE 351
Cdd:COG4913  389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
PTZ00121 PTZ00121
MAEBL; Provisional
140-419 1.46e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   140 AHRMRGTEGLRQWQEEQERKVRALSEMASEQLKRFDELkeLKLHKEFQDLQEVMEKSTREALGHQEKLKEEHRHRAKILN 219
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV--MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   220 LKLREAEQqrVKQAEQEQLRKEEGQVRLRSLYSLQEEVLQLNQQLDASSQHKELLSVDL---AAFQTRGNQLCGLISSII 296
Cdd:PTZ00121 1638 LKKKEAEE--KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkeAEEAKKAEELKKKEAEEK 1715
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   297 RTTLESGYPTAENQAEAERALQEMrdllsdlEQEITRASQVKKKHEEEAKVKrQESQVQQGPAPPTQTSAPSPSPVGAQN 376
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEA-------EEDKKKAEEAKKDEEEKKKIA-HLKKEEEKKAEEIRKEKEAVIEEELDE 1787
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 58037369   377 EDLQVKVQ-----DSTMQWYQQLQDASAKCVLAFEDLTSSKDSQTKKI 419
Cdd:PTZ00121 1788 EDEKRRMEvdkkiKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEV 1835
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
149-333 5.64e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.35  E-value: 5.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   149 LRQWQEEQER----KVRALSEMASEQLKRFDELKELK------------LHKEFQDLQEVMEKSTREALGHQEKLK--EE 210
Cdd:pfam10174 350 LRLRLEEKESflnkKTKQLQDLTEEKSTLAGEIRDLKdmldvkerkinvLQKKIENLQEQLRDKDKQLAGLKERVKslQT 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   211 HRHRAKILNLKLREA--EQQRVKQAEQEQlRKEEGQVRLRSLYSLQEEVLQLNQQLDASSQHKELLSVDLAAFQTRGNQL 288
Cdd:pfam10174 430 DSSNTDTALTTLEEAlsEKERIIERLKEQ-REREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSL 508
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58037369   289 CgliSSIIR-------------------TTLESGYPTAENQAEAERALQEMRDLLSDLEQEITR 333
Cdd:pfam10174 509 A---SSGLKkdsklksleiaveqkkeecSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVAR 569
 
Name Accession Description Interval E-value
GLE1 pfam07817
GLE1-like protein; The members of this family are sequences that are similar to the human ...
411-650 9.51e-107

GLE1-like protein; The members of this family are sequences that are similar to the human protein GLE1. This protein is localized at the nuclear pore complexes and functions in poly(A)+ RNA export to the cytoplasm.


Pssm-ID: 462280  Cd Length: 234  Bit Score: 323.77  E-value: 9.51e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   411 SKDSQTKKIKMDLQKAATIPVSQISTIAgSKLKEIFDKIHSLL-SGKPVQSGgrsvsvtLNPQGLDFVQYKLAEKFVKQG 489
Cdd:pfam07817   1 KQDPELKKYRFQLKRAINPKVGQLSNSS-EQLTDITNELNELLdSGKPVPVG-------HPQLAYIWILNFLAKAIVSQA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   490 EEEVASHHEAAFPIAVVASGIWMLHPKVGDLILAHLHKKCPYSVPFYPAFKEGMALEDYQRMLGYQVT-DSKVEQQDNFL 568
Cdd:pfam07817  73 ETEVSVKPEAAFPLARVAVGLWSRHPELGDLLLARFVKKCPYLVPFYPPKTCGQDTEEYRKRLGYKRSdDGKWETEDKYL 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   569 KRMSGMIRLYAAIIQLQWPYGNRQEAHPHGLNHGWRWLAQVLNMEPLSDVTATLLFDFLEVCGNALMKQYQVQFWKMILL 648
Cdd:pfam07817 153 ERMSGIIRLYAAITQTPLPKSSKQNPHPHGLPIGWRWLARILNTEPLSNTTATLLGAFLEVAGNRLLQAYGKQFIKLLQL 232

                  ..
gi 58037369   649 IK 650
Cdd:pfam07817 233 IQ 234
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
149-351 4.66e-08

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: 56.60  E-value: 4.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    149 LRQWQEEQERKVRALSEMASEQLKRFDELKElKLHKEFQDLQEVMEKS--TREALGHQEKLKEEHRHRAKILNLKLREAE 226
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEE-ELEQLRKELEELSRQIsaLRKDLARLEAEVEQLEERIAQLSKELTELE 760
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    227 QQRVKQAEQEQLRKEEGQVRLRSLYSLQEEVLQLNQQLDA-----SSQHKEL--LSVDLAAFQTRGNQLCGLISSIIRTT 299
Cdd:TIGR02168  761 AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKAlrealDELRAELtlLNEEAANLRERLESLERRIAATERRL 840
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 58037369    300 LESGYPTAENQAEAERALQEMRDL---LSDLEQEITRASQVKKKHEEEAKVKRQE 351
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELeelIEELESELEALLNERASLEEALALLRSE 895
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
154-351 2.78e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 54.15  E-value: 2.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369  154 EEQERKVRALSEMAsEQLKRFDELKElklhkEFQDLQEVMEKSTREALGHQEKLKEEHRHRakiLNLKLREAEQQRV-KQ 232
Cdd:COG4913  245 EDAREQIELLEPIR-ELAERYAAARE-----RLAELEYLRAALRLWFAQRRLELLEAELEE---LRAELARLEAELErLE 315
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369  233 AEQEQLRKEEGQVRLRSLYSLQEEVLQLNQQLDASSQHKELLSVDLAAFQTRGNQLcGLISSIIRTTLesgyptAENQAE 312
Cdd:COG4913  316 ARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAL-GLPLPASAEEF------AALRAE 388
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 58037369  313 AERALQEMRDLLSDLEQEITRASQVKKKHEEEAKVKRQE 351
Cdd:COG4913  389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAE 427
PTZ00121 PTZ00121
MAEBL; Provisional
140-419 1.46e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.07  E-value: 1.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   140 AHRMRGTEGLRQWQEEQERKVRALSEMASEQLKRFDELkeLKLHKEFQDLQEVMEKSTREALGHQEKLKEEHRHRAKILN 219
Cdd:PTZ00121 1560 AEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV--MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQ 1637
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   220 LKLREAEQqrVKQAEQEQLRKEEGQVRLRSLYSLQEEVLQLNQQLDASSQHKELLSVDL---AAFQTRGNQLCGLISSII 296
Cdd:PTZ00121 1638 LKKKEAEE--KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALkkeAEEAKKAEELKKKEAEEK 1715
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   297 RTTLESGYPTAENQAEAERALQEMrdllsdlEQEITRASQVKKKHEEEAKVKrQESQVQQGPAPPTQTSAPSPSPVGAQN 376
Cdd:PTZ00121 1716 KKAEELKKAEEENKIKAEEAKKEA-------EEDKKKAEEAKKDEEEKKKIA-HLKKEEEKKAEEIRKEKEAVIEEELDE 1787
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 58037369   377 EDLQVKVQ-----DSTMQWYQQLQDASAKCVLAFEDLTSSKDSQTKKI 419
Cdd:PTZ00121 1788 EDEKRRMEvdkkiKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEV 1835
PTZ00121 PTZ00121
MAEBL; Provisional
140-351 2.26e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   140 AHRMRGTEGLRQWQEEQERKVRALSEmASEQLKRFDELKELKLHKEFQDLQEVME-KSTREALGHQEKLKEEHRHRAKil 218
Cdd:PTZ00121 1479 AEEAKKADEAKKKAEEAKKKADEAKK-AAEAKKKADEAKKAEEAKKADEAKKAEEaKKADEAKKAEEKKKADELKKAE-- 1555
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   219 nlKLREAEQqrVKQAEQEQLRKEEGQVRLRSlyslQEEVLQLNQQLDASSQHKELLSVDLAAFQTRGNqlcglissiirt 298
Cdd:PTZ00121 1556 --ELKKAEE--KKKAEEAKKAEEDKNMALRK----AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKA------------ 1615
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 58037369   299 tlESGYPTAENQAEAERALQEMRDLLSDLEQEITRASQVKKKhEEEAKVKRQE 351
Cdd:PTZ00121 1616 --EEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA-EEENKIKAAE 1665
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
139-449 4.13e-06

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: 50.44  E-value: 4.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    139 LAHRMRGTEGLRQWQEEQERKVRALSEMASEQLKRFDELKElKLHKEFQDLQEVMEKSTREalgHQEKLKEEHRHRAKIL 218
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE-ELEAQIEQLKEELKALREA---LDELRAELTLLNEEAA 820
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    219 NLKLREAEQQRVKQAEQEQLRKEEGQVRlrslySLQEEVLQLNQQLDASSQHKELLSVDLAAFQTRGNQLCGLISSiirt 298
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIE-----ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL---- 891
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    299 tLESGYPTAENQ-AEAERALQEMRDLLSDLEQEITRASQvkkkHEEEAKVKRQESQVQ-------QGPAPPTQTSAPSPS 370
Cdd:TIGR02168  892 -LRSELEELSEElRELESKRSELRRELEELREKLAQLEL----RLEGLEVRIDNLQERlseeyslTLEEAEALENKIEDD 966
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    371 PVGAQNE--DLQVKVQD------STMQWYQQLQDAsakcvlaFEDLTSSKDSQTKKIKmDLQKAatipVSQISTIAGSKL 442
Cdd:TIGR02168  967 EEEARRRlkRLENKIKElgpvnlAAIEEYEELKER-------YDFLTAQKEDLTEAKE-TLEEA----IEEIDREARERF 1034

                   ....*..
gi 58037369    443 KEIFDKI 449
Cdd:TIGR02168 1035 KDTFDQV 1041
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
154-356 6.16e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 6.16e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 154 EEQERKVRALSEMAsEQLKRF----DELKELK----------LHKEFQDLQEVMEKSTREALGHQEKL----KEEHRHRA 215
Cdd:COG1196 196 GELERQLEPLERQA-EKAERYrelkEELKELEaellllklreLEAELEELEAELEELEAELEELEAELaeleAELEELRL 274
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 216 KILNLKLR-EAEQQRVKQAEQEQLRKEEGQVRLRSLYS-LQEEVLQLNQQLDASSQHKELLSVDLAAFQTRGNQLCGLIS 293
Cdd:COG1196 275 ELEELELElEEAQAEEYELLAELARLEQDIARLEERRReLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58037369 294 SIIRTTLESgyptAENQAEAERALQEMRDLLSDLEQEITRASQvkKKHEEEAKVKRQESQVQQ 356
Cdd:COG1196 355 EAEAELAEA----EEALLEAEAELAEAEEELEELAEELLEALR--AAAELAAQLEELEEAEEA 411
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
139-356 1.55e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.39  E-value: 1.55e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 139 LAHRMRGTEGLRQWQEEQERKVRALSEMASEQLKRFD-ELKELKLH-----KEFQDLQEVMEKSTRE------ALGHQEK 206
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEaELEELRLEleeleLELEEAQAEEYELLAElarleqDIARLEE 309
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 207 LKEEHRHRAKILNLKLREAEQQRVKQAEQEQLRKEEGQVRLRSLYSLQEEVLQLNQQL-DASSQHKELLSVDLAAFQTRG 285
Cdd:COG1196 310 RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALlEAEAELAEAEEELEELAEELL 389
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58037369 286 NQLcgliSSIIRTTLESGYPTAENQAEAERALQEMRDLLSDLEQEITRASQVKKKHEEEAKVKRQESQVQQ 356
Cdd:COG1196 390 EAL----RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE 456
PTZ00121 PTZ00121
MAEBL; Provisional
153-351 3.12e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 47.44  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   153 QEEQERKVRALSEMASEQLKRFDELKELKLHKEFQDLQEVMEKSTREALGHQEKLK--------EEHRHRAKILNLKLRE 224
Cdd:PTZ00121 1503 KKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKkaeekkkaEEAKKAEEDKNMALRK 1582
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   225 AEQQR----------------VKQAEQEQLRK-EEGQVRLRSLYSLQEE---VLQLNQQLDASSQHKELLSVDLAAFQTR 284
Cdd:PTZ00121 1583 AEEAKkaeearieevmklyeeEKKMKAEEAKKaEEAKIKAEELKKAEEEkkkVEQLKKKEAEEKKKAEELKKAEEENKIK 1662
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 58037369   285 GNQLcglissiiRTTLESGYPTAENQAEAERALQEMRDLLSDLEQEITRASQVKKKHEEEAK----VKRQE 351
Cdd:PTZ00121 1663 AAEE--------AKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKkaeeLKKAE 1725
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
146-351 3.46e-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: 3.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    146 TEGLRQWQEEQERKVRALSEMASEQLKRFDELKELKLHKEFQDLQ-EVMEKSTREALGHQEKLKEEHRHRAKILNLKLRE 224
Cdd:TIGR02169  293 KEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEiEELEREIEEERKRRDKLTEEYAELKEELEDLRAE 372
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    225 AEQQRVKQAEqeqLRKEEGQVRlRSLYSLQEEVLQLNQQLDASSQHKELLSVDLAAFQtrgNQLCGLISSI--IRTTLES 302
Cdd:TIGR02169  373 LEEVDKEFAE---TRDELKDYR-EKLEKLKREINELKRELDRLQEELQRLSEELADLN---AAIAGIEAKIneLEEEKED 445
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 58037369    303 gypTAENQAEAERALQEMRDLLSDLEQEITRASQVKKKHEEEAKVKRQE 351
Cdd:TIGR02169  446 ---KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
146-354 5.13e-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: 5.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    146 TEGLRQWQEEQERKVRALSEMAseqlKRFDELKelklhKEFQDLQEVMEKSTREALGHQEKLKEEHRHRAKiLNLKLREA 225
Cdd:TIGR02168  259 TAELQELEEKLEELRLEVSELE----EEIEELQ-----KELYALANEISRLEQQKQILRERLANLERQLEE-LEAQLEEL 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    226 EQQRVKQAEQEQLRKEEgqvrlrsLYSLQEEVLQLNQQLDASSQHKELLSVDLAAFQTRgnqlcglissiiRTTLESGYP 305
Cdd:TIGR02168  329 ESKLDELAEELAELEEK-------LEELKEELESLEAELEELEAELEELESRLEELEEQ------------LETLRSKVA 389
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 58037369    306 TAENQAEAERA-LQEMRDLLSDLEQEITRASQVKKKHE---EEAKVKRQESQV 354
Cdd:TIGR02168  390 QLELQIASLNNeIERLEARLERLEDRRERLQQEIEELLkklEEAELKELQAEL 442
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
149-333 5.64e-05

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 46.35  E-value: 5.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   149 LRQWQEEQER----KVRALSEMASEQLKRFDELKELK------------LHKEFQDLQEVMEKSTREALGHQEKLK--EE 210
Cdd:pfam10174 350 LRLRLEEKESflnkKTKQLQDLTEEKSTLAGEIRDLKdmldvkerkinvLQKKIENLQEQLRDKDKQLAGLKERVKslQT 429
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   211 HRHRAKILNLKLREA--EQQRVKQAEQEQlRKEEGQVRLRSLYSLQEEVLQLNQQLDASSQHKELLSVDLAAFQTRGNQL 288
Cdd:pfam10174 430 DSSNTDTALTTLEEAlsEKERIIERLKEQ-REREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSL 508
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 58037369   289 CgliSSIIR-------------------TTLESGYPTAENQAEAERALQEMRDLLSDLEQEITR 333
Cdd:pfam10174 509 A---SSGLKkdsklksleiaveqkkeecSKLENQLKKAHNAEEAVRTNPEINDRIRLLEQEVAR 569
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
144-356 9.69e-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: 9.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 144 RGTEGLRQWQEEQERKVRALSEMASEQLKRFDELKELKlhKEFQDLQEVMEKSTREALGHQEKLKEEHRHRAKilnlklR 223
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELE--EELEEAEEELEEAEAELAEAEEALLEAEAELAE------A 377
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 224 EAEQQRVKQAEQEQLRKEEgqvrlrslySLQEEVLQLNQQLDASSQHKELLSVDLAAFQTRGNQLCGLISSIIRTTLESg 303
Cdd:COG1196 378 EEELEELAEELLEALRAAA---------ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA- 447
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 58037369 304 yptAENQAEAERALQEMRDLLSDLEQEIT--RASQVKKKHEEEAKVKRQESQVQQ 356
Cdd:COG1196 448 ---AEEEAELEEEEEALLELLAELLEEAAllEAALAELLEELAEAAARLLLLLEA 499
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
155-356 1.76e-04

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: 44.95  E-value: 1.76e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 155 EQERKVRALSEMASEQLKRF---DELKELKLH--KEFQDLQEVMEKSTREALGHQEKLKEEHRHRAKILNLKLREAEQQR 229
Cdd:COG5185 302 TKSIDIKKATESLEEQLAAAeaeQELEESKREteTGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDS 381
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 230 VKQaEQEQLRKEEGQVRLRSLYSLQEEVLQLNQQLDASSQHKELLSVDLAA----FQTRGNQLCGLISSIIRTTLESGYP 305
Cdd:COG5185 382 FKD-TIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQatssNEEVSKLLNELISELNKVMREADEE 460
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 58037369 306 TAENQAEAERAL-----QEMRDLLSDLEQEITRASQVKKKHEE-EAKVKRQESQVQQ 356
Cdd:COG5185 461 SQSRLEEAYDEInrsvrSKKEDLNEELTQIESRVSTLKATLEKlRAKLERQLEGVRS 517
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
173-356 2.05e-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: 44.67  E-value: 2.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    173 RFDELKELKLHKEFQDLQEVMEKSTREALGHQEKLkEEHRHRAKILNLKLREAEQQ-RVKQAEQEQLRKEEGQVRLRsLY 251
Cdd:TIGR02169  663 RGGILFSRSEPAELQRLRERLEGLKRELSSLQSEL-RRIENRLDELSQELSDASRKiGEIEKEIEQLEQEEEKLKER-LE 740
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    252 SLQEEVLQLNQQLDASSQHKELLSVDLAAFQTRGNQLCGLISSIIRTTLESGYPTAENQAEA-ERALQEMRDLLSDLEQE 330
Cdd:TIGR02169  741 ELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKlEEEVSRIEARLREIEQK 820
                          170       180
                   ....*....|....*....|....*.
gi 58037369    331 ITRASQVKKKHEEEakvkRQESQVQQ 356
Cdd:TIGR02169  821 LNRLTLEKEYLEKE----IQELQEQR 842
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
147-247 2.06e-04

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 44.56  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   147 EGLRQWQEEQERKVRALSEMASEQLKRFDE--LKELKLHKEFQDLQEVMEKSTREALGHQEKLKEEHRHRAKILNLKLRE 224
Cdd:pfam15709 359 EQRRLQQEQLERAEKMREELELEQQRRFEEirLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRK 438
                          90       100
                  ....*....|....*....|...
gi 58037369   225 AEQQRVKQAEQEQLRKEEGQVRL 247
Cdd:pfam15709 439 KQQEEAERAEAEKQRQKELEMQL 461
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
184-356 5.58e-04

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: 42.83  E-value: 5.58e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 184 KEFQDLQEVMEKSTREALGHQEKLKEEHRHRAKILNlKLREAEQQRVKQAEQEQLRKEEGQVRLRSLYSLQEEVLQLNQQ 263
Cdd:COG4942  20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLK-QLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 264 LDassQHKELLSVDLAAFQTRGNQ--LCGLISS-----IIRTTLESGYPTAENQAEAErALQEMRDLLSDLEQEITRASQ 336
Cdd:COG4942  99 LE---AQKEELAELLRALYRLGRQppLALLLSPedfldAVRRLQYLKYLAPARREQAE-ELRADLAELAALRAELEAERA 174
                       170       180
                ....*....|....*....|
gi 58037369 337 VKKKHEEEAKVKRQESQVQQ 356
Cdd:COG4942 175 ELEALLAELEEERAALEALK 194
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
147-346 7.39e-04

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 42.33  E-value: 7.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   147 EGLRQWQEEQERKVRalsEMASEQLKRFDELKELKLHKE--FQDLQEVMEKSTREALgHQEKLKEEHRHRAKILNLKLRE 224
Cdd:pfam15558  58 QSQEQWQAEKEQRKA---RLGREERRRADRREKQVIEKEsrWREQAEDQENQRQEKL-ERARQEAEQRKQCQEQRLKEKE 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   225 AEQQRVK-QAEQEQLRKEE--GQVRLRSLYSLQEEVLQLNQqldASSQHKELLSVDLAAfQTRGNQLcglissIIRTTLE 301
Cdd:pfam15558 134 EELQALReQNSLQLQERLEeaCHKRQLKEREEQKKVQENNL---SELLNHQARKVLVDC-QAKAEEL------LRRLSLE 203
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 58037369   302 SGYPTAEN--QAEAERALQEMRDLLSDLEQEITRASQVKKKHEEEAK 346
Cdd:pfam15558 204 QSLQRSQEnyEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERQ 250
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
208-356 1.01e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 42.31  E-value: 1.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 208 KEEHRHRAKILNLKLREAEQQrVKQAEQ--EQLRKEEGqvrlrsLYSLQEEVLQLNQQLDASSQHKELLSVDLAAFQTRG 285
Cdd:COG3206 170 REEARKALEFLEEQLPELRKE-LEEAEAalEEFRQKNG------LVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 58037369 286 NQLcglissiiRTTLESGyPTAENQAEAERALQEMRDLLSDLEQEITRASQV-KKKHEE----EAKVKRQESQVQQ 356
Cdd:COG3206 243 AAL--------RAQLGSG-PDALPELLQSPVIQQLRAQLAELEAELAELSARyTPNHPDvialRAQIAALRAQLQQ 309
PTZ00121 PTZ00121
MAEBL; Provisional
131-257 1.13e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   131 EGCIRMYELAHR----MRGTEGLRQWQEEQERKVRALSEMASEQlKRFDELKElKLHKEFQDLQEVMEKSTREALGHQEK 206
Cdd:PTZ00121 1658 ENKIKAAEEAKKaeedKKKAEEAKKAEEDEKKAAEALKKEAEEA-KKAEELKK-KEAEEKKKAEELKKAEEENKIKAEEA 1735
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 58037369   207 LKEEHRHRAKILNLKLREAEQQRVKQAEQEQLRKEEgQVRLRSLYSLQEEV 257
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAE-EIRKEKEAVIEEEL 1785
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
153-356 1.50e-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: 41.29  E-value: 1.50e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 153 QEEQERKVRALSEMASEQLKRFDELKelklhKEFQDLQEVMEKsTREALGHQEKLKEEHRHRAKILNLKLREAEQQRVKQ 232
Cdd:COG4942  22 AAEAEAELEQLQQEIAELEKELAALK-----KEEKALLKQLAA-LERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 233 AEQEQLRKEEGQVRLRSLYSLQE----EVLQLNQQLDASSQHKELLSVDLAAFQTRGNQLCGLISSIIRTTLEsgypTAE 308
Cdd:COG4942  96 RAELEAQKEELAELLRALYRLGRqpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE----LEA 171
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 58037369 309 NQAEAERALQEMRDLLSDLEQEITRASQVKKKHEEEAKVKRQESQVQQ 356
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
165-351 2.18e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 2.18e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 165 EMASEQLKRFD-ELKELK-LHKEFQDLQEVMEKsTREALGHQEKLKEEHRHRAKILNLKLREAEQQRVKQAEQEQLrkEE 242
Cdd:COG4717  67 ELNLKELKELEeELKEAEeKEEEYAELQEELEE-LEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAEL--AE 143
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 243 GQVRLRSLYSLQEEVLQLNQQLDASSQHKELLSVDLAAFQtrgNQLCGLISSIIRTTLESGYPTAENQAEAERALQEMRD 322
Cdd:COG4717 144 LPERLEELEERLEELRELEEELEELEAELAELQEELEELL---EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
                       170       180
                ....*....|....*....|....*....
gi 58037369 323 LLSDLEQEITRASQVKKKHEEEAKVKRQE 351
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEAR 249
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
210-356 2.68e-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: 41.09  E-value: 2.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369  210 EHRH---RAKILNLKLREAEQQRVKQAEQEQLRKEEGQ---VRLRSLYSLQEEVLQLNQQLDASSQHKELLSVDLAAFQT 283
Cdd:COG3096  506 SQQAlaqRLQQLRAQLAELEQRLRQQQNAERLLEEFCQrigQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 58037369  284 RGNQLCGLISSiirttLESGYPTAENQAEAERALQEMRDLLSDLEQEITRASQVKKKHEEEAKVKRQESQVQQ 356
Cdd:COG3096  586 QLEQLRARIKE-----LAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARK 653
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
153-339 3.98e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.98e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 153 QEEQERKVRALSEMASEQLKRFDELKElKLHKEFQDLQEVMEKSTREALGHQEKLKEEHRHRAKILNLKLR-EAEQQRVK 231
Cdd:COG1196 339 LEELEEELEEAEEELEEAEAELAEAEE-ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAeEALLERLE 417
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 232 QAEQEQLRKEEGQVRLRSLysLQEEVLQLNQQLDASSQHKELLSVDLAAFQTRGNQLCGLISSIIRTTLEsgyptAENQA 311
Cdd:COG1196 418 RLEEELEELEEALAELEEE--EEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEE-----LAEAA 490
                       170       180
                ....*....|....*....|....*...
gi 58037369 312 EAERALQEMRDLLSDLEQEITRASQVKK 339
Cdd:COG1196 491 ARLLLLLEAEADYEGFLEGVKAALLLAG 518
FAM184 pfam15665
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
138-235 4.32e-03

Family with sequence similarity 184, A and B; The function of FAM184 is not known.


Pssm-ID: 464788 [Multi-domain]  Cd Length: 211  Bit Score: 39.26  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   138 ELAHRMRGTEGLRQWQEEQ---ERKVRALS----EMASEQLKRFDELKElKLHKEFQDLQEVMEKSTREALGHQEKLKEE 210
Cdd:pfam15665  91 EAEHRQRVVELSREVEEAKrafEEKLESFEqlqaQFEQEKRKALEELRA-KHRQEIQELLTTQRAQSASSLAEQEKLEEL 169
                          90       100
                  ....*....|....*....|....*
gi 58037369   211 HRHRAKILNLKLREAEQQRVKQAEQ 235
Cdd:pfam15665 170 HKAELESLRKEVEDLRKEKKKLAEE 194
Caldesmon pfam02029
Caldesmon;
138-248 4.61e-03

Caldesmon;


Pssm-ID: 460421 [Multi-domain]  Cd Length: 495  Bit Score: 40.24  E-value: 4.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369   138 ELAHRMRGTEGLRQWQEEQERKVRALSEMASEQLKRFDELKELKLHKEFQDLqEVMEKSTREALGHQEKLKEEHRHRAKI 217
Cdd:pfam02029 214 EEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEF-EKLRQKQQEAELELEELKKKREERRKL 292
                          90       100       110
                  ....*....|....*....|....*....|..
gi 58037369   218 lnlklREAEQQRVKQAEQE-QLRKEEGQVRLR 248
Cdd:pfam02029 293 -----LEEEEQRRKQEEAErKLREEEEKRRMK 319
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
139-343 5.72e-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: 40.32  E-value: 5.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369  139 LAHRMRGTEGLRQWQEEQERkvraLSEMASEqlkrFDELKELKLHKEfQDLQEVMEKSTR--EALGHQEKLKeehRHRAK 216
Cdd:COG3096  288 LELRRELFGARRQLAEEQYR----LVEMARE----LEELSARESDLE-QDYQAASDHLNLvqTALRQQEKIE---RYQED 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369  217 I--LNLKLREAEQQRVKQAEQeqlrKEEGQVRLRslySLQEEVLQLNQQLdASSQHKellsvdLAAFQTRGNQ------- 287
Cdd:COG3096  356 LeeLTERLEEQEEVVEEAAEQ----LAEAEARLE---AAEEEVDSLKSQL-ADYQQA------LDVQQTRAIQyqqavqa 421
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 58037369  288 ------LCGLISsiirTTLESgypTAENQAEAERALQEMRDLLSDLEQEITRASQVKKKHEE 343
Cdd:COG3096  422 lekaraLCGLPD----LTPEN---AEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEK 476
CHASE3 COG5278
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
154-356 6.67e-03

Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];


Pssm-ID: 444089 [Multi-domain]  Cd Length: 530  Bit Score: 39.50  E-value: 6.67e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 154 EEQERKVRALSEMASEQLKRFDELKELkLHKEFQDLQEVMEksTREALGHQEKLKEEHRHRAKILNLKLREAEQQRVKQA 233
Cdd:COG5278  89 DELLAELRSLTADNPEQQARLDELEAL-IDQWLAELEQVIA--LRRAGGLEAALALVRSGEGKALMDEIRARLLLLALAL 165
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369 234 EQEQLRKEEGQVRLRSLYSLQEEVLQLNQQLDASSQHKELLSVDLAAFQTRGNQLCGLISSIIRTTLESGYPTAENQAEA 313
Cdd:COG5278 166 AALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALL 245
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 58037369 314 ERALQEMRDLLSDLEQEITRASQVKKKHEEEAKVKRQESQVQQ 356
Cdd:COG5278 246 LAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAA 288
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
181-426 8.61e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.39  E-value: 8.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    181 KLHKEFQDLQEVMEKSTREALGHQEKLKE----EHRHRAKILNLKLREAEQQRVKQAEQEQLRKEEGQvrlrsLYSLQEE 256
Cdd:pfam01576  149 KLSKERKLLEERISEFTSNLAEEEEKAKSlsklKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGE-----STDLQEQ 223
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    257 VLQLNQQLD---ASSQHKEllsVDLAAFQTRGNQLCGlissiirttlesgyptaeNQAEAERALQEMRDLLSDLEQEITR 333
Cdd:pfam01576  224 IAELQAQIAelrAQLAKKE---EELQAALARLEEETA------------------QKNNALKKIRELEAQISELQEDLES 282
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58037369    334 ASQVKKKHEEEAKVKRQESQVQQGPAPPTQTSAPSPSPVGAQNE----DLQVKVQDSTMQWYQQLQDASAKCVLAFEDLT 409
Cdd:pfam01576  283 ERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREqevtELKKALEEETRSHEAQLQEMRQKHTQALEELT 362
                          250
                   ....*....|....*..
gi 58037369    410 SSKDsQTKKIKMDLQKA 426
Cdd:pfam01576  363 EQLE-QAKRNKANLEKA 378
 
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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